|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-556 |
0e+00 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 1218.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 1 MSSQFVYTMHRVGKVVPPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQPGIKIGYLPQEPK 80
Cdd:PRK11819 1 MMAQYIYTMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 81 LEPQQTVREAVEEAVSEVKSALTRLDEVYALYADPDADFDKLAAEQANLEAIIQAHDGHNLDNQLERAADALRLPDWDAK 160
Cdd:PRK11819 81 LDPEKTVRENVEEGVAEVKAALDRFNEIYAAYAEPDADFDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPPWDAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 161 IEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIP 240
Cdd:PRK11819 161 VTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 241 WEGNYSSWLEQKEKRLEQEQAAENARQKSIAKELEWVRQNPKGRQAKSKARMARFDELNSGEYQKRNETNELFIPPGPRL 320
Cdd:PRK11819 241 WEGNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWVRQSPKARQAKSKARLARYEELLSEEYQKRNETNEIFIPPGPRL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 321 GDKVIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRDAMD 400
Cdd:PRK11819 321 GDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 401 DKKTVWEEVSNGQDILTIGNFEIPSRAYVGRFNFKGVDQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVET 480
Cdd:PRK11819 401 PNKTVWEEISGGLDIIKVGNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 481 LRALENAILEFPGCAMVISHDRWFLDRIATHILDYGDEGKVTFYEGNFSDYEEWKKKTLGDAATQPHRIKYKRIAK 556
Cdd:PRK11819 481 LRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDSQVEWFEGNFQEYEEDKKRRLGADAARPHRIKYKKLTR 556
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-554 |
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: 1150.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 3 SQFVYTMHRVGKVVPPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQPGIKIGYLPQEPKLE 82
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 83 PQQTVREAVEEAVSEVKSALTRLDEVYALYADPDADFDKLAAEQANLEAIIQAHDGHNLDNQLERAADALRLPDWDAKIE 162
Cdd:TIGR03719 81 PTKTVRENVEEGVAEIKDALDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDADVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 163 HLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIPWE 242
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 243 GNYSSWLEQKEKRLEQEQAAENARQKSIAKELEWVRQNPKGRQAKSKARMARFDELNSGEYQKRNETNELFIPPGPRLGD 322
Cdd:TIGR03719 241 GNYSSWLEQKQKRLEQEEKEESARQKTLKRELEWVRQSPKGRQAKSKARLARYEELLSQEFQKRNETAEIYIPPGPRLGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 323 KVIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRDAMDDK 402
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 403 KTVWEEVSNGQDILTIGNFEIPSRAYVGRFNFKGVDQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLR 482
Cdd:TIGR03719 401 KTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLR 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1735515619 483 ALENAILEFPGCAMVISHDRWFLDRIATHILDYGDEGKVTFYEGNFSDYEEWKKKTLGDAATQPHRIKYKRI 554
Cdd:TIGR03719 481 ALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEWFEGNFSEYEEDKKRRLGEDADQPHRIKYKKL 552
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-534 |
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: 736.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 9 MHRVGKVVPpKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQPGIKIGYLPQEPKLEPQQTVR 88
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 89 EAVEEAVSEVKSALTRLDEVYALYADPDADFDKLAAeqanLEAIIQAHDGHNLDNQLERAADALRLP--DWDAKIEHLSG 166
Cdd:COG0488 80 DTVLDGDAELRALEAELEELEAKLAEPDEDLERLAE----LQEEFEALGGWEAEARAEEILSGLGFPeeDLDRPVSELSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYS 246
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 247 SWLEQKEKRLEQEQAAENARQKSIAKELEWVRQN-PKGRQAK-SKARMARFDELNSGEYQKRNETNELFIPPGPRLGDKV 324
Cdd:COG0488 236 AYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFrAKARKAKqAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLGKKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRDAMDDKKT 404
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 405 VWEEVSNGQDiltiGNFEIPSRAYVGRFNFKGVDQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRAL 484
Cdd:COG0488 396 VLDELRDGAP----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEAL 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1735515619 485 ENAILEFPGCAMVISHDRWFLDRIATHILDYGDeGKVTFYEGNFSDYEEW 534
Cdd:COG0488 472 EEALDDFPGTVLLVSHDRYFLDRVATRILEFED-GGVREYPGGYDDYLEK 520
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
32-530 |
3.86e-108 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 336.92 E-value: 3.86e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 32 PGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQPGIKIGYLPQEPKLEPQQTVREAVEEAVSEVKSALTRLDEVYAL 111
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGTVYDFVAEGIEEQAEYLKRYHDISHL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 112 YA-DPDadfDKLAAEQANLEAIIQAHDGHNLDNQLERAADALRLpDWDAKIEHLSGGERRRVALCRLLLEKPDMLLLDEP 190
Cdd:PRK11147 108 VEtDPS---EKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGL-DPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 191 TNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSSWLEQKEK--RLEQEQAAEnaRQK 268
Cdd:PRK11147 184 TNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEalRVEELQNAE--FDR 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 269 SIAKELEWVRQNPKGRQAKSKARMARFDELNSGEYQKRNE--TNELFIPPGPRLGDKVIEVQNLTKSYGDRTLIDDLSFS 346
Cdd:PRK11147 262 KLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVmgTAKMQVEEASRSGKIVFEMENVNYQIDGKQLVKDFSAQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 347 IPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRDAMDDKKTVWEEVSNGQDILTIGNFEIPSR 426
Cdd:PRK11147 342 VQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTVMDNLAEGKQEVMVNGRPRHVL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 427 AYVGRFNFkgvdQQKR----VGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFPGCAMVISHDR 502
Cdd:PRK11147 422 GYLQDFLF----HPKRamtpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDR 497
|
490 500
....*....|....*....|....*...
gi 1735515619 503 WFLDRIATHILDYGDEGKVTFYEGNFSD 530
Cdd:PRK11147 498 QFVDNTVTECWIFEGNGKIGRYVGGYHD 525
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
26-531 |
1.50e-82 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 267.14 E-value: 1.50e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 26 ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQPGIKIGYLPQEPKLEPQQTVREAV---EEAVSEVKSal 102
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTVimgHTELWEVKQ-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 103 trldEVYALYADPDA-DFDKLAAeqANLEAIIQAHDGHNLDNqleRAADALrlpdWDAKIE---H------LSGGERRRV 172
Cdd:PRK15064 98 ----ERDRIYALPEMsEEDGMKV--ADLEVKFAEMDGYTAEA---RAGELL----LGVGIPeeqHyglmseVAPGWKLRV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 173 ALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSSWLEQK 252
Cdd:PRK15064 165 LLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 253 EKRLEQeQAAENARQKSIAKEL-EWVRQ---N-PKGRQAKSKARMA---RFDELNSGEYQKRnetnelFI--PPGPRLGD 322
Cdd:PRK15064 245 TQARER-LLADNAKKKAQIAELqSFVSRfsaNaSKAKQATSRAKQIdkiKLEEVKPSSRQNP------FIrfEQDKKLHR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 323 KVIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLA-----SVDQFrd 397
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGyyaqdHAYDF-- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 398 amDDKKTVWEEVSN----GQDILTIgnfeipsRAYVGRFNFKGVDQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPT 473
Cdd:PRK15064 396 --ENDLTLFDWMSQwrqeGDDEQAV-------RGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1735515619 474 NDLDVETLRALENAILEFPGCAMVISHDRWFLDRIATHILDYGDEGkVTFYEGNFSDY 531
Cdd:PRK15064 467 NHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDG-VVDFSGTYEEY 523
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
327-535 |
3.95e-69 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 231.49 E-value: 3.95e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 327 VQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQfRDAMDDKKTVW 406
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQ-EPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 407 EEVSNG--------------------------------QDILTIGNFEIPSRA--YVGRFNFKGVDQQKRVGELSGGERG 452
Cdd:COG0488 80 DTVLDGdaelraleaeleeleaklaepdedlerlaelqEEFEALGGWEAEARAeeILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 453 RLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFPGCAMVISHDRWFLDRIATHILDYgDEGKVTFYEGNFSDYE 532
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILEL-DRGKLTLYPGNYSAYL 238
|
...
gi 1735515619 533 EWK 535
Cdd:COG0488 239 EQR 241
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-534 |
4.01e-67 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 229.29 E-value: 4.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvDKEFEGEARPQPGI-KIGYLPQE-PKLEpqQTVREAVEEAVSE 97
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKN-EISADGGSYTFPGNwQLAWVNQEtPALP--QPALEYVIDGDRE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 98 VKSALTRLDEvyalyADPDADFDKLAAEQANLEAI----IQAHdGHNLDNQLERAADALRLPdwdakIEHLSGGERRRVA 173
Cdd:PRK10636 91 YRQLEAQLHD-----ANERNDGHAIATIHGKLDAIdawtIRSR-AASLLHGLGFSNEQLERP-----VSDFSGGWRMRLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 174 LCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSSWLEQKE 253
Cdd:PRK10636 160 LAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 254 KRLEQEQAAENARQKSIAKELEWV----RQNPKGRQAKSKARMARFDELNSGEYQKrNETNELFIPPgPRLGDKVIEVQN 329
Cdd:PRK10636 240 TRLAQQQAMYESQQERVAHLQSYIdrfrAKATKAKQAQSRIKMLERMELIAPAHVD-NPFHFSFRAP-ESLPNPLLKMEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 330 LTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRdamddKKTVWEEV 409
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQ-----LEFLRADE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 410 SNGQDILTIGNFEIPS--RAYVGRFNFKGVDQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENA 487
Cdd:PRK10636 393 SPLQHLARLAPQELEQklRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1735515619 488 ILEFPGCAMVISHDRWFLdRIATHILDYGDEGKVTFYEGNFSDYEEW 534
Cdd:PRK10636 473 LIDFEGALVVVSHDRHLL-RSTTDDLYLVHDGKVEPFDGDLEDYQQW 518
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
325-519 |
3.53e-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: 179.95 E-value: 3.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQfrdamddkkt 404
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 405 vweevsngqdiltignfeipsrayvgrfnfkgvdqqkrvgeLSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRAL 484
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....*
gi 1735515619 485 ENAILEFPGCAMVISHDRWFLDRIATHILDYGDEG 519
Cdd:cd03221 110 EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
19-237 |
2.75e-50 |
|
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: 169.55 E-value: 2.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQPGIKIGYLPQepklepqqtvreaveeavsev 98
Cdd:cd03221 12 GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 99 ksaltrldevyalyadpdadfdklaaeqanleaiiqahdghnldnqleraadalrlpdwdakiehLSGGERRRVALCRLL 178
Cdd:cd03221 71 -----------------------------------------------------------------LSGGEKMRLALAKLL 85
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 179 LEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGE 237
Cdd:cd03221 86 LENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-539 |
3.24e-49 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 181.21 E-value: 3.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdKEFEGEARpqpGIKIGYLPQE--------------PKLEPQQ 85
Cdd:PLN03073 190 RDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAM--HAIDGIPK---NCQILHVEQEvvgddttalqcvlnTDIERTQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 TVREavEEAVSEVKSALTRLDEVYALYADPDADFDKLAAEQaNLEAIIQAHDGHNLDNQLERAADALRLPDWDAKIEH-- 163
Cdd:PLN03073 265 LLEE--EAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQ-RLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQVka 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 164 ---LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIP 240
Cdd:PLN03073 342 tktFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVT 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 241 WEGNYSSWLEQKEKRLEQEQAAENARQKSIAKELEWV---RQNPKGR---QAKSKA--RMARFDE-LNSGEYQKRnetne 311
Cdd:PLN03073 422 YKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIdkfRYNAKRAslvQSRIKAldRLGHVDAvVNDPDYKFE----- 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 312 lFIPPGPRLGDKVIEVQNLTKSY-GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLA 390
Cdd:PLN03073 497 -FPTPDDRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 391 SVDQFR-DAMDDKKTVWEEVSNgqdiLTIGNFEIPSRAYVGRFNFKGVDQQKRVGELSGGERGRLHLAKLLQRGGNVLLL 469
Cdd:PLN03073 576 VFSQHHvDGLDLSSNPLLYMMR----CFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLL 651
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 470 DEPTNDLDVETLRALENAILEFPGCAMVISHDRWFLDRiATHILDYGDEGKVTFYEGNFSDYeewkKKTL 539
Cdd:PLN03073 652 DEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISG-SVDELWVVSEGKVTPFHGTFHDY----KKTL 716
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
20-513 |
1.47e-44 |
|
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: 165.08 E-value: 1.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DKEFEGEAR-----------PQPGIKIGYLPQEPklePQQ 85
Cdd:COG1123 19 VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLldgrdllelseALRGRRIGMVFQDP---MTQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 TVREAVEEAVSEVKSALtrldevyalyadpdadfdKLAAEQANLEAIiqahdghnldnqleRAADALRLPD-WDAKIEHL 164
Cdd:COG1123 96 LNPVTVGDQIAEALENL------------------GLSRAEARARVL--------------ELLEAVGLERrLDRYPHQL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIp 240
Cdd:COG1123 144 SGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIV- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 241 wegnysswleqkekrlEQEQAAEnarqksiakelewVRQNPKGRQAKSKARMARFDElnsgeyqkrnetnelfiPPGPRL 320
Cdd:COG1123 223 ----------------EDGPPEE-------------ILAAPQALAAVPRLGAARGRA-----------------APAAAA 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 321 GDKVIEVQNLTKSY-----GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQ 394
Cdd:COG1123 257 AEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdGKDLTKLSRRS 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 395 FRD--------------AMDDKKTVWEEVSNGQDILTIGNF-EIPSRAY-----VG---RFnfkgvdQQKRVGELSGGER 451
Cdd:COG1123 337 LRElrrrvqmvfqdpysSLNPRMTVGDIIAEPLRLHGLLSRaERRERVAellerVGlppDL------ADRYPHELSGGQR 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 452 GRLHLAKLLQRGGNVLLLDEPTNDLDVeTLRAlenAILEF-------PGCAMV-ISHDRWFLDRIATHIL 513
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDV-SVQA---QILNLlrdlqreLGLTYLfISHDLAVVRYIADRVA 476
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
20-237 |
1.00e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 138.03 E-value: 1.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA----RPQPGI-------KIGYLPQEPKLEPQqTVR 88
Cdd:COG4619 13 KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgKPLSAMpppewrrQVAYVPQEPALWGG-TVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 89 EaveeavsevksaltrldevyalyadpdadfdklaaeqaNLEAIIQAHDGHNLDNQLERAADALRLPD--WDAKIEHLSG 166
Cdd:COG4619 92 D--------------------------------------NLPFPFQLRERKFDRERALELLERLGLPPdiLDKPVERLSG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGE 237
Cdd:COG4619 134 GERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
325-514 |
1.03e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 139.04 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSIT-MGETVVLASVDQFR------- 396
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvLGEDVARDPAEVRRrigyvpq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 397 -DAMDDKKTVWEEVSNGQDILTIGNFEIPSRA--YVGRFNFKGVdQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPT 473
Cdd:COG1131 81 ePALYPDLTVRENLRFFARLYGLPRKEARERIdeLLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1735515619 474 NDLDVETLRALENAILEF--PGCAMVIShdrwfldriaTHILD 514
Cdd:COG1131 160 SGLDPEARRELWELLRELaaEGKTVLLS----------THYLE 192
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
20-226 |
3.03e-37 |
|
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: 136.84 E-value: 3.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE----------ARPQPGIKIGYLPQEPKLEPQQTVRE 89
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEvlwngepirdAREDYRRRLAYLGHADGLKPELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 90 aveeavsevksaltrldevyalyadpdadfdklaaeqaNLEAIIQAHDGHNLDNQLERAADALRLPD-WDAKIEHLSGGE 168
Cdd:COG4133 95 --------------------------------------NLRFWAALYGLRADREAIDEALEAVGLAGlADLPVRQLSAGQ 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1735515619 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY---EGTVVAITHDRYFLDNV 226
Cdd:COG4133 137 KRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAA 197
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
324-541 |
2.25e-35 |
|
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: 132.67 E-value: 2.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRDAM---D 400
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIgvlP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 401 DKKTVWEEVSnGQDILTI-----GNF--EIPSRA--YVGRFNFkGVDQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDE 471
Cdd:COG4555 81 DERGLYDRLT-VRENIRYfaelyGLFdeELKKRIeeLIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 472 PTNDLDVETLRALENAILEF---PGCAMVISHDRWFLDRIATHILdYGDEGKVTFYEgnfsDYEEWKKKTLGD 541
Cdd:COG4555 159 PTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVV-ILHKGKVVAQG----SLDELREEIGEE 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
326-513 |
7.66e-35 |
|
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: 130.35 E-value: 7.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 326 EVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLAS-----VDQFRDAm 399
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLEKERkrigyVPQRRSI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 400 dDKK---TVWEEVSNGQDIlTIGNFEIPSRAY----------VGRFNFKgvdqQKRVGELSGGERGRLHLAKLLQRGGNV 466
Cdd:cd03235 80 -DRDfpiSVRDVVLMGLYG-HKGLFRRLSKADkakvdealerVGLSELA----DRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 467 LLLDEPTNDLDVET----------LRALENAILefpgcamVISHDRWFLDRIATHIL 513
Cdd:cd03235 154 LLLDEPFAGVDPKTqediyellreLRREGMTIL-------VVTHDLGLVLEYFDRVL 203
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
322-513 |
9.64e-35 |
|
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: 9.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 322 DKVIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLAS-----VDQF 395
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfGKPPRRARrrigyVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 396 RDAmdDKK---TVWEEVSNGQDiLTIGNFEIPSRAY----------VGRFNFKgvdqQKRVGELSGGERGRLHLAKLLQR 462
Cdd:COG1121 84 AEV--DWDfpiTVRDVVLMGRY-GRRGLFRRPSRADreavdealerVGLEDLA----DRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1735515619 463 GGNVLLLDEPTNDLDVETLRALENAILEFP--GCAM-VISHDRWFLDRIATHIL 513
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRreGKTIlVVTHDLGAVREYFDRVL 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
325-513 |
1.63e-34 |
|
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: 128.28 E-value: 1.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITmgetvvLASVDQFRDAMDDKK- 403
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK------VLGKDIKKEPEEVKRr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 404 --TVWEEVSNGQDiLTignfeipsrayvGRFNFKgvdqqkrvgeLSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETL 481
Cdd:cd03230 75 igYLPEEPSLYEN-LT------------VRENLK----------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESR 131
|
170 180 190
....*....|....*....|....*....|....*
gi 1735515619 482 RALENAILEFP--GCAMVI-SHDRWFLDRIATHIL 513
Cdd:cd03230 132 REFWELLRELKkeGKTILLsSHILEEAERLCDRVA 166
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
326-517 |
2.92e-34 |
|
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: 126.98 E-value: 2.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 326 EVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMgetvvlasvdqfrdamddkktv 405
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 406 weevsNGQDILTIGNFEIpsRAYVGrfnfkgvdqqkRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALE 485
Cdd:cd00267 59 -----DGKDIAKLPLEEL--RRRIG-----------YVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180 190
....*....|....*....|....*....|....*
gi 1735515619 486 NAILEF--PGCAMV-ISHDRWFLDRIATHILDYGD 517
Cdd:cd00267 121 ELLRELaeEGRTVIiVTHDPELAELAADRVIVLKD 155
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
324-517 |
8.21e-34 |
|
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: 127.21 E-value: 8.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFR------- 396
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRrrlaylg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 397 --DAMDDKKTVWEEVSNGQDILTIGNFEIPSRAYVGRFNFKGVdQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTN 474
Cdd:COG4133 82 haDGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1735515619 475 DLDVETLRALENAILEFP---GCAMVISHDRwfLDRIATHILDYGD 517
Cdd:COG4133 161 ALDAAGVALLAELIAAHLargGAVLLTTHQP--LELAAARVLDLGD 204
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-192 |
1.40e-33 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 124.68 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-----------ARPQPGIKIGYLPQEPKLEPQQTVREAV 91
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTilldgqdltddERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 92 EEAvsevksaltrldevyalyadpdadfdklaaeqanleAIIQAHDGHNLDNQLERAADALRLPD-----WDAKIEHLSG 166
Cdd:pfam00005 81 RLG------------------------------------LLLKGLSKREKDARAEEALEKLGLGDladrpVGERPGTLSG 124
|
170 180
....*....|....*....|....*.
gi 1735515619 167 GERRRVALCRLLLEKPDMLLLDEPTN 192
Cdd:pfam00005 125 GQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
326-513 |
1.59e-33 |
|
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: 125.63 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 326 EVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMgetvvlasvdqfrdamddkktv 405
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 406 weevsNGQDILTIGNFEI-PSRAYV-------GRFNFKgvdqQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLD 477
Cdd:cd03214 59 -----DGKDLASLSPKELaRKIAYVpqalellGLAHLA----DRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1735515619 478 ----VETLRALENAILEFPGCAMVISHDRWFLDRIATHIL 513
Cdd:cd03214 130 iahqIELLELLRRLARERGKTVVMVLHDLNLAARYADRVI 169
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
324-513 |
3.08e-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: 127.08 E-value: 3.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVV-----------LASV 392
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaslsrrelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 393 DQFRDAMDDkKTVWEEVSNGQdiltignfeipsRAYVGRFNFKG------VDQ-----------QKRVGELSGGERGRLH 455
Cdd:COG1120 81 PQEPPAPFG-LTVRELVALGR------------YPHLGLFGRPSaedreaVEEalertglehlaDRPVDELSGGERQRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 456 LAKLLQRGGNVLLLDEPTNDLD----VETLRALENAILEFPGCAMVISHDrwfLD---RIATHIL 513
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRLARERGRTVVMVLHD---LNlaaRYADRLV 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
325-514 |
3.59e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 125.70 E-value: 3.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSIT---------------------- 382
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkplsampppewrrqvayvp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 383 -----MGETV--VLASVDQFRDAMDDKKTVweevsngqdiltignfeipsRAYVGRFNFKGVDQQKRVGELSGGERGRLH 455
Cdd:COG4619 81 qepalWGGTVrdNLPFPFQLRERKFDRERA--------------------LELLERLGLPPDILDKPVERLSGGERQRLA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 456 LAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFP----GCAMVISHDRWFLDRIATHILD 514
Cdd:COG4619 141 LIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLT 203
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
19-237 |
3.75e-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: 125.66 E-value: 3.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE---------ARPQPGI--KIGYLPQEPKlepQQTV 87
Cdd:cd03225 13 ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEvlvdgkdltKLSLKELrrKVGLVFQNPD---DQFF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 88 REAVEEavsEVKSALTRLdevyalyadpdadfdKLAAEQANlEAIIQAHDGHNLDNQLERaadalrlpdwdaKIEHLSGG 167
Cdd:cd03225 90 GPTVEE---EVAFGLENL---------------GLPEEEIE-ERVEEALELVGLEGLRDR------------SPFTLSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 168 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHDRYFLDNVAGWILELDRGE 237
Cdd:cd03225 139 QKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
19-237 |
4.83e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 126.33 E-value: 4.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR----------PQPGIKIGYLPQEPKLEPQQTVR 88
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvardpAEVRRRIGYVPQEPALYPDLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 89 EAVeeavsevksaltrldEVYA-LYADPDADFDKLAAEqanleaiiqahdghnldnqlerAADALRLPDW-DAKIEHLSG 166
Cdd:COG1131 92 ENL---------------RFFArLYGLPRKEARERIDE----------------------LLELFGLTDAaDRKVGTLSG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1735515619 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHDRYFLDNVAGWILELDRGE 237
Cdd:COG1131 135 GMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaEGkTVLLSTHYLEEAERLCDRVAIIDKGR 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-236 |
1.05e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.59 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR------PQPGIKIGYLPQEPKLEPQQ--TVREA 90
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVPQRAEVDWDFpiTVRDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 91 VEEAVSEVKSALTRLDEVyalyadpdadfDKLAAEQAnleaiiqahdghnldnqLERA-ADALRlpdwDAKIEHLSGGER 169
Cdd:COG1121 98 VLMGRYGRRGLFRRPSRA-----------DREAVDEA-----------------LERVgLEDLA----DRPIGELSGGQQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 170 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHDRYFLDNVAGWILELDRG 236
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrrEGkTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
18-219 |
1.06e-32 |
|
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: 125.93 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 18 PKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE----------------ARpqpgiKIGYLPQEPKL 81
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEvlldgrdlaslsrrelAR-----RIAYVPQEPPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 82 EPQQTVREAVeeavsevksALTRldevYA---LYADPDADfDKLAAEQAnleaiiqahdghnldnqLERA-ADALRlpdw 157
Cdd:COG1120 87 PFGLTVRELV---------ALGR----YPhlgLFGRPSAE-DREAVEEA-----------------LERTgLEHLA---- 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 158 DAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD-AESVAWLE--RFLHDYEG-TVVAITHD 219
Cdd:COG1120 132 DRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDlAHQLEVLEllRRLARERGrTVVMVLHD 197
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
340-474 |
2.09e-32 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 121.60 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 340 IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSIT-MGETVVLASVDQFR---------DAMDDKKTVWEEV 409
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILlDGQDLTDDERKSLRkeigyvfqdPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 410 SNGQDILTIGNFEIPSRAYVGRFNFKGVDQQKRV-----GELSGGERGRLHLAKLLQRGGNVLLLDEPTN 474
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-517 |
3.12e-31 |
|
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: 127.23 E-value: 3.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDkefegEARPQPG---IKIGYLPQEPKLEPQQTVREAVEEAVSE- 97
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMD-----QYEPTSGriiYHVALCEKCGYVERPSKVGEPCPVCGGTl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 98 -------------VKSALTR-----LDEVYALYADpdadfdklaaeQANLEAIIQA-HD-GHNLDNQLERAADALRLPDW 157
Cdd:TIGR03269 90 epeevdfwnlsdkLRRRIRKriaimLQRTFALYGD-----------DTVLDNVLEAlEEiGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 158 DAKIEH----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV----AWLERFLHDYEGTVVAITHDRYFLDNVAGW 229
Cdd:TIGR03269 159 SHRITHiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 230 ILELDRGEgIPWEGNYSswlEQKEKRLEQEQAAENARqksiakELEwvrqnpkgrqakskarmarfdelnsgeyqkrnet 309
Cdd:TIGR03269 239 AIWLENGE-IKEEGTPD---EVVAVFMEGVSEVEKEC------EVE---------------------------------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 310 nelfippgprLGDKVIEVQNLTKSYG--DRTLI---DDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPdagsiTMG 384
Cdd:TIGR03269 275 ----------VGEPIIKVRNVSKRYIsvDRGVVkavDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEP-----TSG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 385 ETVVLAS---VDQFRDAMDDK-------------------KTVWEEVSNgqdilTIG---NFEIPSRAYVGRFNFKGVDQ 439
Cdd:TIGR03269 340 EVNVRVGdewVDMTKPGPDGRgrakryigilhqeydlyphRTVLDNLTE-----AIGlelPDELARMKAVITLKMVGFDE 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 440 QKRVG-------ELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAIL----EFPGCAMVISHDRWFL--- 505
Cdd:TIGR03269 415 EKAEEildkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILkareEMEQTFIIVSHDMDFVldv 494
|
570
....*....|....*..
gi 1735515619 506 -DRIAT----HILDYGD 517
Cdd:TIGR03269 495 cDRAALmrdgKIVKIGD 511
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-513 |
8.53e-31 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 126.46 E-value: 8.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 32 PGAKIGVLGLNGAGKSTLLRIMAG-----------------VDKEFEG-------EARPQPGIKIGYLPQEPKLEPQQ-- 85
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGelipnlgdyeeepswdeVLKRFRGtelqnyfKKLYNGEIKVVHKPQYVDLIPKVfk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 -TVREAveeavsevksaLTRLDEVYAlyadpdadFDKLAaEQANLEAIiqahdghnldnqleraadalrlpdWDAKIEHL 164
Cdd:PRK13409 178 gKVREL-----------LKKVDERGK--------LDEVV-ERLGLENI------------------------LDRDISEL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDyEGTVVAITHDRYFLDNVAGWILELdrgEGIPw 241
Cdd:PRK13409 214 SGGELQRVAIAAALLRDADFYFFDEPTSYLDIRqrlNVARLIRELAE-GKYVLVVEHDLAVLDYLADNVHIA---YGEP- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 242 eGNYSSWLEQKEKR------LEQEQAAENARqksiakelewVRQNPkgrqakskarmARFDELNSGEYQKRnetnelfip 315
Cdd:PRK13409 289 -GAYGVVSKPKGVRvgineyLKGYLPEENMR----------IRPEP-----------IEFEERPPRDESER--------- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 316 pgprlgDKVIEVQNLTKSYGDRTLIDDLSFsIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETV-------- 387
Cdd:PRK13409 338 ------ETLVEYPDLTKKLGDFSLEVEGGE-IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKIsykpqyik 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 388 --VLASVDQF-RDAMDDKKT--VWEEVSNG---QDILtignfeipsrayvgrfnfkgvdqQKRVGELSGGERGRLHLAKL 459
Cdd:PRK13409 411 pdYDGTVEDLlRSITDDLGSsyYKSEIIKPlqlERLL-----------------------DKNVKDLSGGELQRVAIAAC 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1735515619 460 LQRGGNVLLLDEPTNDLDVE----TLRALENAILEFPGCAMVISHDRWFLDRIATHIL 513
Cdd:PRK13409 468 LSRDADLYLLDEPSAHLDVEqrlaVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
19-237 |
1.11e-30 |
|
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: 117.50 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA--------RPQPGIK--IGYLPQEPKLEPQQTVR 88
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkdikKEPEEVKrrIGYLPEEPSLYENLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 89 EaveeavsevksaltrldevyalyadpdadfdklaaeqanleaiiqahdghNLDnqleraadalrlpdwdakiehLSGGE 168
Cdd:cd03230 92 E--------------------------------------------------NLK---------------------LSGGM 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1735515619 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY---EGTVVAITHDRYFLDNVAGWILELDRGE 237
Cdd:cd03230 101 KQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
325-512 |
1.42e-30 |
|
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: 118.76 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLI--DDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFR------ 396
Cdd:cd03263 1 LQIRNLTKTYKKGTKPavDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARqslgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 397 ---DAMDDKKTVWEE---------VSNGQDILTIGNfeipsraYVGRFNFKGVdQQKRVGELSGGERGRLHLAKLLQRGG 464
Cdd:cd03263 81 pqfDALFDELTVREHlrfyarlkgLPKSEIKEEVEL-------LLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1735515619 465 NVLLLDEPTNDLDVETLRALENAILEF-PGCAMVI-SHDRWFLDRIATHI 512
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVrKGRSIILtTHSMDEAEALCDRI 202
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
326-513 |
2.03e-30 |
|
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: 117.95 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 326 EVQNLTKSYGD--RTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLAS-----------V 392
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLslkelrrkvglV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 393 DQFRDAMDDKKTVWEEVSNGQDILTIGNFEIPSRA--YVGRFNFKGVdQQKRVGELSGGERGRLHLAKLLQRGGNVLLLD 470
Cdd:cd03225 81 FQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVeeALELVGLEGL-RDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1735515619 471 EPTNDLDVETLRALENAILEFPGCAM---VISHDRWFLDRIATHIL 513
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKtiiIVTHDLDLLLELADRVI 205
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
17-237 |
2.06e-30 |
|
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: 118.59 E-value: 2.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 17 PPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG---------------EARPqpgiKIGYLPQEPKl 81
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGevlvdgkditkknlrELRR----KVGLVFQNPD- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 82 epQQTVREAVEEavsEVKSALTRLdevyalyadpdadfdKLAAEQAnleaiiqahdghnlDNQLERAADALRLPDW-DAK 160
Cdd:COG1122 86 --DQLFAPTVEE---DVAFGPENL---------------GLPREEI--------------RERVEEALELVGLEHLaDRP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 161 IEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHDRYFLDNVAGWILELDRGE 237
Cdd:COG1122 132 PHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGkTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
17-261 |
2.56e-30 |
|
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: 125.72 E-value: 2.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 17 PPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpqpgIK-----------------IGYLPQEP 79
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR------ILidgidlrqidpaslrrqIGVVLQDV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 80 KLEpQQTVREAVeeavsevksaltrldevyaLYADPDADFDKL--AAEQANLEAIIQAH-DGhnLDNQL-ERAADalrlp 155
Cdd:COG2274 559 FLF-SGTIRENI-------------------TLGDPDATDEEIieAARLAGLHDFIEALpMG--YDTVVgEGGSN----- 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 156 dwdakiehLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG--TVVAITHDRYFLDNvAGWILEL 233
Cdd:COG2274 612 --------LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL-ADRIIVL 682
|
250 260 270
....*....|....*....|....*....|
gi 1735515619 234 DRGEgIPWEGNYSSWLEQKEK--RLEQEQA 261
Cdd:COG2274 683 DKGR-IVEDGTHEELLARKGLyaELVQQQL 711
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-236 |
5.84e-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: 116.86 E-value: 5.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR--PQPGIK----IGYLPQEPKLEPQQ--TVREAV 91
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfGKPLEKerkrIGYVPQRRSIDRDFpiSVRDVV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 92 eeavsevksALTRLDEVYALYADPDADFDKlaAEQAnleaiiqahdghnldnqLER-AADALRlpdwDAKIEHLSGGERR 170
Cdd:cd03235 92 ---------LMGLYGHKGLFRRLSKADKAK--VDEA-----------------LERvGLSELA----DRQIGELSGGQQQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 171 RVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERF---LHDYEGTVVAITHDRYFLDNVAGWILELDRG 236
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELlreLRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
325-536 |
7.24e-30 |
|
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: 117.05 E-value: 7.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSY-GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSIT-MGETVVLASVDQFRDAM--- 399
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvDGKDITKKNLRELRRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 400 ----DD---KKTVWEEVSNGqdiLTigNF-----EIPSR-----AYVGRFNFKgvdqQKRVGELSGGERGRLHLAKLLQR 462
Cdd:COG1122 81 fqnpDDqlfAPTVEEDVAFG---PE--NLglpreEIRERveealELVGLEHLA----DRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 463 GGNVLLLDEPTNDLDVETLRALENAILEFP--GCAMV-ISHDRWFLDRIATHILdYGDEGKVTFyEGN----FSDYEEWK 535
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNkeGKTVIiVTHDLDLVAELADRVI-VLDDGRIVA-DGTprevFSDYELLE 229
|
.
gi 1735515619 536 K 536
Cdd:COG1122 230 E 230
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
19-257 |
1.89e-29 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 116.50 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR----------PQPGIKIGYLPQEPKLEPQQTVR 88
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgedvrkepREARRQIGVLPDERGLYDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 89 EaveeavsevksaltrldevyalyadpdadfdklaaeqaNLEAIIQAHD--GHNLDNQLERAADALRLPDW-DAKIEHLS 165
Cdd:COG4555 93 E--------------------------------------NIRYFAELYGlfDEELKKRIEELIELLGLEEFlDRRVGELS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY---EGTVVAITHDRYFLDNVAGWILELDRGEgIPWE 242
Cdd:COG4555 135 TGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGK-VVAQ 213
|
250
....*....|....*.
gi 1735515619 243 GNYSSWLEQK-EKRLE 257
Cdd:COG4555 214 GSLDELREEIgEENLE 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
17-252 |
2.27e-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: 122.17 E-value: 2.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 17 PPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-----------ARPQPGIKIGYLPQEPKLePQQ 85
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSilingvdlsdlDPASWRRQIAWVPQNPYL-FAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 TVREAVeeavsevksaltRLdevyalyADPDADFDKL--AAEQANLEAIIQahdghnldnqleraadalRLPD-WDAKI- 161
Cdd:COG4988 426 TIRENL------------RL-------GRPDASDEELeaALEAAGLDEFVA------------------ALPDgLDTPLg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 162 EH---LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY-EG-TVVAITHDRYFLDNvAGWILELDRG 236
Cdd:COG4988 469 EGgrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLaKGrTVILITHRLALLAQ-ADRILVLDDG 547
|
250
....*....|....*.
gi 1735515619 237 EGIPwEGNYSSWLEQK 252
Cdd:COG4988 548 RIVE-QGTHEELLAKN 562
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
325-509 |
3.20e-29 |
|
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: 114.92 E-value: 3.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRD------- 397
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNigmvfqd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 398 -AMDDKKTVWEEVSNGQDILTIGNFEIPSRAY-----VGRFNFkgvdQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDE 471
Cdd:cd03259 81 yALFPHLTVAENIAFGLKLRGVPKAEIRARVRellelVGLEGL----LNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1735515619 472 PTNDLDVET---LRALENAILEFPGCAMV-ISHDR----WFLDRIA 509
Cdd:cd03259 157 PLSALDAKLreeLREELKELQRELGITTIyVTHDQeealALADRIA 202
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
325-520 |
6.06e-29 |
|
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: 112.48 E-value: 6.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRT--LIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMgetvvlasvdqfrdamddk 402
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 403 ktvweevsNGQDILTIGNFEIPSR-AYVG----------RFNFkgvdqqkrvgeLSGGERGRLHLAKLLQRGGNVLLLDE 471
Cdd:cd03228 62 --------DGVDLRDLDLESLRKNiAYVPqdpflfsgtiRENI-----------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1735515619 472 PTNDLDVETLRALENAILEFPGCAMV--ISHdRWFLDRIATHILdYGDEGK 520
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVivIAH-RLSTIRDADRII-VLDDGR 171
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
20-253 |
7.69e-29 |
|
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: 120.64 E-value: 7.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVD-KEFEGEARPQpgiKIGYLPQEPKLEpQQ 85
Cdd:COG4987 348 RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLrfldpqsgsitlgGVDlRDLDEDDLRR---RIAVVPQRPHLF-DT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 TVREAVeeavsevksaltrldevyaLYADPDADFDKL--AAEQANLEAIIQAhdghnldnqleraadalrLPD-WDAKI- 161
Cdd:COG4987 424 TLRENL-------------------RLARPDATDEELwaALERVGLGDWLAA------------------LPDgLDTWLg 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 162 ---EHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV-AWLERFLHDYEG-TVVAITHDRYFLDNVAGwILELDRG 236
Cdd:COG4987 467 eggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEqALLADLLEALAGrTVLLITHRLAGLERMDR-ILVLEDG 545
|
250
....*....|....*..
gi 1735515619 237 EGIPwEGNYSSWLEQKE 253
Cdd:COG4987 546 RIVE-QGTHEELLAQNG 561
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-238 |
1.58e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 119.53 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 17 PPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-ARPqPGIKIGYLPQEPKLePQQTVREAVeeav 95
Cdd:COG4178 373 PDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRiARP-AGARVLFLPQRPYL-PLGTLREAL---- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 96 sevksaltrldevyaLYADPDADFDKLAAEQAnLEAIiqahdghNLDNQLERAADALrlpDWDAKiehLSGGERRRVALC 175
Cdd:COG4178 447 ---------------LYPATAEAFSDAELREA-LEAV-------GLGHLAERLDEEA---DWDQV---LSLGEQQRLAFA 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 176 RLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD--YEGTVVAITHdRYFLDNVAGWILELDRGEG 238
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTGDGS 561
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-513 |
8.22e-28 |
|
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: 117.58 E-value: 8.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 32 PGAKIGVLGLNGAGKSTLLRIMAG-----------------VDKEFEG-------EARPQPGIKIGYLPQEPKLEPQQ-- 85
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGelkpnlgdydeepswdeVLKRFRGtelqdyfKKLANGEIKVAHKPQYVDLIPKVfk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 -TVREAveeavsevksaLTRLDEvyalyadpDADFDKLAaEQANLEAIiqahdghnldnqleraadalrlpdWDAKIEHL 164
Cdd:COG1245 178 gTVREL-----------LEKVDE--------RGKLDELA-EKLGLENI------------------------LDRDISEL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDYEGTVVAITHDRYFLDNVAGWIlELDRGEgipw 241
Cdd:COG1245 214 SGGELQRVAIAAALLRDADFYFFDEPSSYLDIYqrlNVARLIRELAEEGKYVLVVEHDLAILDYLADYV-HILYGE---- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 242 EGNYSSWLEQKEKR------LEQEQAAENARqksiakelewVRQNPkgrqakskarmARFDELNSGEYQKRnetnelfip 315
Cdd:COG1245 289 PGVYGVVSKPKSVRvginqyLDGYLPEENVR----------IRDEP-----------IEFEVHAPRREKEE--------- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 316 pgprlgDKVIEVQNLTKSYGDRTLIDDlSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETV-------- 387
Cdd:COG1245 339 ------ETLVEYPDLTKSYGGFSLEVE-GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKIsykpqyis 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 388 --VLASVDQF-----RDAMDDKKtVWEEVSNGQDIltignfeipSRAYvgrfnfkgvdqQKRVGELSGGERGRLHLAKLL 460
Cdd:COG1245 412 pdYDGTVEEFlrsanTDDFGSSY-YKTEIIKPLGL---------EKLL-----------DKNVKDLSGGELQRVAIAACL 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 461 QRGGNVLLLDEPTNDLDVE----TLRALENAILEFPGCAMVISHDRWFLDRIATHIL 513
Cdd:COG1245 471 SRDADLYLLDEPSAHLDVEqrlaVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
333-534 |
8.36e-28 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 117.74 E-value: 8.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 333 SYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQF--RDAmddKKTVWEEVS 410
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDppRNV---EGTVYDFVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 411 NG---------------------------------QDILTIGN---FEIPSRAYVGRFnfkGVDQQKRVGELSGGERGRL 454
Cdd:PRK11147 89 EGieeqaeylkryhdishlvetdpseknlnelaklQEQLDHHNlwqLENRINEVLAQL---GLDPDAALSSLSGGWLRKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 455 HLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFPGCAMVISHDRWFLDRIATHILDYgDEGKVTFYEGNFSDY--- 531
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDL-DRGKLVSYPGNYDQYlle 244
|
....
gi 1735515619 532 -EEW 534
Cdd:PRK11147 245 kEEA 248
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
23-478 |
8.53e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.66 E-value: 8.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DK---EFEGEARPQPGIK------IGYLPQEPKLEPQQTVREA 90
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVyqpDSgeiLLDGEPVRFRSPRdaqaagIAIIHQELNLVPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 91 VeeavsevksALTRLDEVYALYadpdaDFDKLAAE-QANLEAIiqahdGHNLDnqleraadalrlPDwdAKIEHLSGGER 169
Cdd:COG1129 100 I---------FLGREPRRGGLI-----DWRAMRRRaRELLARL-----GLDID------------PD--TPVGDLSVAQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 170 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHdryFLDNvagwILEL-DR------Gegi 239
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLkaQGvAIIYISH---RLDE----VFEIaDRvtvlrdG--- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 240 pwegnysswleqkekRLEQEQAAENARQKSIAKELewVrqnpkGRqakskarmarfdelnsgeyqkrnETNELFIPPGPR 319
Cdd:COG1129 217 ---------------RLVGTGPVAELTEDELVRLM--V-----GR-----------------------ELEDLFPKRAAA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 320 LGDKVIEVQNLTksygDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVdqfRDA 398
Cdd:COG1129 252 PGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLdGKPVRIRSP---RDA 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 399 MD--------DKKTvweevsNG----QDI---LTIGNFE-------IPSRA-------YVGRFNFKGVDQQKRVGELSGG 449
Cdd:COG1129 325 IRagiayvpeDRKG------EGlvldLSIrenITLASLDrlsrgglLDRRReralaeeYIKRLRIKTPSPEQPVGNLSGG 398
|
490 500
....*....|....*....|....*....
gi 1735515619 450 ERGRLHLAKLLQRGGNVLLLDEPTNDLDV 478
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGIDV 427
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
325-513 |
2.15e-27 |
|
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: 108.43 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMgetvvlasvdqfrdamddkkt 404
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 405 vweevsNGQDILTIGNFEIPSRAYVGRfnfkgVDQQ------KRVGE-----LSGGERGRLHLAKLLQRGGNVLLLDEPT 473
Cdd:cd03229 60 ------DGEDLTDLEDELPPLRRRIGM-----VFQDfalfphLTVLEnialgLSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1735515619 474 NDLDVET---LRALENAILEFPGCAMV-ISHDRWFLDRIATHIL 513
Cdd:cd03229 129 SALDPITrreVRALLKSLQAQLGITVVlVTHDLDEAARLADRVV 172
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-237 |
2.98e-27 |
|
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: 110.28 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGEARPQPGIK-----IGYLPQEPK--LEPQQ 85
Cdd:COG1124 17 RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERpwsgevTFDGRPVTRRRRKafrrrVQMVFQDPYasLHPRH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 TVREAVEEAvsevksaltrldevyalyadpdadfdkLAAeqanleaiiqahdgHNLDNQLERAADALRL----PDWDAKI 161
Cdd:COG1124 97 TVDRILAEP---------------------------LRI--------------HGLPDREERIAELLEQvglpPSFLDRY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 162 EH-LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRG 236
Cdd:COG1124 136 PHqLSGGQRQRVAIARALILEPELLLLDEPTSALDvsvqAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNG 215
|
.
gi 1735515619 237 E 237
Cdd:COG1124 216 R 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
325-512 |
3.33e-27 |
|
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: 108.84 E-value: 3.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM--GETVVLASVDQFRDAMDDK 402
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdgKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 403 KTVWEEVSnGQDiltigNFEIPSRAYvgRFNFKGVDQ-----------QKRVGELSGGERGRLHLAKLLQRGGNVLLLDE 471
Cdd:cd03268 81 PGFYPNLT-ARE-----NLRLLARLL--GIRKKRIDEvldvvglkdsaKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1735515619 472 PTNDLDVETLRALENAILEFP--GCAMVI-SHDRWFLDRIATHI 512
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRdqGITVLIsSHLLSEIQKVADRI 196
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
19-237 |
4.10e-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: 109.12 E-value: 4.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQpGI----------------KIGYLPQEPKLE 82
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVD-GTdisklsekelaafrrrHIGFVFQSFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 83 PQQTVREAVEeavsevksaltrldevyalyadpdadfdklaaeqanLEAIIQahdGHNLDNQLERAADALRLPDWDAKIE 162
Cdd:cd03255 95 PDLTALENVE------------------------------------LPLLLA---GVPKKERRERAEELLERVGLGDRLN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 163 H----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITHDRyFLDNVAGWILELD 234
Cdd:cd03255 136 HypseLSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELR 214
|
...
gi 1735515619 235 RGE 237
Cdd:cd03255 215 DGK 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
18-237 |
1.11e-26 |
|
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: 105.79 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 18 PKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARpqpgikigylpqepklepqqtvreaveeavse 97
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL-------------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 98 vksaltrldevyalyadpdadfdklaaeqanleaiIQAHDGHNLDNQLERAADALrlpdwdakIEHLSGGERRRVALCRL 177
Cdd:cd00267 58 -----------------------------------IDGKDIAKLPLEELRRRIGY--------VPQLSGGQRQRVALARA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 178 LLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHDRYFLDNVAGWILELDRGE 237
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRELaeEGrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
316-514 |
1.22e-26 |
|
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: 114.08 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 316 PGPRLGDKVIEVQNLTKSYGD-RTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVD 393
Cdd:COG4988 328 PLPAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILInGVDLSDLDPA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 394 QFRdamddKKTVWeeVS------NG--QDILTIGNFEIPS--------RAYVGRFnfkgVDQQK-----RVGE----LSG 448
Cdd:COG4988 408 SWR-----RQIAW--VPqnpylfAGtiRENLRLGRPDASDeeleaaleAAGLDEF----VAALPdgldtPLGEggrgLSG 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1735515619 449 GERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFPG--CAMVISHdRWFLDRIATHILD 514
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITH-RLALLAQADRILV 543
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
321-530 |
1.43e-26 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 108.14 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 321 GDKVIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSIT-MGETVVLASVDQFR--- 396
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvDGQDITGLSEKELYelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 397 -------------DAMddkkTVWEevsngqdiltigNFEIPSRAYvGRFNFKGVDQQ-----KRVG----------ELSG 448
Cdd:COG1127 82 rrigmlfqggalfDSL----TVFE------------NVAFPLREH-TDLSEAEIRELvleklELVGlpgaadkmpsELSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 449 GERGRLHLA-------KLlqrggnvLLLDEPTNDLDVETLRALENAILE----FPGCAMVISHDRWFLDRIATHI--Ldy 515
Cdd:COG1127 145 GMRKRVALAralaldpEI-------LLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHDLDSAFAIADRVavL-- 215
|
250
....*....|....*
gi 1735515619 516 gDEGKVTFyEGNFSD 530
Cdd:COG1127 216 -ADGKIIA-EGTPEE 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
18-219 |
1.72e-26 |
|
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: 105.98 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 18 PKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE----------------ARpqpgiKIGYLPQepkl 81
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEilldgkdlaslspkelAR-----KIAYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 82 epqqtvreaveeavsevksALTRLdevyalyadpdadfdklaaeqanleaiiqahdghNLDNQLERaadalrlpdwdaKI 161
Cdd:cd03214 81 -------------------ALELL----------------------------------GLAHLADR------------PF 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1735515619 162 EHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHD 219
Cdd:cd03214 96 NELSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqIELLELLRRLARERGKTVVMVLHD 157
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-219 |
2.35e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 108.25 E-value: 2.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 1 MSSQFVY-TMHRVGKVVPPK---RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR------PQPGI 70
Cdd:COG1116 1 MSAAAPAlELRGVSKRFPTGgggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLvdgkpvTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 71 KIGYLPQEPKLEPQQTVREAVEeavsevksaltrldevyalyadpdadfdkLAAEQAnleaiiqahdGHNLDNQLERAAD 150
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVA-----------------------------LGLELR----------GVPKAERRERARE 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 151 ALR---LPDW-DAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA----WLERFLHDYEGTVVAITHD 219
Cdd:COG1116 122 LLElvgLAGFeDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRErlqdELLRLWQETGKTVLFVTHD 198
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
19-227 |
2.84e-26 |
|
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: 106.82 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGEARPQP--------GIKIGYLPQEP--KLE 82
Cdd:cd03257 17 SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKptsgsiIFDGKDLLKLsrrlrkirRKEIQMVFQDPmsSLN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 83 PQQTVREAVEEAVSEVKsaltrldevyalyadpdadfdKLAAEQANLEAIIQAHDGHNLDNQLERaadalRLPDWdakie 162
Cdd:cd03257 97 PRMTIGEQIAEPLRIHG---------------------KLSKKEARKEAVLLLLVGVGLPEEVLN-----RYPHE----- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 163 hLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD----YEGTVVAITHD----RYFLDNVA 227
Cdd:cd03257 146 -LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqeeLGLTLLFITHDlgvvAKIADRVA 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
324-509 |
3.45e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.55 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVV-------LASvdqfR 396
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLadwspaeLAR----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 397 DAMDDKK-------TVWEEVSNGQDILTIGNFE---IPSRAY--VGRFNFKGVDQQkrvgELSGGERGRLHLAKLL-QR- 462
Cdd:PRK13548 78 RAVLPQHsslsfpfTVEEVVAMGRAPHGLSRAEddaLVAAALaqVDLAHLAGRDYP----QLSGGEQQRVQLARVLaQLw 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 463 ----GGNVLLLDEPTNDLDV----ETLRALENAILEFPGCAMVISHD-----RWfLDRIA 509
Cdd:PRK13548 154 epdgPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHDlnlaaRY-ADRIV 212
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
325-500 |
7.50e-26 |
|
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: 103.66 E-value: 7.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVdqfRDAMDdkk 403
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVdGKEVSFASP---RDARR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 404 tvweevsNGqdILTIgnfeipsrayvgrfnfkgvdQQkrvgeLSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRA 483
Cdd:cd03216 75 -------AG--IAMV--------------------YQ-----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180
....*....|....*....|
gi 1735515619 484 LENAILEF--PGCAMV-ISH 500
Cdd:cd03216 121 LFKVIRRLraQGVAVIfISH 140
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
321-500 |
9.61e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.50 E-value: 9.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 321 GDKVIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASvdqFRDAM 399
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdGKPVRIRS---PRDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 400 D-------------DKKTVWEEVSNGQDILTIGNF-------EIpsRAYVGRFNFKgVDQQKRVGELSGGERGRLHLAKL 459
Cdd:COG3845 79 AlgigmvhqhfmlvPNLTVAENIVLGLEPTKGGRLdrkaaraRI--RELSERYGLD-VDPDAKVEDLSVGEQQRVEILKA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1735515619 460 LQRGGNVLLLDEPT--------NDLdVETLRALENAilefpGCAMV-ISH 500
Cdd:COG3845 156 LYRGARILILDEPTavltpqeaDEL-FEILRRLAAE-----GKSIIfITH 199
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
325-516 |
1.05e-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: 105.60 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQ--------- 394
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFdGEDITGLPPHEiarlgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 395 ------FRDAmddkkTVWEEV------SNGQDILTIGNF----EIPSRA--YVGRFNFKGVDQQkRVGELSGGERGRLHL 456
Cdd:cd03219 81 fqiprlFPEL-----TVLENVmvaaqaRTGSGLLLARARreerEARERAeeLLERVGLADLADR-PAGELSYGQQRRLEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 457 AKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFP--GCA-MVISHDRWFLDRIATHI--LDYG 516
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRerGITvLLVEHDMDVVMSLADRVtvLDQG 219
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-236 |
1.98e-25 |
|
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: 110.22 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 15 VVPP--KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR-----------PQPGIKIGYLPQEPKL 81
Cdd:COG4618 338 VVPPgsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRldgadlsqwdrEELGRHIGYLPQDVEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 82 EPqQTVREAVeeavsevksaltrldevyALYADPDAdfdklaaeqanlEAIIQAhdghnldnqlERAADA----LRLPD- 156
Cdd:COG4618 418 FD-GTIAENI------------------ARFGDADP------------EKVVAA----------AKLAGVhemiLRLPDg 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 157 WDAKIE----HLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD--YEG-TVVAITHDRYFLdNVAGW 229
Cdd:COG4618 457 YDTRIGeggaRLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAlkARGaTVVVITHRPSLL-AAVDK 535
|
....*..
gi 1735515619 230 ILELDRG 236
Cdd:COG4618 536 LLVLRDG 542
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
325-513 |
2.01e-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: 104.11 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGD----RTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRDAMD 400
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 401 DKK--------------TVWEEVSNGQDILTIGNFEIPSRA-----YVG---RFNfkgvdqqKRVGELSGGERGRLHLAK 458
Cdd:cd03255 81 RRHigfvfqsfnllpdlTALENVELPLLLAGVPKKERRERAeelleRVGlgdRLN-------HYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 459 LLQRGGNVLLLDEPTNDLDVETLRALENAILEF---PGCAMVI-SHDRwFLDRIATHIL 513
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELnkeAGTTIVVvTHDP-ELAEYADRII 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
326-522 |
2.34e-25 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 103.49 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 326 EVQNLTKSYGDRTLI-DDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGEtVVLASVDQFRDA---MDD 401
Cdd:cd03226 1 RIENISFSYKKGTEIlDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-KPIKAKERRKSIgyvMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 402 ------KKTVWEEVSNGQDILTIGNFEIpsRAYVGRFN-FKGVDQQKRvgELSGGERGRLHLAKLLQRGGNVLLLDEPTN 474
Cdd:cd03226 80 vdyqlfTDSVREELLLGLKELDAGNEQA--ETVLKDLDlYALKERHPL--SLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1735515619 475 DLDVETLRALENAILEFP--GCAM-VISHDRWFLDRIATHILdYGDEGKVT 522
Cdd:cd03226 156 GLDYKNMERVGELIRELAaqGKAViVITHDYEFLAKVCDRVL-LLANGAIV 205
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-282 |
2.40e-25 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 110.43 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 2 SSQFVYTMHRVGKVVPPKRhILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQPGIKIGYLPQ-EPK 80
Cdd:PRK11147 315 SGKIVFEMENVNYQIDGKQ-LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQhRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 81 LEPQQTVREAVEEAVSEVksaltrldevyalyadpdadfdklaaeqanleaIIQAHDGHNLdNQLE-------RAadalR 153
Cdd:PRK11147 394 LDPEKTVMDNLAEGKQEV---------------------------------MVNGRPRHVL-GYLQdflfhpkRA----M 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 154 LPdwdakIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVA--GWIL 231
Cdd:PRK11147 436 TP-----VKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVteCWIF 510
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1735515619 232 EldrGEGIpWE---GNYSSWLEQKEKRLEQEQAAENARQKSIAKELEWVRQNPK 282
Cdd:PRK11147 511 E---GNGK-IGryvGGYHDARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSK 560
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
22-252 |
2.46e-25 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 109.60 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQPGIKIGYLPQepklepqqtvreaveeavsevksa 101
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQ------------------------ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 102 ltrldevyalyaDPDADFDklaaEQANL-EAIIQ-AHDGHnlDNQLERAAdaL-RL----PDWDAKIEHLSGGERRRVAL 174
Cdd:PRK15064 390 ------------DHAYDFE----NDLTLfDWMSQwRQEGD--DEQAVRGT--LgRLlfsqDDIKKSVKVLSGGEKGRMLF 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1735515619 175 CRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSSWLEQK 252
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQ 527
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
325-501 |
2.57e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 104.78 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMgetvvlasvdqfrDAMDDKKT 404
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLV-------------DGLDVATT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 405 VWEEVSNGQDILTIGNFeIPSRAYV------GRFNF-KG---------VDQ-----------QKRVGELSGGERGRLHLA 457
Cdd:COG4604 69 PSRELAKRLAILRQENH-INSRLTVrelvafGRFPYsKGrltaedreiIDEaiayldledlaDRYLDELSGGQRQRAFIA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1735515619 458 KLLQRGGNVLLLDEPTNDLD----VETLRALENAILEFpGCAMVIS-HD 501
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADEL-GKTVVIVlHD 195
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
324-480 |
3.70e-25 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 103.81 E-value: 3.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDR----TLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSIT-MGETVVLASVDQFRDA 398
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 399 ------------MDDKKTVWEEVSNGQDILTIGNFEIPSRAY-----VGRFNFKgvdqQKRVGELSGGERGRLHLAKLLQ 461
Cdd:cd03258 81 rrrigmifqhfnLLSSRTVFENVALPLEIAGVPKAEIEERVLellelVGLEDKA----DAYPAQLSGGQKQRVGIARALA 156
|
170
....*....|....*....
gi 1735515619 462 RGGNVLLLDEPTNDLDVET 480
Cdd:cd03258 157 NNPKVLLCDEATSALDPET 175
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-219 |
5.23e-25 |
|
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: 102.94 E-value: 5.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 8 TMHRVGKVVPPKR---HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGEARPQPGIKIGYLPQE 78
Cdd:cd03293 2 EVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERptsgevLVDGEPVTGPGPDRGYVFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 79 PKLEPQQTVREAVEeavsevksaltrldevYALyadpdaDFDKLAAEQAnleaiiqahdghnldnqLERAADALR---LP 155
Cdd:cd03293 82 DALLPWLTVLDNVA----------------LGL------ELQGVPKAEA-----------------RERAEELLElvgLS 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 156 DW-DAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESV-AWLERFLHDYEGTVVAITHD 219
Cdd:cd03293 123 GFeNAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltrEQLqEELLDIWRETGKTVLLVTHD 191
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
321-516 |
5.38e-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: 103.97 E-value: 5.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 321 GDKVIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQ----- 394
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFdGRDITGLPPHRiarlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 395 ----------FRDaMddkkTVWEEVSNGQDILTIGNF---------------EIPSRAY--VGRFNFKGVdQQKRVGELS 447
Cdd:COG0411 81 iartfqnprlFPE-L----TVLENVLVAAHARLGRGLlaallrlprarreerEARERAEelLERVGLADR-ADEPAGNLS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 448 GGERGRLHLAKLLQRGGNVLLLDEPT---NDLDVETLRALENAILEFPGCAMV-ISHDRWFLDRIATHI--LDYG 516
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGITILlIEHDMDLVMGLADRIvvLDFG 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-236 |
7.19e-25 |
|
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: 102.67 E-value: 7.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkefegeARPQPG--------IK----------IGYLPQEPK 80
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL-------YKPTSGsvlldgtdIRqldpadlrrnIGYVPQDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 81 LEpQQTVREAVEeavsevksaltrldevyalYADPDADFDKL--AAEQANLEAIIQAHdGHNLDNQL-ERAADalrlpdw 157
Cdd:cd03245 89 LF-YGTLRDNIT-------------------LGAPLADDERIlrAAELAGVTDFVNKH-PNGLDLQIgERGRG------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 158 dakiehLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVawlERFLHDYEG-----TVVAITHdRYFLDNVAGWILE 232
Cdd:cd03245 141 ------LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE---ERLKERLRQllgdkTLIIITH-RPSLLDLVDRIIV 210
|
....
gi 1735515619 233 LDRG 236
Cdd:cd03245 211 MDSG 214
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
20-219 |
8.13e-25 |
|
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: 103.74 E-value: 8.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-----------ARPQPGIKIGYLPQEPKLEPQQTVR 88
Cdd:TIGR03873 14 RLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTvdlagvdlhglSRRARARRVALVEQDSDTAVPLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 89 EAVeeavsevksALTRLDEVYALYADPDADFDKLAAEQANLEAiiqahdghnldnqlerAADALRlpDWDAkiehLSGGE 168
Cdd:TIGR03873 94 DVV---------ALGRIPHRSLWAGDSPHDAAVVDRALARTEL----------------SHLADR--DMST----LSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1735515619 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG---TVVAITHD 219
Cdd:TIGR03873 143 RQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHD 196
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
324-477 |
1.60e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 104.12 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLAS---------VD 393
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVPSRArharqrvgvVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 394 QFrDAMDDKKTVWEevsngqDILTIGN-FEIPS---RAYV-GRFNFKGVDQQ--KRVGELSGGERGRLHLAKLLQRGGNV 466
Cdd:PRK13537 87 QF-DNLDPDFTVRE------NLLVFGRyFGLSAaaaRALVpPLLEFAKLENKadAKVGELSGGMKRRLTLARALVNDPDV 159
|
170
....*....|.
gi 1735515619 467 LLLDEPTNDLD 477
Cdd:PRK13537 160 LVLDEPTTGLD 170
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
307-501 |
2.17e-24 |
|
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: 107.61 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 307 NETNELFIPPGPRLGDkvIEVQNLTKSYGDRT--LIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMG 384
Cdd:COG2274 458 REEGRSKLSLPRLKGD--IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 385 ET---------------VVLASVDQFRDamddkkTVWEevsNgqdiLTIGNFEIPSRAYVGRFNFKGVDQ---------Q 440
Cdd:COG2274 536 GIdlrqidpaslrrqigVVLQDVFLFSG------TIRE---N----ITLGDPDATDEEIIEAARLAGLHDfiealpmgyD 602
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 441 KRVGE----LSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILE-FPGCAM-VISHD 501
Cdd:COG2274 603 TVVGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRlLKGRTViIIAHR 669
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
325-484 |
2.97e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 103.76 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSIT-MGETVV---------LASVDQ 394
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvLGVPVPararlararIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 395 FrDAMDDKKTVWEEV--------SNGQDILTIgnfeIPSRAYVGRFNFKGvdqQKRVGELSGGERGRLHLAKLLQRGGNV 466
Cdd:PRK13536 122 F-DNLDLEFTVRENLlvfgryfgMSTREIEAV----IPSLLEFARLESKA---DARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180
....*....|....*....|....*
gi 1735515619 467 LLLDEPTNDLDV-------ETLRAL 484
Cdd:PRK13536 194 LILDEPTTGLDPharhliwERLRSL 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
18-220 |
3.18e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 104.07 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 18 PKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGE---------ARpqpgiKIGYLPQEPKLE 82
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETpdsgriVLNGRdlftnlpprER-----RVGFVFQHYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 83 PQQTVREAVEEAVsEVKSAltrldevyalyadPDADFDKLAAEQanLEAIiqahdghnldnQLERAADalRLPDwdakie 162
Cdd:COG1118 88 PHMTVAENIAFGL-RVRPP-------------SKAEIRARVEEL--LELV-----------QLEGLAD--RYPS------ 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 163 HLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAeSVA-----WLERFLHDYEGTVVAITHDR 220
Cdd:COG1118 133 QLSGGQRQRVALARALAVEPEVLLLDEPFGALDA-KVRkelrrWLRRLHDELGGTTVFVTHDQ 194
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
325-508 |
3.43e-24 |
|
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: 101.49 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGD-RTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLA-SVDQFRDAMDDK 402
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 403 KTVW------EEVSNGQDILtignfeipsrayVGRFN-----------FKGVDQQ----------------KRVGELSGG 449
Cdd:cd03256 81 GMIFqqfnliERLSVLENVL------------SGRLGrrstwrslfglFPKEEKQralaalervglldkayQRADQLSGG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 450 ERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFP---GCAMVIS-HD----RWFLDRI 508
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreeGITVIVSlHQvdlaREYADRI 215
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
335-532 |
3.71e-24 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 106.79 E-value: 3.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 335 GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRDAMD----------DKK- 403
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPqpaleyvidgDREy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 404 -------TVWEEVSNGQDILT-------IGNFEIPSRA--YVGRFNFKGVDQQKRVGELSGGERGRLHLAKLLQRGGNVL 467
Cdd:PRK10636 92 rqleaqlHDANERNDGHAIATihgkldaIDAWTIRSRAasLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 468 LLDEPTNDLDVETLRALENAILEFPGCAMVISHDRWFLDRIATHILdYGDEGKVTFYEGNFSDYE 532
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKII-HIEQQSLFEYTGNYSSFE 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-509 |
3.88e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.88 E-value: 3.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE----------ARPQPGIK--IGYLPQEPKLEPQQTVREA 90
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEilidgkpvriRSPRDAIAlgIGMVHQHFMLVPNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 91 VeeavsevksaltrldevyALYADPDA----DFDKLAAEqanleaiiqahdghnldnqLERAADALRLP-DWDAKIEHLS 165
Cdd:COG3845 101 I------------------VLGLEPTKggrlDRKAARAR-------------------IRELSERYGLDvDPDAKVEDLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHDryfLDNVagwiLEL-DR------ 235
Cdd:COG3845 144 VGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLaaEGkSIIFITHK---LREV----MAIaDRvtvlrr 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 236 GEGIpwegnysswleqkekrleqeqAAENARQKSIAkELewvrqnpkgrqakskARM--ARfdelnsgeyqkrnETNELF 313
Cdd:COG3845 217 GKVV---------------------GTVDTAETSEE-EL---------------AELmvGR-------------EVLLRV 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 314 IPPGPRLGDKVIEVQNLT-KSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLAS 391
Cdd:COG3845 247 EKAPAEPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLdGEDITGLS 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 392 VDQFRDA-----------------MddkkTVWEevsNgqdiLTIGNFEIP----------------SRAYVGRFNFKGVD 438
Cdd:COG3845 327 PRERRRLgvayipedrlgrglvpdM----SVAE---N----LILGRYRRPpfsrggfldrkairafAEELIEEFDVRTPG 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 439 QQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDV-------ETLRALENAilefpGCA-MVISHDrwfL----- 505
Cdd:COG3845 396 PDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVgaiefihQRLLELRDA-----GAAvLLISED---Ldeila 467
|
....*.
gi 1735515619 506 --DRIA 509
Cdd:COG3845 468 lsDRIA 473
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
325-490 |
4.48e-24 |
|
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: 100.62 E-value: 4.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDR----TLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQ---F- 395
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdGEPVTGPGPDRgyvFq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 396 RDAMDDKKTVWEEVSNGQDILTIGNFEIPSRA--YVGRFNFKGVdQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPT 473
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKAEARERAeeLLELVGLSGF-ENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170
....*....|....*..
gi 1735515619 474 NDLDVETLRALENAILE 490
Cdd:cd03293 160 SALDALTREQLQEELLD 176
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-219 |
1.32e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.07 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 18 PKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQPGIKIGYLPQEPKLEPQ--QTVREAVEEAV 95
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSlpLTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 96 SEVKSALTRLDevyalyadpdADfDKLAAEQAnLEAIiqahdghNLDNQLERAADALrlpdwdakiehlSGGERRRVALC 175
Cdd:NF040873 83 WARRGLWRRLT----------RD-DRAAVDDA-LERV-------GLADLAGRQLGEL------------SGGQRQRALLA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1735515619 176 RLLLEKPDMLLLDEPTNHLDAESVAWLE---RFLHDYEGTVVAITHD 219
Cdd:NF040873 132 QGLAQEADLLLLDEPTTGLDAESRERIIallAEEHARGATVVVVTHD 178
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
17-239 |
1.35e-23 |
|
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: 98.48 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 17 PPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpqpgIKIGylpqepklepqqtvreaveeavS 96
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGS------ILLN----------------------G 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 97 EVKSALTRLDEVYALYADPDadfDKLAAEQANLEAIIQAHDghnLDNQLERAADALRLPD-WDAKIEH---LSGGERRRV 172
Cdd:cd03226 62 KPIKAKERRKSIGYVMQDVD---YQLFTDSVREELLLGLKE---LDAGNEQAETVLKDLDlYALKERHplsLSGGQKQRL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 173 ALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGI 239
Cdd:cd03226 136 AIAAALLSGKDLLIFDEPTSGLDYknmERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
325-523 |
1.37e-23 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 99.50 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSIT-MGETVVLASVDQFRD------ 397
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLiDGEDISGLSEAELYRlrrrmg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 398 ------AMDDKKTVWEEVS-----NGQDILTignfEIPSRA--YVGRFNFKGvDQQKRVGELSGGERGRLHLAKLLQRGG 464
Cdd:cd03261 81 mlfqsgALFDSLTVFENVAfplreHTRLSEE----EIREIVleKLEAVGLRG-AEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 465 NVLLLDEPTNDLDVETLRALENAIL----EFPGCAMVISHDRWFLDRIATHILdYGDEGKVTF 523
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRslkkELGLTSIMVTHDLDTAFAIADRIA-VLYDGKIVA 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
325-491 |
1.67e-23 |
|
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: 99.18 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSG-----QEQPDAGSITMGETVVLASVDQ----- 394
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVDvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 395 ------FRDAMDDKKTVWEEVSNGQDILTIGNFEIP--------SRAYVgrfnFKGVDQQKRVGELSGGERGRLHLAKLL 460
Cdd:cd03260 81 rrvgmvFQKPNPFPGSIYDNVAYGLRLHGIKLKEELderveealRKAAL----WDEVKDRLHALGLSGGQQQRLCLARAL 156
|
170 180 190
....*....|....*....|....*....|.
gi 1735515619 461 QRGGNVLLLDEPTNDLDVETLRALENAILEF 491
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAEL 187
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
10-197 |
1.70e-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: 98.42 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 10 HRVGKVVPpKRHILKDISLSFFPGAkIGVLGLNGAGKSTLLRIMAGVDK------EFEGEARPQPGIK----IGYLPQEP 79
Cdd:cd03264 4 ENLTKRYG-KKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPpssgtiRIDGQDVLKQPQKlrrrIGYLPQEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 80 KLEPQQTVREAveeavsevksaltrLDEVYALYADPDADFDKlAAEQAnLEAIiqahdghnldNQLERAadalrlpdwDA 159
Cdd:cd03264 82 GVYPNFTVREF--------------LDYIAWLKGIPSKEVKA-RVDEV-LELV----------NLGDRA---------KK 126
|
170 180 190
....*....|....*....|....*....|....*...
gi 1735515619 160 KIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE 197
Cdd:cd03264 127 KIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
325-514 |
2.51e-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: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGaIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRDAM----- 399
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIgylpq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 400 ----DDKKTVWEEVSNGQDILTIGNFEIPSRA-----YVGRFNFKGvdqqKRVGELSGGERGRLHLAKLLQRGGNVLLLD 470
Cdd:cd03264 80 efgvYPNFTVREFLDYIAWLKGIPSKEVKARVdevleLVNLGDRAK----KKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1735515619 471 EPTNDLDVETLRALENAILEfpgcamvISHDRWFLdrIATHILD 514
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSE-------LGEDRIVI--LSTHIVE 190
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
9-237 |
3.03e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 98.20 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 9 MHRVGKVVPPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR---------PQPGI-----KIGY 74
Cdd:COG2884 4 FENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlsrlKRREIpylrrRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 75 LPQEPKLEPQQTVREAVeeavsevksALTrldevyalyadpdadfdklaaeqanLEAIiqahdGHNLDNQLERAADALrl 154
Cdd:COG2884 84 VFQDFRLLPDRTVYENV---------ALP-------------------------LRVT-----GKSRKEIRRRVREVL-- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 155 pDW-------DAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvAW-----LERFlHDYEGTVVAITHDRYF 222
Cdd:COG2884 123 -DLvglsdkaKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPET-SWeimelLEEI-NRRGTTVLIATHDLEL 199
|
250
....*....|....*
gi 1735515619 223 LDNVAGWILELDRGE 237
Cdd:COG2884 200 VDRMPKRVLELEDGR 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
20-237 |
3.11e-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: 96.68 E-value: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR----PQPGI-------KIGYLPQEPKLePQQTVR 88
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvDLRDLdleslrkNIAYVPQDPFL-FSGTIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 89 EaveeavsevksaltrldevyalyadpdadfdklaaeqanleaiiqahdghNLdnqleraadalrlpdwdakiehLSGGE 168
Cdd:cd03228 94 E--------------------------------------------------NI----------------------LSGGQ 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1735515619 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG--TVVAITHdRYFLDNVAGWILELDRGE 237
Cdd:cd03228 102 RQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAH-RLSTIRDADRIIVLDDGR 171
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-287 |
3.26e-23 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 103.71 E-value: 3.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQPGIKIGYLPQEpKLEpqqtvreaveeavsevk 99
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQH-QLE----------------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 100 saLTRLDEvyalyaDPDADFDKLAAEQanLEAIIQAHDGhNLDNQLERAADAlrlpdwdakIEHLSGGERRRVALCRLLL 179
Cdd:PRK10636 387 --FLRADE------SPLQHLARLAPQE--LEQKLRDYLG-GFGFQGDKVTEE---------TRRFSGGEKARLVLALIVW 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 180 EKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEG---NYSSWLEQKEKRL 256
Cdd:PRK10636 447 QRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGdleDYQQWLSDVQKQE 526
|
250 260 270
....*....|....*....|....*....|.
gi 1735515619 257 EQEQAAENARQKSIAKElewvRQNPKGRQAK 287
Cdd:PRK10636 527 NQTDEAPKENNANSAQA----RKDQKRREAE 553
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
333-501 |
3.57e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.92 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 333 SYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQfRDAMDDK--KTVWEEVS 410
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ-RSEVPDSlpLTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 411 NG--QDILTIGNFEIPSRAYVG----RFNFKGVDQQkRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRAL 484
Cdd:NF040873 80 MGrwARRGLWRRLTRDDRAAVDdaleRVGLADLAGR-QLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180
....*....|....*....|
gi 1735515619 485 ENAILEFPG---CAMVISHD 501
Cdd:NF040873 159 IALLAEEHArgaTVVVVTHD 178
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
325-484 |
4.04e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 98.65 E-value: 4.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETvvlasvdqfrdAMDDKK- 403
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR-----------PLAAWSp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 404 --------------------TVWEEVSNG---QDILTIGNFEIPSRA--------YVGRFnfkgvdqqkrVGELSGGERG 452
Cdd:COG4559 71 welarrravlpqhsslafpfTVEEVVALGrapHGSSAAQDRQIVREAlalvglahLAGRS----------YQTLSGGEQQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1735515619 453 RLHLAK-LLQ------RGGNVLLLDEPTNDLDV----ETLRAL 484
Cdd:COG4559 141 RVQLARvLAQlwepvdGGPRWLFLDEPTSALDLahqhAVLRLA 183
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
325-514 |
6.02e-23 |
|
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: 97.05 E-value: 6.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTL----IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQFR--- 396
Cdd:cd03266 2 ITADALTKRFRDVKKtvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdGFDVVKEPAEARRrlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 397 -----DAMDDKKTVWEEVSNGQDILTIGNFEIPSRA--YVGRFNFKGVdQQKRVGELSGGERGRLHLAKLLQRGGNVLLL 469
Cdd:cd03266 82 fvsdsTGLYDRLTARENLEYFAGLYGLKGDELTARLeeLADRLGMEEL-LDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1735515619 470 DEPTNDLDVETLRALENAILEF--PGCAMVIShdrwfldriaTHILD 514
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLraLGKCILFS----------THIMQ 197
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
325-480 |
7.49e-23 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 97.06 E-value: 7.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITmgetvvLASVDQFRDAMDDKKT 404
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT------VAGHDVVREPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 405 ---VWEEVSNGQDILTIGNFEIPSRAYvgrfNFKGVDQQKRVGEL-----------------SGGERGRLHLAKLLQRGG 464
Cdd:cd03265 75 igiVFQDLSVDDELTGWENLYIHARLY----GVPGAERRERIDELldfvglleaadrlvktySGGMRRRLEIARSLVHRP 150
|
170
....*....|....*.
gi 1735515619 465 NVLLLDEPTNDLDVET 480
Cdd:cd03265 151 EVLFLDEPTIGLDPQT 166
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
325-485 |
1.01e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 100.30 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASvdqfrdamdDKKT 404
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAL---------SARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 405 VWEEV-SNGQDilTIGNFEIPSRAYV--------GRF---------------NFKGVDQ--QKRVGELSGGERGRLHLAK 458
Cdd:PRK09536 75 ASRRVaSVPQD--TSLSFEFDVRQVVemgrtphrSRFdtwtetdraaveramERTGVAQfaDRPVTSLSGGERQRVLLAR 152
|
170 180
....*....|....*....|....*...
gi 1735515619 459 LLQRGGNVLLLDEPTNDLDV-ETLRALE 485
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDInHQVRTLE 180
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
17-237 |
1.50e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 101.39 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 17 PPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVD-KEFEGEA-RPQpgikIGYLPQEPKL 81
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLrfydptsgrilidGVDiRDLTLESlRRQ----IGVVPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 82 EpQQTVREAVeeavsevksaltrldevyaLYADPDADFDKL--AAEQANLEAIIQahdghnldnqleraadalRLPD-WD 158
Cdd:COG1132 426 F-SGTIRENI-------------------RYGRPDATDEEVeeAAKAAQAHEFIE------------------ALPDgYD 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 159 AKIE----HLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAW----LERFLHDYegTVVAITH--------DRyf 222
Cdd:COG1132 468 TVVGergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALiqeaLERLMKGR--TTIVIAHrlstirnaDR-- 543
|
250
....*....|....*
gi 1735515619 223 ldnvagwILELDRGE 237
Cdd:COG1132 544 -------ILVLDDGR 551
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
325-478 |
3.50e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.85 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETvvlaSVDQFRDAMDDKK- 403
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDK----PISMLSSRQLARRl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 404 -------------TVWEEVSNGQDiltignfeiPSRAYVGRFNFKG---VDQ-----------QKRVGELSGGERGRLHL 456
Cdd:PRK11231 79 allpqhhltpegiTVRELVAYGRS---------PWLSLWGRLSAEDnarVNQameqtrinhlaDRRLTDLSGGQRQRAFL 149
|
170 180
....*....|....*....|..
gi 1735515619 457 AKLLQRGGNVLLLDEPTNDLDV 478
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDI 171
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
17-235 |
4.18e-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: 4.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 17 PPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE----ARPQPGIK-------IGYLPQEPKLePQQ 85
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSiavnGVPLADADadswrdqIAWVPQHPFL-FAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 TVREAVeeavsevksaltrldevyaLYADPDADFDKL--AAEQANLEAIIQAhdghnldnqleraadalrLPD-WDAKI- 161
Cdd:TIGR02857 411 TIAENI-------------------RLARPDASDAEIreALERAGLDEFVAA------------------LPQgLDTPIg 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 162 EH---LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG--TVVAITHDRyfldnvaGWILELDR 235
Cdd:TIGR02857 454 EGgagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRL-------ALAALADR 525
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
324-502 |
6.03e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 97.60 E-value: 6.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMgETVVLASVDQFRD------ 397
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLSHVPPYQRpinmmf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 398 ---AMDDKKTVWEEVSNG--QDILTIGnfEIPSR-----AYVGRFNFKGvdqqKRVGELSGGERGRLHLAKLLQRGGNVL 467
Cdd:PRK11607 98 qsyALFPHMTVEQNIAFGlkQDKLPKA--EIASRvnemlGLVHMQEFAK----RKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1735515619 468 LLDEPTNDLDvETLR---ALENA-ILEFPG--CAMViSHDR 502
Cdd:PRK11607 172 LLDEPMGALD-KKLRdrmQLEVVdILERVGvtCVMV-THDQ 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
324-516 |
6.04e-22 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 94.49 E-value: 6.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSY----GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRdam 399
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 400 ddkKTVWEEVSN-GQD-------ILTIGnfEIPSRAYvgRFNFKGVDQQKR----------VG-----------ELSGGE 450
Cdd:cd03257 78 ---KIRRKEIQMvFQDpmsslnpRMTIG--EQIAEPL--RIHGKLSKKEARkeavllllvgVGlpeevlnryphELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 451 RGRLHLAKLLQRGGNVLLLDEPTNDLDV----ETLRALENAILEFpGCAMV-ISHD----RWFLDRIAthILDYG 516
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVsvqaQILDLLKKLQEEL-GLTLLfITHDlgvvAKIADRVA--VMYAG 222
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
324-545 |
6.75e-22 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 99.20 E-value: 6.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAG--SITMGETVVLASVDQFR----- 396
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGnvSLDPNERLGKLRQDQFAfeeft 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 397 --DA--MDDKKtVWE------------EVSNgQDILTIGNFEipsrayvGRF-NFKGVDQQKRVGEL------------- 446
Cdd:PRK15064 81 vlDTviMGHTE-LWEvkqerdriyalpEMSE-EDGMKVADLE-------VKFaEMDGYTAEARAGELllgvgipeeqhyg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 447 -----SGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENaILEFPGCAMV-ISHDRWFLDRIATHI--LDYgde 518
Cdd:PRK15064 152 lmsevAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLED-VLNERNSTMIiISHDRHFLNSVCTHMadLDY--- 227
|
250 260
....*....|....*....|....*..
gi 1735515619 519 GKVTFYEGNFSDYEEwkkktlgdAATQ 545
Cdd:PRK15064 228 GELRVYPGNYDEYMT--------AATQ 246
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
324-382 |
7.21e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.95 E-value: 7.21e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSIT 382
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVL 59
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
316-513 |
8.17e-22 |
|
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: 99.07 E-value: 8.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 316 PGPRLGDKVIEVQNLTKSY--GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETvvlaSVD 393
Cdd:COG4987 325 PAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGV----DLR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 394 QFRDAmddkkTVWEEVSN-GQDI----------LTIGNfeiPS-----------RAYVGRFnfkgVDQQK-----RVGE- 445
Cdd:COG4987 401 DLDED-----DLRRRIAVvPQRPhlfdttlrenLRLAR---PDatdeelwaaleRVGLGDW----LAALPdgldtWLGEg 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 446 ---LSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILE-FPGCAMV-ISHDRWFLDRiATHIL 513
Cdd:COG4987 469 grrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEaLAGRTVLlITHRLAGLER-MDRIL 540
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
17-227 |
9.98e-22 |
|
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: 98.44 E-value: 9.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 17 PPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGE--------ARPQPGIKIGYLPQEPK-- 80
Cdd:COG1123 275 KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRptsgsiLFDGKdltklsrrSLRELRRRVQMVFQDPYss 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 81 LEPQQTVREAVEEAvsevksaltrldevyalyadpdadfdklaaeqanleaiIQAHDGHNLDNQLERAADALRLPDWDAK 160
Cdd:COG1123 355 LNPRMTVGDIIAEP--------------------------------------LRLHGLLSRAERRERVAELLERVGLPPD 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 161 IEH-----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAeSVAW-----LERFLHDYEGTVVAITHD----RYFLDNV 226
Cdd:COG1123 397 LADrypheLSGGQRQRVAIARALALEPKLLILDEPTSALDV-SVQAqilnlLRDLQRELGLTYLFISHDlavvRYIADRV 475
|
.
gi 1735515619 227 A 227
Cdd:COG1123 476 A 476
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
21-220 |
1.04e-21 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 93.35 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 21 HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE---------ARPQPGIKIGYLPQEPKLEPQQTVREAV 91
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEilidgrdvtGVPPERRNIGMVFQDYALFPHLTVAENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 92 eeavsevksaltrldeVYALYadpDADFDKLAAEQANLEAIIQAHdghnLDNQLERaadalrlpdwdaKIEHLSGGERRR 171
Cdd:cd03259 94 ----------------AFGLK---LRGVPKAEIRARVRELLELVG----LEGLLNR------------YPHELSGGQQQR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 172 VALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITHDR 220
Cdd:cd03259 139 VALARALAREPSLLLLDEPLSALDAKLreelREELKELQRELGITTIYVTHDQ 191
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
324-472 |
1.30e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 93.94 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVV--------------- 388
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhkrarlgigy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 389 L---ASVdqFRdamddKKTVWEevsNgqdILTIGNFEIPSRAyvgrfnfkgvDQQKRVGEL-----------------SG 448
Cdd:COG1137 83 LpqeASI--FR-----KLTVED---N---ILAVLELRKLSKK----------EREERLEELleefgithlrkskayslSG 139
|
170 180
....*....|....*....|....
gi 1735515619 449 GERGRLHLAKLLQRGGNVLLLDEP 472
Cdd:COG1137 140 GERRRVEIARALATNPKFILLDEP 163
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
325-513 |
1.62e-21 |
|
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: 92.98 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASvdqfrdamddkkt 404
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDD------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 405 vweevsnGQDILTIgnfeipsRAYVG----RFNF-----------------KGVDQQ----------KRVG--------- 444
Cdd:cd03262 68 -------KKNINEL-------RQKVGmvfqQFNLfphltvlenitlapikvKGMSKAeaeeralellEKVGladkadayp 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 445 -ELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFP--GCAMVI-SHDRWFLDRIATHIL 513
Cdd:cd03262 134 aQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAeeGMTMVVvTHEMGFAREVADRVI 206
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
324-508 |
2.02e-21 |
|
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: 92.80 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTL----IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSIT-MGETVVLAS------- 391
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLdtrvLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLfNGQSLSKLSsnerakl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 392 -------VDQFRDAMDDKkTVWEEVSNGqdiLTIGNF---EIPSRAY-----VG---RFNfkgvdqqKRVGELSGGERGR 453
Cdd:TIGR02211 81 rnkklgfIYQFHHLLPDF-TALENVAMP---LLIGKKsvkEAKERAYemlekVGlehRIN-------HRPSELSGGERQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 454 LHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEF---PGCAMVI-SHDRWFLDRI 508
Cdd:TIGR02211 150 VAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELnreLNTSFLVvTHDLELAKKL 208
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
324-514 |
2.18e-21 |
|
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: 92.88 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSY-----GDRTL--IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSI---TMGETVVLAS-- 391
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrHDGGWVDLAQas 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 392 --------------VDQF-----------------RDAMDDKKTVWEEVsngQDILTigNFEIPSR---AYVGRFnfkgv 437
Cdd:COG4778 84 preilalrrrtigyVSQFlrviprvsaldvvaeplLERGVDREEARARA---RELLA--RLNLPERlwdLPPATF----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 438 dqqkrvgelSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFP--GCAMV-ISHDRWFLDRIATHILD 514
Cdd:COG4778 154 ---------SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKarGTAIIgIFHDEEVREAVADRVVD 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
325-502 |
2.18e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 95.56 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQfRD------ 397
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdGEDVTHRSIQQ-RDicmvfq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 398 --AMDDKKTVWEEVSNGQDILTIGNFEIPSR-----AYV--GRFNFKGVDQqkrvgeLSGGERGRLHLAKLLQRGGNVLL 468
Cdd:PRK11432 86 syALFPHMSLGENVGYGLKMLGVPKEERKQRvkealELVdlAGFEDRYVDQ------ISGGQQQRVALARALILKPKVLL 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1735515619 469 LDEPTNDLDVETLRALENAILE----FPGCAMVISHDR 502
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRElqqqFNITSLYVTHDQ 197
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
316-502 |
2.25e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 97.74 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 316 PGPRLGDKVIEVQNLTKSYGDRT-LIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVD 393
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVnGVPLADADAD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 394 QFRD---------AMDDkKTVWEEV---SNGQDILTIGnfEIPSRAYVGRFnFKGVDQ--QKRVGE----LSGGERGRLH 455
Cdd:TIGR02857 393 SWRDqiawvpqhpFLFA-GTIAENIrlaRPDASDAEIR--EALERAGLDEF-VAALPQglDTPIGEggagLSGGQAQRLA 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1735515619 456 LAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFPGCAMV--ISHDR 502
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVllVTHRL 517
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
19-219 |
3.22e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 92.41 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARpqpgI-------------------KIGYLPQEP 79
Cdd:COG1136 20 EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVL----IdgqdisslserelarlrrrHIGFVFQFF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 80 KLEPQQTVREAVEEAvsevksaltrldevyALYADPDADFDKLAAEQAnleaiiqahdghnldnqLERaadaLRLPDW-D 158
Cdd:COG1136 96 NLLPELTALENVALP---------------LLLAGVSRKERRERAREL-----------------LER----VGLGDRlD 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 159 AKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITHD 219
Cdd:COG1136 140 HRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHD 204
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
15-236 |
3.40e-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: 97.03 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 15 VVPP--KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR-----------PQPGIKIGYLPQEPKL 81
Cdd:TIGR01842 324 IVPPggKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRldgadlkqwdrETFGKHIGYLPQDVEL 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 82 EPqqtvreaveeavSEVKSALTRLDEvyalyaDPDAdfdklaaeqanlEAIIQAhdghnldnqlERAADA----LRLPD- 156
Cdd:TIGR01842 404 FP------------GTVAENIARFGE------NADP------------EKIIEA----------AKLAGVheliLRLPDg 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 157 WDAKI----EHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYE---GTVVAITHdRYFLDNVAGW 229
Cdd:TIGR01842 444 YDTVIgpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKargITVVVITH-RPSLLGCVDK 522
|
....*..
gi 1735515619 230 ILELDRG 236
Cdd:TIGR01842 523 ILVLQDG 529
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
10-219 |
4.50e-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: 92.25 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 10 HRVGKVVPPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DK---EFEGEARPQPGIK--------IGYL 75
Cdd:cd03256 4 ENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLvepTSgsvLIDGTDINKLKGKalrqlrrqIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 76 PQEPKLEPQQTVREAVEEA----VSEVKSALTRLDEVyalyadpdadfDKLAAEQAnLEAIiqahdghNLDNQLERAADA 151
Cdd:cd03256 84 FQQFNLIERLSVLENVLSGrlgrRSTWRSLFGLFPKE-----------EKQRALAA-LERV-------GLLDKAYQRADQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1735515619 152 lrlpdwdakiehLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLERFLHDYEG-TVVAITHD 219
Cdd:cd03256 145 ------------LSGGQQQRVAIARALMQQPKLILADEPVASLDpasSRQVMDLLKRINREEGiTVIVSLHQ 204
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
325-500 |
7.42e-21 |
|
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: 89.97 E-value: 7.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGD--RTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQFRD---- 397
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADISQWDPNELGDhvgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 398 AMDDkktvweevsngqDILtignfeipsrayvgrfnFKGVdqqkrVGE--LSGGERGRLHLAKLLQRGGNVLLLDEPTND 475
Cdd:cd03246 81 LPQD------------DEL-----------------FSGS-----IAEniLSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180
....*....|....*....|....*...
gi 1735515619 476 LDVETLRALENAILEFPGC---AMVISH 500
Cdd:cd03246 127 LDVEGERALNQAIAALKAAgatRIVIAH 154
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
325-484 |
9.90e-21 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 91.25 E-value: 9.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRD------- 397
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNvgfvfqh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 398 -AMDDKKTVWEEVSNGQDILTIGnfEIPSRAYVGR-----FNFKGVD--QQKRVGELSGGERGRLHLAKLLQRGGNVLLL 469
Cdd:cd03296 83 yALFRHMTVFDNVAFGLRVKPRS--ERPPEAEIRAkvhelLKLVQLDwlADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170
....*....|....*
gi 1735515619 470 DEPTNDLDVETLRAL 484
Cdd:cd03296 161 DEPFGALDAKVRKEL 175
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-218 |
1.13e-20 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 89.92 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 6 VYTMHRVGKVvppKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--VDKEFEGE----ARPQPGIK----IGYL 75
Cdd:cd03213 11 VTVKSSPSKS---GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEvlinGRPLDKRSfrkiIGYV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 76 PQEPKLEPQQTVREAVEeavsevksaltrldevYAlyadpdadfdklaaeqanleaiiqahdghnldnqleraadalrlp 155
Cdd:cd03213 88 PQDDILHPTLTVRETLM----------------FA--------------------------------------------- 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 156 dwdAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLERFLHDYEGTVVAITH 218
Cdd:cd03213 107 ---AKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDsssALQVMSLLRRLADTGRTIICSIH 169
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
324-512 |
1.41e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.93 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQF------R 396
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdGGDIDDPDVAEAchylghR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 397 DAMDDKKTVWEEVSNGQDILtiGNFEIPSRAYVGRFNFKGVdQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDL 476
Cdd:PRK13539 82 NAMKPALTVAENLEFWAAFL--GGEELDIAAALEAVGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1735515619 477 DVETLRALENAI---LEFPGcaMVIshdrwfldrIATHI 512
Cdd:PRK13539 159 DAAAVALFAELIrahLAQGG--IVI---------AATHI 186
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
325-490 |
1.77e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 90.03 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQF-----RDA 398
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdGKPLDIAARNRIgylpeERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 399 MDDKKTVWEEVSNGQDILTIGNFEIPSRA--YVGRFNFKGVdQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDL 476
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLKGLKKEEARRRIdeWLERLELSEY-ANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170
....*....|....
gi 1735515619 477 DVETLRALENAILE 490
Cdd:cd03269 160 DPVNVELLKDVIRE 173
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
325-477 |
2.16e-20 |
|
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: 89.62 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVV---------LASVDQf 395
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtdlppkdrdIAMVFQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 396 RDAMDDKKTVWEEVSNGQDILTIGNFEIPSRAY-VGRfnFKGVDQ--QKRVGELSGGERGRLHLAKLLQRGGNVLLLDEP 472
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVReVAE--LLQIEHllDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
....*
gi 1735515619 473 TNDLD 477
Cdd:cd03301 158 LSNLD 162
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-239 |
3.18e-20 |
|
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: 87.98 E-value: 3.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 15 VVPPKRHIL-KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQPGIKIGYLPQEPKLePQQTVREAVee 93
Cdd:cd03223 8 LATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYL-PLGTLREQL-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 94 avsevksaltrldeVYAlyadpdadfdklaaeqanleaiiqahdghnldnqleraadalrlpdWDAKiehLSGGERRRVA 173
Cdd:cd03223 85 --------------IYP----------------------------------------------WDDV---LSGGEQQRLA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 174 LCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHdRYFLDNVAGWILELDRGEGI 239
Cdd:cd03223 102 FARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGEGGW 166
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-219 |
3.54e-20 |
|
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: 89.28 E-value: 3.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSF-FPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR---------------PQPGIKIGYLPQEPKLE 82
Cdd:cd03297 8 KRLPDFTLKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsrkkinlPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 83 PQQTVREAVEEA--VSEVKSALTRLDEVYALYadpdadfdklaaeqanleaiiqahdghNLDNQLERaadalrlpdwdaK 160
Cdd:cd03297 88 PHLNVRENLAFGlkRKRNREDRISVDELLDLL---------------------------GLDHLLNR------------Y 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 161 IEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITHD 219
Cdd:cd03297 129 PAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLPELKQIKKNLNIPVIFVTHD 191
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
19-216 |
4.09e-20 |
|
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: 88.81 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR---------PQPGIKIGYLPQEPKLEPQQTVRE 89
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdgksyqknIEALRRIGALIEAPGFYPNLTARE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 90 AVeeavsEVKSALTRLdevyalyadPDADFDKLaaeqanLEAIIQAHDGHNldnqleraadalrlpdwdaKIEHLSGGER 169
Cdd:cd03268 92 NL-----RLLARLLGI---------RKKRIDEV------LDVVGLKDSAKK-------------------KVKGFSLGMK 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1735515619 170 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAI 216
Cdd:cd03268 133 QRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLrdQGITVLI 181
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
23-236 |
5.13e-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: 89.32 E-value: 5.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE------FEGEARPQPGIK---IGYLPQEPKLEPQQTVREAVEE 93
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdsgtilFGGEDATDVPVQernVGFVFQHYALFRHMTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 94 AVsEVKSALTRLDEvyalyadpdadfDKLAAEQANLEAIIqahdghnldnQLERAADalRLPdwdakiEHLSGGERRRVA 173
Cdd:cd03296 98 GL-RVKPRSERPPE------------AEIRAKVHELLKLV----------QLDWLAD--RYP------AQLSGGQRQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 174 LCRLLLEKPDMLLLDEPTNHLDA----ESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRG 236
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKG 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
324-512 |
5.70e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.16 E-value: 5.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVdqfRDAMD-- 400
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEPVRFRSP---RDAQAag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 401 -----------DKKTVWEevsNgqdiLTIGNFeiPSRAyvGRFNFK---------------GVDQQKRVGELSGGERGRL 454
Cdd:COG1129 81 iaiihqelnlvPNLSVAE---N----IFLGRE--PRRG--GLIDWRamrrrarellarlglDIDPDTPVGDLSVAQQQLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 455 HLAKLLQRGGNVLLLDEPT---NDLDVETL----RALENAilefpGCAMV-ISHdrwFLD---RIATHI 512
Cdd:COG1129 150 EIARALSRDARVLILDEPTaslTEREVERLfriiRRLKAQ-----GVAIIyISH---RLDevfEIADRV 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
324-513 |
5.91e-20 |
|
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: 93.04 E-value: 5.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSY--GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDA---GSITMGETVVLASVDQFR-- 396
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 397 -------DAMD--DKKTVWEEVSNGQDILTIGNFEIPSRAyVGRFNFKGVDQ--QKRVGELSGGERGRLHLAKLLQRGGN 465
Cdd:COG1123 84 rigmvfqDPMTqlNPVTVGDQIAEALENLGLSRAEARARV-LELLEAVGLERrlDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 466 VLLLDEPTNDLDV----ETLRALENAILEFpGCAMV-ISHDRWFLDRIATHIL 513
Cdd:COG1123 163 LLIADEPTTALDVttqaEILDLLRELQRER-GTTVLlITHDLGVVAEIADRVV 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-219 |
7.05e-20 |
|
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: 92.81 E-value: 7.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 17 PPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE---------ARPQPGIK--IGYLPQEPKLEpQQ 85
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEvtldgvpvsSLDQDEVRrrVSVCAQDAHLF-DT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 TVREAVeeavsevksaltrldevyaLYADPDADFDKL--AAEQANLEAIIQA-HDGhnLDNQL-ERAAdalrlpdwdaki 161
Cdd:TIGR02868 424 TVRENL-------------------RLARPDATDEELwaALERVGLADWLRAlPDG--LDTVLgEGGA------------ 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 162 eHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAITHD 219
Cdd:TIGR02868 471 -RLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAlsGRTVVLITHH 529
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
325-491 |
1.09e-19 |
|
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: 88.16 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSY---------------------GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM 383
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 384 GETVVLASVDQFRD----AMDDKKTVWEEVSNGQDILTIGN-FEIPSRAY------------VGRFnfkgVDQQKRvgEL 446
Cdd:cd03267 81 AGLVPWKRRKKFLRrigvVFGQKTQLWWDLPVIDSFYLLAAiYDLPPARFkkrldelselldLEEL----LDTPVR--QL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1735515619 447 SGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEF 491
Cdd:cd03267 155 SLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEY 199
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
20-218 |
1.14e-19 |
|
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: 88.60 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------------DKEFEGEA----RPqpgiKIGYLPQE--PKL 81
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlpptygndvrlfGERRGGEDvwelRK----RIGLVSPAlqLRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 82 EPQQTVREAVeeavsevksaLTRLDEVYALYADPDadfdklaaeqanleaiiqahdghnlDNQLERAADALRLpdW---- 157
Cdd:COG1119 92 PRDETVLDVV----------LSGFFDSIGLYREPT-------------------------DEQRERARELLEL--Lglah 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 158 --DAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITH 218
Cdd:COG1119 135 laDRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-191 |
1.21e-19 |
|
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: 87.87 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 21 HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGE---ARPQPGI---KIGYLPQEPKLEPQQTVR 88
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPprsgsiRFDGRditGLPPHERaraGIGYVPEGRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 89 E---AVEEAVSEVKSAlTRLDEVYALyadpdadFDKLAaeqanleaiiqahdghnldnqlERaadalrlpdWDAKIEHLS 165
Cdd:cd03224 94 EnllLGAYARRRAKRK-ARLERVYEL-------FPRLK----------------------ER---------RKQLAGTLS 134
|
170 180
....*....|....*....|....*.
gi 1735515619 166 GGERRRVALCRLLLEKPDMLLLDEPT 191
Cdd:cd03224 135 GGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
20-243 |
1.61e-19 |
|
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: 87.56 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGEARPQPG--------IKIGYLPQEPKLEPQQ 85
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRpdsgevLIDGEDISGLSeaelyrlrRRMGMLFQSGALFDSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 TVREAVeeavsevksALtRLDEVYALyadPDADFDKLAAEQanLEAIiqahdGhnldnqLERAADalRLPDwdakieHLS 165
Cdd:cd03261 93 TVFENV---------AF-PLREHTRL---SEEEIREIVLEK--LEAV-----G------LRGAED--LYPA------ELS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLERFLHDYEG-TVVAITHDRYFLDNVAGWILELDRGEgIPW 241
Cdd:cd03261 139 GGMKKRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKKELGlTSIMVTHDLDTAFAIADRIAVLYDGK-IVA 217
|
..
gi 1735515619 242 EG 243
Cdd:cd03261 218 EG 219
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-227 |
1.66e-19 |
|
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: 87.85 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 29 SFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEArPQPGIKIGYLPQEpkLEPQQTVReaveeavsevksaltrldeV 108
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-EIELDTVSYKPQY--IKADYEGT-------------------V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 109 YALYADPDADFdkLAAEQANLEaIIQAHdghnldnQLERAADAlRLPDwdakiehLSGGERRRVALCRLLLEKPDMLLLD 188
Cdd:cd03237 79 RDLLSSITKDF--YTHPYFKTE-IAKPL-------QIEQILDR-EVPE-------LSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1735515619 189 EPTNHLDAE----SVAWLERFLHDYEGTVVAITHDRYFLDNVA 227
Cdd:cd03237 141 EPSAYLDVEqrlmASKVIRRFAENNEKTAFVVEHDIIMIDYLA 183
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
325-472 |
1.67e-19 |
|
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: 87.60 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVL--------------- 389
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITklpmhkrarlgigyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 390 ---ASVdqFRdamddKKTVWEEVSNGQDILTIGNFEIPSR--AYVGRFNFKGVDQQKrVGELSGGERGRLHLAKLLQRGG 464
Cdd:cd03218 81 pqeASI--FR-----KLTVEENILAVLEIRGLSKKEREEKleELLEEFHITHLRKSK-ASSLSGGERRRVEIARALATNP 152
|
....*...
gi 1735515619 465 NVLLLDEP 472
Cdd:cd03218 153 KFLLLDEP 160
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
19-237 |
1.84e-19 |
|
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: 86.09 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGE-------ARPQPGIKIGYLPQEPKLEPQQ 85
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEpdsgsiLIDGEdltdledELPPLRRRIGMVFQDFALFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 TVREAVEEAvsevksaltrldevyalyadpdadfdklaaeqanleaiiqahdghnldnqleraadalrlpdwdakiehLS 165
Cdd:cd03229 92 TVLENIALG---------------------------------------------------------------------LS 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERF---LHDYEG-TVVAITHDRYFLDNVAGWILELDRGE 237
Cdd:cd03229 103 GGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALlksLQAQLGiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
324-472 |
1.93e-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: 87.71 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVL------------- 389
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIdGQDITHlpmherarlgigy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 390 ----ASVdqFRdamddKKTVWEE---VSNGQDILTIGNFEIPSRAYVGRFNFKGVdQQKRVGELSGGERGRLHLAKLLQR 462
Cdd:TIGR04406 81 lpqeASI--FR-----KLTVEENimaVLEIRKDLDRAEREERLEALLEEFQISHL-RDNKAMSLSGGERRRVEIARALAT 152
|
170
....*....|
gi 1735515619 463 GGNVLLLDEP 472
Cdd:TIGR04406 153 NPKFILLDEP 162
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
307-510 |
1.93e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 91.76 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 307 NETNELFIPPGPRLGDKV---IEVQNLTKSY-GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSIT 382
Cdd:COG1132 319 DEPPEIPDPPGAVPLPPVrgeIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 383 MGEtVVLASVDQ--FRDAM----------DDkkTVWEevsNgqdiLTIGNFEIP--------SRAYVGRF--NF-KGVDQ 439
Cdd:COG1132 399 IDG-VDIRDLTLesLRRQIgvvpqdtflfSG--TIRE---N----IRYGRPDATdeeveeaaKAAQAHEFieALpDGYDT 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 440 QkrVGE----LSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEF-PGCAM-VISHdrwfldRIAT 510
Cdd:COG1132 469 V--VGErgvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLmKGRTTiVIAH------RLST 537
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
324-513 |
1.96e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.03 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSY-GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLAS---------- 391
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVnGQDLSRLKrreipylrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 392 ---VDQ-FRDAMDdkKTVWEEVSNGQDILTIGNFEIPSRA-----YVGRFNFKgvdqQKRVGELSGGERGRLHLAkllqR 462
Cdd:COG2884 81 igvVFQdFRLLPD--RTVYENVALPLRVTGKSRKEIRRRVrevldLVGLSDKA----KALPHELSGGEQQRVAIA----R 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1735515619 463 G--GN--VLLLDEPTNDLDVET----LRALE--NAIlefpGCAMVI-SHDRWFLDRIATHIL 513
Cdd:COG2884 151 AlvNRpeLLLADEPTGNLDPETsweiMELLEeiNRR----GTTVLIaTHDLELVDRMPKRVL 208
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
325-491 |
2.29e-19 |
|
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: 85.83 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYG--DRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRDAMddk 402
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 403 ktvweEVSNGQDILtignFEIPSRAYVGRfnfkgvdqqkrvgELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLR 482
Cdd:cd03247 78 -----SVLNQRPYL----FDTTLRNNLGR-------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
....*....
gi 1735515619 483 ALENAILEF 491
Cdd:cd03247 136 QLLSLIFEV 144
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
325-490 |
4.34e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 88.60 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSY----GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLA-SVDQFRDA- 398
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 399 ----MD-------DKKTVWEevsngqdiltigNFEIP------SRAyvgrfnfkgvDQQKRVGE---------------- 445
Cdd:COG1135 82 rkigMIfqhfnllSSRTVAE------------NVALPleiagvPKA----------EIRKRVAEllelvglsdkadayps 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1735515619 446 -LSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRalenAILE 490
Cdd:COG1135 140 qLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTR----SILD 181
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
22-236 |
4.45e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 86.61 E-value: 4.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AGV----DKEFEGEARPQPGI------KIGYLPQEPKLEPQ 84
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQlniaGHQFDFSQKPSEKAirllrqKVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 85 QTVREAVEEAVSEVKsaltrldevyalyadpdadfdKLAAEQANLEAIiqahdghNLDNQLERAADALRLPdwdakiEHL 164
Cdd:COG4161 97 LTVMENLIEAPCKVL---------------------GLSKEQAREKAM-------KLLARLRLTDKADRFP------LHL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRG 236
Cdd:COG4161 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEitaQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKG 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
19-237 |
5.54e-19 |
|
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: 85.66 E-value: 5.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGEARPQPGI-------KIGYLPQEPKLEPQQ 85
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEpdsgtiIIDGLKLTDDKKninelrqKVGMVFQQFNLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 TVREAVEEAVSEVKsaltrldevyalyadpdadfdKLAAEQANleaiiqahdghnldnqlERAADALR---LPDW-DAKI 161
Cdd:cd03262 92 TVLENITLAPIKVK---------------------GMSKAEAE-----------------ERALELLEkvgLADKaDAYP 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 162 EHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD--YEG-TVVAITHDRYFLDNVAGWILELDRGE 237
Cdd:cd03262 134 AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlaEEGmTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-237 |
5.61e-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: 85.54 E-value: 5.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 9 MHRVGKVVPPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR--------------PQPGIKIGY 74
Cdd:cd03292 3 FINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvngqdvsdlrgraiPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 75 LPQEPKLEPQQTVREAVEEA--VSEVKSALTRldevyalyadpdadfdklaaeqanleaiiqahdghnldnqlERAADAL 152
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFAleVTGVPPREIR-----------------------------------------KRVPAAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 153 RLPDWDAKI----EHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL---HDYEGTVVAITHDRYFLDN 225
Cdd:cd03292 122 ELVGLSHKHralpAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLkkiNKAGTTVVVATHAKELVDT 201
|
250
....*....|..
gi 1735515619 226 VAGWILELDRGE 237
Cdd:cd03292 202 TRHRVIALERGK 213
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
330-513 |
6.49e-19 |
|
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: 86.31 E-value: 6.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 330 LTKSYGDRTL-IDDLSFSipKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSI-TMGETVvlASVDQFRDAmDDKKTVWE 407
Cdd:cd03237 6 MKKTLGEFTLeVEGGSIS--ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIeIELDTV--SYKPQYIKA-DYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 408 EVSNGQDILTIGNF---EIpsrayvgrFNFKGVDQ--QKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVE--- 479
Cdd:cd03237 81 LLSSITKDFYTHPYfktEI--------AKPLQIEQilDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrl 152
|
170 180 190
....*....|....*....|....*....|....*
gi 1735515619 480 -TLRALENAILEFPGCAMVISHDRWFLDRIATHIL 513
Cdd:cd03237 153 mASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-473 |
1.26e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 89.80 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 10 HRVGKVVPpkrhiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE------------ARPQPGIKIGYLPQ 77
Cdd:NF033858 9 HRYGKTVA-----LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRvevlggdmadarHRRAVCPRIAYMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 78 E--PKLEPQQTVREAVEeavsevksALTRLdevyalyadpdadFDKLAAE-QANLEAIIQAHDghnLDNQLERAAdalrl 154
Cdd:NF033858 84 GlgKNLYPTLSVFENLD--------FFGRL-------------FGQDAAErRRRIDELLRATG---LAPFADRPA----- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 155 pdwdAKiehLSGGERRRVALCRLLLEKPDMLLLDEPT---------------NHLDAE----SV----AWLE---RFLHd 208
Cdd:NF033858 135 ----GK---LSGGMKQKLGLCCALIHDPDLLILDEPTtgvdplsrrqfweliDRIRAErpgmSVlvatAYMEeaeRFDW- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 209 yegtVVAithdryfLDnvAGWILeldrGEGIPWEgnysswleqkekrLEQEQAAENarqksiakeLEwvrqnpkgrQAks 288
Cdd:NF033858 207 ----LVA-------MD--AGRVL----ATGTPAE-------------LLARTGADT---------LE---------AA-- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 289 karmarFDELNSGEyqKRNETNELFIPPGPRLGDK--VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTL 366
Cdd:NF033858 237 ------FIALLPEE--KRRGHQPVVIPPRPADDDDepAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTT 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 367 FRMLSGQEQPDAGSITM-GETVvlasvdqfrDA--MDDKKTV---------WEEVSNGQDIL------TIGNFEIPSR-- 426
Cdd:NF033858 309 MKMLTGLLPASEGEAWLfGQPV---------DAgdIATRRRVgymsqafslYGELTVRQNLElharlfHLPAAEIAARva 379
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1735515619 427 AYVGRFNFKGVdQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPT 473
Cdd:NF033858 380 EMLERFDLADV-ADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
323-387 |
2.00e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 84.75 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 323 KVIEVQNLTKSY-----GDRTL-----------------IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGS 380
Cdd:COG1134 3 SMIEVENVSKSYrlyhePSRSLkelllrrrrtrreefwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
....*..
gi 1735515619 381 ITMGETV 387
Cdd:COG1134 83 VEVNGRV 89
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
325-523 |
2.21e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.42 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLidDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLA-------------- 390
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAlppaerpvsmlfqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 391 -------SVDQ-----FRDAM----DDKKTVweevsngQDILtignfeipsrAYVGRFNFKgvdqQKRVGELSGGERGRL 454
Cdd:COG3840 80 nnlfphlTVAQniglgLRPGLkltaEQRAQV-------EQAL----------ERVGLAGLL----DRLPGQLSGGQRQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 455 HLAKLLQRGGNVLLLDEPTNDLD----------VETLRALENAILefpgcaMVISHDrwfLD---RIATHILdYGDEGKV 521
Cdd:COG3840 139 ALARCLVRKRPILLLDEPFSALDpalrqemldlVDELCRERGLTV------LMVTHD---PEdaaRIADRVL-LVADGRI 208
|
..
gi 1735515619 522 TF 523
Cdd:COG3840 209 AA 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
19-242 |
3.02e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.44 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAgvdkefeGEARPQPGiKIgYLPQEPK--LEPQQTvreAVEEAVS 96
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS-------GELSPDSG-EV-RLNGRPLadWSPAEL---ARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 97 EVKSALT---RLDEVYALYADPdadfdkLAAEQANLEAIIQAhdghnldnQLERA-ADALRlpdwDAKIEHLSGGERRRV 172
Cdd:PRK13548 82 PQHSSLSfpfTVEEVVAMGRAP------HGLSRAEDDALVAA--------ALAQVdLAHLA----GRDYPQLSGGEQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 173 ALCRLLL------EKPDMLLLDEPTNHLD---AESVAWLER-FLHDYEGTVVAITHD-----RYfldnvAGWILELDRG- 236
Cdd:PRK13548 144 QLARVLAqlwepdGPPRWLLLDEPTSALDlahQHHVLRLARqLAHERGLAVIVVLHDlnlaaRY-----ADRIVLLHQGr 218
|
....*....
gi 1735515619 237 ---EGIPWE 242
Cdd:PRK13548 219 lvaDGTPAE 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
325-483 |
3.09e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 86.28 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRD-AM---- 399
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNiAMvfqs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 400 ---------------------DDKKTVWEEVSNGQDILTIGNFEipsrayvgrfnfkgvdqQKRVGELSGGERGRLHLAK 458
Cdd:COG3839 84 yalyphmtvyeniafplklrkVPKAEIDRRVREAAELLGLEDLL-----------------DRKPKQLSGGQRQRVALGR 146
|
170 180
....*....|....*....|....*
gi 1735515619 459 LLQRGGNVLLLDEPTNDLDVEtLRA 483
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDAK-LRV 170
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-240 |
3.47e-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: 87.92 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 33 GAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEArpQPGIKIGYLPQEPKLEPQQTVREAVEEAVSEvksaltRLDEVYaLY 112
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISPDYDGTVEEFLRSANTD------DFGSSY-YK 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 113 ADpdadfdklaaeqanleaIIQahdGHNLDNQLERaadalrlpdwdaKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTN 192
Cdd:COG1245 437 TE-----------------IIK---PLGLEKLLDK------------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 193 HLDAE---SVA-WLERFLHDYEGTVVAITHDRYFLDNVAgwilelDRG---EGIP 240
Cdd:COG1245 485 HLDVEqrlAVAkAIRRFAENRGKTAMVVDHDIYLIDYIS------DRLmvfEGEP 533
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-219 |
4.95e-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: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE------FEGEARPQPGIKIGYLPQEPKLEPQQTVREAVEEAVS 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPtsggviLEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 97 EVKSALTRldevyalyadpdadfdklaAEQanlEAIIQahdgHNLD-NQLERAADAlrlpdwdaKIEHLSGGERRRVALC 175
Cdd:TIGR01184 81 RVLPDLSK-------------------SER---RAIVE----EHIAlVGLTEAADK--------RPGQLSGGMKQRVAIA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1735515619 176 RLLLEKPDMLLLDEPTNHLDAESVAWLE----RFLHDYEGTVVAITHD 219
Cdd:TIGR01184 127 RALSIRPKVLLLDEPFGALDALTRGNLQeelmQIWEEHRVTVLMVTHD 174
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-478 |
6.51e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 6.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 10 HRVGKVVPPKRhILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE----ARPQ----------PGIKIGYl 75
Cdd:PRK11288 8 DGIGKTFPGVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSilidGQEMrfasttaalaAGVAIIY- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 76 pQEPKLEPQQTVREAVeeAVSEVKSALTRLDEvyalyadpdadfdKLAAEQANLeaiiqahdghnldnQLERAADALrlp 155
Cdd:PRK11288 86 -QELHLVPEMTVAENL--YLGQLPHKGGIVNR-------------RLLNYEARE--------------QLEHLGVDI--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 156 DWDAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVA-ITHdryfldnvagwile 232
Cdd:PRK11288 133 DPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELraEGRVILyVSH-------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 233 ldrgegipwegnysswleqkekRLEQEQAAENArqKSIAKElewvrqnpkGRQAKSKARMARFD-ELNSGEYQKRNETNE 311
Cdd:PRK11288 199 ----------------------RMEEIFALCDA--ITVFKD---------GRYVATFDDMAQVDrDQLVQAMVGREIGDI 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 312 LFIPPGPrLGDKVIEVQNLTksyGDRtLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLA 390
Cdd:PRK11288 246 YGYRPRP-LGEVRLRLDGLK---GPG-LREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdGKPIDIR 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 391 SVdqfRDAM--------DDKK--------TVWEE--VSNGQDILTIGNF------EIPSRAYVGRFNFKGVDQQKRVGEL 446
Cdd:PRK11288 321 SP---RDAIragimlcpEDRKaegiipvhSVADNinISARRHHLRAGCLinnrweAENADRFIRSLNIKTPSREQLIMNL 397
|
490 500 510
....*....|....*....|....*....|..
gi 1735515619 447 SGGERGRLHLAKLLQRGGNVLLLDEPTNDLDV 478
Cdd:PRK11288 398 SGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
325-490 |
6.80e-18 |
|
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: 83.05 E-value: 6.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGD-RTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQFRDAM--- 399
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdGQDIREVTLDSLRRAIgvv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 400 -------DDkkTVWEEVSNGQdiLTIGNFEIPSRAYVG-------RFNFKgvdQQKRVGE----LSGGERGRLHLAKLLQ 461
Cdd:cd03253 81 pqdtvlfND--TIGYNIRYGR--PDATDEEVIEAAKAAqihdkimRFPDG---YDTIVGErglkLSGGEKQRVAIARAIL 153
|
170 180
....*....|....*....|....*....
gi 1735515619 462 RGGNVLLLDEPTNDLDVETLRALENAILE 490
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRD 182
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
325-482 |
7.37e-18 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 82.67 E-value: 7.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGEtVVLASVDQFRD------- 397
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG-KDITNLPPHKRpvntvfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 398 --AMDDKKTVWEEVSNGQDILTIGNFEIPSRA--YVGRFNFKGVdQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPT 473
Cdd:cd03300 80 nyALFPHLTVFENIAFGLRLKKLPKAEIKERVaeALDLVQLEGY-ANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
....*....
gi 1735515619 474 NDLDVEtLR 482
Cdd:cd03300 159 GALDLK-LR 166
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
322-500 |
8.35e-18 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 83.21 E-value: 8.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 322 DKVIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAG-SIT-MGETVVLASV------- 392
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRlFGERRGGEDVwelrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 393 --------DQFRDAMddkkTVWEEV-SNGQDilTIGNFEIPSRAYVGR----FNFKGVDQ--QKRVGELSGGERGRLHLA 457
Cdd:COG1119 81 glvspalqLRFPRDE----TVLDVVlSGFFD--SIGLYREPTDEQRERarelLELLGLAHlaDRPFGTLSQGEQRRVLIA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1735515619 458 KLLQRGGNVLLLDEPTNDLDV---ETLRALENAILEFPGCAMV-ISH 500
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLgarELLLALLDKLAAEGAPTLVlVTH 201
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
19-219 |
1.32e-17 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 81.84 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarPQPGiKIGYLPQEPKlepqqtvreAVEEAVSEV 98
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGA--PDEG-EVLLDGKDIY---------DLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 99 KsalTRLDEVYALyADPdadFDKLAAEqaNLEAIIQAHDGHNLDNQLERAADALRLPD-WD-----AKIEHLSGGERRRV 172
Cdd:cd03260 80 R---RRVGMVFQK-PNP---FPGSIYD--NVAYGLRLHGIKLKEELDERVEEALRKAAlWDevkdrLHALGLSGGQQQRL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1735515619 173 ALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAITHD 219
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
325-520 |
1.42e-17 |
|
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: 80.28 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLT-KSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGEtvvlasvdqfrdamddkk 403
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 404 tvweevsnGQDILtignFeIPSRAYVGRFNFKGV-----DQqkrvgELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDV 478
Cdd:cd03223 63 --------GEDLL----F-LPQRPYLPLGTLREQliypwDD-----VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1735515619 479 ETLRALENAILEFpGCAMV-ISHdRWFLDRIATHILDYGDEGK 520
Cdd:cd03223 125 ESEDRLYQLLKEL-GITVIsVGH-RPSLWKFHDRVLDLDGEGG 165
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-195 |
1.61e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.47 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQPGIKIGYLPQEPKLEPqqTVREAVEEAVsEV 98
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDT--TLPLTVNRFL-RL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 99 KSALTRLDEVYALyadpdadfdklaaeqanleAIIQAhdGHNLdnqleraadalrlpdwDAKIEHLSGGERRRVALCRLL 178
Cdd:PRK09544 93 RPGTKKEDILPAL-------------------KRVQA--GHLI----------------DAPMQKLSGGETQRVLLARAL 135
|
170
....*....|....*..
gi 1735515619 179 LEKPDMLLLDEPTNHLD 195
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVD 152
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
22-218 |
1.65e-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: 81.17 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR-------PQPGIKIGYLPQEPKLEPQQTVREAVeea 94
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldIAARNRIGYLPEERGLYPKMKVIDQL--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 95 vsevksaltrldeVYAlyadpdADFDKLAAEQANleaiiqahdgHNLDNQLERaadaLRLPDW-DAKIEHLSGGERRRVA 173
Cdd:cd03269 92 -------------VYL------AQLKGLKKEEAR----------RRIDEWLER----LELSEYaNKRVEELSKGNQQKVQ 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1735515619 174 LCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG---TVVAITH 218
Cdd:cd03269 139 FIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARagkTVILSTH 186
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
314-491 |
1.73e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.54 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 314 IPPGPRLGDkVIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQE--QPDAGSITMGEtvvlas 391
Cdd:COG2401 21 LDLSERVAI-VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPD------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 392 vDQFrdamDDKKTVWEEVSNGQDILTIgnFEIPSRA-YVGRFNFKgvdqqKRVGELSGGERGRLHLAKLLQRGGNVLLLD 470
Cdd:COG2401 94 -NQF----GREASLIDAIGRKGDFKDA--VELLNAVgLSDAVLWL-----RRFKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180
....*....|....*....|.
gi 1735515619 471 EPTNDLDVETLRALENAILEF 491
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKL 182
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
22-236 |
1.92e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 81.98 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGVDKEFEGEARPQPGI----KIGYLPQEPKLEPQ 84
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprsgtlniAGNHFDFSKTPSDKAIRelrrNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 85 QTVREAVEEAVSEVKsaltrldevyalyadpdadfdKLAAEQANLEAiiqahdghnlDNQLERaadaLRLPDW-DAKIEH 163
Cdd:PRK11124 97 LTVQQNLIEAPCRVL---------------------GLSKDQALARA----------EKLLER----LRLKPYaDRFPLH 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGT---VVAITHDRYFLDNVAGWILELDRG 236
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgitQVIVTHEVEVARKTASRVVYMENG 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-227 |
1.98e-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: 84.00 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 25 DISLSFfPGAKIGVL-GLNGAGKSTLLRIMAGVDKEFEG--------------------EARPqpgikIGYLPQEPKLEP 83
Cdd:COG4148 17 DVDFTL-PGRGVTALfGPSGSGKTTLLRAIAGLERPDSGrirlggevlqdsargiflppHRRR-----IGYVFQEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 84 QQTVREAVEEAVSEVKSALTRldevyalyadpdADFDKLAAeqanLEAIiqahdGHNLDnqleraadalRLPDwdakieH 163
Cdd:COG4148 91 HLSVRGNLLYGRKRAPRAERR------------ISFDEVVE----LLGI-----GHLLD----------RRPA------T 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERfLHDYEGT-VVAITHDryfLDNVA 227
Cdd:COG4148 134 LSGGERQRVAIGRALLSSPRLLLMDEPLAALDlarkAEILPYLER-LRDELDIpILYVSHS---LDEVA 198
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
322-478 |
2.02e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.53 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 322 DKVIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETvVLASVD-------- 393
Cdd:PRK10575 9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQ-PLESWSskafarkv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 394 -----QFRDAmdDKKTVWEEVSngqdiltIGNFeiPSRAYVGRFnfkGVDQQKRVGE-----------------LSGGER 451
Cdd:PRK10575 88 aylpqQLPAA--EGMTVRELVA-------IGRY--PWHGALGRF---GAADREKVEEaislvglkplahrlvdsLSGGER 153
|
170 180
....*....|....*....|....*..
gi 1735515619 452 GRLHLAKLLQRGGNVLLLDEPTNDLDV 478
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
21-220 |
2.09e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 83.61 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 21 HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEG--------EARPqpgikIGYLPQEPKLEPQQT 86
Cdd:COG3842 19 TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETpdsgriLLDGrdvtglppEKRN-----VGMVFQDYALFPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 87 VREAVEeavsevksaltrldevYALyadpdaDFDKLAAEQANleaiiqahdghnldnqlERAADAL---RLPDW-DAKIE 162
Cdd:COG3842 94 VAENVA----------------FGL------RMRGVPKAEIR-----------------ARVAELLelvGLEGLaDRYPH 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1735515619 163 HLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESV-AWLERFLHDYEGTVVAITHDR 220
Cdd:COG3842 135 QLSGGQQQRVALARALAPEPRVLLLDEPLSALDAklrEEMrEELRRLQRELGITFIYVTHDQ 196
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
19-190 |
2.37e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 81.44 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE--------------ARPQPGikIGYLPQEPKLepq 84
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKilldgqditklpmhKRARLG--IGYLPQEASI--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 85 qtvreaveeavsevksaltrldevyalyadpdadFDKLAAEQaNLEAIIQAHdgHNLDNQLERAADALrLPDWdaKIEH- 163
Cdd:cd03218 87 ----------------------------------FRKLTVEE-NILAVLEIR--GLSKKEREEKLEEL-LEEF--HITHl 126
|
170 180 190
....*....|....*....|....*....|....
gi 1735515619 164 -------LSGGERRRVALCRLLLEKPDMLLLDEP 190
Cdd:cd03218 127 rkskassLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
21-219 |
2.63e-17 |
|
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: 81.33 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 21 HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDkefegeaRPQPGikigylpqepklepqqTVREAVEEavsevks 100
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLD-------RPTSG----------------TVRLAGQD------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 101 aLTRLDEvyalyadpdadfDKLAA------------EQ--ANLEAiiqahdghnLDNQL------------ERAADAL-- 152
Cdd:COG4181 76 -LFALDE------------DARARlrarhvgfvfqsFQllPTLTA---------LENVMlplelagrrdarARARALLer 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 153 -----RLpdwDAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHDYEG-TVVAITHD 219
Cdd:COG4181 134 vglghRL---DHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAatgEQIIDLLFELNRERGtTLVLVTHD 206
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
22-219 |
2.70e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.12 E-value: 2.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKEFEGEARPQPGIKIGYLPQEPKLEPQQTVREA 90
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTltptagtvlvaGDDVEALSARAASRRVASVPQDTSLSFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 91 VEEAVSEVKSALTRLDEVyalyadpdadfDKLAAEQAnleaiiqahdghnldnqLERAaDALRLPDWDakIEHLSGGERR 170
Cdd:PRK09536 98 VEMGRTPHRSRFDTWTET-----------DRAAVERA-----------------MERT-GVAQFADRP--VTSLSGGERQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1735515619 171 RVALCRLLLEKPDMLLLDEPTNHLDA-ESVAWLE--RFLHDYEGTVVAITHD 219
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLDInHQVRTLElvRRLVDDGKTAVAAIHD 198
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-226 |
2.73e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 82.46 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR-------PQPGIKIGYLPQEPKLEPQQTVREAV 91
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgepldPEDRRRIGYLPEERGLYPKMKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 92 EeavsevksALTRLdevyalyadpdADFDKLAAEqanleaiiqahdgHNLDNQLERaadaLRLPDW-DAKIEHLSGGERR 170
Cdd:COG4152 93 V--------YLARL-----------KGLSKAEAK-------------RRADEWLER----LGLGDRaNKKVEELSKGNQQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 171 RVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHDryfLDNV 226
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaaKGtTVIFSSHQ---MELV 192
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
325-508 |
3.21e-17 |
|
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: 80.71 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGD--RTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETvvlaSVDQF--RDAMD 400
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT----DIRQLdpADLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 401 DKKTVWEEVS--NG--QDILTIGNFEIPSRAYVGRFNFKGVDQ---------QKRVGE----LSGGERGRLHLAKLLQRG 463
Cdd:cd03245 79 NIGYVPQDVTlfYGtlRDNITLGAPLADDERILRAAELAGVTDfvnkhpnglDLQIGErgrgLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1735515619 464 GNVLLLDEPTNDLDVETLRALENAILEFPG--CAMVISHDRWFL---DRI 508
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLdlvDRI 208
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
325-488 |
3.28e-17 |
|
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: 80.23 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRDAM----- 399
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLlylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 400 -DDKKTVWEEVSNGQDILTIGNFEIPSRAyVGRFNFKGVDQQKrVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDV 478
Cdd:cd03231 81 aPGIKTTLSVLENLRFWHADHSDEQVEEA-LARVGLNGFEDRP-VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170
....*....|
gi 1735515619 479 ETLRALENAI 488
Cdd:cd03231 159 AGVARFAEAM 168
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
325-507 |
3.49e-17 |
|
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: 80.53 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTL-IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVV--------------L 389
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrgraipylrrkI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 390 ASVDQ-FRDAMDdkKTVWEEVSNGQDILTIGNFEIPSRAyVGRFNFKGVDQQKRV--GELSGGERGRLHLAKLLQRGGNV 466
Cdd:cd03292 81 GVVFQdFRLLPD--RNVYENVAFALEVTGVPPREIRKRV-PAALELVGLSHKHRAlpAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1735515619 467 LLLDEPTNDLDVETLRALENAILEF--PGCAMVIS-HDRWFLDR 507
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKInkAGTTVVVAtHAKELVDT 201
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
327-480 |
3.63e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.26 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 327 VQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRDAMDDKKTV- 405
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDARLLp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 406 WEEVSNGQDILTIGNFEIPSRAYVgrfnfKGVDQQKRVGE----LSGGERGRLHLAK-LLQRGGnVLLLDEPTNDLDVET 480
Cdd:PRK11247 95 WKKVIDNVGLGLKGQWRDAALQAL-----AAVGLADRANEwpaaLSGGQKQRVALARaLIHRPG-LLLLDEPLGALDALT 168
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
19-208 |
4.19e-17 |
|
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: 80.80 E-value: 4.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpqpgIKI-GY-LPQEPKlepqqtvreaveeavs 96
Cdd:TIGR03864 13 ARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQ------ISVaGHdLRRAPR---------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 97 evkSALTRLDEVYAlyaDPDADFDkLAAEQ-----ANLEAIIQAHDGHNLDNQLERAADALRLpdwDAKIEHLSGGERRR 171
Cdd:TIGR03864 71 ---AALARLGVVFQ---QPTLDLD-LSVRQnlryhAALHGLSRAEARARIAELLARLGLAERA---DDKVRELNGGHRRR 140
|
170 180 190
....*....|....*....|....*....|....*..
gi 1735515619 172 VALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD 208
Cdd:TIGR03864 141 VEIARALLHRPALLLLDEPTVGLDPASRAAITAHVRA 177
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-218 |
4.51e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.85 E-value: 4.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 25 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQpgikiGylpqepklEPQQTVREAVEEAV------SEV 98
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ-----G--------EPIRRQRDEYHQDLlylghqPGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 99 KSALTRLDEVYALYAdpdadfdklAAEQANLEAIIQAhdghnldnqLERAADALRLpdwDAKIEHLSGGERRRVALCRLL 178
Cdd:PRK13538 86 KTELTALENLRFYQR---------LHGPGDDEALWEA---------LAQVGLAGFE---DVPVRQLSAGQQRRVALARLW 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1735515619 179 LEKPDMLLLDEPTNHLDAESVAWLERFL--H-DYEGTVVAITH 218
Cdd:PRK13538 145 LTRAPLWILDEPFTAIDKQGVARLEALLaqHaEQGGMVILTTH 187
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
19-190 |
5.40e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 80.46 E-value: 5.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDK---EFEGE--------ARPQPGIkiGYLPQEPKLepq 84
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGlvkPDSgriFLDGEdithlpmhKRARLGI--GYLPQEASI--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 85 qtvreaveeavsevksaltrldevyalyadpdadFDKLAAEQaNLEAIIQAHdGHNLDNQLERAADALRlpdwDAKIEH- 163
Cdd:COG1137 90 ----------------------------------FRKLTVED-NILAVLELR-KLSKKEREERLEELLE----EFGITHl 129
|
170 180 190
....*....|....*....|....*....|....
gi 1735515619 164 -------LSGGERRRVALCRLLLEKPDMLLLDEP 190
Cdd:COG1137 130 rkskaysLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
20-258 |
5.75e-17 |
|
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: 80.41 E-value: 5.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGEARPQPGI--------KIGYLPQEPKLEPQQ 85
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRpdsgeiLVDGQDITGLSEkelyelrrRIGMLFQGGALFDSL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 TVREAVeeavsevksALtRLDEVYALyadPDADFDKLAAEQanLEAIiqahdGhnldnqLERAADalRLPDwdakiEhLS 165
Cdd:COG1127 98 TVFENV---------AF-PLREHTDL---SEAEIRELVLEK--LELV-----G------LPGAAD--KMPS-----E-LS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD----YEGTVVAITHDRYFLDNVAGWILELDRGEgIPW 241
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHDLDSAFAIADRVAVLADGK-IIA 222
|
250
....*....|....*..
gi 1735515619 242 EGNYSSWLEQKEKRLEQ 258
Cdd:COG1127 223 EGTPEELLASDDPWVRQ 239
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-478 |
6.01e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.56 E-value: 6.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE----------ARPQPGIKIG-YL-PQEPKLEPQQTVRE 89
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTleiggnpcarLTPAKAHQLGiYLvPQEPLLFPNLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 90 AVeeavsevksaLTRLdevyalyADPDADFDKLAAEQANLeaiiqahdGHNLDnqLERAADALRLPDwdakiehlsggeR 169
Cdd:PRK15439 106 NI----------LFGL-------PKRQASMQKMKQLLAAL--------GCQLD--LDSSAGSLEVAD------------R 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 170 RRVALCRLLLEKPDMLLLDEPTNHLD-AESVAWLERF--LHDYEGTVVAITHDRYFLDNVAGWILELdRGEGIPWEGnys 246
Cdd:PRK15439 147 QIVEILRGLMRDSRILILDEPTASLTpAETERLFSRIreLLAQGVGIVFISHKLPEIRQLADRISVM-RDGTIALSG--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 247 swleqKEKRLEQEQAAENARQKSIAKELewvrqnpkgrqakskarmarfdelnsgeyqkrNETNELFIP-PGPR----LG 321
Cdd:PRK15439 223 -----KTADLSTDDIIQAITPAAREKSL--------------------------------SASQKLWLElPGNRrqqaAG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 322 DKVIEVQNLTKSyGDRtlidDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVlaSVDQFRDAMD- 400
Cdd:PRK15439 266 APVLTVEDLTGE-GFR----NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEI--NALSTAQRLAr 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 401 ----------------DKKTVWEEVSngqdiLTIGN---FEIPSR--AYVGRF----NFKGVDQQKRVGELSGGERGRLH 455
Cdd:PRK15439 339 glvylpedrqssglylDAPLAWNVCA-----LTHNRrgfWIKPARenAVLERYrralNIKFNHAEQAARTLSGGNQQKVL 413
|
490 500
....*....|....*....|...
gi 1735515619 456 LAKLLQRGGNVLLLDEPTNDLDV 478
Cdd:PRK15439 414 IAKCLEASPQLLIVDEPTRGVDV 436
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-218 |
6.04e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.53 E-value: 6.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR--------PQPGIKIGYLPQEPKLEPQQTVREav 91
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKldggdiddPDVAEACHYLGHRNAMKPALTVAE-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 92 eeavsevksaltrldevyalyadpdadfdklaaeqaNLEAIIQAHDGHNLDnqLERAADALRLPDwdakIEH-----LSG 166
Cdd:PRK13539 93 ------------------------------------NLEFWAAFLGGEELD--IAAALEAVGLAP----LAHlpfgyLSA 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY---EGTVVAITH 218
Cdd:PRK13539 131 GQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHlaqGGIVIAATH 185
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
324-490 |
6.70e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 81.67 E-value: 6.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSY-----------GDRTL----------IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSIT 382
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkgALKGLfrreyreveaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 383 mgetvVLaSVDQFRDAMDDKKTVweEVSNGQ------DILTIGNFE-------IPSRAY-------VGRFNFKG-VDQQK 441
Cdd:COG4586 81 -----VL-GYVPFKRRKEFARRI--GVVFGQrsqlwwDLPAIDSFRllkaiyrIPDAEYkkrldelVELLDLGElLDTPV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1735515619 442 RvgELSGGERGRLHL-AKLLQRgGNVLLLDEPTNDLDVETLRALENAILE 490
Cdd:COG4586 153 R--QLSLGQRMRCELaAALLHR-PKILFLDEPTIGLDVVSKEAIREFLKE 199
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
325-473 |
6.92e-17 |
|
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: 79.79 E-value: 6.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVV-LASVDQFRDAMddk 402
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdGRDITgLPPHERARAGI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 403 ktVWeeVSNGQDI---LTIG-NFEIPSRAYVGRFNFKGVDQ------------QKRVGELSGGERGRLHLAKLLQRGGNV 466
Cdd:cd03224 78 --GY--VPEGRRIfpeLTVEeNLLLGAYARRRAKRKARLERvyelfprlkerrKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
....*..
gi 1735515619 467 LLLDEPT 473
Cdd:cd03224 154 LLLDEPS 160
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
38-372 |
8.69e-17 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 83.14 E-value: 8.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPQPgikigylpQEP---KLEPQQTVreaVEEavsEVKSALTRLdevyaLYAD 114
Cdd:PRK10938 34 FVGANGSGKSALARALAGELPLLSGERQSQF--------SHItrlSFEQLQKL---VSD---EWQRNNTDM-----LSPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 115 PDaDFDKLAAEqanleaIIQahDGHNLDNQLERAADALRLPDW-DAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNH 193
Cdd:PRK10938 95 ED-DTGRTTAE------IIQ--DEVKDPARCEQLAQQFGITALlDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 194 LDAESVAWLERFLHDYEGTVVAIthdryfldnvagwILELDRGEGIPwegnysswleqkekrleqeqaaENARQKSIAKE 273
Cdd:PRK10938 166 LDVASRQQLAELLASLHQSGITL-------------VLVLNRFDEIP----------------------DFVQFAGVLAD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 274 LEWVRQNPKgRQAKSKARMAR--FDELNSG-------EYQKRNEtnelfIPPG-PRlgdkvIEVQNLTKSYGDRTLIDDL 343
Cdd:PRK10938 211 CTLAETGER-EEILQQALVAQlaHSEQLEGvqlpepdEPSARHA-----LPANePR-----IVLNNGVVSYNDRPILHNL 279
|
330 340
....*....|....*....|....*....
gi 1735515619 344 SFSIPKGAIVGIIGANGAGKSTLFRMLSG 372
Cdd:PRK10938 280 SWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
20-219 |
1.03e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.11 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE--------ARPQPGIKIGYlpQEPKLEPQQTVreav 91
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEllagtaplAEAREDTRLMF--QDARLLPWKKV---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 92 eeavsevksaltrLDEV-YALYADPdadfdKLAAEQAnLEAIIQAhdghnldnqlERAADalrlpdWDAKiehLSGGERR 170
Cdd:PRK11247 99 -------------IDNVgLGLKGQW-----RDAALQA-LAAVGLA----------DRANE------WPAA---LSGGQKQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 171 RVALCRLLLEKPDMLLLDEPTNHLDA----ESVAWLERFLHDYEGTVVAITHD 219
Cdd:PRK11247 141 RVALARALIHRPGLLLLDEPLGALDAltriEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-218 |
1.07e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 78.55 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG----------EARPQPGIKIGYLPQEPKLEPQQTVRE 89
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGevrwngtplaEQRDEPHENILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 90 aveeavsevksaltrldevyalyadpdadfdklaaeqaNLEAIIQAHDGHnlDNQLERAADALRLPDW-DAKIEHLSGGE 168
Cdd:TIGR01189 93 --------------------------------------NLHFWAAIHGGA--QRTIEDALAAVGLTGFeDLPAAQLSAGQ 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY---EGTVVAITH 218
Cdd:TIGR01189 133 QRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
324-500 |
1.07e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.69 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRDAM---- 399
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlylg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 400 -----DDKKTVWEEVS-NGQDILTIGNFEIpsRAYVGRFNFKGVDQQKrVGELSGGERGRLHLAKLLQRGGNVLLLDEPT 473
Cdd:PRK13538 81 hqpgiKTELTALENLRfYQRLHGPGDDEAL--WEALAQVGLAGFEDVP-VRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|
gi 1735515619 474 NDLD---VETLRALENAILEFPGCAMVISH 500
Cdd:PRK13538 158 TAIDkqgVARLEALLAQHAEQGGMVILTTH 187
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
21-219 |
1.11e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 79.41 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 21 HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE--------------ARPqpgIKIgyLPQEPKLEPQQT 86
Cdd:COG3840 13 DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRilwngqdltalppaERP---VSM--LFQENNLFPHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 87 VREAVeeavsevksaltrldevyALYADPDAdfdKLAAEQAnlEAIIQAHDGHNLDNQLERaadalrLPdwdakiEHLSG 166
Cdd:COG3840 88 VAQNI------------------GLGLRPGL---KLTAEQR--AQVEQALERVGLAGLLDR------LP------GQLSG 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 167 GERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHD 219
Cdd:COG3840 133 GQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD 189
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
17-218 |
1.15e-16 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 78.95 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 17 PPKRHI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkefegearpqpgikigylpqepkLEPQQTVREaVE-- 92
Cdd:cd03266 13 DVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL------------------------LEPDAGFAT-VDgf 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 93 EAVSEVKSALTRLdevyALYADPDADFDKLAAeQANLEAIIQAH--DGHNLDNQLERAADALRLPDW-DAKIEHLSGGER 169
Cdd:cd03266 68 DVVKEPAEARRRL----GFVSDSTGLYDRLTA-RENLEYFAGLYglKGDELTARLEELADRLGMEELlDRRVGGFSTGMR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1735515619 170 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITH 218
Cdd:cd03266 143 QKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLraLGkCILFSTH 194
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
21-237 |
1.19e-16 |
|
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: 79.40 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 21 HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGE--------ARPQPGikIGYLPQEPKLEPQQT 86
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRptsgsvLFDGEditglpphEIARLG--IGRTFQIPRLFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 87 VREAVEEAVsevksaltRLDEVYALYADPDADFDKLAAEQAnleaiiqahdghnldnqlERAADALRLPD-WDAKIEHLS 165
Cdd:cd03219 92 VLENVMVAA--------QARTGSGLLLARARREEREARERA------------------EELLERVGLADlADRPAGELS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 166 GGERRRVALCRLLLEKPDMLLLDEPT---NHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGE 237
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
19-220 |
1.41e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 81.28 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE------------ARPQpgiKIGYLPQEPKLEPQQT 86
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHirfhgtdvsrlhARDR---KVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 87 VREAVEEAVSevksALTRLDEvyalyadPDADFDKLAAEQAnLEAIiqahdghnldnQLERAADalRLPdwdakiEHLSG 166
Cdd:PRK10851 91 VFDNIAFGLT----VLPRRER-------PNAAAIKAKVTQL-LEMV-----------QLAHLAD--RYP------AQLSG 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDA----ESVAWLeRFLH-DYEGTVVAITHDR 220
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWL-RQLHeELKFTSVFVTHDQ 197
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
21-191 |
1.70e-16 |
|
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: 78.87 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 21 HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGE--------ARPQPGikIGYLPQEPKLEPQQT 86
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPprsgsiRFDGEditglpphRIARLG--IGYVPEGRRIFPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 87 VRE---AVEEAVSEVKSALTRLDEVYALyadpdadFDKLAaeqanleaiiqahdghnldnqlERaadalrlpdWDAKIEH 163
Cdd:COG0410 95 VEEnllLGAYARRDRAEVRADLERVYEL-------FPRLK----------------------ER---------RRQRAGT 136
|
170 180
....*....|....*....|....*...
gi 1735515619 164 LSGGERRRVALCRLLLEKPDMLLLDEPT 191
Cdd:COG0410 137 LSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
332-501 |
2.12e-16 |
|
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: 78.11 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 332 KSYGDRTLidDLSFSIPkGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRDAMDDKK-------- 403
Cdd:cd03297 8 KRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKiglvfqqy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 404 ------TVWEEVSNGQDILTIGNFEIPSRAYVGRFNFKGVdQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLD 477
Cdd:cd03297 85 alfphlNVRENLAFGLKRKRNREDRISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180
....*....|....*....|....*...
gi 1735515619 478 VET---LRALENAIL-EFPGCAMVISHD 501
Cdd:cd03297 164 RALrlqLLPELKQIKkNLNIPVIFVTHD 191
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
250-539 |
2.59e-16 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 82.22 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 250 EQKEKRLEQEQAAENARQKSIAKELEWVRQNPKGRQAKSKARMARFDELNSGE---YQKRNETNElfippGPRLGDkvIE 326
Cdd:PLN03073 107 SEVAKKKPEPDDGPLLSERDLAKIERRKRKEERQREVQYQAHVAEMEAAKAGMpgvYVNHDGNGG-----GPAIKD--IH 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 327 VQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQ--------------EQPDAGSITMGETVVLAS- 391
Cdd:PLN03073 180 MENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHaidgipkncqilhvEQEVVGDDTTALQCVLNTd 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 392 ------VDQFRDAMDDKKTVWEEVSNGQD-----------------------ILTIGNFEIPSRA--YVGRFNFKGVDQQ 440
Cdd:PLN03073 260 iertqlLEEEAQLVAQQRELEFETETGKGkgankdgvdkdavsqrleeiykrLELIDAYTAEARAasILAGLSFTPEMQV 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 441 KRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFPGCAMVISHDRWFLDRIATHILDYGDEgK 520
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQ-K 418
|
330
....*....|....*....
gi 1735515619 521 VTFYEGNFSDYEEWKKKTL 539
Cdd:PLN03073 419 LVTYKGDYDTFERTREEQL 437
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
326-489 |
2.82e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.50 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 326 EVQNLTKSY-GDRTLiDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVdqfRDAMDD-- 401
Cdd:PRK11288 6 SFDGIGKTFpGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdGQEMRFAST---TAALAAgv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 402 -----------KKTVWEEVSNGQdiltignfeIPSRA---------YVGRFNFKG----VDQQKRVGELSGGERGRLHLA 457
Cdd:PRK11288 82 aiiyqelhlvpEMTVAENLYLGQ---------LPHKGgivnrrllnYEAREQLEHlgvdIDPDTPLKYLSIGQRQMVEIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1735515619 458 KLLQRGGNVLLLDEPTNDLD----------VETLRALENAIL 489
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSareieqlfrvIRELRAEGRVIL 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
4-237 |
2.83e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 78.08 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 4 QFVYTMHRVGKVVP---PKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE---------FEGEARPQPGIK 71
Cdd:cd03234 1 QRVLPWWDVGLKAKnwnKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggttsgqilFNGQPRKPDQFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 72 --IGYLPQEPKLEPQQTVREAVEEAVsevKSALTRLDevyalyadPDADFDKLAaEQANLEAIIQAHDGHNLdnqleraa 149
Cdd:cd03234 81 kcVAYVRQDDILLPGLTVRETLTYTA---ILRLPRKS--------SDAIRKKRV-EDVLLRDLALTRIGGNL-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 150 dalrlpdwdakIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAIT-H----DRY- 221
Cdd:cd03234 141 -----------VKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLarRNRIVILTiHqprsDLFr 209
|
250
....*....|....*.
gi 1735515619 222 FLDNvagwILELDRGE 237
Cdd:cd03234 210 LFDR----ILLLSSGE 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
318-477 |
3.13e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 80.38 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 318 PRLGDKVIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQfR 396
Cdd:PRK09452 8 PSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLdGQDITHVPAEN-R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 397 D--------AMDDKKTVWEEVSNGQDILTIGNFEIPSR-----AYVGRFNFKgvdqQKRVGELSGGERGRLHLAKLLQRG 463
Cdd:PRK09452 87 HvntvfqsyALFPHMTVFENVAFGLRMQKTPAAEITPRvmealRMVQLEEFA----QRKPHQLSGGQQQRVAIARAVVNK 162
|
170
....*....|....
gi 1735515619 464 GNVLLLDEPTNDLD 477
Cdd:PRK09452 163 PKVLLLDESLSALD 176
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
23-219 |
3.93e-16 |
|
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: 77.76 E-value: 3.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR-------PQPGIK--IGYLPQEPKLEPQQTVREAVEe 93
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkditNLPPEKrdISYVPQNYALFPHMTVYKNIA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 94 avsevksaltrldevYALyadpdadfDKLAAEQANLEA-IIQAHDGHNLDNQLERaadalrlpdwdaKIEHLSGGERRRV 172
Cdd:cd03299 94 ---------------YGL--------KKRKVDKKEIERkVLEIAEMLGIDHLLNR------------KPETLSGGEQQRV 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1735515619 173 ALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHD-YEGTVVAITHD 219
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVrtkEKLREELKKIRKeFGVTVLHVTHD 189
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
325-516 |
4.48e-16 |
|
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: 76.80 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPdagSITMGETVVlasvdqfrdamddkkt 404
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKY---EVTEGEILF---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 405 vweevsNGQDILtigNFEIPSRAYVGRF-------NFKGV---DQQKRVGE-LSGGERGRLHLAKLLQRGGNVLLLDEPT 473
Cdd:cd03217 62 ------KGEDIT---DLPPEERARLGIFlafqyppEIPGVknaDFLRYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1735515619 474 NDLDVETLRALENAILEF--PGCAM-VISHDRWFLDRIAT---HILDYG 516
Cdd:cd03217 133 SGLDIDALRLVAEVINKLreEGKSVlIITHYQRLLDYIKPdrvHVLYDG 181
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
324-490 |
4.89e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 79.46 E-value: 4.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSY--GDRTLI--DDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQFRDA 398
Cdd:PRK11153 1 MIELKNISKVFpqGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVdGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 399 MDD------------KKTVWEEVSNGQDILTIGNFEIPSR-----AYVGRfnfkgVDQQKRV-GELSGGERGRLHLAKLL 460
Cdd:PRK11153 81 RRQigmifqhfnllsSRTVFDNVALPLELAGTPKAEIKARvtellELVGL-----SDKADRYpAQLSGGQKQRVAIARAL 155
|
170 180 190
....*....|....*....|....*....|
gi 1735515619 461 QRGGNVLLLDEPTNDLDVETLRalenAILE 490
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTR----SILE 181
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-229 |
5.07e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 78.24 E-value: 5.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 21 HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkefegearpqpgikigYLPQEPKLepqqTV--REAVEEAVSEV 98
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGI-----------------YLPQRGRV----KVmgREVNAENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 99 KSaltrldEVYALYADPDAD-FDKLAAEQANLEAIIQAHDGHNLDNQLERAADALRLPDWDAKIE-HLSGGERRRVALCR 176
Cdd:PRK13647 78 RS------KVGLVFQDPDDQvFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPyHLSYGQKKRVAIAG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 177 LLLEKPDMLLLDEPTNHLD----AESVAWLERfLHDYEGTVVAITHDryfLDNVAGW 229
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDprgqETLMEILDR-LHNQGKTVIVATHD---VDLAAEW 204
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-232 |
5.73e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 78.19 E-value: 5.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 18 PKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQpGIKIGYLPQEPK----------------- 80
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR-GEPLAKLNRAQRkafrrdiqmvfqdsisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 81 LEPQQTVREAVEEAVSEvksaLTRLDEvyalyadpdadfdklAAEQANLEAIIQAHDghnLDnqlerAADALRLPdwdak 160
Cdd:PRK10419 102 VNPRKTVREIIREPLRH----LLSLDK---------------AERLARASEMLRAVD---LD-----DSVLDKRP----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 161 iEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHD----RYFLDNVA----G 228
Cdd:PRK10419 150 -PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlqAGVIRLLKKLQQQFGTACLFITHDlrlvERFCQRVMvmdnG 228
|
....
gi 1735515619 229 WILE 232
Cdd:PRK10419 229 QIVE 232
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
21-240 |
5.86e-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: 77.77 E-value: 5.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 21 HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGE--------ARPQPGIKIGYlpQEPKLEPQQT 86
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRptsgriLFDGRditglpphRIARLGIARTF--QNPRLFPELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 87 VREAVEEAV-----SEVKSALTRLDevyaLYADPDADFDKLAAEQanLEAIiqahdghNLDNQLERAADAlrlpdwdaki 161
Cdd:COG0411 96 VLENVLVAAharlgRGLLAALLRLP----RARREEREARERAEEL--LERV-------GLADRADEPAGN---------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 162 ehLSGGERRRVALCRLLLEKPDMLLLDEPT---NHLDAESVAWLERFLHDYEG-TVVAITHDRYFLDNVAGWILELDRG- 236
Cdd:COG0411 153 --LSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVVLDFGr 230
|
....*..
gi 1735515619 237 ---EGIP 240
Cdd:COG0411 231 viaEGTP 237
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-478 |
6.78e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.43 E-value: 6.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGEARPQPGIK------IGYLPQEPKLEPQQTVREA 90
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTrdagsiLYLGKEVTFNGPKssqeagIGIIHQELNLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 91 VEEAvSEVKSALTRLD--EVYAlyadpdaDFDKLAAeQANLEaiiqaHDGHNLDNQLeraadalrlpdwdakiehlSGGE 168
Cdd:PRK10762 100 IFLG-REFVNRFGRIDwkKMYA-------EADKLLA-RLNLR-----FSSDKLVGEL-------------------SIGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 169 RRRVALCRLLLEKPDMLLLDEPTNHL-DAESVAWLE--RFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIPwegny 245
Cdd:PRK10762 147 QQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFRviRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIA----- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 246 sswlEQKEKRLEQEQAAENArqksiakelewvrqnpKGRqakskarmaRFDElnsgEYqkrnetnelfippgPRL----G 321
Cdd:PRK10762 222 ----EREVADLTEDSLIEMM----------------VGR---------KLED----QY--------------PRLdkapG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 322 DKVIEVQNLTKSyGdrtlIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVV-------LA--- 390
Cdd:PRK10762 255 EVRLKVDNLSGP-G----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdGHEVVtrspqdgLAngi 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 391 ---SVDQFRD---------------AMDDKKTVWEEVSNGQDILTIGNFeipsrayVGRFNFKGVDQQKRVGELSGGERG 452
Cdd:PRK10762 330 vyiSEDRKRDglvlgmsvkenmsltALRYFSRAGGSLKHADEQQAVSDF-------IRLFNIKTPSMEQAIGLLSGGNQQ 402
|
490 500
....*....|....*....|....*.
gi 1735515619 453 RLHLAKLLQRGGNVLLLDEPTNDLDV 478
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVDV 428
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
19-190 |
6.80e-16 |
|
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: 77.31 E-value: 6.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE--------------ARPQPGIkiGYLPQEPKLEPQ 84
Cdd:TIGR04406 13 KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKilidgqdithlpmhERARLGI--GYLPQEASIFRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 85 QTVREAVeEAVSEVKSALTRldevyalyadpdadfdklAAEQANLEAIIQahdghnlDNQLERAADALRLpdwdakieHL 164
Cdd:TIGR04406 91 LTVEENI-MAVLEIRKDLDR------------------AEREERLEALLE-------EFQISHLRDNKAM--------SL 136
|
170 180
....*....|....*....|....*.
gi 1735515619 165 SGGERRRVALCRLLLEKPDMLLLDEP 190
Cdd:TIGR04406 137 SGGERRRVEIARALATNPKFILLDEP 162
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
231-292 |
6.93e-16 |
|
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: 72.61 E-value: 6.93e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 231 LELDRGEGIPWEGNYSSWLEQKEKRLEQEQAAENARQKSIAKELEWVRQNP----KGRQAKSKARM 292
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRakasKAKQAQSRIKA 66
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-219 |
8.00e-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: 8.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAgvdkefeGEARPQPGiKIGYLPQE-PKLEPQQ--TVReaveeAV 95
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLT-------GELTPSSG-EVRLNGRPlAAWSPWElaRRR-----AV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 96 SEVKSALT---RLDEVYALYADPdadfdkLAAEQANLEAIIQAhdghnldnQLERaADALRLpdWDAKIEHLSGGERRRV 172
Cdd:COG4559 80 LPQHSSLAfpfTVEEVVALGRAP------HGSSAAQDRQIVRE--------ALAL-VGLAHL--AGRSYQTLSGGEQQRV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 173 ALCRLLL-------EKPDMLLLDEPTNHLD-AESVAWLE--RFLHDYEGTVVAITHD 219
Cdd:COG4559 143 QLARVLAqlwepvdGGPRWLFLDEPTSALDlAHQHAVLRlaRQLARRGGGVVAVLHD 199
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
321-501 |
9.99e-16 |
|
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: 75.16 E-value: 9.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 321 GDKVIEVQNLTKSYGdrtlIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQFRDA- 398
Cdd:cd03215 1 GEPVLEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdGKPVTRRSPRDAIRAg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 399 ----MDDKK--------TVWEevsngqdiltigNFEIPSRayvgrfnfkgvdqqkrvgeLSGGERGRLHLAKLLQRGGNV 466
Cdd:cd03215 77 iayvPEDRKreglvldlSVAE------------NIALSSL-------------------LSGGNQQKVVLARWLARDPRV 125
|
170 180 190
....*....|....*....|....*....|....*...
gi 1735515619 467 LLLDEPTNDLDVETLRALENAILEF--PGCA-MVISHD 501
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELadAGKAvLLISSE 163
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
23-242 |
1.04e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 76.25 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA--------RPQPGIK--IGYLPQEPKLEPQQTVREAVE 92
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAtvaghdvvREPREVRrrIGIVFQDLSVDDELTGWENLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 93 eavsevksaltrldevyalyadpdadfdklaaeqanLEAIIQAHDGHNLDNQLERAADALRLpdWDAK---IEHLSGGER 169
Cdd:cd03265 96 ------------------------------------IHARLYGVPGAERRERIDELLDFVGL--LEAAdrlVKTYSGGMR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 170 RRVALCRLLLEKPDMLLLDEPTNHLDAESVA--W--LERFLHDYEGTVVAITHDRYFLDNVAGWILELDRG----EGIPW 241
Cdd:cd03265 138 RRLEIARSLVHRPEVLFLDEPTIGLDPQTRAhvWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGriiaEGTPE 217
|
.
gi 1735515619 242 E 242
Cdd:cd03265 218 E 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
322-501 |
1.26e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.08 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 322 DKVIEVQNLTKSYGDRT-LIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQ------ 394
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvrskv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 395 ---FRDAmDDK---KTVWEEVSNGQDILTIGNFEIPSRA-----YVGRFNFKgvdqQKRVGELSGGERGRLHLAKLLQRG 463
Cdd:PRK13647 82 glvFQDP-DDQvfsSTVWDDVAFGPVNMGLDKDEVERRVeealkAVRMWDFR----DKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1735515619 464 GNVLLLDEPTNDLD---VETLRALENAILEFPGCAMVISHD 501
Cdd:PRK13647 157 PDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
325-388 |
1.32e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 76.03 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSY----------------------GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSIT 382
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
....*.
gi 1735515619 383 MGETVV 388
Cdd:cd03220 81 VRGRVS 86
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
325-523 |
1.32e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.05 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYG-----DRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVlasvdqfrdam 399
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 400 ddkkTVWEEVSNGQDI--------------LTIG-NFEIpsrAY--VGRFNFK-GVDQQKR------------------- 442
Cdd:COG1101 71 ----TKLPEYKRAKYIgrvfqdpmmgtapsMTIEeNLAL---AYrrGKRRGLRrGLTKKRRelfrellatlglglenrld 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 443 --VGELSGGERGRLHL--AKLLQrgGNVLLLDEPTNDLDVET----LRALENAILEFPGCAMVISHDrwfldriATHILD 514
Cdd:COG1101 144 tkVGLLSGGQRQALSLlmATLTK--PKLLLLDEHTAALDPKTaalvLELTEKIVEENNLTTLMVTHN-------MEQALD 214
|
250
....*....|....*
gi 1735515619 515 YG------DEGKVTF 523
Cdd:COG1101 215 YGnrlimmHEGRIIL 229
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
325-524 |
1.36e-15 |
|
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: 79.79 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSY--GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGetvvLASVDQfrdamddk 402
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLD----GADLSQ-------- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 403 ktvWEEVSNG-------QDI-L---TIGnfEIPSRayvgrfnFKGVDQQK-----------------------RVGE--- 445
Cdd:COG4618 399 ---WDREELGrhigylpQDVeLfdgTIA--ENIAR-------FGDADPEKvvaaaklagvhemilrlpdgydtRIGEgga 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 446 -LSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEF---PGCAMVISHDRWFL---DRIAthILdygDE 518
Cdd:COG4618 467 rLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkarGATVVVITHRPSLLaavDKLL--VL---RD 541
|
....*.
gi 1735515619 519 GKVTFY 524
Cdd:COG4618 542 GRVQAF 547
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-219 |
1.55e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 76.22 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARpqpgiKIGYLP--QEPKLEPQQTVREAVEEAVSEVKS 100
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR-----VAGLVPwkRRKKFLRRIGVVFGQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 101 ALTRLDEVYALYADPDADFDKlaaeqanleaiiqahdghnldnQLERAADALRL-PDWDAKIEHLSGGERRRVALCRLLL 179
Cdd:cd03267 112 VIDSFYLLAAIYDLPPARFKK----------------------RLDELSELLDLeELLDTPVRQLSLGQRMRAEIAAALL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1735515619 180 EKPDMLLLDEPTNHLDAESVAWLERFLHDY----EGTVVAITHD 219
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHY 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
324-473 |
1.78e-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: 75.79 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSIT-MGETVVLASVDQ-------- 394
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfDGEDITGLPPHRiarlgigy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 395 -------FRDaMddkkTVWEevsNgqdiLTIGnfeipsrAYVGRFNFKGVDQQKRV---------------GELSGGERG 452
Cdd:COG0410 83 vpegrriFPS-L----TVEE---N----LLLG-------AYARRDRAEVRADLERVyelfprlkerrrqraGTLSGGEQQ 143
|
170 180
....*....|....*....|.
gi 1735515619 453 RLHLAKLLQRGGNVLLLDEPT 473
Cdd:COG0410 144 MLAIGRALMSRPKLLLLDEPS 164
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
18-219 |
1.95e-15 |
|
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: 75.37 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 18 PKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpqpgIKIGylpqepklepqqtvreavEEAVSE 97
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGR------IYIG------------------GRDVTD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 98 VKSALTRLDEV---YALYADPDAdFDKLAAeqaNLEAIIQAHDghNLDNQLERAADALRLPDW-DAKIEHLSGGERRRVA 173
Cdd:cd03301 67 LPPKDRDIAMVfqnYALYPHMTV-YDNIAF---GLKLRKVPKD--EIDERVREVAELLQIEHLlDRKPKQLSGGQRQRVA 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1735515619 174 LCRLLLEKPDMLLLDEPTNHLDA----ESVAWLERFLHDYEGTVVAITHD 219
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAklrvQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-218 |
1.98e-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: 74.00 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 21 HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpqpgIKIGylpqepklepqqtvreavEEAVSevks 100
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGE------ILVD------------------GKEVS---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 101 altrldevyalYADPDadfdklAAEQANLEAIIQahdghnldnqleraadalrlpdwdakiehLSGGERRRVALCRLLLE 180
Cdd:cd03216 66 -----------FASPR------DARRAGIAMVYQ-----------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1735515619 181 KPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITH 218
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRLraQGvAVIFISH 140
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
325-500 |
2.40e-15 |
|
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: 78.99 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYG--DRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMG----ETVVLAS------- 391
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDghdlADYTLASlrrqval 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 392 VDQFRDAMDDkkTVWEEVSNGqDILTIGNFEIPS---RAYVGRF---NFKGVDQQkrVGE----LSGGERGRLHLAKLLQ 461
Cdd:TIGR02203 411 VSQDVVLFND--TIANNIAYG-RTEQADRAEIERalaAAYAQDFvdkLPLGLDTP--IGEngvlLSGGQRQRLAIARALL 485
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1735515619 462 RGGNVLLLDEPTNDLDVETLRALENAILEF-PG-CAMVISH 500
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLmQGrTTLVIAH 526
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
32-219 |
2.45e-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: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 32 PGAKI-GVLGLNGAGKSTLLRIMAGVDKEFEGE--------ARPQPGI-------KIGYLPQEPKLEPQQTVREAVEEAV 95
Cdd:TIGR02142 21 PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEivlngrtlFDSRKGIflppekrRIGYVFQEARLFPHLSVRGNLRYGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 96 SEVKSALTRldevyalyadpdadfdklaaeqANLEAIIQAHdghNLDNQLERaadalrLPDwdakieHLSGGERRRVALC 175
Cdd:TIGR02142 101 KRARPSERR----------------------ISFERVIELL---GIGHLLGR------LPG------RLSGGEKQRVAIG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1735515619 176 RLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHD 219
Cdd:TIGR02142 144 RALLSSPRLLLMDEPLAALDdprkYEILPYLERLHAEFGIPILYVSHS 191
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
15-218 |
2.61e-15 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 73.79 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 15 VVPP--KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR-----------PQPGIKIGYLPQEPKL 81
Cdd:cd03246 8 FRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRldgadisqwdpNELGDHVGYLPQDDEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 82 EPQqTVREAVeeavsevksaltrldevyalyadpdadfdklaaeqanleaiiqahdghnldnqleraadalrlpdwdaki 161
Cdd:cd03246 88 FSG-SIAENI---------------------------------------------------------------------- 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 162 ehLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD---YEGTVVAITH 218
Cdd:cd03246 97 --LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAlkaAGATRIVIAH 154
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-218 |
2.69e-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: 74.84 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQPGikigylpqepklePQQTVREAVEEAV---- 95
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-------------PLDFQRDSIARGLlylg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 96 --SEVKSALTRLDEVYALYADPDAdfdklaaeqanlEAIIQAHDGHNLdNQLEraadalrlpdwDAKIEHLSGGERRRVA 173
Cdd:cd03231 80 haPGIKTTLSVLENLRFWHADHSD------------EQVEEALARVGL-NGFE-----------DRPVAQLSAGQQRRVA 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1735515619 174 LCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY---EGTVVAITH 218
Cdd:cd03231 136 LARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHcarGGMVVLTTH 183
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-219 |
2.74e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 75.65 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdKEFEGEA----RPQPGIKI-------GYLPQepklepQQTVREAV 91
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEIllngRPLSDWSAaelarhrAYLSQ------QQSPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 92 eeavsevksaltrldEVY---ALYADPdadfdklaaeQANLEAIIQAhdghnldnqLERAADALRLPDWDAK-IEHLSGG 167
Cdd:COG4138 85 ---------------PVFqylALHQPA----------GASSEAVEQL---------LAQLAEALGLEDKLSRpLTQLSGG 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 168 ERRRVALCRLLLE-----KPD--MLLLDEPTNHLD-AESVA---WLERFlHDYEGTVVAITHD 219
Cdd:COG4138 131 EWQRVRLAAVLLQvwptiNPEgqLLLLDEPMNSLDvAQQAAldrLLREL-CQQGITVVMSSHD 192
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
325-490 |
2.87e-15 |
|
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: 75.34 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSY-GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGET---------------VV 388
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslrsmigVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 389 LASVDQFRDamddkkTVWEEVSNGQDILTIGNFEIPSRAyVGRFNF-----KGVDQQkrVGE----LSGGERGRLHLAKL 459
Cdd:cd03254 83 LQDTFLFSG------TIMENIRLGRPNATDEEVIEAAKE-AGAHDFimklpNGYDTV--LGEnggnLSQGERQLLAIARA 153
|
170 180 190
....*....|....*....|....*....|.
gi 1735515619 460 LQRGGNVLLLDEPTNDLDVETLRALENAILE 490
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEK 184
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-198 |
3.25e-15 |
|
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: 74.85 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA----------RPQPGIKIGYLPQEPKLEPQQTVRE 89
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingysirtdRKAARQSLGYCPQFDALFDELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 90 AVEeavsevksaltrldevyaLYadpdadfdklaaeqanleAIIQAHDGHNLDNQLERAADALRLPD-WDAKIEHLSGGE 168
Cdd:cd03263 95 HLR------------------FY------------------ARLKGLPKSEIKEEVELLLRVLGLTDkANKRARTLSGGM 138
|
170 180 190
....*....|....*....|....*....|
gi 1735515619 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
Cdd:cd03263 139 KRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-218 |
3.58e-15 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 74.93 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 8 TMHRVGKVVPPKR---HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE--------------ARPQPGI 70
Cdd:cd03258 3 ELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSvlvdgtdltllsgkELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 71 KIGYLPQEPKLEPQQTVREAVEeavsevksaltrldevYALyadpdadfdKLAaeqanleaiiqahdGHNLDNQLERAAD 150
Cdd:cd03258 83 RIGMIFQHFNLLSSRTVFENVA----------------LPL---------EIA--------------GVPKAEIEERVLE 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 151 ALRLPDW----DAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDYEG-TVVAITH 218
Cdd:cd03258 124 LLELVGLedkaDAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPEttqSILALLRDINRELGlTIVLITH 199
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
19-221 |
3.64e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.44 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE------------ARpQPGIKIGYLPQEPkLEPQQ- 85
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTvflgdkpismlsSR-QLARRLALLPQHH-LTPEGi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 TVREAVEEAVSEVKSALTRLdevyalyadpdADFDKLAAEQAnLEaiiqahdghnlDNQLERAADAlrlpdwdaKIEHLS 165
Cdd:PRK11231 92 TVRELVAYGRSPWLSLWGRL-----------SAEDNARVNQA-ME-----------QTRINHLADR--------RLTDLS 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAwLERFLHDYEGTVVAITHD-----RY 221
Cdd:PRK11231 141 GGQRQRAFLAMVLAQDTPVVLLDEPTTYLDinhqVELMR-LMRELNTQGKTVVTVLHDlnqasRY 204
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
325-530 |
4.23e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 78.08 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSY-GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GE---TVVLASVDQ----- 394
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTdirTVTRASLRRniavv 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 395 FRDAMDDKKTVWEEVSNGQDILTigNFEI---PSRAYVGRF---NFKGVDqqKRVGE----LSGGERGRLHLAKLLQRGG 464
Cdd:PRK13657 415 FQDAGLFNRSIEDNIRVGRPDAT--DEEMraaAERAQAHDFierKPDGYD--TVVGErgrqLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1735515619 465 NVLLLDEPTNDLDVETLRALENAIlefpGCAM------VISHdRWFLDRIATHILDYgDEGKVTfYEGNFSD 530
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAAL----DELMkgrttfIIAH-RLSTVRNADRILVF-DNGRVV-ESGSFDE 555
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
22-220 |
4.45e-15 |
|
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: 74.31 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpqpgikIGYLPQEPKlepqqtvreaveeAVSEVKSA 101
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGE--------VLFNGQSLS-------------KLSSNERA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 102 LTRLDEVYALYadpdaDFDKLAAEQANLE--AIIQAHDGHNLDNQLERAADALRLPDWDAKIEH----LSGGERRRVALC 175
Cdd:TIGR02211 79 KLRNKKLGFIY-----QFHHLLPDFTALEnvAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHrpseLSGGERQRVAIA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1735515619 176 RLLLEKPDMLLLDEPTNHLD---AESVAWLERFLHDYEGT-VVAITHDR 220
Cdd:TIGR02211 154 RALVNQPSLVLADEPTGNLDnnnAKIIFDLMLELNRELNTsFLVVTHDL 202
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
325-499 |
4.57e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.69 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGD-RTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRDAM--DD 401
Cdd:PRK15056 7 IVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYvpQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 402 KKTVWEEVSNGQDILTIGNF------EIPSR----------AYVGRFNFKgvdqQKRVGELSGGERGRLHLAKLLQRGGN 465
Cdd:PRK15056 87 EEVDWSFPVLVEDVVMMGRYghmgwlRRAKKrdrqivtaalARVDMVEFR----HRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1735515619 466 VLLLDEPTNDLDVET-------LRALENAilefpGCAMVIS 499
Cdd:PRK15056 163 VILLDEPFTGVDVKTeariislLRELRDE-----GKTMLVS 198
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
327-501 |
4.66e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 75.35 E-value: 4.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 327 VQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM----GETVVLASVD--QFRDAMd 400
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdGQLRDLYALSeaERRRLL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 401 dkKTVW------------EEVSNGQDI----LTIGNfeipsRAYvGRFNFKGVDQQKRV-----------GELSGGERGR 453
Cdd:PRK11701 88 --RTEWgfvhqhprdglrMQVSAGGNIgerlMAVGA-----RHY-GDIRATAGDWLERVeidaariddlpTTFSGGMQQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 454 LHLAKLLQRGGNVLLLDEPTNDLDV-------ETLRALENAIlefpGCAMVI-SHD 501
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVsvqarllDLLRGLVREL----GLAVVIvTHD 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
325-516 |
5.69e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 77.56 E-value: 5.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTL--IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGE---------------TV 387
Cdd:PRK11160 339 LTLNNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqaiSV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 388 VLASVDQF----RD--------AMDDK-KTVWEEVsnGQDILTIGNfeipsrayvgrfnfKGVDQQkrVGE----LSGGE 450
Cdd:PRK11160 419 VSQRVHLFsatlRDnlllaapnASDEAlIEVLQQV--GLEKLLEDD--------------KGLNAW--LGEggrqLSGGE 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 451 RGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFpgCA----MVISHDRWFL---DRIatHILDYG 516
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH--AQnktvLMITHRLTGLeqfDRI--CVMDNG 549
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
320-513 |
7.44e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.62 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 320 LGDKVIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQFRDA 398
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVnGQTINLVRDKDGQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 399 MDDKK----------------------TVWEEVSNGQ-DILTIGNFEIPSRA--YVGRFNFKGVDQQKRVGELSGGERGR 453
Cdd:PRK10619 81 VADKNqlrllrtrltmvfqhfnlwshmTVLENVMEAPiQVLGLSKQEARERAvkYLAKVGIDERAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 454 LHLAKLLQRGGNVLLLDEPTNDLDV----ETLRALENAILEfpGCAM-VISHDRWFLDRIATHIL 513
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPelvgEVLRIMQQLAEE--GKTMvVVTHEMGFARHVSSHVI 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
320-501 |
8.89e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 74.67 E-value: 8.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 320 LGDKVIEVQNLTKSYGD--RTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMG------ETV---- 387
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlseETVwdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 388 -----VLASVD-QFRDAmddkkTVWEEVSNGqdiltIGNFEIPSRAYVGRfnfkgVDQQ-KRVG----------ELSGGE 450
Cdd:PRK13635 81 rqvgmVFQNPDnQFVGA-----TVQDDVAFG-----LENIGVPREEMVER-----VDQAlRQVGmedflnrephRLSGGQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 451 RGRLHLAKLLQRGGNVLLLDEPTNDLD-------VETLRALENAilefpGCAMVIS--HD 501
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDprgrrevLETVRQLKEQ-----KGITVLSitHD 200
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
10-219 |
1.10e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 75.49 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 10 HRVGKVvppkrHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpqpgIKIG---------------Y 74
Cdd:COG3839 11 KSYGGV-----EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGE------ILIGgrdvtdlppkdrniaM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 75 LPQEPKLEPQQTVREAVEeavsevksaltrldevYALyadpdadfdKLA----AEQanleaiiqahdghnlDNQLERAAD 150
Cdd:COG3839 80 VFQSYALYPHMTVYENIA----------------FPL---------KLRkvpkAEI---------------DRRVREAAE 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1735515619 151 ALRLPDW-DAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA--------EsvawLERFLHDYEGTVVAITHD 219
Cdd:COG3839 120 LLGLEDLlDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAklrvemraE----IKRLHRRLGTTTIYVTHD 193
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-219 |
1.18e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.05 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 18 PKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA--RPQP---------GIKIGYLPQEPKLEPQQT 86
Cdd:PRK10575 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIllDAQPleswsskafARKVAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 87 VREAVEEAVSEVKSALTRLDevyalyadpdadfdklAAEQANLEAIIQAHDGHNLDNQLeraadalrlpdwdakIEHLSG 166
Cdd:PRK10575 102 VRELVAIGRYPWHGALGRFG----------------AADREKVEEAISLVGLKPLAHRL---------------VDSLSG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 167 GERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHD 219
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLALVHRLSQERGLTVIAVLHD 207
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
324-492 |
1.21e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.45 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSY-GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQFRDAM-- 399
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIREVRKFVgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 400 -----DDK---KTVWEEVSNGQDILTIGNFEIPSRAYVGRFNFKGVDQQKRV-GELSGGERGRLHLAKLLQRGGNVLLLD 470
Cdd:PRK13652 83 vfqnpDDQifsPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVpHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180
....*....|....*....|..
gi 1735515619 471 EPTNDLDVETLRALENAILEFP 492
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLP 184
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
325-477 |
1.22e-14 |
|
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: 72.91 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLidDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRDAmddkKT 404
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPV----SM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 405 VWEEvSNGQDILTIgnFEIPSRAYVGRFNFKGVDQQK------RVG----------ELSGGERGRLHLAKLLQRGGNVLL 468
Cdd:cd03298 75 LFQE-NNLFAHLTV--EQNVGLGLSPGLKLTAEDRQAievalaRVGlaglekrlpgELSGGERQRVALARVLVRDKPVLL 151
|
....*....
gi 1735515619 469 LDEPTNDLD 477
Cdd:cd03298 152 LDEPFAALD 160
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-252 |
1.25e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.79 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 21 HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAgvdKEFEgearPQPG-IKIGYLP----QEPKLEPQQTVreaveeaV 95
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT---RAWD----PQQGeILLNGQPiadySEAALRQAISV-------V 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 96 SE---VKSALTRlDEVyaLYADPDADFDKLAA--EQANLEAIIQAHDGhnLDNQLeraADALRLpdwdakiehLSGGERR 170
Cdd:PRK11160 420 SQrvhLFSATLR-DNL--LLAAPNASDEALIEvlQQVGLEKLLEDDKG--LNAWL---GEGGRQ---------LSGGEQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 171 RVALCRLLLEKPDMLLLDEPTNHLDAESvawlER------FLHDYEGTVVAITHDRYFLDNVAGWILeLDRGEGIPwEGN 244
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAET----ERqilellAEHAQNKTVLMITHRLTGLEQFDRICV-MDNGQIIE-QGT 556
|
....*...
gi 1735515619 245 YSSWLEQK 252
Cdd:PRK11160 557 HQELLAQQ 564
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-218 |
1.31e-14 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 73.42 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 17 PPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGVD-KEFEGEARPQpgiKIGYLPQEPKLE 82
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvssgsiliDGQDiREVTLDSLRR---AIGVVPQDTVLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 83 pQQTVREAVEeavsevksaltrldevyalYADPDADFDKL--AAEQANLEAIIqahdghnldnqleraadaLRLPD-WDA 159
Cdd:cd03253 88 -NDTIGYNIR-------------------YGRPDATDEEVieAAKAAQIHDKI------------------MRFPDgYDT 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 160 KI-EH---LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG--TVVAITH 218
Cdd:cd03253 130 IVgERglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKgrTTIVIAH 194
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
20-237 |
1.44e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 75.64 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE--------------ARPqpgikIGYLPQEPKLEPQQ 85
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQimldgvdlshvppyQRP-----INMMFQSYALFPHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 TVREAVEEAVSEvksaltrldevyalyadpdadfDKLAAEQANLeaiiQAHDGHNLDNQLERAAdalRLPdwdakiEHLS 165
Cdd:PRK11607 107 TVEQNIAFGLKQ----------------------DKLPKAEIAS----RVNEMLGLVHMQEFAK---RKP------HQLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDA--------ESVAWLERFlhdyEGTVVAITHDRYFLDNVAGWILELDRGE 237
Cdd:PRK11607 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdrmqlEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-219 |
1.49e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.09 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdkEFEGEARPQpGIKIG---YLPQEP--KLEPQQTVR-EAVEE 93
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG---DLTGGGAPR-GARVTgdvTLNGEPlaAIDAPRLARlRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 94 AVSEVKSALTrLDEVYALYADPDAdfdKLAAEQANleaiiqaHDGHNLDNQLERA-ADALRLPDwdakIEHLSGGERRRV 172
Cdd:PRK13547 90 QAAQPAFAFS-AREIVLLGRYPHA---RRAGALTH-------RDGEIAWQALALAgATALVGRD----VTTLSGGELARV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 173 ALCRLLLE---------KPDMLLLDEPTNHLD-------AESVAWLERflhDYEGTVVAITHD 219
Cdd:PRK13547 155 QFARVLAQlwpphdaaqPPRYLLLDEPTAALDlahqhrlLDTVRRLAR---DWNLGVLAIVHD 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
21-225 |
1.67e-14 |
|
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: 71.58 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 21 HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEArpqpgikigYLPQEPKLEPQQTVREAVeeavsevkS 100
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGVPVSDLEKALSSLI--------S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 101 ALTRldEVYaLYADpdadfdklaaeqanleaiiqahdghNLDNQLERaadalrlpdwdakieHLSGGERRRVALCRLLLE 180
Cdd:cd03247 79 VLNQ--RPY-LFDT-------------------------TLRNNLGR---------------RFSGGERQRLALARILLQ 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 181 KPDMLLLDEPTNHLDAES-VAWLERFLHDYEG-TVVAITH--------DR-YFLDN 225
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITeRQLLSLIFEVLKDkTLIWITHhltgiehmDKiLFLEN 171
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
22-204 |
2.00e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.48 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE----ARPQPG------IKIGYLPQEPKLEPQQTVREAV 91
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKitvlGVPVPArarlarARIGVVPQFDNLDLEFTVRENL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 92 eeavsevksaltrldEVYALYadpdadFDKLAAEqanLEAIIQAHdghnLD-NQLERAAdalrlpdwDAKIEHLSGGERR 170
Cdd:PRK13536 136 ---------------LVFGRY------FGMSTRE---IEAVIPSL----LEfARLESKA--------DARVSDLSGGMKR 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 1735515619 171 RVALCRLLLEKPDMLLLDEPTNHLD--AESVAWlER 204
Cdd:PRK13536 180 RLTLARALINDPQLLILDEPTTGLDphARHLIW-ER 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-242 |
2.30e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 73.51 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkefegeARPQPG-IKIGYLPQEpklepqqtvreavEEAVSE 97
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGL-------LLPEAGtITVGGMVLS-------------EETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 98 VKSaltrldEVYALYADPDADF------DKLAAeqaNLEAIiqahdGHNLDNQLERAADALRL----PDWDAKIEHLSGG 167
Cdd:PRK13635 79 VRR------QVGMVFQNPDNQFvgatvqDDVAF---GLENI-----GVPREEMVERVDQALRQvgmeDFLNREPHRLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 168 ERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHDYEG-TVVAITHDryfLDNVAGW--ILELDRG----E 237
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPrgrREVLETVRQLKEQKGiTVLSITHD---LDEAAQAdrVIVMNKGeileE 221
|
....*
gi 1735515619 238 GIPWE 242
Cdd:PRK13635 222 GTPEE 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
20-237 |
2.35e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 73.68 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA--RPQPGIKigylpqepklepqqtvreaveEAVSE 97
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVliRGEPITK---------------------ENIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 98 VKSAltrldeVYALYADPDADFDKLAAEQ-ANLEAIIQAHDGHNLDNQLERAADALRLPDWDAKI-EHLSGGERRRVALC 175
Cdd:PRK13652 76 VRKF------VGLVFQNPDDQIFSPTVEQdIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVpHHLSGGEKKRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 176 RLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD----YEGTVVAITHDRYFLDNVAGWILELDRGE 237
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDlpetYGMTVIFSTHQLDLVPEMADYIYVMDKGR 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
325-521 |
2.90e-14 |
|
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: 72.37 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLiDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQfRD------ 397
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDITNLPPEK-RDisyvpq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 398 --AMDDKKTVWEEVSNGQDILTIGNFEIPSRAY-VGRFnfKGVDQ--QKRVGELSGGERGRLHLAKLLQRGGNVLLLDEP 472
Cdd:cd03299 79 nyALFPHMTVYKNIAYGLKKRKVDKKEIERKVLeIAEM--LGIDHllNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1735515619 473 TNDLDVET----LRALENAILEFPGCAMVISHD----RWFLDRIAT----HILDYGDEGKV 521
Cdd:cd03299 157 FSALDVRTkeklREELKKIRKEFGVTVLHVTHDfeeaWALADKVAImlngKLIQVGKPEEV 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
22-204 |
3.19e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.69 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR----PQPG------IKIGYLPQEPKLEPQQTVREAV 91
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgePVPSrarharQRVGVVPQFDNLDPDFTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 92 EeavsevksaltrldeVYALYADPDAdfdklAAEQANLEAIIQAhdghnldNQLERAADAlrlpdwdaKIEHLSGGERRR 171
Cdd:PRK13537 102 L---------------VFGRYFGLSA-----AAARALVPPLLEF-------AKLENKADA--------KVGELSGGMKRR 146
|
170 180 190
....*....|....*....|....*....|....*
gi 1735515619 172 VALCRLLLEKPDMLLLDEPTNHLD--AESVAWlER 204
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDpqARHLMW-ER 180
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
325-500 |
4.03e-14 |
|
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: 74.84 E-value: 4.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQ--PDAGSI--------------------- 381
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 382 ---TMGETVVLASVD-------QFRD-------------AMDDKKTVWEEVsngqdILTIGNFEIPSRAYVGRFN--FKG 436
Cdd:TIGR03269 81 pcpVCGGTLEPEEVDfwnlsdkLRRRirkriaimlqrtfALYGDDTVLDNV-----LEALEEIGYEGKEAVGRAVdlIEM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1735515619 437 VDQQKRVG----ELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEF---PGCAMVI-SH 500
Cdd:TIGR03269 156 VQLSHRIThiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkaSGISMVLtSH 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
325-488 |
4.19e-14 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 71.88 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGD--RTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMG----ETVVLAS------- 391
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghdvRDYTLASlrrqigl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 392 VDQ----FRDamddkkTVWEEVSNGQDILTIGNFEIPSR-AYVGRF--NF-KGVDQQkrVGE----LSGGERGRLHLAKL 459
Cdd:cd03251 81 VSQdvflFND------TVAENIAYGRPGATREEVEEAARaANAHEFimELpEGYDTV--IGErgvkLSGGQRQRIAIARA 152
|
170 180
....*....|....*....|....*....
gi 1735515619 460 LQRGGNVLLLDEPTNDLDVETLRALENAI 488
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAAL 181
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
323-500 |
4.35e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.82 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 323 KVIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETvvlaSVDQFRDAMDDK 402
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI----NYNKLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 403 ---KTVWEEVSngqdilTIGNFEIPSRAYVGRFNFKGV--------------------------DQQKRVGELSGGERGR 453
Cdd:PRK09700 80 lgiGIIYQELS------VIDELTVLENLYIGRHLTKKVcgvniidwremrvraammllrvglkvDLDEKVANLSISHKQM 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1735515619 454 LHLAKLLQRGGNVLLLDEPTNDL---DVETLRALENAiLEFPGCAMV-ISH 500
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQ-LRKEGTAIVyISH 203
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
22-258 |
4.94e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 72.31 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGearpqpgiKIGYLPQEPKL--EPQQTVREAVEEAVSEVK 99
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEG--------SIVVNGQTINLvrDKDGQLKVADKNQLRLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 100 SALTRLDEVYALYAdpdadfdKLAAEQANLEAIIQAHdGHNLDNQLERAADALRLPDWDAKIE-----HLSGGERRRVAL 174
Cdd:PRK10619 92 TRLTMVFQHFNLWS-------HMTVLENVMEAPIQVL-GLSKQEARERAVKYLAKVGIDERAQgkypvHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 175 CRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHDRYFLDNVAGWILELDRGEgIPWEGNYSSWLEQ 251
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaeEGkTMVVVTHEMGFARHVSSHVIFLHQGK-IEEEGAPEQLFGN 242
|
....*...
gi 1735515619 252 -KEKRLEQ 258
Cdd:PRK10619 243 pQSPRLQQ 250
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
325-484 |
5.23e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 72.09 E-value: 5.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLAS---------VDQF 395
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkglIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 396 RDAMD---------DKKTVWEEVSNGQDILTignfEIPSRAYVGRfnfkGVDQQKRVG----------ELSGGERGRLHL 456
Cdd:PRK11264 84 RQHVGfvfqnfnlfPHRTVLENIIEGPVIVK----GEPKEEATAR----ARELLAKVGlagketsyprRLSGGQQQRVAI 155
|
170 180 190
....*....|....*....|....*....|....*
gi 1735515619 457 AKLLQRGGNVLLLDEPTNDLDVE-------TLRAL 484
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPElvgevlnTIRQL 190
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
324-501 |
5.29e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.07 E-value: 5.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQfRDAMDdkK 403
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ-KLYLD--T 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 404 TVWEEVS---------NGQDILtignfeiPSRAYVGRFNFKGVDQQKrvgeLSGGERGRLHLAKLLQRGGNVLLLDEPTN 474
Cdd:PRK09544 81 TLPLTVNrflrlrpgtKKEDIL-------PALKRVQAGHLIDAPMQK----LSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190
....*....|....*....|....*....|.
gi 1735515619 475 DLDVETLRALENAILEFP---GCA-MVISHD 501
Cdd:PRK09544 150 GVDVNGQVALYDLIDQLRrelDCAvLMVSHD 180
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
325-502 |
6.21e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 73.19 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVlaSVDQFRD------- 397
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV--SRLHARDrkvgfvf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 398 ---AMDDKKTVWEEVSNGQDILTigNFEIPSRAYVGRFNFKGVD--QQKRVGE-----LSGGERGRLHLAKLLQRGGNVL 467
Cdd:PRK10851 81 qhyALFRHMTVFDNIAFGLTVLP--RRERPNAAAIKAKVTQLLEmvQLAHLADrypaqLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1735515619 468 LLDEPTNDLDVET-------LRALENailEFPGCAMVISHDR 502
Cdd:PRK10851 159 LLDEPFGALDAQVrkelrrwLRQLHE---ELKFTSVFVTHDQ 197
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
329-522 |
6.31e-14 |
|
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: 73.22 E-value: 6.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 329 NLTKSYGDRTLidDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVvLASVDQFRDAMDDKKT---V 405
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRT-LFDSRKGIFLPPEKRRigyV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 406 WEEVSNGQDILTIGNFEI---PSRAYVGRFNFKGVDQ--------QKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTN 474
Cdd:TIGR02142 81 FQEARLFPHLSVRGNLRYgmkRARPSERRISFERVIEllgighllGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1735515619 475 DLDV----ETLRALENAILEFPGCAMVISHDRWFLDRIATHILdYGDEGKVT 522
Cdd:TIGR02142 161 ALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVV-VLEDGRVA 211
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
27-218 |
6.57e-14 |
|
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: 74.40 E-value: 6.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 27 SLSF-FP-GAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-ARPQPGiKIGYLPQEPKLEpQQTVREAVeeavsevksalt 103
Cdd:TIGR00954 470 SLSFeVPsGNNLLICGPNGCGKSSLFRILGELWPVYGGRlTKPAKG-KLFYVPQRPYMT-LGTLRDQI------------ 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 104 rldevyaLYADPDADFDKLAAEQANLEAIIQAHDghnLDNQLERAA--DALRlpDWdakIEHLSGGERRRVALCRLLLEK 181
Cdd:TIGR00954 536 -------IYPDSSEDMKRRGLSDKDLEQILDNVQ---LTHILEREGgwSAVQ--DW---MDVLSGGEKQRIAMARLFYHK 600
|
170 180 190
....*....|....*....|....*....|....*..
gi 1735515619 182 PDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITH 218
Cdd:TIGR00954 601 PQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
21-237 |
7.10e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 71.18 E-value: 7.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 21 HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGEARPQPGI-------KIGYLPQEPKLEPQQTV 87
Cdd:COG1126 15 EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEpdsgtiTVDGEDLTDSKKdinklrrKVGMVFQQFNLFPHLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 88 REAVEEAVSEVKsaltrldevyalyadpdadfdKLAAEQANLEAIiqahdghnldNQLERaadaLRLPD-WDAKIEHLSG 166
Cdd:COG1126 95 LENVTLAPIKVK---------------------KMSKAEAEERAM----------ELLER----VGLADkADAYPAQLSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1735515619 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD--YEG-TVVAITHDRYFLDNVAGWILELDRGE 237
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDlaKEGmTMVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
22-237 |
7.48e-14 |
|
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: 71.76 E-value: 7.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQpGIKIGYLPQEPKLEPQQTVREAVEEAVSEVKSA 101
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFR-GQDLYQLDRKQRRAFRRDVQLVFQDSPSAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 102 LTrldeVYALYADPDADFDKL-AAEQanleaiiQAHDGHNLDNQLERAADALRLPdwdakiEHLSGGERRRVALCRLLLE 180
Cdd:TIGR02769 105 MT----VRQIIGEPLRHLTSLdESEQ-------KARIAELLDMVGLRSEDADKLP------RQLSGGQLQRINIARALAV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1735515619 181 KPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGE 237
Cdd:TIGR02769 168 KPKLIVLDEAVSNLDmvlqAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
324-522 |
7.59e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 71.28 E-value: 7.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRDAMDDKK 403
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 404 TVWEEVSNGQDILTIGNFEIPSRAYVGRFNFKGVDQQK----RVG----------ELSGGERGRLHLAKLLQRGGNVLLL 469
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARellaKVGlaerahhypsELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1735515619 470 DEPTNDLDV----ETLRALENAILEfpGCAMVI-SHDRWFLDRIATHILdYGDEGKVT 522
Cdd:PRK09493 161 DEPTSALDPelrhEVLKVMQDLAEE--GMTMVIvTHEIGFAEKVASRLI-FIDKGRIA 215
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-478 |
8.78e-14 |
|
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: 73.71 E-value: 8.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKD---------ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV--DKEFEGEarpqpgikIGYLPQEPKlepQQTVR 88
Cdd:TIGR02633 5 KGIVKTfggvkaldgIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGE--------IYWSGSPLK---ASNIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 89 EAVEEAVSEVKSALTRLDEVYALYADPDADFDKLAAEQANLEAIIqaHDGHNLDNQLERAADALRLPdwdakIEHLSGGE 168
Cdd:TIGR02633 74 DTERAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMY--LRAKNLLRELQLDADNVTRP-----VGDYGGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVagwileldrgegipwegnyssw 248
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEV---------------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 249 leqkekrleqeqaaenarqKSIAKELEWVRQnpkGRQAKSKArMARFDELNSGEYQKRNETNELFiPPGPR-LGDKVIEV 327
Cdd:TIGR02633 205 -------------------KAVCDTICVIRD---GQHVATKD-MSTMSEDDIITMMVGREITSLY-PHEPHeIGDVILEA 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 328 QNLTKSYGD---RTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSG-------------QEQPD--------AGSITM 383
Cdd:TIGR02633 261 RNLTCWDVInphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaypgkfegnvfinGKPVDirnpaqaiRAGIAM 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 384 ----------------GETVVLASVDQFrdamdDKKTVWEEVSNGQDIltignfeipsRAYVGRFNFKGVDQQKRVGELS 447
Cdd:TIGR02633 341 vpedrkrhgivpilgvGKNITLSVLKSF-----CFKMRIDAAAELQII----------GSAIQRLKVKTASPFLPIGRLS 405
|
490 500 510
....*....|....*....|....*....|.
gi 1735515619 448 GGERGRLHLAKLLQRGGNVLLLDEPTNDLDV 478
Cdd:TIGR02633 406 GGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-478 |
8.86e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.81 E-value: 8.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DKE--FEGE---AR-----PQPGIKIGYlpQEPKLEPQQT 86
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyEGEiiFEGEelqASnirdtERAGIAIIH--QELALVKELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 87 VREAVEEAVSEVKSALTRLDEVYAlyadpdaDFDKLAAEqanleaiiqahdghnldnqleraadaLRLP-DWDAKIEHLS 165
Cdd:PRK13549 99 VLENIFLGNEITPGGIMDYDAMYL-------RAQKLLAQ--------------------------LKLDiNPATPVGNLG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVA---ITHDryfLDNV---AGWILELDRGEGI 239
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIAciyISHK---LNEVkaiSDTICVIRDGRHI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 240 pwegnysswleqkekrlEQEQAAENARQKSIAKELewvrqnpkGRqakskarmarfdelnsgeyqkrnETNELFiPPGPR 319
Cdd:PRK13549 223 -----------------GTRPAAGMTEDDIITMMV--------GR-----------------------ELTALY-PREPH 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 320 -LGDKVIEVQNLT---KSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSG----------------------Q 373
Cdd:PRK13549 254 tIGEVILEVRNLTawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaypgrwegeifidgkpvkirnpQ 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 374 EQPDAGsITM----------------GETVVLASVDQFrdamddkkTVWEEVSNGQDILTIgnfeipsRAYVGRFNFKGV 437
Cdd:PRK13549 334 QAIAQG-IAMvpedrkrdgivpvmgvGKNITLAALDRF--------TGGSRIDDAAELKTI-------LESIQRLKVKTA 397
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1735515619 438 DQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDV 478
Cdd:PRK13549 398 SPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
328-478 |
9.68e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.56 E-value: 9.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 328 QNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVV-LASVDQFRD-------- 397
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHIQhYASKEVARRigllaqna 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 398 AMDDKKTVWEEVSNG----QDILTIGNFEiPSRAYVGRFNFKGVDQ--QKRVGELSGGERGRLHLAKLLQRGGNVLLLDE 471
Cdd:PRK10253 91 TTPGDITVQELVARGryphQPLFTRWRKE-DEEAVTKAMQATGITHlaDQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
....*..
gi 1735515619 472 PTNDLDV 478
Cdd:PRK10253 170 PTTWLDI 176
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-237 |
1.04e-13 |
|
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: 70.58 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 18 PKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE----ARPQPGIKIGYL-------PQEPKLEpQQT 86
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQvlldGKPISQYEHKYLhskvslvGQEPVLF-ARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 87 VREAVEeavsevksaltrldevyalYADPDADFDKLAAEQanleaiiQAHDGHNLDNQLERAADAlrlpDWDAKIEHLSG 166
Cdd:cd03248 104 LQDNIA-------------------YGLQSCSFECVKEAA-------QKAHAHSFISELASGYDT----EVGEKGSQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAITHdRYFLDNVAGWILELDRGE 237
Cdd:cd03248 154 GQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH-RLSTVERADQILVLDGGR 225
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-219 |
1.19e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.58 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 1 MSSQFVYTMHRVGKVVPPKRH---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARpqpgikigyLPQ 77
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGQGEHelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVS---------LVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 78 EPKLEPQQTVREAVE-EAVSEVKSALTRLDEVYALyadpdadfdklaaEQANLEAIIQahdGHNLDNQLERAADALRLPD 156
Cdd:PRK10584 72 QPLHQMDEEARAKLRaKHVGFVFQSFMLIPTLNAL-------------ENVELPALLR---GESSRQSRNGAKALLEQLG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1735515619 157 WDAKIEH----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL----HDYEGTVVAITHD 219
Cdd:PRK10584 136 LGKRLDHlpaqLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
20-235 |
1.57e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 69.82 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKEF--EGE---------ARPQPGIKIGYLPQEPKLEPQQTV 87
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAFsaSGEvllngrrltALPAEQRRIGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 88 RE----AVEEAVSevKSAltRLDEVYAlyadpdadfdklAAEQANLEAIiqahdghnldnqleraadALRLPDwdakieH 163
Cdd:COG4136 94 GEnlafALPPTIG--RAQ--RRARVEQ------------ALEEAGLAGF------------------ADRDPA------T 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1735515619 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERF----LHDYEGTVVAITHDRyflDNV--AGWILELDR 235
Cdd:COG4136 134 LSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDE---EDApaAGRVLDLGN 208
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-206 |
1.72e-13 |
|
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: 69.19 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--VDKEFEGE----ARPQPG---IKIGYLPQEPKLEPQQTVRE 89
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEilinGRPLDKnfqRSTGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 90 AVEeavsevksaltrldevyalyadpdadfdklaaeqanleaiiqahdghnldnqleraadalrlpdWDAKIEHLSGGER 169
Cdd:cd03232 99 ALR----------------------------------------------------------------FSALLRGLSVEQR 114
|
170 180 190
....*....|....*....|....*....|....*..
gi 1735515619 170 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL 206
Cdd:cd03232 115 KRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-478 |
1.75e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 9 MHRVGKVVPPKrHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKefegearPQPGIKIGYLPQEPKLEPqqtvR 88
Cdd:PRK09700 8 MAGIGKSFGPV-HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-------PTKGTITINNINYNKLDH----K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 89 EAVEEAVSEVKSALTRLDEVYAL-------------YADPDADFDKLAAEQANLEAIIQAHdghnldnqleraadalrlP 155
Cdd:PRK09700 76 LAAQLGIGIIYQELSVIDELTVLenlyigrhltkkvCGVNIIDWREMRVRAAMMLLRVGLK------------------V 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 156 DWDAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGT-VVAITH---------DRYfl 223
Cdd:PRK09700 138 DLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLrkEGTaIVYISHklaeirricDRY-- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 224 dnvagwileldrgeGIPWEGNYSSwleqkeKRLEQEQAAENARQKSIAKELEwvrqnpkgrqakskarmARFDELNSGEY 303
Cdd:PRK09700 216 --------------TVMKDGSSVC------SGMVSDVSNDDIVRLMVGRELQ-----------------NRFNAMKENVS 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 304 QKRNETnelfippgprlgdkVIEVQNLTKSygDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM 383
Cdd:PRK09700 259 NLAHET--------------VFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRL 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 384 -GETVVLASVdqfRDAMddKKTVWEEVSNGQDILTIGNFEIPSRAYVGRF----NFKG-------VDQQK---------- 441
Cdd:PRK09700 323 nGKDISPRSP---LDAV--KKGMAYITESRRDNGFFPNFSIAQNMAISRSlkdgGYKGamglfheVDEQRtaenqrella 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1735515619 442 --------RVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDV 478
Cdd:PRK09700 398 lkchsvnqNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-252 |
1.87e-13 |
|
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: 69.95 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 18 PKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE----ARPQPGI-------KIGYLPQEPKLEPqQT 86
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQilidGIDIRDIsrkslrsMIGVVLQDTFLFS-GT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 87 VREAVeeavsevksaltrldevyaLYADPDADFD--KLAAEQANL-EAIIQAHDGhnLDNQL-ERAADalrlpdwdakie 162
Cdd:cd03254 93 IMENI-------------------RLGRPNATDEevIEAAKEAGAhDFIMKLPNG--YDTVLgENGGN------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 163 hLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYegTVVAITHDRYFLDNvAGWILELDRGEg 238
Cdd:cd03254 140 -LSQGERQLLAIARAMLRDPKILILDEATSNIDTETekliQEALEKLMKGR--TSIIIAHRLSTIKN-ADKILVLDDGK- 214
|
250
....*....|....
gi 1735515619 239 IPWEGNYSSWLEQK 252
Cdd:cd03254 215 IIEEGTHDELLAKK 228
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-252 |
2.03e-13 |
|
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: 70.56 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-------ARPQPGI-------KIGYLPQEPKlepQQ 85
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTvtidgrdITAKKKKklkdlrkKVGLVFQFPE---HQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 TVREAVEEavsevksaltrldevyalyadpDADFDKLaaeqaNLeaiiqahdGHNLDNQLERAADALRLPDWDAKIEH-- 163
Cdd:TIGR04521 95 LFEETVYK----------------------DIAFGPK-----NL--------GLSEEEAEERVKEALELVGLDEEYLErs 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 164 ---LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES-VAWLERF--LHDYEG-TVVAITHDryfLDNVAGW---ILEL 233
Cdd:TIGR04521 140 pfeLSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGrKEILDLFkrLHKEKGlTVILVTHS---MEDVAEYadrVIVM 216
|
250 260
....*....|....*....|....
gi 1735515619 234 DRG----EGIPWE-GNYSSWLEQK 252
Cdd:TIGR04521 217 HKGkivlDGTPREvFSDVDELEKI 240
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
325-521 |
2.08e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 70.04 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGEtvvlASVDqFRDAMDDKKT 404
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAG----HQFD-FSQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 405 ---------------VWEEVSNGQDILtignfEIPSRAY-----VGRFNFKGVDQQKRVGE--------LSGGERGRLHL 456
Cdd:COG4161 78 rllrqkvgmvfqqynLWPHLTVMENLI-----EAPCKVLglskeQAREKAMKLLARLRLTDkadrfplhLSGGQQQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1735515619 457 AKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFPGCAM---VISHDRWFLDRIATHILdYGDEGKV 521
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGItqvIVTHEVEFARKVASQVV-YMEKGRI 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-58 |
3.60e-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: 3.60e-13
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK 58
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILE 77
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
315-518 |
4.18e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.26 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 315 PPGPRLGDKVIEVQNLTKSYGDRT-----LIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVL 389
Cdd:PRK13631 12 VPNPLSDDIILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 390 ASVD---------------------------QFRDAMDDKKTVWEEVSNGQDILTIGNFEIPSRA--YVGRFNFKGVDQQ 440
Cdd:PRK13631 92 DKKNnhelitnpyskkiknfkelrrrvsmvfQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAkfYLNKMGLDDSYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 441 KRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFPG---CAMVISHDrwfldriATHILDYGD 517
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITHT-------MEHVLEVAD 244
|
.
gi 1735515619 518 E 518
Cdd:PRK13631 245 E 245
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
322-539 |
4.88e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.88 E-value: 4.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 322 DKVIEVQNLTKSYGDRT-LIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLAS--------- 391
Cdd:PRK13636 3 DYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSrkglmklre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 392 ----VDQFRDAMDDKKTVWEEVSNGQDILTIGNFEIPSRayVGRFNFK-GVD--QQKRVGELSGGERGRLHLAKLLQRGG 464
Cdd:PRK13636 83 svgmVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKR--VDNALKRtGIEhlKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 465 NVLLLDEPTNDLD---VETLRALENAILEFPGCAMVI-SHDrwfLDRIATHIlDYG---DEGKVTFyEGN----FSDYEE 533
Cdd:PRK13636 161 KVLVLDEPTAGLDpmgVSEIMKLLVEMQKELGLTIIIaTHD---IDIVPLYC-DNVfvmKEGRVIL-QGNpkevFAEKEM 235
|
....*.
gi 1735515619 534 WKKKTL 539
Cdd:PRK13636 236 LRKVNL 241
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
325-521 |
5.07e-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: 68.29 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGD--RTLIDDLSFSIPKGAIVGIIGANGAGKST----LFRMLsgqeQPDAGSITmgetvvlasVDqfrda 398
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSIL---------ID----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 399 mddkktvweevsnGQDILTIGNFEIPSR----------------------------------------AYVGRFNFKGVD 438
Cdd:cd03244 65 -------------GVDISKIGLHDLRSRisiipqdpvlfsgtirsnldpfgeysdeelwqalervglkEFVESLPGGLDT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 439 QQKRVGE-LSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAI-LEFPGCAMV-ISHdrwfldRIAThILDY 515
Cdd:cd03244 132 VVEEGGEnLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIrEAFKDCTVLtIAH------RLDT-IIDS 204
|
250
....*....|.
gi 1735515619 516 G-----DEGKV 521
Cdd:cd03244 205 DrilvlDKGRV 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-490 |
5.44e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 71.27 E-value: 5.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKS-TLLRIM----------AGVDKEFEGEA---------RPQPGIKIGYLPQEP 79
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpsppvvyPSGDIRFHGESllhaseqtlRGVRGNKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 80 --KLEPQQTVreavEEAVSEVKSaLTRldevyalyadpdadfdKLAAEQANLEaIIQAhdghnLDNQLERAAdALRLPDW 157
Cdd:PRK15134 102 mvSLNPLHTL----EKQLYEVLS-LHR----------------GMRREAARGE-ILNC-----LDRVGIRQA-AKRLTDY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 158 DakiEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG----TVVAITHD----RYFLDNVAgw 229
Cdd:PRK15134 154 P---HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNlsivRKLADRVA-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 230 ileldrgegipwegnysswLEQKEKRLEQEQAAE--NARQKSIAKELewVRQNPKGRQakskarmarfdelnsgeyqkrn 307
Cdd:PRK15134 229 -------------------VMQNGRCVEQNRAATlfSAPTHPYTQKL--LNSEPSGDP---------------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 308 etnelfiPPGPRLGDKVIEVQNLTKSY-----------GDRTLIDDLSFSIPKGAIVGIIGANGAGKST----LFRMLSG 372
Cdd:PRK15134 266 -------VPLPEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 373 QeqpdaGSITM-GETVVLASVDQ-----------FRD---AMDDKKTVWEEVSNG----QDILTIGNFEIPSRAYVGRFN 433
Cdd:PRK15134 339 Q-----GEIWFdGQPLHNLNRRQllpvrhriqvvFQDpnsSLNPRLNVLQIIEEGlrvhQPTLSAAQREQQVIAVMEEVG 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 434 FKGVDQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDvetlRALENAILE 490
Cdd:PRK15134 414 LDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAQILA 466
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
8-236 |
6.57e-13 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 68.23 E-value: 6.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 8 TMHRV-GKVVPPkrhiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdkefegearpqpgikiGYLPQepklepQQT 86
Cdd:COG4778 15 TLHLQgGKRLPV----LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG-----------------NYLPD------SGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 87 VREAVEEAVSEVKSALTRldEVYALYAD------------PdadfdKLAAEQANLEAIIqaHDGHNLDNQLERAADALR- 153
Cdd:COG4778 68 ILVRHDGGWVDLAQASPR--EILALRRRtigyvsqflrviP-----RVSALDVVAEPLL--ERGVDREEARARARELLAr 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 154 --LPD--WDAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGT-VVAITHDRYFLDNV 226
Cdd:COG4778 139 lnLPErlWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkaRGTaIIGIFHDEEVREAV 218
|
250
....*....|
gi 1735515619 227 AGWILELDRG 236
Cdd:COG4778 219 ADRVVDVTPF 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-218 |
6.84e-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: 68.34 E-value: 6.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 18 PKRHILKDISLSFFPGAKIGVLGLNGAGKST----LLR---------IMAGVD-KEFEGEARPQpgiKIGYLPQEPKLEP 83
Cdd:cd03249 14 PDVPILKGLSLTIPPGKTVALVGSSGCGKSTvvslLERfydptsgeiLLDGVDiRDLNLRWLRS---QIGLVSQEPVLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 84 QqTVREAVeeavsevksaltrldevyaLYADPDADF--DKLAAEQANLEAIIQAhdghnldnqleraadalrLPD-WDAK 160
Cdd:cd03249 91 G-TIAENI-------------------RYGKPDATDeeVEEAAKKANIHDFIMS------------------LPDgYDTL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 161 I-EH---LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAW----LERFLhdyEG-TVVAITH 218
Cdd:cd03249 133 VgERgsqLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLvqeaLDRAM---KGrTTIVIAH 196
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
21-219 |
7.52e-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: 68.03 E-value: 7.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 21 HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQpGIKIGYLPqePKLEPQQTVREAveeavsevks 100
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD-GKDITNLP--PHKRPVNTVFQN---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 101 altrldevYALYadPDAD-FDKLA--AEQANL-EAIIQahdghnldnqlERAADALRLPDWDA----KIEHLSGGERRRV 172
Cdd:cd03300 81 --------YALF--PHLTvFENIAfgLRLKKLpKAEIK-----------ERVAEALDLVQLEGyanrKPSQLSGGQQQRV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1735515619 173 ALCRLLLEKPDMLLLDEPTNHLDAESVAWLE---RFLHDYEG-TVVAITHD 219
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLKLRKDMQlelKRLQKELGiTFVFVTHD 190
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
322-523 |
7.75e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.99 E-value: 7.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 322 DKVIEVQNLT-KSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM--GETVVLASvdQ---- 394
Cdd:COG4178 360 DGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLP--Qrpyl 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 395 ----FRDA---------MDDkktvwEEVsngQDILTIGNFEipsrAYVGRFnfkgvDQQKRVG-ELSGGERGRLHLAKLL 460
Cdd:COG4178 438 plgtLREAllypataeaFSD-----AEL---REALEAVGLG----HLAERL-----DEEADWDqVLSLGEQQRLAFARLL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 461 QRGGNVLLLDEPTNDLDVETLRALENAIL-EFPGCAMV-ISHdRWFLDRIATHILDYGDEGKVTF 523
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLReELPGTTVIsVGH-RSTLAAFHDRVLELTGDGSWQL 564
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
22-252 |
8.24e-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: 68.03 E-value: 8.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVD-KEFE-GEARPQpgikIGYLPQEPKLEpQQT 86
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPrfydvdsgrilidGHDvRDYTlASLRRQ----IGLVSQDVFLF-NDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 87 VREAVeeavsevksaltrldevyaLYADPDADFDKL--AAEQANLEAIIQahdghnldnqleraadalRLPD-WDAKIEH 163
Cdd:cd03251 92 VAENI-------------------AYGRPGATREEVeeAARAANAHEFIM------------------ELPEgYDTVIGE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 164 ----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYegTVVAITHDRYFLDNvAGWILELDR 235
Cdd:cd03251 135 rgvkLSGGQRQRIAIARALLKDPPILILDEATSALDTESerlvQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLED 211
|
250
....*....|....*..
gi 1735515619 236 GEgIPWEGNYSSWLEQK 252
Cdd:cd03251 212 GK-IVERGTHEELLAQG 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
324-500 |
8.26e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.80 E-value: 8.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSIT-MGETVVLASVDQFRDAmddk 402
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFNGPKSSQEA---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 403 ktvweevsnG-----QDILTIGNFEIPSRAYVGR---FNFKGVDQQK--------------------RVGELSGGERGRL 454
Cdd:PRK10762 80 ---------GigiihQELNLIPQLTIAENIFLGRefvNRFGRIDWKKmyaeadkllarlnlrfssdkLVGELSIGEQQMV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1735515619 455 HLAKLLQRGGNVLLLDEPTNDL-DVETlRALENAI--LEFPGCAMV-ISH 500
Cdd:PRK10762 151 EIAKVLSFESKVIIMDEPTDALtDTET-ESLFRVIreLKSQGRGIVyISH 199
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
322-521 |
8.79e-13 |
|
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: 67.88 E-value: 8.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 322 DKVIEVQNLTKSY---GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETV---------- 387
Cdd:cd03248 9 KGIVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdGKPIsqyehkylhs 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 388 VLASVDQfrDAMDDKKTVWEEVSNG-QDILTIGNFEIPSRAYVGRFNFK---GVDQQ--KRVGELSGGERGRLHLAKLLQ 461
Cdd:cd03248 89 KVSLVGQ--EPVLFARSLQDNIAYGlQSCSFECVKEAAQKAHAHSFISElasGYDTEvgEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1735515619 462 RGGNVLLLDEPTNDLDVETLRALENAILEFPG--CAMVISHDRWFLDRiATHILdYGDEGKV 521
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAHRLSTVER-ADQIL-VLDGGRI 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
318-524 |
9.93e-13 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 67.44 E-value: 9.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 318 PRLGDkvIEVQNLTKSYGDR--TLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMgetvvlasvdqf 395
Cdd:cd03369 2 PEHGE--IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 396 rDAMDDKKTVWEEVSNGqdiLTIgnfeIPS---------RAYVGRFNfKGVDQQ----KRVGE----LSGGERGRLHLAK 458
Cdd:cd03369 68 -DGIDISTIPLEDLRSS---LTI----IPQdptlfsgtiRSNLDPFD-EYSDEEiygaLRVSEgglnLSQGQRQLLCLAR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 459 LLQRGGNVLLLDEPTNDLDVETLRALENAILE-FPGCAMV-ISHdrwfldRIAThILDYG-----DEGKVTFY 524
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALIQKTIREeFTNSTILtIAH------RLRT-IIDYDkilvmDAGEVKEY 204
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
334-517 |
1.40e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.61 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 334 YGDRTLIDdLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLAS---------------VDQFRDA 398
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqkeikpvrkkvgvVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 399 MDDKKTVWEEVSNGQDILTIGNFEIPSRAyVGRFNFKGVDQ---QKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTND 475
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNFGIPKEKAEKIA-AEKLEMVGLADefwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1735515619 476 LD----VETLRALEnAILEFPGCAMVISHdrwFLDRIAthilDYGD 517
Cdd:PRK13643 175 LDpkarIEMMQLFE-SIHQSGQTVVLVTH---LMDDVA----DYAD 212
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
325-477 |
1.48e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 68.15 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRT-----LIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM------GETVVLAS-- 391
Cdd:PRK13637 3 IKIENLTHIYMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditDKKVKLSDir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 392 -----VDQFRDAMDDKKTVWEEVSNGQDILTIGNFEIPSRAYVGrFNFKGVD----QQKRVGELSGGERGRLHLAKLLQR 462
Cdd:PRK13637 83 kkvglVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRA-MNIVGLDyedyKDKSPFELSGGQKRRVAIAGVVAM 161
|
170
....*....|....*
gi 1735515619 463 GGNVLLLDEPTNDLD 477
Cdd:PRK13637 162 EPKILILDEPTAGLD 176
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
324-477 |
1.65e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.80 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTL-IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETV-----VLASVDQ-- 394
Cdd:PRK13639 1 ILETRDLKYSYPDGTEaLKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPIkydkkSLLEVRKtv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 395 ---FRDAmDDK---KTVWEEVSNGQDILTIGNFEIPSRAyvgrfnfkgVDQQKRVG----------ELSGGERGRLHLAK 458
Cdd:PRK13639 81 givFQNP-DDQlfaPTVEEDVAFGPLNLGLSKEEVEKRV---------KEALKAVGmegfenkpphHLSGGQKKRVAIAG 150
|
170
....*....|....*....
gi 1735515619 459 LLQRGGNVLLLDEPTNDLD 477
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLD 169
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
347-519 |
1.96e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.84 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 347 IPK-GAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMG---ETVVlasvDQFR-DAMddkKTVWEEVSNGQ-------- 413
Cdd:PRK13409 95 IPKeGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEpswDEVL----KRFRgTEL---QNYFKKLYNGEikvvhkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 414 --------------DILT----IGNFeipsRAYVGRFNFKGV-DQqkRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTN 474
Cdd:PRK13409 168 yvdlipkvfkgkvrELLKkvdeRGKL----DEVVERLGLENIlDR--DISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1735515619 475 DLDV-ETLRAlENAILEF-PGCA-MVISHDRWFLDRIA--THILdYGDEG 519
Cdd:PRK13409 242 YLDIrQRLNV-ARLIRELaEGKYvLVVEHDLAVLDYLAdnVHIA-YGEPG 289
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
324-486 |
2.10e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 69.75 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSY---GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVV----------L 389
Cdd:TIGR00958 478 LIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLdGVPLVqydhhylhrqV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 390 ASVDQ----------------FRDAMDDKKTVWEEVSNGQDIltIGNFEipsrayvgrfnfKGVDQQkrVGE----LSGG 449
Cdd:TIGR00958 558 ALVGQepvlfsgsvreniaygLTDTPDEEIMAAAKAANAHDF--IMEFP------------NGYDTE--VGEkgsqLSGG 621
|
170 180 190
....*....|....*....|....*....|....*..
gi 1735515619 450 ERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALEN 486
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE 658
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
345-519 |
2.11e-12 |
|
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: 69.81 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 345 FSIP---KGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSItmgetvvlasvdqfrdamdDKKTVWEEV------SNGQDI 415
Cdd:COG1245 91 YGLPvpkKGKVTGILGPNGIGKSTALKILSGELKPNLGDY-------------------DEEPSWDEVlkrfrgTELQDY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 416 LT-IGNFEIpsRA--------YVGRFnFKG--------VDQQ-----------------KRVGELSGGERGRLHLAKLLQ 461
Cdd:COG1245 152 FKkLANGEI--KVahkpqyvdLIPKV-FKGtvrellekVDERgkldelaeklglenildRDISELSGGELQRVAIAAALL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1735515619 462 RGGNVLLLDEPTNDLDV-ETLRAlENAILEF--PGCA-MVISHDRWFLDRIA--THILdYGDEG 519
Cdd:COG1245 229 RDADFYFFDEPSSYLDIyQRLNV-ARLIRELaeEGKYvLVVEHDLAILDYLAdyVHIL-YGEPG 290
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-196 |
2.25e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 67.19 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR------PQPGIKIGYLPQEPKLEPQQTVREAVEe 93
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITldgvpvTGPGADRGVVFQKDALLPWLNVLDNVA- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 94 avsevksaltrldevYALyadpdadfdKLAaeqanleaiiqahdGHNLDNQLERAADALRLPDW----DAKIEHLSGGER 169
Cdd:COG4525 99 ---------------FGL---------RLR--------------GVPKAERRARAEELLALVGLadfaRRRIWQLSGGMR 140
|
170 180
....*....|....*....|....*..
gi 1735515619 170 RRVALCRLLLEKPDMLLLDEPTNHLDA 196
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
23-237 |
2.58e-12 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 67.33 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVL-GLNGAGKSTLLRIMA----GVDKEFEGEARPQPGIKIGYLPQEPKL----EPQQTVREAVEE 93
Cdd:COG3950 14 FEDLEIDFDNPPRLTVLvGENGSGKTTLLEAIAlalsGLLSRLDDVKFRKLLIRNGEFGDSAKLilyyGTSRLLLDGPLK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 94 AVSEVKSALTRLDEVYALYADPDADFDKLAAEQANLEAIIQAHDGHNLDNQLERAADALR--LPDWDA------------ 159
Cdd:COG3950 94 KLERLKEEYFSRLDGYDSLLDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVREALNklLPDFKDiridrdpgrlvi 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 160 --------KIEHLSGGERRRVALC-----RLLLEKPDM---------LLLDEPTNHLdaeSVAWLERFLHDYEGT----- 212
Cdd:COG3950 174 ldkngeelPLNQLSDGERSLLALVgdlarRLAELNPALenplegegiVLIDEIDLHL---HPKWQRRILPDLRKIfpniq 250
|
250 260
....*....|....*....|....*.
gi 1735515619 213 VVAITHDRYFLDNV-AGWILELDRGE 237
Cdd:COG3950 251 FIVTTHSPLILSSLeDEEVIVLERDE 276
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
325-521 |
2.85e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.58 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVlasvdQFRDAMDDKK- 403
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHF-----DFSKTPSDKAi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 404 --------------TVWEEVSNGQD-------ILTIGNFEIPSRA-----------YVGRFNFkgvdqqkrvgELSGGER 451
Cdd:PRK11124 78 relrrnvgmvfqqyNLWPHLTVQQNlieapcrVLGLSKDQALARAekllerlrlkpYADRFPL----------HLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 452 GRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFPGCAM---VISHDRWFLDRIATHILdYGDEGKV 521
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHEVEVARKTASRVV-YMENGHI 219
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-247 |
2.95e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.10 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKeFEGEARPQpGI------------KIGYLPQEPKLePQQTVRE 89
Cdd:PRK11174 365 LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKIN-GIelreldpeswrkHLSWVGQNPQL-PHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 90 AVeeavsevksaltrldevyaLYADPDADFDKL--AAEQANLEAIIQAHDgHNLDNQL-ERAADalrlpdwdakiehLSG 166
Cdd:PRK11174 442 NV-------------------LLGNPDASDEQLqqALENAWVSEFLPLLP-QGLDTPIgDQAAG-------------LSV 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAITHDryfLDNVAGW--ILELDRGEgIPWE 242
Cdd:PRK11174 489 GQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAsrRQTTLMVTHQ---LEDLAQWdqIWVMQDGQ-IVQQ 564
|
....*
gi 1735515619 243 GNYSS 247
Cdd:PRK11174 565 GDYAE 569
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
325-500 |
3.20e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.89 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSY-GDRTL-IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMG-------------ETVVL 389
Cdd:PRK11176 342 IEFRNVTFTYpGKEVPaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDghdlrdytlaslrNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 390 AS--VDQFRDAmddkktvweeVSNG-----QDILTIGNFEIPSR-AYVGRFNFK---GVDQQkrVGE----LSGGERGRL 454
Cdd:PRK11176 422 VSqnVHLFNDT----------IANNiayarTEQYSREQIEEAARmAYAMDFINKmdnGLDTV--IGEngvlLSGGQRQRI 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1735515619 455 HLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFPG--CAMVISH 500
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH 537
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
326-513 |
3.20e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 66.63 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 326 EVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQE--QPDAGSITMgetvvlasvdqfrdamddkk 403
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILL-------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 404 tvweevsNGQDILtigNFEIPSRAYVGRF-------NFKGV---------------------DQQKRVGE---------- 445
Cdd:COG0396 62 -------DGEDIL---ELSPDERARAGIFlafqypvEIPGVsvsnflrtalnarrgeelsarEFLKLLKEkmkelglded 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 446 ---------LSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEF--PGCAM-VISHDRWFLDRIA---T 510
Cdd:COG0396 132 fldryvnegFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLrsPDRGIlIITHYQRILDYIKpdfV 211
|
...
gi 1735515619 511 HIL 513
Cdd:COG0396 212 HVL 214
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-198 |
3.72e-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: 69.08 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 18 PKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdkeFegeaR---PQPG-IKI-GylpQEPKLEPQQTVREAV- 91
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLL------F----RfydVTSGrILIdG---QDIRDVTQASLRAAIg 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 92 ---EEAVsevksaltrL--DEVYA--LYADPDADFDKL--AAEQANLEAIIQahdghnldnqleraadalRLPD-WDAKI 161
Cdd:COG5265 436 ivpQDTV---------LfnDTIAYniAYGRPDASEEEVeaAARAAQIHDFIE------------------SLPDgYDTRV 488
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1735515619 162 -EH---LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
Cdd:COG5265 489 gERglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
22-219 |
3.74e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 66.38 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEArpqpgikigylpqepkLEPQQTVREAVEEAVSEVKSa 101
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV----------------IFNGQPMSKLSSAAKAELRN- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 102 lTRLDEVYALY-ADPDADfdklAAEQANLEAIIqahDGHNLDNQLERAADALRLPDWDAKIEH----LSGGERRRVALCR 176
Cdd:PRK11629 87 -QKLGFIYQFHhLLPDFT----ALENVAMPLLI---GKKKPAEINSRALEMLAAVGLEHRANHrpseLSGGERQRVAIAR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1735515619 177 LLLEKPDMLLLDEPTNHLD---AESVAWLERFLHDYEGTV-VAITHD 219
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGTAfLVVTHD 205
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
322-477 |
4.03e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 66.75 E-value: 4.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 322 DKVIEVQNLTKSYGD--RTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGS----ITMGETVVLASVDQF 395
Cdd:PRK13640 3 DNIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskiTVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 396 RDAM-------DDK---KTVWEEVSNG--------QDILTIGNFEIpsrAYVGRFNFKGVDQQKrvgeLSGGERGRLHLA 457
Cdd:PRK13640 83 REKVgivfqnpDNQfvgATVGDDVAFGlenravprPEMIKIVRDVL---ADVGMLDYIDSEPAN----LSGGQKQRVAIA 155
|
170 180
....*....|....*....|
gi 1735515619 458 KLLQRGGNVLLLDEPTNDLD 477
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLD 175
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-195 |
4.17e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.14 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 27 SLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE--------------ARPqpgikIGYLPQEPKLEPQQTVREAVe 92
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSltlngqdhtttppsRRP-----VSMLFQENNLFSHLTVAQNI- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 93 eavsevksaltrldevyALYADPDAdfdKLAAEQ-ANLEAIIQAHdghNLDNQLERaadalrLPdwdakiEHLSGGERRR 171
Cdd:PRK10771 93 -----------------GLGLNPGL---KLNAAQrEKLHAIARQM---GIEDLLAR------LP------GQLSGGQRQR 137
|
170 180
....*....|....*....|....
gi 1735515619 172 VALCRLLLEKPDMLLLDEPTNHLD 195
Cdd:PRK10771 138 VALARCLVREQPILLLDEPFSALD 161
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-230 |
4.34e-12 |
|
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: 66.24 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 32 PGAKIGVLGLNGAGKSTLLRIMAGvdkefegEARPQPGikigylpqepKLEPQQTVREAVEE-AVSEVKSALTRL--DEV 108
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAG-------KLKPNLG----------KFDDPPDWDEILDEfRGSELQNYFTKLleGDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 109 YALYADPDADFDKLAAEQANLEAIIQAHDGHNLDNQLERaadaLRL-PDWDAKIEHLSGGERRRVALCRLLLEKPDMLLL 187
Cdd:cd03236 88 KVIVKPQYVDLIPKAVKGKVGELLKKKDERGKLDELVDQ----LELrHVLDRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1735515619 188 DEPTNHLDAE---SVAWLERFLHDYEGTVVAITHDRYFLDNVAGWI 230
Cdd:cd03236 164 DEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
321-501 |
4.44e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 66.71 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 321 GDKVIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQFRDAM 399
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENIPAMSRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 400 DDKKTVWEEVSNGQDILTIGNFEIPSRAY------------------VGrfnFKGVDQQKRvGELSGGERGRLHLAKLLQ 461
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDNVAYPLREHtqlpapllhstvmmkleaVG---LRGAAKLMP-SELSGGMARRAALARAIA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1735515619 462 RGGNVLLLDEPTNDLDVETLRALENAILEFPGC----AMVISHD 501
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlgvtCVVVSHD 203
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
322-477 |
4.54e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.55 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 322 DKVIEVQNLTKSYGD--RTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQFRda 398
Cdd:PRK13632 5 SVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKENLKEIR-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 399 mddKKtvweevsngqdiltIG-NFEIPSRAYVG--------------RFNFKGV-----DQQKRVG----------ELSG 448
Cdd:PRK13632 83 ---KK--------------IGiIFQNPDNQFIGatveddiafglenkKVPPKKMkdiidDLAKKVGmedyldkepqNLSG 145
|
170 180
....*....|....*....|....*....
gi 1735515619 449 GERGRLHLAKLLQRGGNVLLLDEPTNDLD 477
Cdd:PRK13632 146 GQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
340-501 |
4.61e-12 |
|
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: 65.95 E-value: 4.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 340 IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQ---FRD-AMDDKKTVWEEVSNGQD 414
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQITEPGPDRmvvFQNySLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 415 ILtIGNFEIPSRAYVGRFNFKGVD----QQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILE 490
Cdd:TIGR01184 81 RV-LPDLSKSERRAIVEEHIALVGlteaADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170
....*....|....*.
gi 1735515619 491 F-----PGCAMViSHD 501
Cdd:TIGR01184 160 IweehrVTVLMV-THD 174
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
23-219 |
4.92e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 66.64 E-value: 4.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQpGIKIGYlPQEPKLEPQQTVREAVEEAVsevksal 102
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIK-GEPIKY-DKKSLLEVRKTVGIVFQNPD------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 103 trlDEVYALYADPDADFDKLaaeqaNLeaiiqahdGHNLDNQLERAADALR---LPDWDAKI-EHLSGGERRRVALCRLL 178
Cdd:PRK13639 89 ---DQLFAPTVEEDVAFGPL-----NL--------GLSKEEVEKRVKEALKavgMEGFENKPpHHLSGGQKKRVAIAGIL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1735515619 179 LEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHD 219
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGiTIIISTHD 196
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
325-484 |
5.09e-12 |
|
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: 68.16 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSY-GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQFR------ 396
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLdGVPVSSLDQDEVRrrvsvc 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 397 --------------------DAMDdkktvwEEVSngqDILTIGNFEIPSRAYVGrfnfkGVDQqkRVGE----LSGGERG 452
Cdd:TIGR02868 415 aqdahlfdttvrenlrlarpDATD------EELW---AALERVGLADWLRALPD-----GLDT--VLGEggarLSGGERQ 478
|
170 180 190
....*....|....*....|....*....|..
gi 1735515619 453 RLHLAKLLQRGGNVLLLDEPTNDLDVETLRAL 484
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADEL 510
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-242 |
7.35e-12 |
|
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: 65.91 E-value: 7.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQpGI-------------KIGYLPQEPKlepQQ 85
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD-GLdtldeenlweirkKVGMVFQNPD---NQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 TVREAVEEAV-----------SEVKsalTRLDEvyalyadpdadfdklAAEQANLEaiiqahdghnldNQLERAadalrl 154
Cdd:TIGR04520 90 FVGATVEDDVafglenlgvprEEMR---KRVDE---------------ALKLVGME------------DFRDRE------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 155 PdwdakiEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLERFLHDYEG-TVVAITHDryfLDNV--AG 228
Cdd:TIGR04520 134 P------HLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGrkeVLETIRKLNKEEGiTVISITHD---MEEAvlAD 204
|
250
....*....|....*...
gi 1735515619 229 WILELDRG----EGIPWE 242
Cdd:TIGR04520 205 RVIVMNKGkivaEGTPRE 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
328-477 |
7.47e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 65.30 E-value: 7.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 328 QNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMG-ETVVL----------------- 389
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdEDISLlplhararrgigylpqe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 390 ASVDQFRDAMDDKKTVWEEvsngQDILTIGNFEIPSRAYVGRFNFKGVdqQKRVGE-LSGGERGRLHLAKLLQRGGNVLL 468
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQI----RDDLSAEQREDRANELMEEFHIEHL--RDSMGQsLSGGERRRVEIARALAANPKFIL 160
|
....*....
gi 1735515619 469 LDEPTNDLD 477
Cdd:PRK10895 161 LDEPFAGVD 169
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
289-489 |
7.55e-12 |
|
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: 68.23 E-value: 7.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 289 KARMA--RFDE--LNSGEYQKRNETNELFIPpgprLGDkvIEVQNLTKSYG-DRTLIDDLSFSIPKGAIVGIIGANGAGK 363
Cdd:TIGR01193 440 AARVAnnRLNEvyLVDSEFINKKKRTELNNL----NGD--IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGK 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 364 STLFRMLSGQEQPDAGSITMGETVvLASVD--QFRDAMD---------------------DKKTVWEEVSNGQDILTI-G 419
Cdd:TIGR01193 514 STLAKLLVGFFQARSGEILLNGFS-LKDIDrhTLRQFINylpqepyifsgsilenlllgaKENVSQDEIWAACEIAEIkD 592
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 420 NFEIPSRAYVGRFNFKGvdqqkrvGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAIL 489
Cdd:TIGR01193 593 DIENMPLGYQTELSEEG-------SSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLL 655
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-227 |
8.06e-12 |
|
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: 66.62 E-value: 8.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 21 HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE---------FEG---------EARPQPGIKIGYLPQEPK-- 80
Cdd:COG0444 19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgitsgeilFDGedllklsekELRKIRGREIQMIFQDPMts 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 81 LEPQQTVREAVEEAvsevksaltrldevyalyadpdadfdklaaeqanleaiIQAHDGHNLDNQLERAADALR---LPDW 157
Cdd:COG0444 99 LNPVMTVGDQIAEP--------------------------------------LRIHGGLSKAEARERAIELLErvgLPDP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 158 DAKIE---H-LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHD----RYFLDN 225
Cdd:COG0444 141 ERRLDrypHeLSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqAQILNLLKDLQRELGLAILFITHDlgvvAEIADR 220
|
..
gi 1735515619 226 VA 227
Cdd:COG0444 221 VA 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
20-217 |
9.71e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 65.30 E-value: 9.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG--------------EARPQPGIkiGYLPQEPklepqq 85
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGniiiddedisllplHARARRGI--GYLPQEA------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 tvreaveeavsevkSALTRLdevyalyadpdADFDklaaeqaNLEAIIQAHDGHNLDNQLERAADALRlpdwDAKIEHL- 164
Cdd:PRK10895 88 --------------SIFRRL-----------SVYD-------NLMAVLQIRDDLSAEQREDRANELME----EFHIEHLr 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 165 -------SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERF---LHDYeGTVVAIT 217
Cdd:PRK10895 132 dsmgqslSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIiehLRDS-GLGVLIT 193
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
325-477 |
1.04e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 65.27 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYG----DRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVL------ASVDQ 394
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpgadrGVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 395 fRDAMDDKKTVWEEVSNGQDILTIGNFEIPSRA--YVGRFNFKGVdQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEP 472
Cdd:COG4525 84 -KDALLPWLNVLDNVAFGLRLRGVPKAERRARAeeLLALVGLADF-ARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
....*
gi 1735515619 473 TNDLD 477
Cdd:COG4525 162 FGALD 166
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-191 |
1.06e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.35 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR----------PQPGIK--IGYLPQEPKLE---PQ 84
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRldgkpvrirsPRDAIRagIAYVPEDRKGEglvLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 85 QTVREAVeeavsevksALTRLDEV-YALYADPdadfdklAAEQANLEAIIQAHDghnldnqleraadaLRLPDWDAKIEH 163
Cdd:COG1129 345 LSIRENI---------TLASLDRLsRGGLLDR-------RRERALAEEYIKRLR--------------IKTPSPEQPVGN 394
|
170 180
....*....|....*....|....*...
gi 1735515619 164 LSGGERRRVALCRLLLEKPDMLLLDEPT 191
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
322-490 |
1.11e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.54 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 322 DKVIEVQNLTKSY-GDRTL-IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVlaSVDQFRDAM 399
Cdd:PRK13648 5 NSIIVFKNVSFQYqSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI--TDDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 400 DDKKTVWEEVSNgQDILTI---------GNFEIPSRAYVGRFN--FKGVDQQKRVGE----LSGGERGRLHLAKLLQRGG 464
Cdd:PRK13648 83 KHIGIVFQNPDN-QFVGSIvkydvafglENHAVPYDEMHRRVSeaLKQVDMLERADYepnaLSGGQKQRVAIAGVLALNP 161
|
170 180
....*....|....*....|....*.
gi 1735515619 465 NVLLLDEPTNDLDVETLRALENAILE 490
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRK 187
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-89 |
1.13e-11 |
|
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: 64.48 E-value: 1.13e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 17 PPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA----RPQPGIKIGYlpqepKLEPQQTVRE 89
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVtvrgRVSSLLGLGG-----GFNPELTGRE 103
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
322-509 |
1.22e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 65.52 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 322 DKVIEVQNLTKSYG---DRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQFRD 397
Cdd:PRK13650 2 SNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 398 AM-------DDK---KTVWEEVSNGQDILTIGNFEIPSR-----AYVGRFNFKgvdqQKRVGELSGGERGRLHLAKLLQR 462
Cdd:PRK13650 82 KIgmvfqnpDNQfvgATVEDDVAFGLENKGIPHEEMKERvnealELVGMQDFK----EREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1735515619 463 GGNVLLLDEPTNDLD----VETLRALENAILEFPGCAMVISHDrwfLDRIA 509
Cdd:PRK13650 158 RPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD---LDEVA 205
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-196 |
1.34e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.99 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 18 PKRHILKDISLSFFPGAKIGVLGLNGAGKSTLL-----RIMAGVDKE----FEGEARPQPGIKI--GYLPQEPKLEPQQT 86
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVKGSgsvlLNGMPIDAKEMRAisAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 87 VREAVeeavseVKSALTRLDEVYALyadpdadfdklAAEQANLEAIIQahdghnlDNQLERAADAL-RLPDwdaKIEHLS 165
Cdd:TIGR00955 116 VREHL------MFQAHLRMPRRVTK-----------KEKRERVDEVLQ-------ALGLRKCANTRiGVPG---RVKGLS 168
|
170 180 190
....*....|....*....|....*....|.
gi 1735515619 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDA 196
Cdd:TIGR00955 169 GGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
21-237 |
1.42e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.21 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 21 HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpqpgIKIGylpqepklepqqtvreavEEAVSEVKS 100
Cdd:PRK11000 17 VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD------LFIG------------------EKRMNDVPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 101 ALTRLDEV---YALY-----ADPDADFDKLA-AEQANLeaiiqahdghnlDNQLERAADALRLPDW-DAKIEHLSGGERR 170
Cdd:PRK11000 73 AERGVGMVfqsYALYphlsvAENMSFGLKLAgAKKEEI------------NQRVNQVAEVLQLAHLlDRKPKALSGGQRQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1735515619 171 RVALCRLLLEKPDMLLLDEPTNHLDAE-------SVAWLERFLhdyEGTVVAITHDRYFLDNVAGWILELDRGE 237
Cdd:PRK11000 141 RVAIGRTLVAEPSVFLLDEPLSNLDAAlrvqmriEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGR 211
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-224 |
1.46e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdkefegEARPQPGIKIGYLPQEPkLEPQQTVREAVeeavsev 98
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG-------ALKGTPVAGCVDVPDNQ-FGREASLIDAI------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 99 ksaltrldevyalyadpDADFDKLAAeqanLEAIIQAhdGHNlDNQLeraadalrlpdWDAKIEHLSGGERRRVALCRLL 178
Cdd:COG2401 107 -----------------GRKGDFKDA----VELLNAV--GLS-DAVL-----------WLRRFKELSTGQKFRFRLALLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1735515619 179 LEKPDMLLLDEPTNHLD---AESVAW-LERFLHDYEGTVVAITHDRYFLD 224
Cdd:COG2401 152 AERPKLLVIDEFCSHLDrqtAKRVARnLQKLARRAGITLVVATHHYDVID 201
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
22-244 |
1.58e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 64.34 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------------IMAGVD----KEFEGEARPQPGIKIgylpQEPKLEPQ 84
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdlIVDGLKvndpKVDERLIRQEAGMVF----QQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 85 QTVREAVEEAVSEVKSAltrldevyalyadpdadfDKLAAEQanleaiiQAHDghnLDNQLERAADALRLPdwdakiEHL 164
Cdd:PRK09493 92 LTALENVMFGPLRVRGA------------------SKEEAEK-------QARE---LLAKVGLAERAHHYP------SEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDyEG-TVVAITHDRYFLDNVAGWILELDRGeGIP 240
Cdd:PRK09493 138 SGGQQQRVAIARALAVKPKLMLFDEPTSALDPElrhEVLKVMQDLAE-EGmTMVIVTHEIGFAEKVASRLIFIDKG-RIA 215
|
....
gi 1735515619 241 WEGN 244
Cdd:PRK09493 216 EDGD 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-237 |
1.66e-11 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 64.43 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 17 PPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRI------------------MAGVDKEFegeARPQpgikIGYLPQE 78
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLiqrfyvpengrvlvdghdLALADPAW---LRRQ----VGVVLQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 79 PKLEpQQTVREAVeeavsevksALTrldevyalyaDPDADFDKL--AAEQANLEAII-QAHDGHNldnQL--ERAADalr 153
Cdd:cd03252 85 NVLF-NRSIRDNI---------ALA----------DPGMSMERVieAAKLAGAHDFIsELPEGYD---TIvgEQGAG--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 154 lpdwdakiehLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG--TVVAITHdRYFLDNVAGWIL 231
Cdd:cd03252 139 ----------LSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAgrTVIIIAH-RLSTVKNADRII 207
|
....*.
gi 1735515619 232 ELDRGE 237
Cdd:cd03252 208 VMEKGR 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
324-484 |
1.84e-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: 63.34 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTK------SYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQ--EQPDAGSITMGETVVlaSVDQF 395
Cdd:cd03213 3 TLSFRNLTVtvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPL--DKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 396 RDAM-----DD----KKTVWEevsngqdiltigNFEIPSrayvgrfNFKGvdqqkrvgeLSGGERGRLHLA-KLLQRGGn 465
Cdd:cd03213 81 RKIIgyvpqDDilhpTLTVRE------------TLMFAA-------KLRG---------LSGGERKRVSIAlELVSNPS- 131
|
170 180
....*....|....*....|....*.
gi 1735515619 466 VLLLDEPTNDLD-------VETLRAL 484
Cdd:cd03213 132 LLFLDEPTSGLDsssalqvMSLLRRL 157
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
19-224 |
1.91e-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: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK--------EFEG--------EARPQPGIKIGYlpQEPKLE 82
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyevtsgtiLFKGqdllelepDERARAGLFLAF--QYPEEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 83 PQQTVREAVEEAVSEVKSAltRLDEVYalyadPDADFDKLAAEQANLEAIIQAHdghnldnqLERAADalrlpdwdakiE 162
Cdd:TIGR01978 90 PGVSNLEFLRSALNARRSA--RGEEPL-----DLLDFEKLLKEKLALLDMDEEF--------LNRSVN-----------E 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 163 HLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY---EGTVVAITHDRYFLD 224
Cdd:TIGR01978 144 GFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLN 208
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
324-507 |
2.05e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMgetvvlasvdqFRDAMDDKK 403
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILF-----------ERQSIKKDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 404 TVWEE----VSNGQDI---LTIGN---FEIPSRAyvgrfNFKGVDQQKRV-----------GELSGGERGRLHLAKLLQR 462
Cdd:PRK13540 70 CTYQKqlcfVGHRSGInpyLTLREnclYDIHFSP-----GAVGITELCRLfslehlidypcGLLSSGQKRQVALLRLWMS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1735515619 463 GGNVLLLDEPTNDLDVETLRALENAILEFP---GCAMVISHDRWFLDR 507
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSLLTIITKIQEHRakgGAVLLTSHQDLPLNK 192
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-243 |
2.08e-11 |
|
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: 63.67 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 25 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQpGIKIGYLP----------QEPKLEPQQTVREAVEEA 94
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN-GVDVTAAPpadrpvsmlfQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 95 VSevksalTRLdevyalyadpdadfdKLAAEQANLEAIIQAHDGhnLDNQLeraadaLRLPDwdakieHLSGGERRRVAL 174
Cdd:cd03298 95 LS------PGL---------------KLTAEDRQAIEVALARVG--LAGLE------KRLPG------ELSGGERQRVAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 175 CRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEgIPWEG 243
Cdd:cd03298 140 ARVLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR-IAAQG 211
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
329-488 |
2.12e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 64.73 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 329 NLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLA-SVDQFRDAMDDKKTVWE 407
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGrSIFNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 408 --EVSNGQDILTIGNFEIPSRAY--VGRFNFKGVDQQK--RVG--------------ELSGGERGRLHLAKLLQRGGNVL 467
Cdd:PRK14271 106 lfQRPNPFPMSIMDNVLAGVRAHklVPRKEFRGVAQARltEVGlwdavkdrlsdspfRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180
....*....|....*....|.
gi 1735515619 468 LLDEPTNDLDVETLRALENAI 488
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFI 206
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
22-237 |
2.17e-11 |
|
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: 63.67 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKST----LLRIMAGVDKEFEGEARPQPGI-------KIGYLPQEPKLEpQQTVREa 90
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVELSSGSILIDGVDISKIglhdlrsRISIIPQDPVLF-SGTIRS- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 91 veeavsevksaltRLDEvYALYADpdadfDKL--AAEQANLEAIIQAHDGHnLDNQLERAAdalrlpdwdakiEHLSGGE 168
Cdd:cd03244 97 -------------NLDP-FGEYSD-----EELwqALERVGLKEFVESLPGG-LDTVVEEGG------------ENLSVGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAITH--------DRyfldnvagwILELDRGE 237
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAHrldtiidsDR---------ILVLDKGR 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
325-509 |
2.26e-11 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 64.59 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRT-----LID-------------------DLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGS 380
Cdd:cd03294 1 IKIKGLYKIFGKNPqkafkLLAkgkskeeilkktgqtvgvnDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 381 ITM-GETVVLASVDQFRDAMDDK-------------KTVWEEVSNGQDILTIGNFEIPSRA-----YVGRFNFKgvdqQK 441
Cdd:cd03294 81 VLIdGQDIAAMSRKELRELRRKKismvfqsfallphRTVLENVAFGLEVQGVPRAEREERAaealeLVGLEGWE----HK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 442 RVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAIL----EFPGCAMVISHDrwfL-------DRIA 509
Cdd:cd03294 157 YPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLrlqaELQKTIVFITHD---LdealrlgDRIA 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-219 |
2.40e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 64.34 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQpGIKIGYLP------------QEPKL--EPQQ 85
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILID-GKDVTKLPeykrakyigrvfQDPMMgtAPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 TVREAVEEAVSEVKS-----ALTRldEVYALYAdpdadfDKLAAeqanleaiiqahdghnLDNQLERaadalRLpdwDAK 160
Cdd:COG1101 98 TIEENLALAYRRGKRrglrrGLTK--KRRELFR------ELLAT----------------LGLGLEN-----RL---DTK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 161 IEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWL-ERFLHDYEGTVVAITHD 219
Cdd:COG1101 146 VGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDpktAALVLELtEKIVEENNLTTLMVTHN 208
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-509 |
2.91e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.03 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKS-TLLRIMAGVDkefegearpQPGikiGYLPQEPKL--EPQQTVREAVEEAVSEVK 99
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLE---------QAG---GLVQCDKMLlrRRSRQVIELSEQSAAQMR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 100 SalTRLDEVYALYADPDADFDKLAAEQANLEAIIQAHDGHNLDNQL---ERAADALRLPDWDAKI----EHLSGGERRRV 172
Cdd:PRK10261 100 H--VRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMveaKRMLDQVRIPEAQTILsrypHQLSGGMRQRV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 173 ALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIPwegnySSW 248
Cdd:PRK10261 178 MIAMALSCRPAVLIADEPTTALDvtiqAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVE-----TGS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 249 LEQkekrleqeqaAENARQKSIAKELewVRQNPKGRQAKSKARMARFDELNSGEYQKRNETNE--LFIPpgprlGDKVIE 326
Cdd:PRK10261 253 VEQ----------IFHAPQHPYTRAL--LAAVPQLGAMKGLDYPRRFPLISLEHPAKQEPPIEqdTVVD-----GEPILQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 327 VQNLTKSYGDRT-----------LIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQ 394
Cdd:PRK10261 316 VRNLVTRFPLRSgllnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFnGQRIDTLSPGK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 395 FRDAMDDKKTVWEEVSNGQDI-LTIGnFEIPSRAYVGRFnFKGVDQQKRVG------------------ELSGGERGRLH 455
Cdd:PRK10261 396 LQALRRDIQFIFQDPYASLDPrQTVG-DSIMEPLRVHGL-LPGKAAAARVAwllervgllpehawryphEFSGGQRQRIC 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1735515619 456 LAKLLQRGGNVLLLDEPTNDLDVETLRALENAIL----EFPGCAMVISHDRWFLDRIA 509
Cdd:PRK10261 474 IARALALNPKVIIADEAVSALDVSIRGQIINLLLdlqrDFGIAYLFISHDMAVVERIS 531
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-237 |
3.03e-11 |
|
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: 62.87 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAgvdkefeGEARPQPGI-----KIGYLPQEPKLEPqQTVREAV----- 91
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALL-------GELEKLSGSvsvpgSIAYVSQEPWIQN-GTIRENIlfgkp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 92 --EEavsevksaltRLDEVY---ALyadpDADFDKLAaeqanleaiiqahDGhnlDNQL--ERAADalrlpdwdakiehL 164
Cdd:cd03250 92 fdEE----------RYEKVIkacAL----EPDLEILP-------------DG---DLTEigEKGIN-------------L 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1735515619 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWL-ER----FLHDyEGTVVAITHDRYFLDNVAgWILELDRGE 237
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENcilgLLLN-NKTRILVTHQLQLLPHAD-QIVVLDNGR 204
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
329-508 |
3.06e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 63.68 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 329 NLTKSYGDRTL----IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVV--------------L 389
Cdd:PRK11629 10 NLCKRYQEGSVqtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFnGQPMSklssaakaelrnqkL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 390 ASVDQFRDAMDDkktvWEEVSNGQDILTIGNF---EIPSRAyvgRFNFKGVDQQKRV----GELSGGERGRLHLAKLLQR 462
Cdd:PRK11629 90 GFIYQFHHLLPD----FTALENVAMPLLIGKKkpaEINSRA---LEMLAAVGLEHRAnhrpSELSGGERQRVAIARALVN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1735515619 463 GGNVLLLDEPTNDLDVETLRALENAILEF---PGCA-MVISHDRWFLDRI 508
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELnrlQGTAfLVVTHDLQLAKRM 212
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-237 |
3.20e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.26 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkefegeARPQPGikiGYLPQEPKLEPQQTVREAVEEAVSEVksa 101
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGL-------LRPQKG---AVLWQGKPLDYSKRGLLALRQQVATV--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 102 lTRLDEVYALYADPDADfdkLAAEQANLeaiiqahdGHNLDNQLERAADALRLPDWD----AKIEHLSGGERRRVALCRL 177
Cdd:PRK13638 83 -FQDPEQQIFYTDIDSD---IAFSLRNL--------GVPEAEITRRVDEALTLVDAQhfrhQPIQCLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 178 LLEKPDMLLLDEPTNHLD----AESVAWLERFLHdyEGTVVAI-THDRYFLDNVAGWILELDRGE 237
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDpagrTQMIAIIRRIVA--QGNHVIIsSHDIDLIYEISDAVYVLRQGQ 213
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
329-477 |
3.98e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 64.67 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 329 NLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGET-------------VVLASVdqf 395
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvppaergvgMVFQSY--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 396 rdAMDDKKTVWEEVSNGQDILTIGNFEIPSRayvgrfnfkgVDQ-----------QKRVGELSGGERGRLHLAKLLQRGG 464
Cdd:PRK11000 85 --ALYPHLSVAENMSFGLKLAGAKKEEINQR----------VNQvaevlqlahllDRKPKALSGGQRQRVAIGRTLVAEP 152
|
170
....*....|...
gi 1735515619 465 NVLLLDEPTNDLD 477
Cdd:PRK11000 153 SVFLLDEPLSNLD 165
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
340-523 |
4.34e-11 |
|
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: 61.96 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 340 IDDLSFSIPKGAIVGIIGANGAGKSTL-FRML--SGQEQPDAGSITMGETVVLaSVDQFRDAMDdkktvweevsNGQDIL 416
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLvNEGLyaSGKARLISFLPKFSRNKLI-FIDQLQFLID----------VGLGYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 417 TIGnfeipsrayvgrfnfkgvdqqKRVGELSGGERGRLHLAKLLQRG--GNVLLLDEPTNDLDVETLRALENAILEFPGC 494
Cdd:cd03238 80 TLG---------------------QKLSTLSGGELQRVKLASELFSEppGTLFILDEPSTGLHQQDINQLLEVIKGLIDL 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 1735515619 495 A---MVISHDRWFLDRiATHILDYG-----DEGKVTF 523
Cdd:cd03238 139 GntvILIEHNLDVLSS-ADWIIDFGpgsgkSGGKVVF 174
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
325-480 |
4.41e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 63.57 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVL------ASVDQfRDA 398
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgaerGVVFQ-NEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 399 MDDKKTVWEEVSNGqdiLTIGNFEIPSRAYVGRFNFKGVD----QQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTN 474
Cdd:PRK11248 81 LLPWRNVQDNVAFG---LQLAGVEKMQRLEIAHQMLKKVGlegaEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
....*.
gi 1735515619 475 DLDVET 480
Cdd:PRK11248 158 ALDAFT 163
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
324-489 |
5.14e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 65.81 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRT--LIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVD-------- 393
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISdvhqnmgy 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 394 --QFrDAMDDKKTVWEEV--------SNGQDILTIGNFEIPS---RAYVGRFnfkgvdqqkrVGELSGGERGRLHLAKLL 460
Cdd:TIGR01257 2017 cpQF-DAIDDLLTGREHLylyarlrgVPAEEIEKVANWSIQSlglSLYADRL----------AGTYSGGNKRKLSTAIAL 2085
|
170 180
....*....|....*....|....*....
gi 1735515619 461 QRGGNVLLLDEPTNDLDVETLRALENAIL 489
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-505 |
5.38e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 63.01 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGEtVVLASVDQFR-DAMDDK 402
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGE-VYLDGQDIFKmDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 403 K---------------TVWEEVSNGQDI--LTIGNFEIPSRAYVGRFNFKGVDQQKR-----VGELSGGERGRLHLAKLL 460
Cdd:PRK14247 82 RrvqmvfqipnpipnlSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLWDEVKDrldapAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 461 QRGGNVLLLDEPTNDLDVETLRALENAILE------------FPGCAMVISHDRWFL 505
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLElkkdmtivlvthFPQQAARISDYVAFL 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
321-512 |
6.26e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.14 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 321 GDKVIEVQNLTKSY---GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFR- 396
Cdd:PRK14246 4 GKSAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 397 DAMDDKK---TVWEEVSNGQDILTIGNFEIP--SRAYVGRFNFKGVDQQ--KRVG--------------ELSGGERGRLH 455
Cdd:PRK14246 84 DAIKLRKevgMVFQQPNPFPHLSIYDNIAYPlkSHGIKEKREIKKIVEEclRKVGlwkevydrlnspasQLSGGQQQRLT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 456 LAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFPG--CAMVISHDRWFLDRIATHI 512
Cdd:PRK14246 164 IARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYV 222
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
342-477 |
6.46e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 63.50 E-value: 6.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 342 DLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQfRDAMDDKKTV-----------WEEVS 410
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKN-KKLKPLRKKVgivfqfpehqlFEETV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 411 NgQDILtignfeipsrayVGRFNFkGVDQQ----------KRVG-----------ELSGGERGRLHLAKLLQRGGNVLLL 469
Cdd:PRK13634 104 E-KDIC------------FGPMNF-GVSEEdakqkaremiELVGlpeellarspfELSGGQMRRVAIAGVLAMEPEVLVL 169
|
....*...
gi 1735515619 470 DEPTNDLD 477
Cdd:PRK13634 170 DEPTAGLD 177
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
343-501 |
7.48e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.64 E-value: 7.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 343 LSFSIPKGAIVGIIGANGAGKSTLFRMLSGQeQPDAGSITMGETVV----LASVDQFRD----------AMDdkktVWEE 408
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLeawsAAELARHRAylsqqqtppfAMP----VFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 409 VS-NGQDILTIGNFEIPSRAYVGRFNFKgvDQQKR-VGELSGGERGRLHLAK-LLQ------RGGNVLLLDEPTNDLDVE 479
Cdd:PRK03695 90 LTlHQPDKTRTEAVASALNEVAEALGLD--DKLGRsVNQLSGGEWQRVRLAAvVLQvwpdinPAGQLLLLDEPMNSLDVA 167
|
170 180
....*....|....*....|....*
gi 1735515619 480 TLRALENAILEFP--GCAMVIS-HD 501
Cdd:PRK03695 168 QQAALDRLLSELCqqGIAVVMSsHD 192
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
23-229 |
7.54e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.18 E-value: 7.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpqpgIKIGYLPQEPKlepqqTVREAVEEAVSEVKSAL 102
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGT------IEWIFKDEKNK-----KKTKEKEKVLEKLVIQK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 103 TRLDEV------------------YALYadpdadfdklaaEQANLEAIIQAHDGHNLDNQ--LERAADALRLPDWDAKIE 162
Cdd:PRK13651 92 TRFKKIkkikeirrrvgvvfqfaeYQLF------------EQTIEKDIIFGPVSMGVSKEeaKKRAAKYIELVGLDESYL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 163 H-----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA-WLERF--LHDYEGTVVAITHDryfLDNVAGW 229
Cdd:PRK13651 160 QrspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKeILEIFdnLNKQGKTIILVTHD---LDNVLEW 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-501 |
7.71e-11 |
|
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: 64.71 E-value: 7.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKS----TLLRIMAGVDKEFEGEAR---------PQP------GIKIGYLPQEP- 79
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILfdgqdllglSERelrrirGNRIAMIFQEPm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 80 -KLEPQQTVreavEEAVSEVksaltrldevyalyadpdadfdklaaeqanleaiIQAHDGHNLDNQLERAADALR---LP 155
Cdd:COG4172 103 tSLNPLHTI----GKQIAEV----------------------------------LRLHRGLSGAAARARALELLErvgIP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 156 DWDAKIE---H-LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHD----RYFL 223
Cdd:COG4172 145 DPERRLDaypHqLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqAQILDLLKDLQRELGMALLLITHDlgvvRRFA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 224 DNVAgwileldrgegipwegnysswLEQKEKRLEQEQAAE---NAR----QKSIAKElewvrqnPKGRQakskarmarfd 296
Cdd:COG4172 225 DRVA---------------------VMRQGEIVEQGPTAElfaAPQhpytRKLLAAE-------PRGDP----------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 297 elnsgeyqkrnetnelfiPPGPRLGDKVIEVQNLTKSY-----------GDRTLIDDLSFSIPKGAIVGIIGANGAGKST 365
Cdd:COG4172 266 ------------------RPVPPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKST 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 366 LFRMLSGQeQPDAGSIT-MGETVVLASVDQFRD--------------AMDDKKTVWEEVSNGQDILTIGnfeiPSRAyvg 430
Cdd:COG4172 328 LGLALLRL-IPSEGEIRfDGQDLDGLSRRALRPlrrrmqvvfqdpfgSLSPRMTVGQIIAEGLRVHGPG----LSAA--- 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 431 rfnfkgvDQQKRVG------------------ELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDV-------ETLRALE 485
Cdd:COG4172 400 -------ERRARVAealeevgldpaarhryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVsvqaqilDLLRDLQ 472
|
570
....*....|....*..
gi 1735515619 486 NailEFpGCAMV-ISHD 501
Cdd:COG4172 473 R---EH-GLAYLfISHD 485
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
18-219 |
9.10e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 62.41 E-value: 9.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 18 PKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGEARPQPGIKIGYLPQEPKLEPQQTVREAV 91
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPyqhgsiTLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 92 EeavsevksaltrldevYALyadpdadfdKLAaeqanleaiiqahdGHNLDNQLERAADALRLPDWDA----KIEHLSGG 167
Cdd:PRK11248 92 A----------------FGL---------QLA--------------GVEKMQRLEIAHQMLKKVGLEGaekrYIWQLSGG 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 168 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL----HDYEGTVVAITHD 219
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLlklwQETGKQVLLITHD 188
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
325-487 |
9.38e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 64.48 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLT-KSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQeQPDAGSITMGeTVVLASVD--QFRdamdd 401
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKIN-GIELRELDpeSWR----- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 402 KKTVWEevsnGQ----------DILTIGNFEIP--------SRAYVGRF---NFKGVDQQkrVGE----LSGGERGRLHL 456
Cdd:PRK11174 423 KHLSWV----GQnpqlphgtlrDNVLLGNPDASdeqlqqalENAWVSEFlplLPQGLDTP--IGDqaagLSVGQAQRLAL 496
|
170 180 190
....*....|....*....|....*....|....*
gi 1735515619 457 AKLLQRGGNVLLLDEPTNDLDVET----LRALENA 487
Cdd:PRK11174 497 ARALLQPCQLLLLDEPTASLDAHSeqlvMQALNAA 531
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
343-501 |
9.88e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.17 E-value: 9.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 343 LSFSIPKGAIVGIIGANGAGKSTLFRMLSGqEQPDAGSITMGETVV----LASVDQFRD----------AMDdkktVWE- 407
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLsdwsAAELARHRAylsqqqsppfAMP----VFQy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 408 -------EVSNGQDILTIGnfEIPSRayvgrfnFKGVDQQKR-VGELSGGERGRLHLAK-LLQ------RGGNVLLLDEP 472
Cdd:COG4138 90 lalhqpaGASSEAVEQLLA--QLAEA-------LGLEDKLSRpLTQLSGGEWQRVRLAAvLLQvwptinPEGQLLLLDEP 160
|
170 180 190
....*....|....*....|....*....|..
gi 1735515619 473 TNDLDVETLRALENAILEF--PGCAMVIS-HD 501
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELcqQGITVVMSsHD 192
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
11-219 |
1.25e-10 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 61.93 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 11 RVGKVVPPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-------ARPQPGI----KIGYLPQEP 79
Cdd:cd03295 5 NVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEifidgedIREQDPVelrrKIGYVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 80 KLEPQQTVREAVE-----EAVSEVKSAlTRLDEVYALYADPDADFdklaaeqanleaiiqahdghnldnqleraadALRL 154
Cdd:cd03295 85 GLFPHMTVEENIAlvpklLKWPKEKIR-ERADELLALVGLDPAEF-------------------------------ADRY 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1735515619 155 PDwdakieHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA-------ESVAWLERFLHDyegTVVAITHD 219
Cdd:cd03295 133 PH------ELSGGQQQRVGVARALAADPPLLLMDEPFGALDPitrdqlqEEFKRLQQELGK---TIVFVTHD 195
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-218 |
1.28e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.10 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRI---MAGVDKE--------FEGEARPQPGI-------KIGYLPQEPK 80
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSinrMNDLNPEvtitgsivYNGHNIYSPRTdtvdlrkEIGMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 81 LEPQqTVREAVeeavsevksaltrldeVYALyadpdadfdKLAAEqanleaiiqaHDGHNLDNQLERAADALRLpdWDAK 160
Cdd:PRK14239 97 PFPM-SIYENV----------------VYGL---------RLKGI----------KDKQVLDEAVEKSLKGASI--WDEV 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 161 IEHL-------SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL----HDYegTVVAITH 218
Cdd:PRK14239 139 KDRLhdsalglSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLlglkDDY--TMLLVTR 205
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-236 |
1.31e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.43 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDkefegeaRPQPGiKIGYLPQEpklepqqtvreaveeaVSEVK 99
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIE-------RPSAG-KIWFSGHD----------------ITRLK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 100 SA----LTRldEVYALYADPDADFDKLAAEQANLEAIIQAHDGHNLDNQLERAADALRLPDWDAKIE-HLSGGERRRVAL 174
Cdd:PRK10908 71 NRevpfLRR--QIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPiQLSGGEQQRVGI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 175 CRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG---TVVAITHDRYFLDNVAGWILELDRG 236
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
335-477 |
1.63e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 61.27 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 335 GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQFRDAMDD--------KKTV 405
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDISTLKPEIYRQQVSYcaqtptlfGDTV 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1735515619 406 WEEVSNGQDILTIGNFEIPSRAYVGRFNFKGVDQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLD 477
Cdd:PRK10247 98 YDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-218 |
1.72e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 63.59 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 18 PKRHILKDISLSFFPGAKIGVLGLNGAGKST---LLR----------IMAGVD-KEFEGEARPQpgiKIGYLPQEPKLEp 83
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTvaaLLQnlyqptggqvLLDGVPlVQYDHHYLHR---QVALVGQEPVLF- 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 84 QQTVREAVeeavsevksaltrldeVYALYADPDADFdKLAAEQANleaiiqahdGHNLDNQLERAADAlrlpDWDAKIEH 163
Cdd:TIGR00958 568 SGSVRENI----------------AYGLTDTPDEEI-MAAAKAAN---------AHDFIMEFPNGYDT----EVGEKGSQ 617
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITH 218
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
330-522 |
1.78e-10 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 59.89 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 330 LTKSYGDRTLIDDLSfSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDagsitmgetvvlasvdqfrdamdDKKTVWeev 409
Cdd:cd03222 6 CVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPN-----------------------GDNDEW--- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 410 sngqDILTIGnfeipsrayvgrfnfkgVDQQKRvgELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVE----TLRALE 485
Cdd:cd03222 59 ----DGITPV-----------------YKPQYI--DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIR 115
|
170 180 190
....*....|....*....|....*....|....*...
gi 1735515619 486 NAILEFPGCAMVISHDRWFLDRIATHI-LDYGDEGKVT 522
Cdd:cd03222 116 RLSEEGKKTALVVEHDLAVLDYLSDRIhVFEGEPGVYG 153
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
325-516 |
1.84e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 61.63 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSY---------GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVV--LASVD 393
Cdd:PRK10419 4 LNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLakLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 394 Q----------FRD---AMDDKKTVWEEVSNGQDILTigNFEIPSRAYVGRFNFKGVD-----QQKRVGELSGGERGRLH 455
Cdd:PRK10419 84 RkafrrdiqmvFQDsisAVNPRKTVREIIREPLRHLL--SLDKAERLARASEMLRAVDlddsvLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 456 LAKLLQRGGNVLLLDEPTNDLDV----ETLRALENAILEFPGCAMVISHD----RWFLDRIAthILDYG 516
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDlrlvERFCQRVM--VMDNG 228
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-219 |
1.86e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.49 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 26 ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdKEFEGEAR---------PQPGIKI--GYLPQEPK----------LE-- 82
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQfagqpleawSAAELARhrAYLSQQQTppfampvfqyLTlh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 83 -PQQTVREAVEEAVSEVKSALtrldevyalyadpdadfdklaaeqanleaiiqahdghNLDNQLERAadalrlpdwdakI 161
Cdd:PRK03695 94 qPDKTRTEAVASALNEVAEAL-------------------------------------GLDDKLGRS------------V 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1735515619 162 EHLSGGERRRVALCRLLLE-----KPD--MLLLDEPTNHLDAESVAWLERFLHDYE---GTVVAITHD 219
Cdd:PRK03695 125 NQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
324-482 |
1.92e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.57 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLS----GQEQPDAGSITMGETVVLASvdqfRDAM 399
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSglitGDKSAGSHIELLGRTVQREG----RLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 400 DDKK------------------TVWEEVSNG--------QDILTIGNFEIPSRAY-----VGRFNFKgvdqQKRVGELSG 448
Cdd:PRK09984 80 DIRKsrantgyifqqfnlvnrlSVLENVLIGalgstpfwRTCFSWFTREQKQRALqaltrVGMVHFA----HQRVSTLSG 155
|
170 180 190
....*....|....*....|....*....|....
gi 1735515619 449 GERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLR 482
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESAR 189
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
336-484 |
1.92e-10 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 61.13 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 336 DRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQpdAGSITMGETVV-------------LASVDQFrDAMDDK 402
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSGQILFngqprkpdqfqkcVAYVRQD-DILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 403 KTVWEEV-----SNGQDILTigNFEIPSRAYVGRFNFKGVDQ--QKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTND 475
Cdd:cd03234 96 LTVRETLtytaiLRLPRKSS--DAIRKKRVEDVLLRDLALTRigGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170
....*....|....*.
gi 1735515619 476 LD-------VETLRAL 484
Cdd:cd03234 174 LDsftalnlVSTLSQL 189
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
38-218 |
1.94e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.58 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 38 VLGLNGAGKSTLLRIMAGVDKEFEGEAR--------PQPGI-------KIGYLPQEPKLEPQQTVREAVEeavsevksal 102
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVlngrvlfdAEKGIclppekrRIGYVFQDARLFPHYKVRGNLR---------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 103 trldevYALYADPDADFDKLAAeqanLEAIiqahdGHNLDnqleraadalRLPdwdakiEHLSGGERRRVALCRLLLEKP 182
Cdd:PRK11144 99 ------YGMAKSMVAQFDKIVA----LLGI-----EPLLD----------RYP------GSLSGGEKQRVAIGRALLTAP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1735515619 183 DMLLLDEPTNHLDA----ESVAWLERFLHDYEGTVVAITH 218
Cdd:PRK11144 148 ELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSH 187
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
23-219 |
1.97e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 61.65 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGearpqpgikigylpqepklepqqTVREAVEEAVSEVKSAL 102
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG-----------------------KVKIDGELLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 103 TRldEVYALYADPDADFdkLAAEQANLEAIIQAHDGHNLDNQLERAADAL---RLPDWDAK-IEHLSGGERRRVALCRLL 178
Cdd:PRK13642 80 RR--KIGMVFQNPDNQF--VGATVEDDVAFGMENQGIPREEMIKRVDEALlavNMLDFKTRePARLSGGQKQRVAVAGII 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1735515619 179 LEKPDMLLLDEPTNHLDAESVAWLERFLHD----YEGTVVAITHD 219
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEikekYQLTVLSITHD 200
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
19-226 |
2.29e-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: 60.23 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK--------EFEGE--------ARPQPGIKIGYlpQEPkle 82
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyevtegeiLFKGEditdlppeERARLGIFLAF--QYP--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 83 pqqtvreaveEAVSEVKSAltrldevyalyadpdaDFdklaaeqanleaiiqahdghnldnqleraadaLRLPDwdakiE 162
Cdd:cd03217 87 ----------PEIPGVKNA----------------DF--------------------------------LRYVN-----E 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 163 HLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERF---LHDYEGTVVAITHDRYFLDNV 226
Cdd:cd03217 104 GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVinkLREEGKSVLIITHYQRLLDYI 170
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
324-500 |
2.36e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQeQPDA---GSITM-GETVVLASVdqfRD-- 397
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFeGEELQASNI---RDte 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 398 -----------AMDDKKTVWEEVSNGQDILTIG--NF-EIPSRAY--VGRFNFkGVDQQKRVGELSGGERGRLHLAKLLQ 461
Cdd:PRK13549 81 ragiaiihqelALVKELSVLENIFLGNEITPGGimDYdAMYLRAQklLAQLKL-DINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1735515619 462 RGGNVLLLDEPTNDLDVETLRALENAI--LEFPGCAMV-ISH 500
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIrdLKAHGIACIyISH 201
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
325-477 |
2.70e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.20 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSY--GDRTL--IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVlASVDqfRDAMD 400
Cdd:PRK10535 5 LELKDIRRSYpsGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDV-ATLD--ADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 401 -----------DKKTVWEEVSNGQdiltigNFEIP--------------SRAYVGRFNFkGVDQQKRVGELSGGERGRLH 455
Cdd:PRK10535 82 qlrrehfgfifQRYHLLSHLTAAQ------NVEVPavyaglerkqrllrAQELLQRLGL-EDRVEYQPSQLSGGQQQRVS 154
|
170 180
....*....|....*....|..
gi 1735515619 456 LAKLLQRGGNVLLLDEPTNDLD 477
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALD 176
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
325-491 |
3.02e-10 |
|
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: 59.79 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDR-----TLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVvlASVDQ----- 394
Cdd:cd03250 1 ISVEDASFTWDSGeqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--AYVSQepwiq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 395 ---------FRDAMDDKKtvWEEVSNG----QDIltignfEIpsrayvgrfnFKGVDqQKRVGE----LSGGERGRLHLA 457
Cdd:cd03250 79 ngtirenilFGKPFDEER--YEKVIKAcalePDL------EI----------LPDGD-LTEIGEkginLSGGQKQRISLA 139
|
170 180 190
....*....|....*....|....*....|....*
gi 1735515619 458 KLLQRGGNVLLLDEPTNDLDVETLRAL-ENAILEF 491
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGL 174
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-219 |
3.07e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.82 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDkEFEGEARPQPGIkigylpqepklepqqtvrEAVEEAVSEVKSA 101
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMN-ELESEVRVEGRV------------------EFFNQNIYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 102 LTRLD-EVYALYADPD----ADFDKLAAEQAnleaIIQAHDGHNLDNQLERAADALRLpdWDaKIEH--------LSGGE 168
Cdd:PRK14258 83 LNRLRrQVSMVHPKPNlfpmSVYDNVAYGVK----IVGWRPKLEIDDIVESALKDADL--WD-EIKHkihksaldLSGGQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY----EGTVVAITHD 219
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHN 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-219 |
3.18e-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: 61.12 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGEA---------RPQPGIKIGYLPQEPKLEPQQTV 87
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEptsgkvLIDGQDiaamsrkelRELRRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 88 REAVEEAVsEVKsaltrldevyalyadpdadfdklaaeqanleaiiqahdGHNLDNQLERAADALR---LPDW-DAKIEH 163
Cdd:cd03294 120 LENVAFGL-EVQ--------------------------------------GVPRAEREERAAEALElvgLEGWeHKYPDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHD 219
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHD 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
325-484 |
3.40e-10 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 60.58 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYG--DRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMgETVVLASVD------QFR 396
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLV-DGHDLALADpawlrrQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 397 DAMDD----KKTVWEEVSNGQDILTIGNFEIPSRaYVGRFNF-----KGVDQQkrVGE----LSGGERGRLHLAKLLQRG 463
Cdd:cd03252 80 VVLQEnvlfNRSIRDNIALADPGMSMERVIEAAK-LAGAHDFiselpEGYDTI--VGEqgagLSGGQRQRIAIARALIHN 156
|
170 180
....*....|....*....|.
gi 1735515619 464 GNVLLLDEPTNDLDVETLRAL 484
Cdd:cd03252 157 PRILIFDEATSALDYESEHAI 177
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
315-490 |
3.41e-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: 62.53 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 315 PPGPR---LGDKVIEVQNLTKSY-GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMG----ET 386
Cdd:COG5265 345 APDAPplvVGGGEVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDgqdiRD 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 387 VVLASVdqfRDAMddkktvweevsnG---QDIL----TIGnFEIpsrAYvGRfnfKGVDQ-------------------- 439
Cdd:COG5265 425 VTQASL---RAAI------------GivpQDTVlfndTIA-YNI---AY-GR---PDASEeeveaaaraaqihdfieslp 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1735515619 440 ---QKRVGE----LSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETlralENAILE 490
Cdd:COG5265 482 dgyDTRVGErglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT----ERAIQA 535
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
324-501 |
3.44e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.00 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQ----EQPDAGSITMGETV---VLASVDQFR 396
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltggGAPRGARVTGDVTLngePLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 397 DAMddKKTVWEEVS------NGQDILTIGNFEIPSRAYVGRFNFKGVDQQ------------KRVGELSGGERGRLHLAK 458
Cdd:PRK13547 81 LAR--LRAVLPQAAqpafafSAREIVLLGRYPHARRAGALTHRDGEIAWQalalagatalvgRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 459 LL---------QRGGNVLLLDEPTNDLD-------VETLRALENailEFPGCAMVISHD 501
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDlahqhrlLDTVRRLAR---DWNLGVLAIVHD 214
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
22-242 |
3.74e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.40 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLrimagvdKEFEGEARPQPG-IKIGYLPQEPKLEPQQTVREAVEEAVSEVKS 100
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLV-------THFNGLIKSKYGtIQVGDIYIGDKKNNHELITNPYSKKIKNFKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 101 ALTRLDEV-----YALYAD---PDADFDKLAAEQANLEAIIQAH---DGHNLDNQ-LERAADALrlpdwdakiehlSGGE 168
Cdd:PRK13631 114 LRRRVSMVfqfpeYQLFKDtieKDIMFGPVALGVKKSEAKKLAKfylNKMGLDDSyLERSPFGL------------SGGQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG---TVVAITHDRYFLDNVAGWILELDRGE----GIPW 241
Cdd:PRK13631 182 KRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITHTMEHVLEVADEVIVMDKGKilktGTPY 261
|
.
gi 1735515619 242 E 242
Cdd:PRK13631 262 E 262
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
322-510 |
3.79e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.88 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 322 DKVIEVQNLTKSY---GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQFRD 397
Cdd:PRK13642 2 NKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 398 AM-------DDK---KTVWEEVSNGQDILTIGNFEIPSRAYVGRFNFKGVDQQKR-VGELSGGERGRLHLAKLLQRGGNV 466
Cdd:PRK13642 82 KIgmvfqnpDNQfvgATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTRePARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1735515619 467 LLLDEPTNDLD----VETLRALENAILEFPGCAMVISHDrwfLDRIAT 510
Cdd:PRK13642 162 IILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD---LDEAAS 206
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-219 |
4.65e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.03 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 21 HILKDISLSFFPGAKIGVLGLNGAGKST----LLRIMAGVDK-EFEGEARPQPGIKiGYLP---------QEP--KLEPQ 84
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQGEiWFDGQPLHNLNRR-QLLPvrhriqvvfQDPnsSLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 85 QTVREAVEEAVSEVKSALTrldevyalyadpdadfdklAAEQAnlEAIIQAHDGHNLDnqlerAADALRLPdwdakiEHL 164
Cdd:PRK15134 379 LNVLQIIEEGLRVHQPTLS-------------------AAQRE--QQVIAVMEEVGLD-----PETRHRYP------AEF 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHD 219
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLFISHD 485
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
340-544 |
5.18e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 60.61 E-value: 5.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 340 IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLAS--------------VDQFRDAMDDKKT 404
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIaGYHITPETgnknlkklrkkvslVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 405 VWEEVSNGQdiLTIGNFEIPSRAyvgrfnfKGVDQQKRVG-----------ELSGGERGRLHLAKLLQRGGNVLLLDEPT 473
Cdd:PRK13641 103 VLKDVEFGP--KNFGFSEDEAKE-------KALKWLKKVGlsedliskspfELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 474 NDLDVETLRALENAILEFPGCA---MVISHDrwfLDRIATH-----ILDYGDEGKVTFYEGNFSDYEEWKKKTLGDAAT 544
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGhtvILVTHN---MDDVAEYaddvlVLEHGKLIKHASPKEIFSDKEWLKKHYLDEPAT 249
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
324-473 |
5.61e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.89 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVV------------LAS 391
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwqtakimreaVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 392 VDQFRDAMdDKKTVWEEvsngqdiLTIGNFEIPSRAYVGRFN-----FKGVDQQK--RVGELSGGERGRLHLAKLLQRGG 464
Cdd:PRK11614 85 VPEGRRVF-SRMTVEEN-------LAMGGFFAERDQFQERIKwvyelFPRLHERRiqRAGTMSGGEQQMLAIGRALMSQP 156
|
....*....
gi 1735515619 465 NVLLLDEPT 473
Cdd:PRK11614 157 RLLLLDEPS 165
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-198 |
5.62e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.20 E-value: 5.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-------VDKEFEGEARPQPGI--KIGYLPQEPKLEPQQTVRE 89
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriqgnnfTGTILANNRKPTKQIlkRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 90 A-VEEAVSEVKSALTRLDEVyalyadpdadfdkLAAEQANLEAIIQAHDGHNLDNQLERAadalrlpdwdakiehLSGGE 168
Cdd:PLN03211 160 TlVFCSLLRLPKSLTKQEKI-------------LVAESVISELGLTKCENTIIGNSFIRG---------------ISGGE 211
|
170 180 190
....*....|....*....|....*....|
gi 1735515619 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
Cdd:PLN03211 212 RKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
324-382 |
6.18e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.06 E-value: 6.18e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSIT 382
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVE 59
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
22-219 |
6.20e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 62.05 E-value: 6.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARpqpgikigylpqepklepqqtvreAVEEAVSEVKS- 100
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYR------------------------VAGQDVATLDAd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 101 ALTRLD--------EVYALYAdpdadfdKLAAEQaNLEaIIQAHDGHNLDNQLERAADALRLPDWDAKIEH----LSGGE 168
Cdd:PRK10535 79 ALAQLRrehfgfifQRYHLLS-------HLTAAQ-NVE-VPAVYAGLERKQRLLRAQELLQRLGLEDRVEYqpsqLSGGQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1735515619 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLERFLHDYEGTVVAITHD 219
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIVTHD 203
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
324-500 |
6.94e-10 |
|
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: 61.38 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSG-------------QEQP-DAGSITMGETVVL 389
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywSGSPlKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 390 ASVDQfRDAMDDKKTVWEEVSNGQDILTIGNF----EIPSRAY--VGRFNFKGVDQQKRVGELSGGERGRLHLAKLLQRG 463
Cdd:TIGR02633 81 VIIHQ-ELTLVPELSVAENIFLGNEITLPGGRmaynAMYLRAKnlLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1735515619 464 GNVLLLDEPTNDLDVETLRALENAI--LEFPGCAMV-ISH 500
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIrdLKAHGVACVyISH 199
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-240 |
7.32e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 60.00 E-value: 7.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTL-------LR------IMAGVDKefeGEARPQPGIK--IGYLPQEPKlepQQTV 87
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLalhlnglLRpqkgkvLVSGIDT---GDFSKLQGIRklVGIVFQNPE---TQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 88 REAVEEAVSevksaltrldevyalyadpdadfdkLAAEQANLEAIiqahdghNLDNQLERAADALRLPDWDAKI-EHLSG 166
Cdd:PRK13644 92 GRTVEEDLA-------------------------FGPENLCLPPI-------EIRKRVDRALAEIGLEKYRHRSpKTLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAES-VAWLERF--LHDYEGTVVAITHDRYFLdNVAGWILELDRG----EGI 239
Cdd:PRK13644 140 GQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIkkLHEKGKTIVYITHNLEEL-HDADRIIVMDRGkivlEGE 218
|
.
gi 1735515619 240 P 240
Cdd:PRK13644 219 P 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-239 |
7.66e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.86 E-value: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 21 HILKDISLSFFPGAKIGVLGLNGAGKSTLLR-----IMAGVDKEFEGEARP------QPGI-------KIGYLPQEPKLE 82
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLfgrniySPDVdpievrrEVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 83 PQQTVREAVEEAVSevksaltrldevyalyadpdadFDKLAAEQANLEAIIQAhdghnldnQLERAA--DAL--RLPDWD 158
Cdd:PRK14267 98 PHLTIYDNVAIGVK----------------------LNGLVKSKKELDERVEW--------ALKKAAlwDEVkdRLNDYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 159 AkieHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAITHDRYFLDNVAGWILELDRG 236
Cdd:PRK14267 148 S---NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTHSPAQAARVSDYVAFLYLG 224
|
...
gi 1735515619 237 EGI 239
Cdd:PRK14267 225 KLI 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
325-502 |
8.69e-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: 61.85 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSY--GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTL----FRMLS--GQEQPDA---GSITMGE-----TVV 388
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLlsalLRLLSteGEIQIDGvswNSVTLQTwrkafGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 389 LASV----DQFRDAMDDkktvWEEVSNgQDILTIGNfEIPSRAYV----GRFNFKGVDQQKRvgeLSGGERGRLHLAKLL 460
Cdd:TIGR01271 1298 PQKVfifsGTFRKNLDP----YEQWSD-EEIWKVAE-EVGLKSVIeqfpDKLDFVLVDGGYV---LSNGHKQLMCLARSI 1368
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1735515619 461 QRGGNVLLLDEPTNDLDVETLRALENAILE-FPGCAMVISHDR 502
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRKTLKQsFSNCTVILSEHR 1411
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
22-236 |
1.17e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.99 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR-------------PQPGI------KIGYLPQEPKLE 82
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtarslsQQKGLirqlrqHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 83 PQQTVREAVEEAVSEVK-----SALTRLDEVYALYAdpdadfdkLAAEQanleaiiqahdghnldnqleraadalrlpdw 157
Cdd:PRK11264 98 PHRTVLENIIEGPVIVKgepkeEATARARELLAKVG--------LAGKE------------------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 158 DAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLE---RFLHDYEGTVVAITHDRYFLDNVAGWILELD 234
Cdd:PRK11264 139 TSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLntiRQLAQEKRTMVIVTHEMSFARDVADRAIFMD 218
|
..
gi 1735515619 235 RG 236
Cdd:PRK11264 219 QG 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-242 |
1.37e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 58.99 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpqpgikIGYLPQEPKLEPQQTVREaveeavsevksal 102
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGE--------IFYNNQAITDDNFEKLRK------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 103 trldEVYALYADPDADFdklaaeqanLEAIIQAHDGHNLDNQL-------ERAADALRLPDWDAKIEH----LSGGERRR 171
Cdd:PRK13648 84 ----HIGIVFQNPDNQF---------VGSIVKYDVAFGLENHAvpydemhRRVSEALKQVDMLERADYepnaLSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 172 VALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLH----DYEGTVVAITHDryfLDNVAG--WILELDRG----EGIPW 241
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRkvksEHNITIISITHD---LSEAMEadHVIVMNKGtvykEGTPT 227
|
.
gi 1735515619 242 E 242
Cdd:PRK13648 228 E 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
325-486 |
1.41e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.33 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRT-----LIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMgetvvlasvdQFRDAM 399
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEW----------IFKDEK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 400 DDKKTVWEEVSNGQDILTIGNF-------EIpsRAYVGR-FNFK--------------------GVDQQ----------K 441
Cdd:PRK13651 73 NKKKTKEKEKVLEKLVIQKTRFkkikkikEI--RRRVGVvFQFAeyqlfeqtiekdiifgpvsmGVSKEeakkraakyiE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 442 RVG-----------ELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLD----VETLRALEN 486
Cdd:PRK13651 151 LVGldesylqrspfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDN 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-229 |
1.44e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 59.36 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 17 PPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQpGIKIGYLPQEPKLEPqqtVREAVEEAVS 96
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG-DIVVSSTSKQKEIKP---VRKKVGVVFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 97 EVKSAL---TRLDEVY---ALYADPDADFDKLAAEQanLEAIiqahdghnldnqleraadALRLPDWDAKIEHLSGGERR 170
Cdd:PRK13643 92 FPESQLfeeTVLKDVAfgpQNFGIPKEKAEKIAAEK--LEMV------------------GLADEFWEKSPFELSGGQMR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1735515619 171 RVALCRLLLEKPDMLLLDEPTNHLDAES-VAWLERF--LHDYEGTVVAITHdryFLDNVAGW 229
Cdd:PRK13643 152 RVAIAGILAMEPEVLVLDEPTAGLDPKArIEMMQLFesIHQSGQTVVLVTH---LMDDVADY 210
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
322-490 |
1.52e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 58.89 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 322 DKVIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLF----RMLsgQEQPDA---GSITM-GETVVLASVD 393
Cdd:COG1117 9 EPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnRMN--DLIPGArveGEILLdGEDIYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 394 Q----------F-------------------------RDAMDDKktV---------WEEVSngqDILtignfeipsrayv 429
Cdd:COG1117 87 VvelrrrvgmvFqkpnpfpksiydnvayglrlhgiksKSELDEI--VeeslrkaalWDEVK---DRL------------- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1735515619 430 grfnfkgvdqQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLD-VETLRaLENAILE 490
Cdd:COG1117 149 ----------KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILE 199
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
318-478 |
1.60e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.19 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 318 PRLGDKVIEVQNLT---KSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQE--QPDAGSITM-GETVVLAS 391
Cdd:NF040905 251 PKIGEVVFEVKNWTvyhPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKdGKEVDVST 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 392 VdqfRDAMD--------DKKTvweevsNG----QDI---LTIGNFEIPSRA--------------YVGRFNFK--GVDQQ 440
Cdd:NF040905 331 V---SDAIDaglayvteDRKG------YGlnliDDIkrnITLANLGKVSRRgvideneeikvaeeYRKKMNIKtpSVFQK 401
|
170 180 190
....*....|....*....|....*....|....*...
gi 1735515619 441 krVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDV 478
Cdd:NF040905 402 --VGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
334-477 |
2.21e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.48 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 334 YGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSIT-MGETV------VLASVDQ----FRDAmdDK 402
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwQGKPLdyskrgLLALRQQvatvFQDP--EQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 403 KTVWEEVSNgqDI-LTIGNFEIPSRAYVGRFN--FKGVD----QQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTND 475
Cdd:PRK13638 89 QIFYTDIDS--DIaFSLRNLGVPEAEITRRVDeaLTLVDaqhfRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
..
gi 1735515619 476 LD 477
Cdd:PRK13638 167 LD 168
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
325-477 |
2.40e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.48 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRT-----LIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRDAM 399
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 400 DDKK----------------TVWEEVSNGQDILTIGNFE----IPS--------RAYVGRFNFkgvdqqkrvgELSGGER 451
Cdd:PRK13645 87 RLRKeiglvfqfpeyqlfqeTIEKDIAFGPVNLGENKQEaykkVPEllklvqlpEDYVKRSPF----------ELSGGQK 156
|
170 180
....*....|....*....|....*.
gi 1735515619 452 GRLHLAKLLQRGGNVLLLDEPTNDLD 477
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLD 182
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
22-219 |
2.61e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 58.17 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE----------------ARpqpgiKIGYLPQEPKLEPQQ 85
Cdd:COG4604 16 VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEvlvdgldvattpsrelAK-----RLAILRQENHINSRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 TVREAV----------------EEAVSEvksALTRLDevyalyadpdadfdklaaeqanLEAIIQAHdghnLDNqleraa 149
Cdd:COG4604 91 TVRELVafgrfpyskgrltaedREIIDE---AIAYLD----------------------LEDLADRY----LDE------ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1735515619 150 dalrlpdwdakiehLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD-AESVAW---LERFLHDYEGTVVAITHD 219
Cdd:COG4604 136 --------------LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmKHSVQMmklLRRLADELGKTVVIVLHD 195
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
22-195 |
2.81e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 59.19 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQpGIKIGYLPQEPK----------LEPQQTVREAV 91
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD-GQDITHVPAENRhvntvfqsyaLFPHMTVFENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 92 EEAVsevksaltRLDEVyalyadPDADFDklaaeqanleaiiqahdghnldnqlERAADALR---LPDW-DAKIEHLSGG 167
Cdd:PRK09452 108 AFGL--------RMQKT------PAAEIT-------------------------PRVMEALRmvqLEEFaQRKPHQLSGG 148
|
170 180
....*....|....*....|....*...
gi 1735515619 168 ERRRVALCRLLLEKPDMLLLDEPTNHLD 195
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
325-477 |
3.42e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 58.70 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSY-GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVV---------LASVDQ 394
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnelepadrdIAMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 395 ---------FRDAMD--------DKKTVWEEVSNGQDILTIGNFeipsrayvgrfnfkgVDQQKRvgELSGGERGRLHLA 457
Cdd:PRK11650 84 nyalyphmsVRENMAyglkirgmPKAEIEERVAEAARILELEPL---------------LDRKPR--ELSGGQRQRVAMG 146
|
170 180
....*....|....*....|
gi 1735515619 458 KLLQRGGNVLLLDEPTNDLD 477
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLD 166
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
324-517 |
4.86e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.81 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSY-GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMG--ETVVLASVDQ------ 394
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghDITRLKNREVpflrrq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 395 ----FRD---AMDdkKTVWEEVSNGQDILTIGNFEIPSRAYVGRFNFKGVDQQKRVG-ELSGGERGRLHLAKLLQRGGNV 466
Cdd:PRK10908 81 igmiFQDhhlLMD--RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPiQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1735515619 467 LLLDEPTNDLDvetlRALENAIL----EFPGCAMVI---SHDRWFLDRIATHILDYGD 517
Cdd:PRK10908 159 LLADEPTGNLD----DALSEGILrlfeEFNRVGVTVlmaTHDIGLISRRSYRMLTLSD 212
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
339-532 |
4.95e-09 |
|
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: 57.56 E-value: 4.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 339 LIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSI------------------TMGETVVLA-SVDQFRdam 399
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIkhsgrisfssqfswimpgTIKENIIFGvSYDEYR--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 400 ddKKTVWEEVSNGQDILtignfeipsrayvgrfnfKGVDQQKRV-GE----LSGGERGRLHLAKLLQRGGNVLLLDEPTN 474
Cdd:cd03291 129 --YKSVVKACQLEEDIT------------------KFPEKDNTVlGEggitLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1735515619 475 DLDVETlralENAILEFPGCAMVISHDRWFLD------RIATHILDYgDEGKVTFYeGNFSDYE 532
Cdd:cd03291 189 YLDVFT----EKEIFESCVCKLMANKTRILVTskmehlKKADKILIL-HEGSSYFY-GTFSELQ 246
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
322-381 |
5.39e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.49 E-value: 5.39e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 322 DKVIEVQNLTKSYGDRT---------LIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSI 381
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL 70
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
325-477 |
5.45e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 57.45 E-value: 5.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLID-----DLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLAS-------- 391
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgralfDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 392 -------VDQFRDAMDDKKTVWEEVSNGQDILTIGNFEIPSRAYvGRFNFKGVDQQ---KRVGELSGGERGRLHLAKLLQ 461
Cdd:PRK13649 83 irkkvglVFQFPESQLFEETVLKDVAFGPQNFGVSQEEAEALAR-EKLALVGISESlfeKNPFELSGGQMRRVAIAGILA 161
|
170
....*....|....*.
gi 1735515619 462 RGGNVLLLDEPTNDLD 477
Cdd:PRK13649 162 MEPKILVLDEPTAGLD 177
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
325-491 |
5.80e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.16 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGEtVVLASVDQFRDAMDDKK- 403
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGE-VRLFGRNIYSPDVDPIEv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 404 -----------------TVWEEVSNGQDI--LTIGNFEIPSRAyvgRFNFKGVDQQKRV--------GELSGGERGRLHL 456
Cdd:PRK14267 84 rrevgmvfqypnpfphlTIYDNVAIGVKLngLVKSKKELDERV---EWALKKAALWDEVkdrlndypSNLSGGQRQRLVI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1735515619 457 AKLLQRGGNVLLLDEPTNDLDVETLRALENAILEF 491
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL 195
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
321-536 |
6.09e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 57.40 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 321 GDKVIEVQNLTKSYGD------RTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSItmgetvvlasvdq 394
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 395 FRDAMD--DKKTVW-----------------------EEVSNGQDILTIGNFEIPSRayvgrfnfkgVDQQ-KRVGE--- 445
Cdd:PRK13633 68 YVDGLDtsDEENLWdirnkagmvfqnpdnqivativeEDVAFGPENLGIPPEEIRER----------VDESlKKVGMyey 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 446 -------LSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFPG----CAMVISHdrwFL------DRI 508
Cdd:PRK13633 138 rrhaphlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkygiTIILITH---YMeeaveaDRI 214
|
250 260 270
....*....|....*....|....*....|..
gi 1735515619 509 ATHildygDEGKVTFyEGN----FSDYEEWKK 536
Cdd:PRK13633 215 IVM-----DSGKVVM-EGTpkeiFKEVEMMKK 240
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
12-219 |
7.38e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 57.40 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 12 VGKVVPPKR---HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEG------------EARPqpgi 70
Cdd:COG1135 7 LSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERptsgsvLVDGvdltalserelrAARR---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 71 KIGYLPQEPKLEPQQTVREAVEeavsevksaltrldevYALYAdpdADFDKlaAEQAnleaiiqahdghnldnqlERAAD 150
Cdd:COG1135 83 KIGMIFQHFNLLSSRTVAENVA----------------LPLEI---AGVPK--AEIR------------------KRVAE 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 151 ALRLPDWDAKIEH----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDYEG-TVVAITHD 219
Cdd:COG1135 124 LLELVGLSDKADAypsqLSGGQKQRVGIARALANNPKVLLCDEATSALDPEttrSILDLLKDINRELGlTIVLITHE 200
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
324-486 |
7.71e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 56.92 E-value: 7.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRT-LIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM------------GETVVLA 390
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidtgdfsklqGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 391 SVDQFRDAMDDKKTVWEEVSNGQDILTIGNFEIPSR-----AYVGRFNFKgvdqQKRVGELSGGERGRLHLAKLLQRGGN 465
Cdd:PRK13644 81 IVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRvdralAEIGLEKYR----HRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180
....*....|....*....|..
gi 1735515619 466 VLLLDEPTNDLDVETLRA-LEN 486
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAvLER 178
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
325-513 |
8.26e-09 |
|
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: 55.69 E-value: 8.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLtKSYGDRTLIDdlsFSIPkgaIVGIIGANGAGKSTLFRML-------------SGQEQPDAgsitMGETVVLAS 391
Cdd:cd03240 4 LSIRNI-RSFHERSEIE---FFSP---LTLIVGQNGAGKTTIIEALkyaltgelppnskGGAHDPKL----IREGEVRAQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 392 VD-QFRDAMDDKKTVWEEVsngqDILTignfeipSRAYV--GRFNFKGVDQQKRvgeLSGGERG------RLHLAKLLQR 462
Cdd:cd03240 73 VKlAFENANGKKYTITRSL----AILE-------NVIFChqGESNWPLLDMRGR---CSGGEKVlasliiRLALAETFGS 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 463 GGNVLLLDEPTNDLDVETLR-ALENAILEFPGCA----MVISHDRWFLDRiATHIL 513
Cdd:cd03240 139 NCGILALDEPTTNLDEENIEeSLAEIIEERKSQKnfqlIVITHDEELVDA-ADHIY 193
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
323-385 |
1.09e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 56.15 E-value: 1.09e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 323 KVIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGE 385
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG 66
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-218 |
1.10e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 58.32 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 16 VPPKR-HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--VDKEFEGEARPQPGIKI--------GYLPQEPKLEPQ 84
Cdd:PLN03140 888 VTEDRlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGrkTGGYIEGDIRISGFPKKqetfarisGYCEQNDIHSPQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 85 QTVREaveeavSEVKSALTRL-DEVyalyadpdADFDKLAAEQANLEAIiqahdghnldnQLERAADAL-RLPDwdakIE 162
Cdd:PLN03140 968 VTVRE------SLIYSAFLRLpKEV--------SKEEKMMFVDEVMELV-----------ELDNLKDAIvGLPG----VT 1018
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 163 HLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLH---DYEGTVVAITH 218
Cdd:PLN03140 1019 GLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRntvDTGRTVVCTIH 1077
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
339-532 |
1.12e-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: 58.38 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 339 LIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSI------------------TMGETVVLA-SVDQFRDAM 399
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIkhsgrisfspqtswimpgTIKDNIIFGlSYDEYRYTS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 400 DDKKTVWEEvsngqdilTIGNFEIPSRAYVGRfnfKGVdqqkrvgELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVE 479
Cdd:TIGR01271 521 VIKACQLEE--------DIALFPEKDKTVLGE---GGI-------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 480 TlralENAILEFPGCAMVISHDRWFLDRIATHiLDYGD------EGKVTFYeGNFSDYE 532
Cdd:TIGR01271 583 T----EKEIFESCLCKLMSNKTRILVTSKLEH-LKKADkilllhEGVCYFY-GTFSELQ 635
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-241 |
1.20e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.07 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdKEFEGEARpqpgikigyLPQEPKLEPQQTVREAVEE------AV 95
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRL-IELYPEAR---------VSGEVYLDGQDIFKMDVIElrrrvqMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 96 SEVKSALTRLD--EVYALyadpDADFDKLAAEQANLEAIIQahdghnldNQLERAADALRLPD-WDAKIEHLSGGERRRV 172
Cdd:PRK14247 88 FQIPNPIPNLSifENVAL----GLKLNRLVKSKKELQERVR--------WALEKAQLWDEVKDrLDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1735515619 173 ALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAITHDRYFLDNVAGWILELDRGEGIPW 241
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELkkDMTIVLVTHFPQQAARISDYVAFLYKGQIVEW 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
22-237 |
1.28e-08 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 55.11 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTL-LRIMAGVDKEfEGEARPQpGIKIGYLPQEpklepqqtvreAVEEAVSEVKS 100
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLiLALFRFLEAE-EGKIEID-GIDISTIPLE-----------DLRSSLTIIPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 101 ALTRLDEVYALYADPdadFDKLAAEQAnLEAIIQAHDGHNLdnqleraadalrlpdwdakiehlSGGERRRVALCRLLLE 180
Cdd:cd03369 90 DPTLFSGTIRSNLDP---FDEYSDEEI-YGALRVSEGGLNL-----------------------SQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1735515619 181 KPDMLLLDEPTNHLDAESVAWLERFLHD--YEGTVVAITHDryfLDNVAGW--ILELDRGE 237
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREefTNSTILTIAHR---LRTIIDYdkILVMDAGE 200
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-227 |
1.41e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.28 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DKEFEGEARPQPGI-----KIGYLPQEPKlepQQTVR 88
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLleaesgQIIIDGDLLTEENVwdirhKIGMVFQNPD---NQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 89 EAVEEAVSevksaltrldevyalyadpdadfdklaaeqANLEaiiqaHDGHNLDNQLERAADALRLPDW----DAKIEHL 164
Cdd:PRK13650 97 ATVEDDVA------------------------------FGLE-----NKGIPHEEMKERVNEALELVGMqdfkEREPARL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITHDryfLDNVA 227
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGrlelIKTIKGIRDDYQMTVISITHD---LDEVA 205
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
22-220 |
1.68e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.11 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQpGIKIGYLPQEpklepqqTVREAVEEAVsevksa 101
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFE-GEDISTLKPE-------IYRQQVSYCA------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 102 ltrldEVYALYADPDADfdklaaeqaNLEAIIQAHDGHNLDNQLERAADALRLPD--WDAKIEHLSGGERRRVALCRLLL 179
Cdd:PRK10247 88 -----QTPTLFGDTVYD---------NLIFPWQIRNQQPDPAIFLDDLERFALPDtiLTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1735515619 180 EKPDMLLLDEPTNHLDAESVAWLERFLHDY----EGTVVAITHDR 220
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYvreqNIAVLWVTHDK 198
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
11-196 |
1.75e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 56.65 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 11 RVGKVVppkrhILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpqpgIKIGylpqepklepqqtvrea 90
Cdd:PRK11432 15 RFGSNT-----VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQ------IFID----------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 91 vEEAVSevKSALTRLD-----EVYALyadpdadFDKLAaeqanleaiIQAHDGHNLDNQ-------LERAADALRLPDW- 157
Cdd:PRK11432 67 -GEDVT--HRSIQQRDicmvfQSYAL-------FPHMS---------LGENVGYGLKMLgvpkeerKQRVKEALELVDLa 127
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1735515619 158 ---DAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 196
Cdd:PRK11432 128 gfeDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-220 |
1.96e-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: 57.61 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRI---MAGVDKEFEGEARPQPGIKIgylpqepklepqQTVREA---VEE 93
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAllrLLSTEGEIQIDGVSWNSVTL------------QTWRKAfgvIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 94 AVSEVKSALTRLDEVYALYADPDAdfdKLAAEQANLEAIIQAHDGhNLDNQLERAADAlrlpdwdakiehLSGGERRRVA 173
Cdd:TIGR01271 1300 KVFIFSGTFRKNLDPYEQWSDEEI---WKVAEEVGLKSVIEQFPD-KLDFVLVDGGYV------------LSNGHKQLMC 1363
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1735515619 174 LCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL-HDYEGTVVAITHDR 220
Cdd:TIGR01271 1364 LARSILSKAKILLLDEPSAHLDPVTLQIIRKTLkQSFSNCTVILSEHR 1411
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-219 |
1.97e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 56.25 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpqpgIKI-GYLPQEPKLE-----------PQQ----- 85
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGE------VRVlGYVPFKRRKEfarrigvvfgqRSQlwwdl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 TVREAVEeavsevksaLTRldEVYALyadPDADFDKlaaeqaNLEAIIQAHDghnLDNQLERAadalrlpdwdakIEHLS 165
Cdd:COG4586 112 PAIDSFR---------LLK--AIYRI---PDAEYKK------RLDELVELLD---LGELLDTP------------VRQLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1735515619 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY---EG-TVVAITHD 219
Cdd:COG4586 157 LGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnreRGtTILLTSHD 214
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-195 |
2.34e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.76 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 15 VVPPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DKEFEGEA----------RPQPGI--KIGYLPQEPK- 80
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVfingkpvdirNPAQAIraGIAMVPEDRKr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 81 --LEPQQTVREAVEEAVSEVKSALTRLDEvyalyadpdadfdklAAEQANLEAIIQahdghnldnQLERAADALRLPdwd 158
Cdd:TIGR02633 348 hgIVPILGVGKNITLSVLKSFCFKMRIDA---------------AAELQIIGSAIQ---------RLKVKTASPFLP--- 400
|
170 180 190
....*....|....*....|....*....|....*..
gi 1735515619 159 akIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
Cdd:TIGR02633 401 --IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-224 |
2.91e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 54.69 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK--------EFEGE----------AR---------PQ--PGIKI 72
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyevtsgsiLLDGEdilelspderARagiflafqyPVeiPGVSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 73 GYLpqepklepqqtVREAVEEavsevksalTRLDEVYALyadpdaDFDKLAAEQANLEaiiqahdghNLDNQ-LERAADa 151
Cdd:COG0396 95 SNF-----------LRTALNA---------RRGEELSAR------EFLKLLKEKMKEL---------GLDEDfLDRYVN- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 152 lrlpdwdakiEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLERFLHDYEGTVVAITHDRYFLD 224
Cdd:COG0396 139 ----------EGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDAlriVAEGVNKLRSPDRGILIITHYQRILD 204
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
347-519 |
3.42e-08 |
|
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: 54.68 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 347 IPK-GAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITmGETVVLASVDQFRDAmdDKKTVWEEVSNGQ------------ 413
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDWDEILDEFRGS--ELQNYFTKLLEGDvkvivkpqyvdl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 414 ----------DILT----IGNFEIpsraYVGRFNFKGVDQQKrVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDV- 478
Cdd:cd03236 99 ipkavkgkvgELLKkkdeRGKLDE----LVDQLELRHVLDRN-IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIk 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1735515619 479 ------ETLRAL---ENAILefpgcamVISHDRWFLDRIA--THILdYGDEG 519
Cdd:cd03236 174 qrlnaaRLIRELaedDNYVL-------VVEHDLAVLDYLSdyIHCL-YGEPG 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
19-237 |
3.51e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.19 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkefegearpqpgikigYLPQE-PKLEPQQTVREAVEEAVSE 97
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL-----------------LLPDDnPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 98 VKsaltrlDEVYALYADPDADFdklaaeqanLEAIIQAHDGHNLDN-QLERA----------ADALRLPDWDAKIEHLSG 166
Cdd:PRK13640 82 IR------EKVGIVFQNPDNQF---------VGATVGDDVAFGLENrAVPRPemikivrdvlADVGMLDYIDSEPANLSG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITHDryfLD--NVAGWILELDRGE 237
Cdd:PRK13640 147 GQKQRVAIAGILAVEPKIIILDESTSMLDPAGkeqiLKLIRKLKKKNNLTVISITHD---IDeaNMADQVLVLDDGK 220
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
292-523 |
3.72e-08 |
|
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: 56.30 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 292 MARFDELNSGEYQKRNETNELFIPPGPRLG------------DKVIEVQN--LTKSYGDrTLIDDLSFSIPKGAIVGIIG 357
Cdd:TIGR00954 407 LQVLDDVKSGNFKRPRVEEIESGREGGRNSnlvpgrgiveyqDNGIKFENipLVTPNGD-VLIESLSFEVPSGNNLLICG 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 358 ANGAGKSTLFRMLSG--------------------QEQPDAGSITMGETVVL--ASVDQFRDAMDDK--KTVWEEVSNGq 413
Cdd:TIGR00954 486 PNGCGKSSLFRILGElwpvyggrltkpakgklfyvPQRPYMTLGTLRDQIIYpdSSEDMKRRGLSDKdlEQILDNVQLT- 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 414 DILTI-GNFEIpsrayvgrfnfkgvdQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFP 492
Cdd:TIGR00954 565 HILEReGGWSA---------------VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFG 629
|
250 260 270
....*....|....*....|....*....|.
gi 1735515619 493 GCAMVISHdRWFLDRIATHILDYGDEGKVTF 523
Cdd:TIGR00954 630 ITLFSVSH-RKSLWKYHEYLLYMDGRGGYQF 659
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
21-253 |
3.78e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 54.85 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 21 HILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpqpgIKIGYLPQEPKLEPQQTVREAVEeavsevks 100
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGR------ILFDGKPIDYSRKGLMKLRESVG-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 101 altrldevyALYADPDAD-FDKLAAEQANLEAIIQAHDGHNLDNQLERAADALRLPDWDAKIEH-LSGGERRRVALCRLL 178
Cdd:PRK13636 86 ---------MVFQDPDNQlFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHcLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 179 LEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHDryfLDNVAGW---ILELDRGEGIpWEGNYSSWLEQ 251
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD---IDIVPLYcdnVFVMKEGRVI-LQGNPKEVFAE 232
|
..
gi 1735515619 252 KE 253
Cdd:PRK13636 233 KE 234
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
288-397 |
4.01e-08 |
|
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: 55.96 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 288 SKARMA--RFDELNSGEYQKRNETNELFIPPGPRLGDKvIEVQNLTKSYGDRTliDD-------LSFSIPKGAIVGIIGA 358
Cdd:COG4615 290 SRANVAlrKIEELELALAAAEPAAADAAAPPAPADFQT-LELRGVTYRYPGED--GDegftlgpIDLTIRRGELVFIVGG 366
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1735515619 359 NGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQFRD 397
Cdd:COG4615 367 NGSGKSTLAKLLTGLYRPESGEILLdGQPVTADNREAYRQ 406
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
330-516 |
4.40e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.70 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 330 LTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQFRDAMDDKKTVwee 408
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTATRGDRSRFMAYLGHLPGL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 409 vsnGQDILTIGNF------------EIPSRAY--VGRFNFkgvdQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTN 474
Cdd:PRK13543 94 ---KADLSTLENLhflcglhgrrakQMPGSALaiVGLAGY----EDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1735515619 475 DLDVETLRALENAI---LEFPGCAMVISHDRWFLDRIATHILDYG 516
Cdd:PRK13543 167 NLDLEGITLVNRMIsahLRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-195 |
4.43e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 1 MSSQFVYTMHRVGKVV------------PPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK-EFEGEA--- 64
Cdd:PRK13549 244 LTALYPREPHTIGEVIlevrnltawdpvNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIfid 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 65 -------RPQPGIK--IGYLPQEPK---LEPQQTVREAVEEAVSEVKSALTRLDEvyalyadpdadfdklAAEQANLEAI 132
Cdd:PRK13549 324 gkpvkirNPQQAIAqgIAMVPEDRKrdgIVPVMGVGKNITLAALDRFTGGSRIDD---------------AAELKTILES 388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 133 IQahdghnldnQLEraadaLRLPDWDAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
Cdd:PRK13549 389 IQ---------RLK-----VKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
321-501 |
4.88e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.97 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 321 GDKVIEVQNLTKSY--------GDRTL--IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVL 389
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvkrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 390 ASVDQFRD--------------AMDDKKTVWEEVSNGQDILTigNFEIPSRAYvgrfnfKGVDQQKRVG---E------- 445
Cdd:PRK11308 82 ADPEAQKLlrqkiqivfqnpygSLNPRKKVGQILEEPLLINT--SLSAAERRE------KALAMMAKVGlrpEhydryph 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 446 -LSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVeTLRAlenAIL--------EFpGCAMV-ISHD 501
Cdd:PRK11308 154 mFSGGQRQRIAIARALMLDPDVVVADEPVSALDV-SVQA---QVLnlmmdlqqEL-GLSYVfISHD 214
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
32-221 |
5.40e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.70 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 32 PGAKIGVLGLNGAGKSTLLRIMAGVdkefegeARPQPG-IKIGYLPQepklepqqtvreaveeAVSEVKSALTRLDEVYA 110
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGL-------LHVESGqIQIDGKTA----------------TRGDRSRFMAYLGHLPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 111 LYADPDAdfdklaaeQANLEAIIQAHDGHnlDNQLERAADAL-RLPDW-DAKIEHLSGGERRRVALCRLLLEKPDMLLLD 188
Cdd:PRK13543 93 LKADLST--------LENLHFLCGLHGRR--AKQMPGSALAIvGLAGYeDTLVRQLSAGQKKRLALARLWLSPAPLWLLD 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 1735515619 189 EPTNHLDAESVAWLERFLHDY---EGTVVAITHDRY 221
Cdd:PRK13543 163 EPYANLDLEGITLVNRMISAHlrgGGAALVTTHGAY 198
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
314-477 |
5.54e-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: 56.11 E-value: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 314 IPPGprlGDKVIEVQNLTKSY--GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVvlAS 391
Cdd:TIGR00957 629 IKPG---EGNSITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV--AY 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 392 VDQfrDAMDDKKTVWEEVSNG------------QDILTIGNFEI-PS--RAYVGRfnfKGVDqqkrvgeLSGGERGRLHL 456
Cdd:TIGR00957 704 VPQ--QAWIQNDSLRENILFGkalnekyyqqvlEACALLPDLEIlPSgdRTEIGE---KGVN-------LSGGQKQRVSL 771
|
170 180
....*....|....*....|.
gi 1735515619 457 AKLLQRGGNVLLLDEPTNDLD 477
Cdd:TIGR00957 772 ARAVYSNADIYLFDDPLSAVD 792
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
17-219 |
5.55e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 54.23 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 17 PPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKefegearPQPG-IKI-GYLPQepklepQQTVREAveea 94
Cdd:PRK13632 19 NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLK-------PQSGeIKIdGITIS------KENLKEI---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 95 vsevksaltRlDEVYALYADPDADFDKLAAEQA---NLE----------AII-QAHDGHNLDNQLERAAdalrlpdwdak 160
Cdd:PRK13632 82 ---------R-KKIGIIFQNPDNQFIGATVEDDiafGLEnkkvppkkmkDIIdDLAKKVGMEDYLDKEP----------- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 161 iEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG----TVVAITHD 219
Cdd:PRK13632 141 -QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrkkTLISITHD 202
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
324-384 |
5.80e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.44 E-value: 5.80e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMG 384
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG 71
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
323-477 |
6.09e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.36 E-value: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 323 KVIEVQNLTKSYGDRTL-IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQFRDAMd 400
Cdd:PRK10522 321 QTLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdGKPVTAEQPEDYRKLF- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 401 dkKTVWEEVSNGQDILTIGNFEIPSRAYVGRFNFKGVDQQKRVGE-------LSGGERGRLHL--AKLLQRggNVLLLDE 471
Cdd:PRK10522 400 --SAVFTDFHLFDQLLGPEGKPANPALVEKWLERLKMAHKLELEDgrisnlkLSKGQKKRLALllALAEER--DILLLDE 475
|
....*.
gi 1735515619 472 PTNDLD 477
Cdd:PRK10522 476 WAADQD 481
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
322-485 |
6.85e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.02 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 322 DKVIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQ--PDA---GSITMGETVVLAS-VDQ- 394
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLYAPdVDPv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 395 ---------FRDAMDDKKTVWEEVSNGQDILTI-GNF-EIPSRAYVGRFNFKGV-DQQKRVG-ELSGGERGRLHLAKLLQ 461
Cdd:PRK14243 88 evrrrigmvFQKPNPFPKSIYDNIAYGARINGYkGDMdELVERSLRQAALWDEVkDKLKQSGlSLSGGQQQRLCIARAIA 167
|
170 180
....*....|....*....|....*
gi 1735515619 462 RGGNVLLLDEPTNDLD-VETLRALE 485
Cdd:PRK14243 168 VQPEVILMDEPCSALDpISTLRIEE 192
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-241 |
7.87e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.51 E-value: 7.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 2 SSQFVYTMHRVGKVVPPKRhILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQPgiKIGYLPQEpkl 81
Cdd:PRK14246 6 SAEDVFNISRLYLYINDKA-ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYFGKD--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 82 epqqtvreaveeaVSEVKSALTRlDEVYALYADPDAdFDKLAAEQaNLEAIIQAH---DGHNLDNQLERAADALRLpdW- 157
Cdd:PRK14246 80 -------------IFQIDAIKLR-KEVGMVFQQPNP-FPHLSIYD-NIAYPLKSHgikEKREIKKIVEECLRKVGL--Wk 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 158 ------DAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAITHDRYFLDNVAGW 229
Cdd:PRK14246 142 evydrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELknEIAIVIVSHNPQQVARVADY 221
|
250
....*....|..
gi 1735515619 230 ILELDRGEGIPW 241
Cdd:PRK14246 222 VAFLYNGELVEW 233
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
25-227 |
8.21e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 54.35 E-value: 8.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 25 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQpGIKIGYLP---------------QEP--KLEPQQTV 87
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFD-GQDITGLSgrelrplrrrmqmvfQDPyaSLNPRMTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 88 REAVEEA--VSEVKSALTRLDEVYALyadpdadFDK--LAAEQANleaiiqahdghnldnqleraadalRLPdwdakieH 163
Cdd:COG4608 115 GDIIAEPlrIHGLASKAERRERVAEL-------LELvgLRPEHAD------------------------RYP-------H 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1735515619 164 -LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERfLHDYEG-TVVAITHD----RYFLDNVA 227
Cdd:COG4608 157 eFSGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQVLNLLED-LQDELGlTYLFISHDlsvvRHISDRVA 229
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
325-502 |
1.03e-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: 53.70 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSY--GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLF----RMLS--GQEQPDA---GSITMGE-----TVV 388
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLNteGDIQIDGvswNSVPLQKwrkafGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 389 LASVDQFRDAMDDKKTVWEEVSNgQDILTIGNfEIPSRAYV----GRFNFKGVDQQKrvgELSGGERGRLHLAKLLQRGG 464
Cdd:cd03289 83 PQKVFIFSGTFRKNLDPYGKWSD-EEIWKVAE-EVGLKSVIeqfpGQLDFVLVDGGC---VLSHGHKQLMCLARSVLSKA 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1735515619 465 NVLLLDEPTNDLDVETLRALENAILE-FPGCAMVISHDR 502
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQaFADCTVILSEHR 196
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
344-490 |
1.18e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 52.66 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 344 SFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQFRDAMDDKK-------TVWEEVSNGQDi 415
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLnGQDHTTTPPSRRPVSMLFQEnnlfshlTVAQNIGLGLN- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 416 ltignfeiPSRayvgRFNfkgVDQQKRV-----------------GELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDv 478
Cdd:PRK10771 98 --------PGL----KLN---AAQREKLhaiarqmgiedllarlpGQLSGGQRQRVALARCLVREQPILLLDEPFSALD- 161
|
170
....*....|..
gi 1735515619 479 etlRALENAILE 490
Cdd:PRK10771 162 ---PALRQEMLT 170
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
325-522 |
1.20e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.12 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDagsitmGETVVLASVDQFRDAMDDKK- 403
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE------SEVRVEGRVEFFNQNIYERRv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 404 ---------------------TVWEEVSNGQDIltIG---NFEIPSrayVGRFNFKGVDQ--------QKRVGELSGGER 451
Cdd:PRK14258 82 nlnrlrrqvsmvhpkpnlfpmSVYDNVAYGVKI--VGwrpKLEIDD---IVESALKDADLwdeikhkiHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1735515619 452 GRLHLAKLLQRGGNVLLLDEPTNDLD------VETLraLENAILEFPGCAMVISHDRWFLDRIATHILDY-GDEGKVT 522
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDpiasmkVESL--IQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkGNENRIG 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
325-488 |
1.20e-07 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 52.93 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDR---TLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQFRD--- 397
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDIRDLNLRWLRSqig 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 398 ---------AMddkkTVWEEVSNGQDILTIGNFEIPSR-AYVGRFNFKGVDQ-QKRVGE----LSGGERGRLHLAKLLQR 462
Cdd:cd03249 81 lvsqepvlfDG----TIAENIRYGKPDATDEEVEEAAKkANIHDFIMSLPDGyDTLVGErgsqLSGGQKQRIAIARALLR 156
|
170 180
....*....|....*....|....*.
gi 1735515619 463 GGNVLLLDEPTNDLDVETLRALENAI 488
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEAL 182
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
349-514 |
1.26e-07 |
|
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: 51.22 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 349 KGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSitmgetVVLASVDQFRDAMDDKktvweevsngqdiltignfeipsray 428
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG------VIYIDGEDILEEVLDQ-------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 429 vgrfnFKGVDQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVET---------LRALENAILEFPGCAMVIS 499
Cdd:smart00382 49 -----LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllleeLRLLLLLKSEKNLTVILTT 123
|
170
....*....|....*.
gi 1735515619 500 HDR-WFLDRIATHILD 514
Cdd:smart00382 124 NDEkDLGPALLRRRFD 139
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-200 |
1.29e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.20 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 17 PPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkeFEgearPQPG-IKI-----------------GYLPQE 78
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRV---FD----PQSGrILIdgtdirtvtraslrrniAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 79 PKLEpQQTVREAV----EEAVSEvksaltrldEVYAlyadpdadfdklAAEQAnleaiiQAHDghnldnQLERAADALrl 154
Cdd:PRK13657 418 AGLF-NRSIEDNIrvgrPDATDE---------EMRA------------AAERA------QAHD------FIERKPDGY-- 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1735515619 155 pdwDAKI----EHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA 200
Cdd:PRK13657 462 ---DTVVgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEA 508
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
325-500 |
1.40e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 54.34 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSY-GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSI--------TMGETVV---LASV 392
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIrldgrplsSLSHSVLrqgVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 393 DQFRDAMDDkkTVWEEVSNGQDI---LTIGNFEIPSRAYVGRFNFKGVdqQKRVGE----LSGGERGRLHLAKLLQRGGN 465
Cdd:PRK10790 421 QQDPVVLAD--TFLANVTLGRDIseeQVWQALETVQLAELARSLPDGL--YTPLGEqgnnLSVGQKQLLALARVLVQTPQ 496
|
170 180 190
....*....|....*....|....*....|....*..
gi 1735515619 466 VLLLDEPTNDLDVETLRALENAILEFPGCA--MVISH 500
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVREHTtlVVIAH 533
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-195 |
1.40e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.53 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARpQPGiKIGYLPQEPKLEPQqTVREAVeeavsevksa 101
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-HSG-RISFSPQTSWIMPG-TIKDNI---------- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 102 ltrldeVYALYADpdadfdklaaeQANLEAIIQAHdghNLDNQLERAADALRLPDWDAKIEhLSGGERRRVALCRLLLEK 181
Cdd:TIGR01271 508 ------IFGLSYD-----------EYRYTSVIKAC---QLEEDIALFPEKDKTVLGEGGIT-LSGGQRARISLARAVYKD 566
|
170
....*....|....
gi 1735515619 182 PDMLLLDEPTNHLD 195
Cdd:TIGR01271 567 ADLYLLDSPFTHLD 580
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
121-218 |
2.25e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 121 KLAAEQANLEAIIQAHDGHNLDNQLERaadalrLPD-WDAKI----EHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
Cdd:PTZ00265 1317 KFGKEDATREDVKRACKFAAIDEFIES------LPNkYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
90 100
....*....|....*....|....*..
gi 1735515619 196 AESVAWLERFLHDY----EGTVVAITH 218
Cdd:PTZ00265 1391 SNSEKLIEKTIVDIkdkaDKTIITIAH 1417
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
10-218 |
2.37e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 52.71 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 10 HRVGKVVPPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-----EARPQPGI----------KIGY 74
Cdd:PRK13634 10 HRYQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtvtigERVITAGKknkklkplrkKVGI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 75 LPQEPKlepQQTVREAVEE---------AVSEvKSALTRLDEVYALYADPDADFDKLAAEqanleaiiqahdghnldnql 145
Cdd:PRK13634 90 VFQFPE---HQLFEETVEKdicfgpmnfGVSE-EDAKQKAREMIELVGLPEELLARSPFE-------------------- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1735515619 146 eraadalrlpdwdakiehLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA----ESVAWLERfLHDYEG-TVVAITH 218
Cdd:PRK13634 146 ------------------LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPkgrkEMMEMFYK-LHKEKGlTTVLVTH 204
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-195 |
2.97e-07 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 53.20 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-----------ARPQPGIKIGYLPQEPklepqqtvr 88
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEillngfslkdiDRHTLRQFINYLPQEP--------- 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 89 eaveeavseVKSALTRLDEVYaLYADPDADFDKlaaeqanleaIIQAHDGHNLDNQLERAADALRlPDWDAKIEHLSGGE 168
Cdd:TIGR01193 558 ---------YIFSGSILENLL-LGAKENVSQDE----------IWAACEIAEIKDDIENMPLGYQ-TELSEEGSSISGGQ 616
|
170 180
....*....|....*....|....*..
gi 1735515619 169 RRRVALCRLLLEKPDMLLLDEPTNHLD 195
Cdd:TIGR01193 617 KQRIALARALLTDSKVLILDESTSNLD 643
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
25-228 |
3.00e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.42 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 25 DISLSFFPGAKIGVLGLNGAGKS-TLLRIMAGVDK--EFEGEARPQpGIKIGYLPQepklepqqtvreaveeavsevkSA 101
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAAngRIGGSATFN-GREILNLPE----------------------KE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 102 LTRL--DEVYALYADPDADFDKLAAEQANLEAIIQAHDGHNLDNQLE---RAADALRLPDWDAKIE---H-LSGGERRRV 172
Cdd:PRK09473 91 LNKLraEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEesvRMLDAVKMPEARKRMKmypHeFSGGMRQRV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 173 ALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHDryfLDNVAG 228
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD---LGVVAG 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
327-517 |
3.03e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.86 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 327 VQNLTKSY--GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRDAMD---D 401
Cdd:TIGR01257 931 VKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGmcpQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 402 KKTVWEEVSNGQDILTIGNFEIPSRAYV-----GRFNFKGVDQQK--RVGELSGGERGRLHLAKLLQRGGNVLLLDEPTN 474
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAqlemeAMLEDTGLHHKRneEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1735515619 475 DLDVETLRALENAILEFPGCAMVIshdrwfldrIATHILDYGD 517
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKYRSGRTII---------MSTHHMDEAD 1124
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-218 |
3.23e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 51.96 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM---------AGVDKE--FEGEARPQPGI-------KIGYLPQEPK 80
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlipgARVEGEilLDGEDIYDPDVdvvelrrRVGMVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 81 LEPQqTVREAVeeavsevksaltrldeVYALyadpdadfdklaaeqanleAIIQAHDGHNLDnqlERAADALR---LpdW 157
Cdd:COG1117 103 PFPK-SIYDNV----------------AYGL-------------------RLHGIKSKSELD---EIVEESLRkaaL--W 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 158 DakiE----------HLSGGERRRvaLC--RLLLEKPDMLLLDEPTNHLDAESVAWLERFLH----DYegTVVAITH 218
Cdd:COG1117 142 D---EvkdrlkksalGLSGGQQQR--LCiaRALAVEPEVLLMDEPTSALDPISTAKIEELILelkkDY--TIVIVTH 211
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-478 |
3.33e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpqpgikIGYLPQEPKLepqQTVREAVEEAVSEVKSAL 102
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGS--------ILFQGKEIDF---KSSKEALENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 103 TRLDEVYALyadpdadfDKLAAEQANLEAIIQAHDghNLDNQLERAADALRLP-DWDAKIEHLSGGERRRVALCRLLLEK 181
Cdd:PRK10982 83 NLVLQRSVM--------DNMWLGRYPTKGMFVDQD--KMYRDTKAIFDELDIDiDPRAKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 182 PDMLLLDEPTNHLDAESVAWLERFLHDYEgtvvaithdryfldnvagwilelDRGEGIpwegnysSWLEQKekrleQEQA 261
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLK-----------------------ERGCGI-------VYISHK-----MEEI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 262 AENARQKSIAKELEWVRQNP-KGRQAKSKARMARFDELNSGEYQKRNETNELfippgprlgdkVIEVQNLTKSygDRTLI 340
Cdd:PRK10982 198 FQLCDEITILRDGQWIATQPlAGLTMDKIIAMMVGRSLTQRFPDKENKPGEV-----------ILEVRNLTSL--RQPSI 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 341 DDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVvlasvdqfrdamdDKKTVWEEVSNGQDILT-- 417
Cdd:PRK10982 265 RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLhGKKI-------------NNHNANEAINHGFALVTee 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 418 ------IGNFEIP-------SRAYVGRF-------------------NFKGVDQQKRVGELSGGERGRLHLAKLLQRGGN 465
Cdd:PRK10982 332 rrstgiYAYLDIGfnslisnIRNYKNKVglldnsrmksdtqwvidsmRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPE 411
|
490
....*....|...
gi 1735515619 466 VLLLDEPTNDLDV 478
Cdd:PRK10982 412 ILMLDEPTRGIDV 424
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
8-217 |
3.34e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.94 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 8 TMHRVGKVVPPKRH--ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkeFEGEARPQPGIKI------------- 72
Cdd:PRK09984 3 TIIRVEKLAKTFNQhqALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSAGSHIELlgrtvqregrlar 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 73 ---------GYLPQEPKLEPQQTVREAVeeAVSEVKSA---------LTRLDEVYALYAdpdadfdklaaeqanLEAIIQ 134
Cdd:PRK09984 80 dirksrantGYIFQQFNLVNRLSVLENV--LIGALGSTpfwrtcfswFTREQKQRALQA---------------LTRVGM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 135 AHDGHNldnqleraadalrlpdwdaKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY---EG 211
Cdd:PRK09984 143 VHFAHQ-------------------RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqnDG 203
|
....*.
gi 1735515619 212 TVVAIT 217
Cdd:PRK09984 204 ITVVVT 209
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
329-500 |
3.48e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 329 NLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSIT-MGETVvlasvdqfrdamdDKKTVWE 407
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILfQGKEI-------------DFKSSKE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 408 EVSNG-----QDILTIGNFEIPSRAYVGRFNFKG--VDQQK--------------------RVGELSGGERGRLHLAKLL 460
Cdd:PRK10982 70 ALENGismvhQELNLVLQRSVMDNMWLGRYPTKGmfVDQDKmyrdtkaifdeldididpraKVATLSVSQMQMIEIAKAF 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1735515619 461 QRGGNVLLLDEPTNDLDVETLRALENAI--LEFPGCAMV-ISH 500
Cdd:PRK10982 150 SYNAKIVIMDEPTSSLTEKEVNHLFTIIrkLKERGCGIVyISH 192
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
23-252 |
3.68e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 53.10 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKST---LLRIMAGVDkefEGEarpqpgIKI-GYLPQEPKLepqQTVREAVEeAVSEv 98
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTianLLTRFYDID---EGE------ILLdGHDLRDYTL---ASLRNQVA-LVSQ- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 99 ksaltrldEVYaLYADPDADfdklaaeqanleAIIQAHDGHNLDNQLERAADALRLPDWDAKIEH------------LSG 166
Cdd:PRK11176 425 --------NVH-LFNDTIAN------------NIAYARTEQYSREQIEEAARMAYAMDFINKMDNgldtvigengvlLSG 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawlERFLH------DYEGTVVAITHDRYFLDNvAGWILELDRGEgIP 240
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTES----ERAIQaaldelQKNRTSLVIAHRLSTIEK-ADEILVVEDGE-IV 557
|
250
....*....|..
gi 1735515619 241 WEGNYSSWLEQK 252
Cdd:PRK11176 558 ERGTHAELLAQN 569
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-302 |
3.80e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.24 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 18 PKRhILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdkEFE-GEARPQPGIKIGYLPQEPKLEpQQTVREAVeeavs 96
Cdd:PTZ00243 672 PKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS---QFEiSEGRVWAERSIAYVPQQAWIM-NATVRGNI----- 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 97 evksaltrldevyaLYADPDadfdklaaEQANLEAIIQAhdghnldNQLEraADALRLP-----DWDAKIEHLSGGERRR 171
Cdd:PTZ00243 742 --------------LFFDEE--------DAARLADAVRV-------SQLE--ADLAQLGggletEIGEKGVNLSGGQKAR 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 172 VALCRLLLEKPDMLLLDEPTNHLDA---ESVAwLERFLHDYEG-TVVAITHDRYFLDNvAGWILELDRGEgIPWEGNYSS 247
Cdd:PTZ00243 791 VSLARAVYANRDVYLLDDPLSALDAhvgERVV-EECFLGALAGkTRVLATHQVHVVPR-ADYVVALGDGR-VEFSGSSAD 867
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 248 WLEQKekrLEQEQAAEnarqksiakelewVRQNPKGRQAKSKARMARFDELNSGE 302
Cdd:PTZ00243 868 FMRTS---LYATLAAE-------------LKENKDSKEGDADAEVAEVDAAPGGA 906
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-218 |
4.09e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLL-----RIMAGVdkeFEGEARPQPGIK--------IGYLPQEPKLEPQQ 85
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTGV---ITGGDRLVNGRPldssfqrsIGYVQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 TVREAVEeavsevKSALTRLDEVYALYADPDAdfdklaaeqanLEAIIQAHdghnldnQLERAADAL-RLPDwdakiEHL 164
Cdd:TIGR00956 852 TVRESLR------FSAYLRQPKSVSKSEKMEY-----------VEEVIKLL-------EMESYADAVvGVPG-----EGL 902
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 165 SGGERRRVALCRLLLEKPDMLL-LDEPTNHLDAESvAW----LERFLHDYEGTVVAITH 218
Cdd:TIGR00956 903 NVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT-AWsickLMRKLADHGQAILCTIH 960
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
12-196 |
5.31e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.77 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 12 VGKVVPPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpqpgIKIG-----YLpqEPK------ 80
Cdd:PRK11650 9 VRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE------IWIGgrvvnEL--EPAdrdiam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 81 ------LEPQQTVREAVEeavsevksaltrldevYALyadPDADFDKlaaeqanleAIIQAhdghnldnQLERAADALRL 154
Cdd:PRK11650 81 vfqnyaLYPHMSVRENMA----------------YGL---KIRGMPK---------AEIEE--------RVAEAARILEL 124
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1735515619 155 -PDWDAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 196
Cdd:PRK11650 125 ePLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
340-381 |
5.57e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.20 E-value: 5.57e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1735515619 340 IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSI 381
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
343-500 |
5.59e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 343 LSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGE--------------------TVVLAS------VDQFR 396
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfglmdlrkvlgiipqAPVLFSgtvrfnLDPFN 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 397 DAMDdkKTVWEEVSngqdiltignfeipsRAY---VGRFNFKGVDQQ-KRVGE-LSGGERGRLHLAKLLQRGGNVLLLDE 471
Cdd:PLN03130 1338 EHND--ADLWESLE---------------RAHlkdVIRRNSLGLDAEvSEAGEnFSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190
....*....|....*....|....*....|.
gi 1735515619 472 PTNDLDVETLRALENAIL-EFPGCAM-VISH 500
Cdd:PLN03130 1401 ATAAVDVRTDALIQKTIReEFKSCTMlIIAH 1431
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
36-219 |
7.11e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 50.01 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 36 IGVLGLNGAGKSTLLRIMAGVdkeFEGEARPQPGIK---IGYLPQEPKLE--------------PQQTVREAVEEAVSEV 98
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIRYA---LYGKARSRSKLRsdlINVGSEEASVElefehggkryrierRQGEFAEFLEAKPSER 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 99 KSALTRL--DEVYALYADpdadfdKLAAEQANLEAIIQAhdghnLDNQLERAADALRLPDWDAKIEHLSGGERRRVALCR 176
Cdd:COG0419 103 KEALKRLlgLEIYEELKE------RLKELEEALESALEE-----LAELQKLKQEILAQLSGLDPIETLSGGERLRLALAD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1735515619 177 LLlekpdMLLLDepTNHLDAESvawLERFLHDYEGTVVaITHD 219
Cdd:COG0419 172 LL-----SLILD--FGSLDEER---LERLLDALEELAI-ITHV 203
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
164-239 |
7.60e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.98 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG---TVVAITHDryfLDNVAGW---ILELDRGE 237
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHN---MDDVAEYaddVLVLEHGK 222
|
..
gi 1735515619 238 GI 239
Cdd:PRK13641 223 LI 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-200 |
9.93e-07 |
|
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: 49.35 E-value: 9.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE--------ARPQPG----IKIGYLPQEPKLE---PQQTV 87
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEitldgkpvTRRSPRdairAGIAYVPEDRKREglvLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 88 REaveeavsevksaltrldevyalyadpdadfdklaaeqaNLeaiiqahdghnldnqleraadALRLpdwdakieHLSGG 167
Cdd:cd03215 96 AE--------------------------------------NI---------------------ALSS--------LLSGG 108
|
170 180 190
....*....|....*....|....*....|...
gi 1735515619 168 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA 200
Cdd:cd03215 109 NQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-219 |
1.03e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 51.19 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQpGIKIGYLPQepklepqQTVREAVEEAVSEVKSAL 102
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLID-GVDIAKISD-------AELREVRRKKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 103 TRLDEVYALyadpdaDFDKLAAEQANLEAiiqahdghnlDNQLERAADALR---LPDW-DAKIEHLSGGERRRVALCRLL 178
Cdd:PRK10070 116 ALMPHMTVL------DNTAFGMELAGINA----------EERREKALDALRqvgLENYaHSYPDELSGGMRQRVGLARAL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1735515619 179 LEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHD 219
Cdd:PRK10070 180 AINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHD 224
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
332-485 |
1.03e-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: 49.57 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 332 KSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQ----EQPDaGSITMGETVVLASVDQFRDamddkktvwE 407
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegnVSVE-GDIHYNGIPYKEFAEKYPG---------E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 408 EVSNGQD-----ILTIG---NFEIPSRayvGRFNFKGVdqqkrvgelSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVE 479
Cdd:cd03233 85 IIYVSEEdvhfpTLTVRetlDFALRCK---GNEFVRGI---------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
....*.
gi 1735515619 480 TlrALE 485
Cdd:cd03233 153 T--ALE 156
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-217 |
1.08e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQPG------------IKIGYLPQEPKLEpQQTVRE 89
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrSKIGVVSQDPLLF-SNSIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 90 AVEEAVSEVKSaLTRLDEVY-----ALYADPDADFDKLAAEQANLEAIIQAHDGHNL-----------DNQLERAADAL- 152
Cdd:PTZ00265 479 NIKYSLYSLKD-LEALSNYYnedgnDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELiemrknyqtikDSEVVDVSKKVl 557
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 153 ------RLPD-WDAKI----EHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAIT 217
Cdd:PTZ00265 558 ihdfvsALPDkYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-195 |
1.11e-06 |
|
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: 50.24 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdkefegEARPQPGI-----KIGYLPQEPKLEPQqTVREAVEEAVS 96
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILG-------ELEPSEGKikhsgRISFSSQFSWIMPG-TIKENIIFGVS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 97 evksaltrldevyalyadpdadfdklaAEQANLEAIIQAhdghnldNQLERaaDALRLPDWDAKIE-----HLSGGERRR 171
Cdd:cd03291 124 ---------------------------YDEYRYKSVVKA-------CQLEE--DITKFPEKDNTVLgeggiTLSGGQRAR 167
|
170 180
....*....|....*....|....
gi 1735515619 172 VALCRLLLEKPDMLLLDEPTNHLD 195
Cdd:cd03291 168 ISLARAVYKDADLYLLDSPFGYLD 191
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
322-516 |
1.13e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.03 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 322 DKVIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGqeQPdAGSITMGETVVlasvdqfrdamdd 401
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HP-AYKILEGDILF------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 402 kktvweevsNGQDILTI--------GNF-------EIPS--------RAYVGRFNFKGVDQ------------------- 439
Cdd:CHL00131 69 ---------KGESILDLepeerahlGIFlafqypiEIPGvsnadflrLAYNSKRKFQGLPEldplefleiineklklvgm 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 440 -----QKRVGE-LSGGERGR---LHLAkLLQrgGNVLLLDEPTNDLDVETLRALENAILEFPG---CAMVISHDRWFLDR 507
Cdd:CHL00131 140 dpsflSRNVNEgFSGGEKKRneiLQMA-LLD--SELAILDETDSGLDIDALKIIAEGINKLMTsenSIILITHYQRLLDY 216
|
250
....*....|..
gi 1735515619 508 IA---THILDYG 516
Cdd:CHL00131 217 IKpdyVHVMQNG 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
343-500 |
1.32e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 343 LSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMG--------------------ETVVLAS------VDQFR 396
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDdcdvakfgltdlrrvlsiipQSPVLFSgtvrfnIDPFS 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 397 DAMDdkKTVWE--EVSNGQDILTIGNFEIPSRAYVGRFNFkgvdqqkrvgelSGGERGRLHLAKLLQRGGNVLLLDEPTN 474
Cdd:PLN03232 1335 EHND--ADLWEalERAHIKDVIDRNPFGLDAEVSEGGENF------------SVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180
....*....|....*....|....*...
gi 1735515619 475 DLDVETLRALENAIL-EFPGCAM-VISH 500
Cdd:PLN03232 1401 SVDVRTDSLIQRTIReEFKSCTMlVIAH 1428
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
325-501 |
1.34e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 49.24 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLtKSYGDRTLIDdlsfsIPKGaIVGIIGANGAGKSTLFR----MLSGQ-------------EQPDAGSITM---- 383
Cdd:COG0419 5 LRLENF-RSYRDTETID-----FDDG-LNLIVGPNGAGKSTILEairyALYGKarsrsklrsdlinVGSEEASVELefeh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 384 -----------GETVVLAS---------------VDQFRDAMDDKKTVWEEVSngQDILTIGNFEIPSRAYVGRFN-FKG 436
Cdd:COG0419 78 ggkryrierrqGEFAEFLEakpserkealkrllgLEIYEELKERLKELEEALE--SALEELAELQKLKQEILAQLSgLDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 437 VDQqkrvgeLSGGERGRLHLAKLLQrggnvLLLDepTNDLDVETLRALENAILEfpgcAMVISHD 501
Cdd:COG0419 156 IET------LSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
19-219 |
1.40e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 49.98 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 19 KRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-----------ARPQPGIKIGYLPQEPKLEPQQTV 87
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHvwldgehiqhyASKEVARRIGLLAQNATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 88 REAVEEAVSEVKSALTRLDEvyalyADPDAdfdklaaeqanLEAIIQAHDGHNLDNQleraadalrlpdwdaKIEHLSGG 167
Cdd:PRK10253 99 QELVARGRYPHQPLFTRWRK-----EDEEA-----------VTKAMQATGITHLADQ---------------SVDTLSGG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 168 ERRRVALCRLLLEKPDMLLLDEPTNHLD-AESVAWLERF--LHDYEG-TVVAITHD 219
Cdd:PRK10253 148 QRQRAWIAMVLAQETAIMLLDEPTTWLDiSHQIDLLELLseLNREKGyTLAAVLHD 203
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-242 |
1.66e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 49.70 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGVDKEFEG---EARPqpgiKIGYLPQEPKlepQQT 86
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMnallipsegkvyvDGLDTSDEEnlwDIRN----KAGMVFQNPD---NQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 87 VREAVEEAVsevksaltrldevyalyadpdadfdklAAEQANLeaiiqahdGHNLDNQLERAADAL-RLPDWDAKiEH-- 163
Cdd:PRK13633 99 VATIVEEDV---------------------------AFGPENL--------GIPPEEIRERVDESLkKVGMYEYR-RHap 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 164 --LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA----ESVAWLERFLHDYEGTVVAITHdryFLDNV--AGWILELDR 235
Cdd:PRK13633 143 hlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPsgrrEVVNTIKELNKKYGITIILITH---YMEEAveADRIIVMDS 219
|
250
....*....|.
gi 1735515619 236 G----EGIPWE 242
Cdd:PRK13633 220 GkvvmEGTPKE 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
164-227 |
2.68e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 49.36 E-value: 2.68e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERF---LHDYEGTVVAITHdryFLDNVA 227
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLfkkLHQSGMTIVLVTH---LMDDVA 209
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
324-488 |
3.40e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.94 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDdLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSI----------------TMGETV 387
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIyykncninniakpyctYIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 388 VLasvdQFRDAMDDKKTVWEEVSNGQDILtignfeipsraYVGRFNFKGVD-QQKRVGELSGGERGRLHLAKLLQRGGNV 466
Cdd:PRK13541 80 GL----KLEMTVFENLKFWSEIYNSAETL-----------YAAIHYFKLHDlLDEKCYSLSSGMQKIVAIARLIACQSDL 144
|
170 180
....*....|....*....|..
gi 1735515619 467 LLLDEPTNDLDVETLRALENAI 488
Cdd:PRK13541 145 WLLDEVETNLSKENRDLLNNLI 166
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
161-224 |
3.45e-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: 3.45e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 161 IEHLSGGERR------RVALCRLLLEKPDMLLLDEPTNHLDAESVAW-LERFLHDYEGT----VVAITHDRYFLD 224
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQknfqLIVITHDEELVD 187
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
340-521 |
4.13e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 48.62 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 340 IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLAS---------------VDQFRDAMDDKKT 404
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdkyirpvrkrigmVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 405 VWEEVSNGQDILTIGNFEIPSRAY--VGRFNFKGVDQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLD----V 478
Cdd:PRK13646 103 VEREIIFGPKNFKMNLDEVKNYAHrlLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDpqskR 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1735515619 479 ETLRALENAILEFPGCAMVISHDrwfLDRIAThildYGDEGKV 521
Cdd:PRK13646 183 QVMRLLKSLQTDENKTIILVSHD---MNEVAR----YADEVIV 218
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
20-215 |
4.16e-06 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 49.72 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE----ARPQPGIKIGYLPQEPKLEPQQTV--REAVEE 93
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQilldGHDLADYTLASLRRQVALVSQDVVlfNDTIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 94 AVsevksALTRLDEVyalyadPDADFDKlAAEQANLEAIIqahDGHNLDNQLERAADALRLpdwdakiehlSGGERRRVA 173
Cdd:TIGR02203 425 NI-----AYGRTEQA------DRAEIER-ALAAAYAQDFV---DKLPLGLDTPIGENGVLL----------SGGQRQRLA 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1735515619 174 LCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVA 215
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESerlvQAALERLMQGRTTLVIA 525
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-219 |
5.05e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 49.30 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 13 GKVVPPKRhILKDISLSFFPGAKIGVLGLNGAGKSTL----LRIMagvdkEFEGEARPQpGIKIGYLP------------ 76
Cdd:COG4172 293 RRTVGHVK-AVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFD-GQDLDGLSrralrplrrrmq 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 77 ---QEP--KLEPQQTVREAVEEAVSEVKSALTRldevyalyadpdadfdklaaeQANLEAIIQAHDGHNLDnqlerAADA 151
Cdd:COG4172 366 vvfQDPfgSLSPRMTVGQIIAEGLRVHGPGLSA---------------------AERRARVAEALEEVGLD-----PAAR 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 152 LRLPdwdakieH-LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHD 219
Cdd:COG4172 420 HRYP-------HeFSGGQRQRIAIARALILEPKLLVLDEPTSALDvsvqAQILDLLRDLQREHGLAYLFISHD 485
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-219 |
5.14e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.17 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGeARPQPGIKIGylpqepklepqqtvreavEEAVSEVK 99
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLG------------------GRSIFNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 100 SALTRLDEVYALYADPDAdfdklaAEQANLEAIIQAHDGHNLDNQLE-RAADALRLPD---WDAKIEHLS-------GGE 168
Cdd:PRK14271 95 DVLEFRRRVGMLFQRPNP------FPMSIMDNVLAGVRAHKLVPRKEfRGVAQARLTEvglWDAVKDRLSdspfrlsGGQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG--TVVAITHD 219
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
164-237 |
5.16e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 48.51 E-value: 5.16e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1735515619 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHD-YEGTVVAITHDRYFLDNVAGWILELDRGE 237
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkgrDEILNKIKELHKeYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
445-519 |
5.33e-06 |
|
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: 47.99 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 445 ELSGGERGRLHLAKLLQRG--GNVL-LLDEPTNDL---DVETLRALENAILEFPGCAMVISHDrwfLD--RIATHILDYG 516
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRstGKTLyILDEPTTGLhfhDVKKLLEVLQRLVDKGNTVVVIEHN---LDviKCADWIIDLG 245
|
...
gi 1735515619 517 DEG 519
Cdd:cd03271 246 PEG 248
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
323-512 |
5.48e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.16 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 323 KVIEVQNLTkSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKS--------TL---FRMLSGQ----EQPDAGSITMGETV 387
Cdd:PRK10418 3 QQIELRNIA-LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaaalgILpagVRQTAGRvlldGKPVAPCALRGRKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 388 vlASVDQF-RDAMDDKKTVweeVSNGQDILTIGNFEIPSRAYVGRFNFKGVDQQKRVG-----ELSGGERGRLHLAKLLQ 461
Cdd:PRK10418 82 --ATIMQNpRSAFNPLHTM---HTHARETCLALGKPADDATLTAALEAVGLENAARVLklypfEMSGGMLQRMMIALALL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 462 RGGNVLLLDEPTNDLD-VETLRALE--NAILEFPGCAMVI-SHDRWFLDRIATHI 512
Cdd:PRK10418 157 CEAPFIIADEPTTDLDvVAQARILDllESIVQKRALGMLLvTHDMGVVARLADDV 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
163-236 |
6.01e-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: 47.71 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 163 HLSGGERRRVALCRLLLEKPDMLLLDEP--------TNHLDAESVAwleRFLHDYEGTVVAITHDRYFLDNvAGWILELD 234
Cdd:cd03290 140 NLSGGQRQRICVARALYQNTNIVFLDDPfsaldihlSDHLMQEGIL---KFLQDDKRTLVLVTHKLQYLPH-ADWIIAMK 215
|
..
gi 1735515619 235 RG 236
Cdd:cd03290 216 DG 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
337-477 |
6.34e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 337 RTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVvlASVDQFRDAMDdkKTVW--------EE 408
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSI--AYVPQQAWIMN--ATVRgnilffdeED 748
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735515619 409 VSNGQDILTIGNFEIPSRAYVGrfnfkGVDQQkrVGE----LSGGERGRLHLAKLLQRGGNVLLLDEPTNDLD 477
Cdd:PTZ00243 749 AARLADAVRVSQLEADLAQLGG-----GLETE--IGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
140-224 |
7.58e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.83 E-value: 7.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 140 NLDNQLERAADALRLPDWDAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWL---------ERFLHDYE 210
Cdd:smart00382 37 DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleelrllLLLKSEKN 116
|
90
....*....|....
gi 1735515619 211 GTVVAITHDRYFLD 224
Cdd:smart00382 117 LTVILTTNDEKDLG 130
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
324-372 |
8.23e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 8.23e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSG 372
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
335-480 |
9.24e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 46.47 E-value: 9.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 335 GDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEqpDAGSITmGE------------TVVLASVDQFrDAMDDK 402
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRK--TAGVIT-GEilingrpldknfQRSTGYVEQQ-DVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 403 KTVWEEVsngqdiltignfeipsrayvgRF--NFKGvdqqkrvgeLSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVET 480
Cdd:cd03232 94 LTVREAL---------------------RFsaLLRG---------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
22-220 |
9.73e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 47.54 E-value: 9.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRI---MAGVDKEFEGEARPQPGIkigylpqepklePQQTVREA---VEEAV 95
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAflrLLNTEGDIQIDGVSWNSV------------PLQKWRKAfgvIPQKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 96 SEVKSALTRLDEVYALYADPDAdfdKLAAEQANLEAIIQAHDGHnLDNQLERAADAlrlpdwdakiehLSGGERRRVALC 175
Cdd:cd03289 87 FIFSGTFRKNLDPYGKWSDEEI---WKVAEEVGLKSVIEQFPGQ-LDFVLVDGGCV------------LSHGHKQLMCLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1735515619 176 RLLLEKPDMLLLDEPTNHLDAESVAWLERFL-HDYEGTVVAITHDR 220
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTLkQAFADCTVILSEHR 196
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
23-219 |
1.08e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.18 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFfPGAKIGVL-GLNGAGKSTLLRIMAGVDKEFEGEAR--PQPGIK------IGYLPQEPKLEPQQTVreAVEE 93
Cdd:PRK15056 23 LRDASFTV-PGGSIAALvGVNGSGKSTLFKALMGFVRLASGKISilGQPTRQalqknlVAYVPQSEEVDWSFPV--LVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 94 AVsevksALTRLDEVYALyadpdadfdklaaeqanleAIIQAHDGHNLDNQLERAaDALRLPDwdAKIEHLSGGERRRVA 173
Cdd:PRK15056 100 VV-----MMGRYGHMGWL-------------------RRAKKRDRQIVTAALARV-DMVEFRH--RQIGELSGGQKKRVF 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1735515619 174 LCRLLLEKPDMLLLDEPTNHLDAESVAW---LERFLHDYEGTVVAITHD 219
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARiisLLRELRDEGKTMLVSTHN 201
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
23-219 |
1.09e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 47.08 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFfPGAKI-GVLGLNGAGKSTLLRIMAGVDKEFEGeARPQPgiKIGYLPQE---PKLEPqqtvreaveeavSEV 98
Cdd:PRK14243 26 VKNVWLDI-PKNQItAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEG--KVTFHGKNlyaPDVDP------------VEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 99 KSaltRLDEVYAL-YADPDADFDKLAaeqanLEAIIQAHDGhNLDNQLERAADALRLpdWDA---KIEH----LSGGERR 170
Cdd:PRK14243 90 RR---RIGMVFQKpNPFPKSIYDNIA-----YGARINGYKG-DMDELVERSLRQAAL--WDEvkdKLKQsglsLSGGQQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1735515619 171 RVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAITHD 219
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELkeQYTIIIVTHN 209
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
33-227 |
1.10e-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: 46.03 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 33 GAKIGVLGLNGAGKSTLLRIMAGVDKEfEGEARPQPGIKIGYLPQEPKlepqqtvreaveeavsevksaltrldevyaly 112
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIP-NGDNDEWDGITPVYKPQYID-------------------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 113 adpdadfdklaaeqanleaiiqahdghnldnqleraadalrlpdwdakiehLSGGERRRVALCRLLLEKPDMLLLDEPTN 192
Cdd:cd03222 72 ---------------------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSA 100
|
170 180 190
....*....|....*....|....*....|....*....
gi 1735515619 193 HLDAE----SVAWLERFLHDYEGTVVAITHDRYFLDNVA 227
Cdd:cd03222 101 YLDIEqrlnAARAIRRLSEEGKKTALVVEHDLAVLDYLS 139
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-227 |
1.21e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 47.08 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 1 MSSQFVYTMHRVGKVVPPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPQpGIKIGYLPQEPK 80
Cdd:PRK13646 1 MTIRFDNVSYTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-DITITHKTKDKY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 81 LEPqqtVREaveeavsevksaltrldEVYALYADPDAdfdKLAAEQANLEAIIQAHD-GHNLDNQLERAADALRLPDWDA 159
Cdd:PRK13646 80 IRP---VRK-----------------RIGMVFQFPES---QLFEDTVEREIIFGPKNfKMNLDEVKNYAHRLLMDLGFSR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1735515619 160 KIE-----HLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITHDryfLDNVA 227
Cdd:PRK13646 137 DVMsqspfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSkrqvMRLLKSLQTDENKTIILVSHD---MNEVA 210
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
23-195 |
1.23e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 47.27 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE--------ARPQPGI------KIGYLPQEP--KLEPQQT 86
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGElyyqgqdlLKADPEAqkllrqKIQIVFQNPygSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 87 VREAVEEAVsEVKSALTrldevyalyadpdadfdklAAEQAnleaiiqahdghnldnqlERAADALRL----PDWDAKIE 162
Cdd:PRK11308 111 VGQILEEPL-LINTSLS-------------------AAERR------------------EKALAMMAKvglrPEHYDRYP 152
|
170 180 190
....*....|....*....|....*....|....
gi 1735515619 163 HL-SGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
Cdd:PRK11308 153 HMfSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
10-218 |
1.39e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 47.49 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 10 HRVGKVVP-PKRHI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDkefegeaRPQPGikigylpqepklepqQT 86
Cdd:PRK11153 5 KNISKVFPqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLE-------RPTSG---------------RV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 87 VREAVEeavsevksaLTRLDEvyalyadpdadfDKLAAEQANLEAIIQahdgH-NL-------DNqlerAADALRLPDWD 158
Cdd:PRK11153 63 LVDGQD---------LTALSE------------KELRKARRQIGMIFQ----HfNLlssrtvfDN----VALPLELAGTP 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 159 -AKIE---------------------HLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SV-AWLERFLHDYEGT 212
Cdd:PRK11153 114 kAEIKarvtellelvglsdkadrypaQLSGGQKQRVAIARALASNPKVLLCDEATSALDPAttrSIlELLKDINRELGLT 193
|
....*.
gi 1735515619 213 VVAITH 218
Cdd:PRK11153 194 IVLITH 199
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
23-198 |
1.40e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.02 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-----------ARPQpgikIGYLPQEPKLEPQQTVREAV 91
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNiyykncninniAKPY----CTYIGHNLGLKLEMTVFENL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 92 eeavsevksaltrldevyalyadpdadfdKLAAEQANLEAIIQAhdghnldnqlerAADALRLPDW-DAKIEHLSGGERR 170
Cdd:PRK13541 92 -----------------------------KFWSEIYNSAETLYA------------AIHYFKLHDLlDEKCYSLSSGMQK 130
|
170 180
....*....|....*....|....*...
gi 1735515619 171 RVALCRLLLEKPDMLLLDEPTNHLDAES 198
Cdd:PRK13541 131 IVAIARLIACQSDLWLLDEVETNLSKEN 158
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
23-226 |
1.65e-05 |
|
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: 47.30 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGakIGVL-GLNGAGKSTLLRIM---------AGVDKE--FEGEARPQPGIKI---------GYLPQEPKL 81
Cdd:COG3593 14 IKDLSIELSDD--LTVLvGENNSGKSSILEALrlllgpsssRKFDEEdfYLGDDPDLPEIEIeltfgsllsRLLRLLLKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 82 EPQQTVREAVEEAVSEVKSALTRLDE-----VYALYADPDADFDKLAAEQANLEAIIQAH--DGHNLDnqleraadalrl 154
Cdd:COG3593 92 EDKEELEEALEELNEELKEALKALNEllseyLKELLDGLDLELELSLDELEDLLKSLSLRieDGKELP------------ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 155 pdwdakIEHLSGGERRRV--ALCRLLLE-----KPDMLLLDEPTNHLDAESVAWLERFLHDYEGT---VVAITHDRYFLD 224
Cdd:COG3593 160 ------LDRLGSGFQRLIllALLSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKpnqVIITTHSPHLLS 233
|
..
gi 1735515619 225 NV 226
Cdd:COG3593 234 EV 235
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-199 |
1.94e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.71 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkefegeARPQPGiKIGYLPQEPKLEpqqtvREAVEEAV------ 95
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGL-------LNPEKG-EILFERQSIKKD-----LCTYQKQLcfvghr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 96 SEVKSALTRLDEVYAlyadpDADFDKLAAEQANLEAIIQAhdGHNLDnqleraadalrLPdwdakIEHLSGGERRRVALC 175
Cdd:PRK13540 83 SGINPYLTLRENCLY-----DIHFSPGAVGITELCRLFSL--EHLID-----------YP-----CGLLSSGQKRQVALL 139
|
170 180
....*....|....*....|....
gi 1735515619 176 RLLLEKPDMLLLDEPTNHLDAESV 199
Cdd:PRK13540 140 RLWMSKAKLWLLDEPLVALDELSL 163
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-199 |
2.01e-05 |
|
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: 45.72 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 18 PKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-------------EARPQPGIKIGYLPQEPKLEPQ 84
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSvegdihyngipykEFAEKYPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 85 QTVREAVeeavsevksaltrldevyalyadpdaDFdklaaeqanleaiiqahdghnldnqleraadALRLPDwDAKIEHL 164
Cdd:cd03233 98 LTVRETL--------------------------DF-------------------------------ALRCKG-NEFVRGI 119
|
170 180 190
....*....|....*....|....*....|....*
gi 1735515619 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV 199
Cdd:cd03233 120 SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
340-390 |
2.03e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.35 E-value: 2.03e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1735515619 340 IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLA 390
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRnGEVSVIA 91
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
14-242 |
2.64e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 46.15 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 14 KVVPPKRHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----DKEFEGEARPQPGIKigylpqepklepqqtvr 88
Cdd:PRK13645 18 KKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetGQTIVGDYAIPANLK----------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 89 eaveeAVSEVKSaLTRldEVYALYADPDAD-FDKLAAEQANLEAIIQAHDGHNLDNQLERAADALRLPDWDAKIE--HLS 165
Cdd:PRK13645 81 -----KIKEVKR-LRK--EIGLVFQFPEYQlFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSpfELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGE---- 237
Cdd:PRK13645 153 GGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGeedfINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKvisi 232
|
....*
gi 1735515619 238 GIPWE 242
Cdd:PRK13645 233 GSPFE 237
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
340-501 |
3.01e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 46.57 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 340 IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITM-GETVVLASVDQFRDAMDDK-------------KTV 405
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIdGVDIAKISDAELREVRRKKiamvfqsfalmphMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 406 WEEVSNGQDILTIGNFEIPSRAyvgrfnfkgVDQQKRVG----------ELSGGERGRLHLAKLLQRGGNVLLLDEPTND 475
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKA---------LDALRQVGlenyahsypdELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190
....*....|....*....|....*....|
gi 1735515619 476 LDVETLRALENAILEFPG----CAMVISHD 501
Cdd:PRK10070 195 LDPLIRTEMQDELVKLQAkhqrTIVFISHD 224
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
340-491 |
3.46e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 45.40 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 340 IDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETVVLASVDQFRDAMDD------KKTVWEEVSNGQ 413
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRysvayaAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 414 DILTignFEIPsrayvgrFN---FKGVDQ---------------QKRVGE----LSGGERGRLHLAKLLQRGGNVLLLDE 471
Cdd:cd03290 97 ENIT---FGSP-------FNkqrYKAVTDacslqpdidllpfgdQTEIGErginLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180
....*....|....*....|.
gi 1735515619 472 PTNDLDVE-TLRALENAILEF 491
Cdd:cd03290 167 PFSALDIHlSDHLMQEGILKF 187
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
322-501 |
4.39e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.87 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 322 DKVIEVQNLTKSY----GDRTLIDDLSFSIPKGAIVGIIGANGAGKS-TLFRML---------------SGQE---QPD- 377
Cdd:PRK09473 10 DALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMgllaangriggsatfNGREilnLPEk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 378 ------AGSITM---------------GETvvLASVDQFRDAMdDKKTVWEEvsngqDILTIGNFEIPsrayvgrfnfkg 436
Cdd:PRK09473 90 elnklrAEQISMifqdpmtslnpymrvGEQ--LMEVLMLHKGM-SKAEAFEE-----SVRMLDAVKMP------------ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1735515619 437 vDQQKRVG----ELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVeTLRALENAIL-----EFPGCAMVISHD 501
Cdd:PRK09473 150 -EARKRMKmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAQIMTLLnelkrEFNTAIIMITHD 221
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
20-219 |
5.24e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 44.92 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 20 RHILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAgvdkefeGEARPQPGiKIGYLPQEPKLEPQQTVREAveeavseVK 99
Cdd:PRK11701 19 RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALS-------ARLAPDAG-EVHYRMRDGQLRDLYALSEA-------ER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 100 SALTRLDEVYaLYADPdADFDKLAAEQ-AN----LEAIIQAHDGhnldNQLERAADALRLPDWDA-KIEHL----SGGER 169
Cdd:PRK11701 84 RRLLRTEWGF-VHQHP-RDGLRMQVSAgGNigerLMAVGARHYG----DIRATAGDWLERVEIDAaRIDDLpttfSGGMQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1735515619 170 RRVALCRLLLEKPDMLLLDEPTNHLDAeSVA-----WLERFLHDYEGTVVAITHD 219
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDV-SVQarlldLLRGLVRELGLAVVIVTHD 211
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
325-480 |
6.40e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.50 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 325 IEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAG--KSTLFRMLSGqeqPDAGSITMGETVVLASVDQFRDAMDDK 402
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 403 KTV----WEEVSNGQDILTIGNFEIPSRA--------YVGRFNFKGVdQQKRVGELSGGERGRLHLAKLLQRGGNVLLLD 470
Cdd:NF000106 91 RPVr*grRESFSGRENLYMIGR*LDLSRKdararadeLLERFSLTEA-AGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170
....*....|
gi 1735515619 471 EPTNDLDVET 480
Cdd:NF000106 170 EPTTGLDPRT 179
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
324-509 |
9.75e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 45.06 E-value: 9.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGD----RTLIDDLSFSIPKGAIVGIIGANGAGKS----TLFRMLSGQEQPDAGSITM-GETVVLASVDQ 394
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFdGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 395 FRDAmddkktvweevsNGQDI--------------LTIGN--FEI----------PSRAYVgrfnfkgVDQQKRVG---- 444
Cdd:COG4172 86 LRRI------------RGNRIamifqepmtslnplHTIGKqiAEVlrlhrglsgaAARARA-------LELLERVGipdp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 445 ---------ELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVeTLRAlenAILEF-------PGCAMV-ISHD----RW 503
Cdd:COG4172 147 errldayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVQA---QILDLlkdlqreLGMALLlITHDlgvvRR 222
|
....*.
gi 1735515619 504 FLDRIA 509
Cdd:COG4172 223 FADRVA 228
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
337-501 |
1.10e-04 |
|
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: 42.73 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 337 RTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRmlsgqeqpDAGSITMGETVVLASVDQFRdamddkktvweevsngqdil 416
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILD--------AIGLALGGAQSATRRRSGVK-------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 417 tignfeipSRAYVGR----FNFkgvdqqkRVGELSGGERGRLHLAKLLQ----RGGNVLLLDEPTNDLDVETLRALENAI 488
Cdd:cd03227 60 --------AGCIVAAvsaeLIF-------TRLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAI 124
|
170
....*....|....*.
gi 1735515619 489 LEF--PGC-AMVISHD 501
Cdd:cd03227 125 LEHlvKGAqVIVITHL 140
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
164-242 |
1.21e-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: 45.00 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 164 LSGGERRRVALCRLLLEK---PDMLLLDEPTNHLDAESVAWLERFLH---DYEGTVVAITHDryfLD--NVAGWILEL-- 233
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQrlvDKGNTVVVIEHN---LDviKTADYIIDLgp 906
|
90
....*....|....*..
gi 1735515619 234 ---DRG-----EGIPWE 242
Cdd:TIGR00630 907 eggDGGgtvvaSGTPEE 923
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
22-174 |
1.44e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIgVLGLNGAGKSTLLR-IMAGVDKEFEGEA----RPQPGIKIGYLPQEPKLEpqQTVREAvEEAVS 96
Cdd:COG4717 13 KFRDRTIEFSPGLNV-IYGPNEAGKSTLLAfIRAMLLERLEKEAdelfKPQGRKPELNLKELKELE--EELKEA-EEKEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 97 EVKSALTRLDEVYALYADPDADFDKLAAEQANLEAIIQAHDGHNLDNQLERAADAL--RLPDWDAKIEHLSGGERRRVAL 174
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELpeRLEELEERLEELRELEEELEEL 168
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
446-519 |
1.57e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.62 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 446 LSGGERGRLHLAKLLQR---GGNVLLLDEPTNDL---DVETLRALENAILEFPGCAMVISHDrwfLDRI--ATHILDYGD 517
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLhfdDIKKLLEVLQRLVDKGNTVVVIEHN---LDVIktADYIIDLGP 906
|
..
gi 1735515619 518 EG 519
Cdd:TIGR00630 907 EG 908
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
329-387 |
1.74e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.09 E-value: 1.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1735515619 329 NLTKSYGDRTLidDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPDAGSITMGETV 387
Cdd:PRK11144 5 NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRV 61
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
446-519 |
1.93e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.25 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 446 LSGGERGRLHLAKLLQR---GGNVLLLDEPTNDL---DVETL-RALE------NAILefpgcamVISHDrwfLDRIAT-- 510
Cdd:COG0178 827 LSGGEAQRVKLASELSKrstGKTLYILDEPTTGLhfhDIRKLlEVLHrlvdkgNTVV-------VIEHN---LDVIKTad 896
|
....*....
gi 1735515619 511 HILDYGDEG 519
Cdd:COG0178 897 WIIDLGPEG 905
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
164-239 |
2.42e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.92 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 164 LSGGERRRVALCRLLLE--KPDMLLLDEPTNHLDAESvawLERFLHDYEG------TVVAITHDRYFLDNvAGWILELDR 235
Cdd:cd03238 88 LSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQD---INQLLEVIKGlidlgnTVILIEHNLDVLSS-ADWIIDFGP 163
|
....
gi 1735515619 236 GEGI 239
Cdd:cd03238 164 GSGK 167
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
26-219 |
4.22e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.81 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 26 ISLSFFPGAKIGVLGLNGAGKS-TLLRIMAGVDkeFEGEARPQpgiKIGYLPQEPKLEPQQTVREAVEEAVSEV-KSALT 103
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLID--YPGRVMAE---KLEFNGQDLQRISEKERRNLVGAEVAMIfQDPMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 104 RLDEVYALyadpdaDFDKLAAeqanleaiIQAHDGHNLDNQLERAADALRL---PDWDAKIE----HLSGGERRRVALCR 176
Cdd:PRK11022 101 SLNPCYTV------GFQIMEA--------IKVHQGGNKKTRRQRAIDLLNQvgiPDPASRLDvyphQLSGGMSQRVMIAM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1735515619 177 LLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG----TVVAITHD 219
Cdd:PRK11022 167 AIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkenmALVLITHD 213
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
161-224 |
4.23e-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: 42.38 E-value: 4.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 161 IEHLSGGERR---RVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL---HDYEGTVVAITHDRYFLD 224
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLkelSRNGAQLILTTHSPLLLD 303
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
352-549 |
5.28e-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: 42.38 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 352 IVGIIGANGAGKSTLFRMLSgqeqpdagSITMGETVVLASVDQFRDAMDDKKTVWEEVSNG---QDILTIGNFEIPSRAY 428
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALR--------FLADFDALVIGLTDERSRNGGIGGIPSLLNGIDpkePIEFEISEFLEDGVRY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 429 VGRFNFKGVDQQKRVGELSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILEFPG--CAMVISHDRWFLD 506
Cdd:pfam13304 73 RYGLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDliSGLLLLSIISPLS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1735515619 507 RIATHILDYGDEGKVTFYEGNFSDYEEWKKKTLGDAATQPHRI 549
Cdd:pfam13304 153 FLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLA 195
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
323-364 |
6.83e-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: 6.83e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1735515619 323 KVIEVQNLtKSYGDRTLIDdlsfsIPKGaIVGIIGANGAGKS 364
Cdd:cd03278 2 KKLELKGF-KSFADKTTIP-----FPPG-LTAIVGPNGSGKS 36
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
446-519 |
7.06e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 446 LSGGERGRLHLAKLLQR---GGNVLLLDEPTNDL---DVETLraLE---------NAILefpgcamVISHDrwfLDRI-- 508
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKrstGKTLYILDEPTTGLhfeDIRKL--LEvlhrlvdkgNTVV-------VIEHN---LDVIkt 898
|
90
....*....|.
gi 1735515619 509 ATHILDYGDEG 519
Cdd:PRK00349 899 ADWIIDLGPEG 909
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
337-486 |
1.12e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 41.96 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 337 RTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQEQPD---AGSITM-GE-------TVVLASVDQF---------R 396
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLnGMpidakemRAISAYVQQDdlfiptltvR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 397 DA--------MDDKKTVWEEVSNGQDILTIGNFEIPSRAYVGrfnfkgvdQQKRVGELSGGERGRLHLAKLLQRGGNVLL 468
Cdd:TIGR00955 118 EHlmfqahlrMPRRVTKKEKRERVDEVLQALGLRKCANTRIG--------VPGRVKGLSGGERKRLAFASELLTDPPLLF 189
|
170 180
....*....|....*....|....*
gi 1735515619 469 LDEPTNDLD-------VETLRALEN 486
Cdd:TIGR00955 190 CDEPTSGLDsfmaysvVQVLKGLAQ 214
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
22-224 |
1.74e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.40 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK----------------EFEGEARPQPGIKIGYlpQEPklepqq 85
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykilegdilfkgesilDLEPEERAHLGIFLAF--QYP------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 86 tvreaVE-EAVSEVKSALTRLDEVYALYADPDAD---FDKLAAEQANLEAIIQAHDGHNLDnqleraadalrlpdwdaki 161
Cdd:CHL00131 94 -----IEiPGVSNADFLRLAYNSKRKFQGLPELDpleFLEIINEKLKLVGMDPSFLSRNVN------------------- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 162 EHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDYEGTVVAITHDRYFLD 224
Cdd:CHL00131 150 EGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDalkIIAEGINKLMTSENSIILITHYQRLLD 215
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
324-515 |
1.75e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.16 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 324 VIEVQNLTKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGQE--QPDAGSITM--------------GETV 387
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFkgkdllelspedraGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 388 VLAsvdqFRDAMDDKKtvweeVSNGQDILTIGNfeiPSRAYVG-----RFNFKGVDQQK---------------RVGeLS 447
Cdd:PRK09580 81 FMA----FQYPVEIPG-----VSNQFFLQTALN---AVRSYRGqepldRFDFQDLMEEKiallkmpedlltrsvNVG-FS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1735515619 448 GGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENailefpGCAMVISHDRWFLdrIATH---ILDY 515
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAD------GVNSLRDGKRSFI--IVTHyqrILDY 210
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
164-233 |
2.52e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 2.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1735515619 164 LSGGERRRVALCRLLL---EKPDMLLLDEPTNHLDAESVAWLERFLHD--YEG-TVVAITHDRYFLdNVAGWILEL 233
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSltHQGhTVVIIEHNMHVV-KVADYVLEL 884
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
446-490 |
3.20e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.40 E-value: 3.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1735515619 446 LSGGERGRLHLAKLLQRGGNVLLLDEPTNDLDVETLRALENAILE 490
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1403
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
286-388 |
3.26e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.48 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 286 AKSKARMARFDELNSGEYQKRNETN--ELFIPPGprLGDKVIEVQNLTK----SYGDRTLIDDLSFSIPKGAIVGIIGAN 359
Cdd:TIGR00956 721 ASNKNDIEAGEVLGSTDLTDESDDVndEKDMEKE--SGEDIFHWRNLTYevkiKKEKRVILNNVDGWVKPGTLTALMGAS 798
|
90 100
....*....|....*....|....*....
gi 1735515619 360 GAGKSTLFRMLSgqEQPDAGSITMGETVV 388
Cdd:TIGR00956 799 GAGKTTLLNVLA--ERVTTGVITGGDRLV 825
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
23-63 |
4.76e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.03 E-value: 4.76e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE 63
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
161-238 |
7.15e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.50 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 161 IEHLSGGERR------RVALCRLLLEKPDMLLLDEPTNHLDAESVAWL----ERFLHDYEG--TVVAITHDRYFLdNVAG 228
Cdd:PRK01156 799 IDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLkdiiEYSLKDSSDipQVIMISHHRELL-SVAD 877
|
90
....*....|
gi 1735515619 229 WILELDRGEG 238
Cdd:PRK01156 878 VAYEVKKSSG 887
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
23-62 |
8.25e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.10 E-value: 8.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1735515619 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG 62
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKG 79
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
147-195 |
8.69e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.62 E-value: 8.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1735515619 147 RAADALRLPDWDAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
Cdd:NF040905 388 RKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
405-508 |
9.23e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 38.87 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735515619 405 VWEEVSNGQDILTI-----GNFEIPSRAYVGRFNF-----KGVDQQKRVGELSGGERG------RLHLAKLLQRGGNVLL 468
Cdd:TIGR00606 1149 LWRSTYRGQDIEYIeirsdADENVSASDKRRNYNYrvvmlKGDTALDMRGRCSAGQKVlasliiRLALAETFCLNCGIIA 1228
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1735515619 469 LDEPTNDLDVETLRALENAILEFPGC--------AMVISHDRWFLDRI 508
Cdd:TIGR00606 1229 LDEPTTNLDRENIESLAHALVEIIKSrsqqrnfqLLVITHDEDFVELL 1276
|
|
| |
