|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-635 |
0e+00 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 1328.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVE 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 81 GSVYDFVAEGIEEQAEYLKRYHDISRLVMNDPSEKNLNELAKVQEQLDHHNLWQLENRINEVLAQLGLDPNVALSSLSGG 160
Cdd:PRK11147 81 GTVYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAALSSLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 161 WLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQ 240
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 241 YLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKAMRRERGERREVMGTAKMQVEEASRSGKIVF 320
Cdd:PRK11147 241 YLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVMGTAKMQVEEASRSGKIVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAELDPDKTV 400
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 MDNLAEGKQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:PRK11147 401 MDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 481 ELIDSYQGTVLLVSHDRQFVDNTVTECWIFEGGGKIGRYVGGYHDARGQQEQYVALKQPAVKKNEEPAAPKAETVKRSSS 560
Cdd:PRK11147 481 ELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGYHDARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSK 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287 561 KLSYKLQRELEQLPQLLEDLEAKLEALQTQVADASFFSQPHEQTQKVLADMAAAEQELEQAFERWEYLEALKNGG 635
Cdd:PRK11147 561 KLSYKLQRELEQLPQLLEDLEAEIEALQAQVADADFFSQPHEQTQKVLADLADAEQELEVAFERWEELEALKNGG 635
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-525 |
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: 669.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 6 MHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVEGSVYD 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 86 FVAEGIEEQAEYLKRYHDISRLvMNDPSEkNLNELAKVQEQLDHHNLWQLENRINEVLAQLGL---DPNVALSSLSGGWL 162
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAK-LAEPDE-DLERLAELQEEFEALGGWEAEARAEEILSGLGFpeeDLDRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 163 RKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYL 242
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 243 LEKEEALRVEELQNAEFDRKLAQEEVWIRQ-GIKARR-TRNEGRVRALKAMRRERGERREvmGTAKMQVEEASRSGKIVF 320
Cdd:COG0488 239 EQRAERLEQEAAAYAKQQKKIAKEEEFIRRfRAKARKaKQAQSRIKALEKLEREEPPRRD--KTVEIRFPPPERLGKKVL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAELDPDKTV 400
Cdd:COG0488 317 ELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKTV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 MDNLAEGKQevmvNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:COG0488 397 LDELRDGAP----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15830287 481 ELIDSYQGTVLLVSHDRQFVDNTVTECWIFEGGGkIGRYVGGYHD 525
Cdd:COG0488 473 EALDDFPGTVLLVSHDRYFLDRVATRILEFEDGG-VREYPGGYDD 516
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
34-525 |
1.08e-126 |
|
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: 385.06 E-value: 1.08e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 34 LVGRNGAGKSTLMKILnreQGLD---DGRIIYEQDLIVARLQQDPPRNVEGSVYDFVAEGIEEQAEYLKRYHDISRLvMN 110
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIM---AGVDkdfNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFNEISAK-YA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 111 DPS---EKNLNELAKVQEQLDHHNLWQLENRINEVLAQLGLDPNVA-LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNH 186
Cdd:TIGR03719 112 EPDadfDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDAdVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNH 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 187 LDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYLLEKEEALRVEELQNAEFDRKLAQE 266
Cdd:TIGR03719 192 LDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQKRLEQEEKEESARQKTLKRE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 267 EVWIRQGIKARRTRNEGRVRALKAMRRERGERREvmGTAKMQVEEASRSGKIVFEMEDVCYQVDGKQLVKDFSAQVLRGD 346
Cdd:TIGR03719 272 LEWVRQSPKGRQAKSKARLARYEELLSQEFQKRN--ETAEIYIPPGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 347 KIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAELDPDKTVMDNLAEGKQEVMVNGKPRHVLGYLQD 426
Cdd:TIGR03719 350 IVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGR 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 427 FLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVDNTVTE 506
Cdd:TIGR03719 430 FNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATH 509
|
490
....*....|....*....
gi 15830287 507 CWIFEGGGKIGRYVGGYHD 525
Cdd:TIGR03719 510 ILAFEGDSHVEWFEGNFSE 528
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-525 |
4.83e-122 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 372.91 E-value: 4.83e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 34 LVGRNGAGKSTLMKILnreQGLD---DGRIIYEQDLIVARLQQDPPRNVEGSVYDFVAEGIEEQAEYLKRYHDISRLvMN 110
Cdd:PRK11819 38 VLGLNGAGKSTLLRIM---AGVDkefEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAEVKAALDRFNEIYAA-YA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 111 DP---SEKNLNELAKVQEQLDHHNLWQLENRINEVLAQLGLDPNVA-LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNH 186
Cdd:PRK11819 114 EPdadFDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPPWDAkVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNH 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 187 LDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYLLEKEEALRVEELQNAEFDRKLAQE 266
Cdd:PRK11819 194 LDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKAKRLAQEEKQEAARQKALKRE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 267 EVWIRQGIKARRTRNEGRVRALKAMRRERGERREvmGTAKMQVEEASRSGKIVFEMEDVCYQVDGKQLVKDFSAQVLRGD 346
Cdd:PRK11819 274 LEWVRQSPKARQAKSKARLARYEELLSEEYQKRN--ETNEIFIPPGPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 347 KIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAELDPDKTVMDNLAEGKQEVMVNGKPRHVLGYLQD 426
Cdd:PRK11819 352 IVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKVGNREIPSRAYVGR 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 427 FLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVDNTVTE 506
Cdd:PRK11819 432 FNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATH 511
|
490
....*....|....*....
gi 15830287 507 CWIFEGGGKIGRYVGGYHD 525
Cdd:PRK11819 512 ILAFEGDSQVEWFEGNFQE 530
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-525 |
2.46e-84 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 274.08 E-value: 2.46e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVEGSVYDFVAEGIE 92
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTVIMGHT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 93 EQAEyLKRYHDisRLVMN-DPSEKNLNELAKVQEQLDHHNLWQLENRINEVLAQLGLDP---NVALSSLSGGWLRKAALG 168
Cdd:PRK15064 91 ELWE-VKQERD--RIYALpEMSEEDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEeqhYGLMSEVAPGWKLRVLLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 169 RALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYLlekEEA 248
Cdd:PRK15064 168 QALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYM---TAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 249 LRVEELQNAEFDRKLAQ-EEVwirQGIKARRTRNEGRVRA----LKAMRrergerrevmgtaKMQVEE---ASR-SGKIV 319
Cdd:PRK15064 245 TQARERLLADNAKKKAQiAEL---QSFVSRFSANASKAKQatsrAKQID-------------KIKLEEvkpSSRqNPFIR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEM-----------EDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFD 388
Cdd:PRK15064 309 FEQdkklhrnalevENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 389 Q-HRAELDPDKTVMDNLAEGKQ----EVMVngkpRHVLGYLqdfLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK15064 389 QdHAYDFENDLTLFDWMSQWRQegddEQAV----RGTLGRL---LFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830287 464 LDEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVDNTVTEcwIFE-GGGKIGRYVGGYHD 525
Cdd:PRK15064 462 MDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATR--IIEiTPDGVVDFSGTYEE 522
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-631 |
9.81e-68 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 232.75 E-value: 9.81e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRnVEGSVYDFVAEGIEEQAEY 97
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPA-LPQPALEYVIDGDREYRQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 98 LKRyhdisrlvMNDPSEKNL-NELAKVQEQLDHHNLWQLENRINEVLAQLGLDPNV---ALSSLSGGWLRKAALGRALVS 173
Cdd:PRK10636 95 EAQ--------LHDANERNDgHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQlerPVSDFSGGWRMRLNLAQALIC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 174 NPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYllEKEEALRVEE 253
Cdd:PRK10636 167 RSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSF--EVQRATRLAQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 254 lQNAEFD---RKLAQEEVWI-RQGIKARRTRN-EGRVRALKAMRRERGERreVMGTAKMQVEEASRSGKIVFEMEDVCYQ 328
Cdd:PRK10636 245 -QQAMYEsqqERVAHLQSYIdRFRAKATKAKQaQSRIKMLERMELIAPAH--VDNPFHFSFRAPESLPNPLLKMEKVSAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 329 VDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAE-LDPDKTVMDNLAEG 407
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEfLRADESPLQHLARL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 408 KQEVMvngkPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQ 487
Cdd:PRK10636 402 APQEL----EQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 488 GTVLLVSHDRQFVDNTVTECWIFEgGGKIGRYVGGYHDAR----GQQEQYVALKQPAVKKNEEPAAPKAETVKRSSS--K 561
Cdd:PRK10636 478 GALVVVSHDRHLLRSTTDDLYLVH-DGKVEPFDGDLEDYQqwlsDVQKQENQTDEAPKENNANSAQARKDQKRREAElrT 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287 562 LSYKLQRELEQLPQLLEDLEAKLEALQTQVADASFFSQPHEQT-QKVLADMAAAEQELEQAFERW----EYLEAL 631
Cdd:PRK10636 557 QTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAElTACLQQQASAKSGLEECEMAWleaqEQLEQM 631
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-525 |
5.72e-55 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 199.32 E-value: 5.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMK---------------ILNREQGLDDGRIIYEQDLIV 68
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhaidgipkncqILHVEQEVVGDDTTALQCVLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 69 ARLQQDPPRNVEGSVYDFVAEgIEEQAEYLKRYHDISRLVMNDPSEKNLNELAKVQEQLDHHNLwqlENRINEVLAQLGL 148
Cdd:PLN03073 258 TDIERTQLLEEEAQLVAQQRE-LEFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTA---EARAASILAGLSF 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 149 DPNV---ALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVD 225
Cdd:PLN03073 334 TPEMqvkATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILH 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 226 LDRGKLVTYPGNYDQYLLEKEEALRVEELQNAEFDRKLAQEEVWI---RQGIKaRRTRNEGRVRALKAMrrerGERREVM 302
Cdd:PLN03073 414 LHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIdkfRYNAK-RASLVQSRIKALDRL----GHVDAVV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 303 GTAKMQVEEAS---RSGKIVFEMEDVCYQVDGKQLV-KDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV 378
Cdd:PLN03073 489 NDPDYKFEFPTpddRPGPPIISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 379 GTKLEVAYFDQHRAE-LDPDKTVMDNLAEgkqevMVNGKPRHVL-GYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFL 456
Cdd:PLN03073 569 SAKVRMAVFSQHHVDgLDLSSNPLLYMMR-----CFPGVPEQKLrAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITF 643
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 457 KPSNLLILDEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVDNTVTECWIFEgGGKIGRYVGGYHD 525
Cdd:PLN03073 644 KKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVS-EGKVTPFHGTFHD 711
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
321-514 |
3.48e-51 |
|
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: 173.40 E-value: 3.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQhraeldpdktv 400
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 mdnlaegkqevmvngkprhvlgylqdflfhpkramtpvraLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:cd03221 71 ----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALE 110
|
170 180 190
....*....|....*....|....*....|....
gi 15830287 481 ELIDSYQGTVLLVSHDRQFVDNTVTECWIFEGGG 514
Cdd:cd03221 111 EALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-242 |
3.21e-46 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 171.02 E-value: 3.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDpprnvegs 82
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQH-------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 83 vydfvaegieeqAEYLkryhdisrlvmnDPSEKNLNELAKVQEQLDHHNLWQLenrinevLAQLGLDPNVAL---SSLSG 159
Cdd:COG0488 387 ------------QEEL------------DPDKTVLDELRDGAPGGTEQEVRGY-------LGRFLFSGDDAFkpvGVLSG 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 160 GWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYD 239
Cdd:COG0488 436 GEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYD 515
|
...
gi 15830287 240 QYL 242
Cdd:COG0488 516 DYL 518
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-230 |
1.04e-44 |
|
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: 156.07 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQdpprnvegsv 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 84 ydfvaegieeqaeylkryhdisrlvmndpseknlnelakvqeqldhhnlwqlenrinevlaqlgldpnvalssLSGGWLR 163
Cdd:cd03221 71 -------------------------------------------------------------------------LSGGEKM 77
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 164 KAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd03221 78 RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-496 |
4.39e-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: 4.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFS----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNR---EQGLDDGRIIYE-QDL----------IVARLQ 72
Cdd:COG1123 10 LSVRypggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDgRDLlelsealrgrRIGMVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 73 QDPPRNVEG-SVYDFVAEGIEEQaeylkryhDISRLVMndpseknlnelakvqeqldhhnlwqlENRINEVLAQLGLDP- 150
Cdd:COG1123 90 QDPMTQLNPvTVGDQIAEALENL--------GLSRAEA--------------------------RARVLELLEAVGLERr 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 151 -NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVD 225
Cdd:COG1123 136 lDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 226 LDRGKLVtypgnydqyllekeEALRVEELQnaefdrklaqeevwirqgikarrtrneGRVRALKAMRRergerrevMGTA 305
Cdd:COG1123 216 MDDGRIV--------------EDGPPEEIL---------------------------AAPQALAAVPR--------LGAA 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 306 KMQVEEASRSGKIVFEMEDVC--YQVDGK---QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG- 379
Cdd:COG1123 247 RGRAAPAAAAAEPLLEVRNLSkrYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDg 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 380 ---TKLEVAYFDQHRAE-----------LDPDKTVMDNLAEG--------KQEVMvngkpRHVLGYLQDFLFHPKRAMTP 437
Cdd:COG1123 327 kdlTKLSRRSLRELRRRvqmvfqdpyssLNPRMTVGDIIAEPlrlhgllsRAERR-----ERVAELLERVGLPPDLADRY 401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 438 VRALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLELLEELIDSYQ----GTVLLVSHD 496
Cdd:COG1123 402 PHELSGGQRQRVAIARaLALEPK-LLILDEPTSALDVSVQAQILNLLRDLQrelgLTYLFISHD 464
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
320-513 |
4.11e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.08 E-value: 4.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKL-----------EVAYFD 388
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 389 QhRAELdPDKTVMDNLAEGKQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLAR-LFLKPSNLLiLDEP 467
Cdd:COG4619 81 Q-EPAL-WGGTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRaLLLQPDVLL-LDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15830287 468 TNDLDVETLELLEELIDSY----QGTVLLVSHDRQFVDNTVTECWIFEGG 513
Cdd:COG4619 158 TSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
12-258 |
7.78e-33 |
|
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: 126.51 E-value: 7.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqdlivarlqqdpprnvegsvydfvAEGI 91
Cdd:COG4555 10 KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID------------------------GEDV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 92 EEQAEYLKRyhDISRLVMNDPSEKNLnelaKVQEQLDH----HNLW--QLENRINEVLAQLGLDP--NVALSSLSGGWLR 163
Cdd:COG4555 66 RKEPREARR--QIGVLPDERGLYDRL----TVRENIRYfaelYGLFdeELKKRIEELIELLGLEEflDRRVGELSTGMKK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 164 KAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISHDRSFIRNMATRIVDLDRGKLV---TYPGN 237
Cdd:COG4555 140 KVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKVVaqgSLDEL 219
|
250 260
....*....|....*....|.
gi 15830287 238 YDQYLLEKEEALRVEELQNAE 258
Cdd:COG4555 220 REEIGEENLEDAFVALIGSEE 240
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-231 |
7.79e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 126.36 E-value: 7.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLIVARL------QQ 73
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrLFGKPPRRARRrigyvpQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 74 dppRNVEG----SVYDFVAEGieeqaeylkRYHDISRLVMNDPSEKnlnelAKVQEQLDHHNLWQLENRinevlaqlgld 149
Cdd:COG1121 84 ---AEVDWdfpiTVRDVVLMG---------RYGRRGLFRRPSRADR-----EAVDEALERVGLEDLADR----------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 150 pnvALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDL 226
Cdd:COG1121 136 ---PIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLL 212
|
....*
gi 15830287 227 DRGKL 231
Cdd:COG1121 213 NRGLV 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-232 |
1.46e-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: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDL----------IVARL 71
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgRDLaslsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 72 QQDPPRNVEGSVYDFVAEGieeqaeylkRYhdisrlvmndPseknlnelakvqeqldHHNLWQLENR-----INEVLAQL 146
Cdd:COG1120 81 PQEPPAPFGLTVRELVALG---------RY----------P----------------HLGLFGRPSAedreaVEEALERT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 147 GLDP--NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMA 220
Cdd:COG1120 126 GLEHlaDRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHDLNLAARYA 205
|
250
....*....|..
gi 15830287 221 TRIVDLDRGKLV 232
Cdd:COG1120 206 DRLVLLKDGRIV 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
12-232 |
1.39e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 122.86 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRI-IYEQDliVARLQQDPPRNV-----EGS 82
Cdd:COG1131 9 RYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLL---GLlrpTSGEVrVLGED--VARDPAEVRRRIgyvpqEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 83 VYDFVAegIEEQAEYLKRYHDISRlvmndpseknlnelakvqeqldhhnlWQLENRINEVLAQLGLDP--NVALSSLSGG 160
Cdd:COG1131 84 LYPDLT--VRENLRFFARLYGLPR--------------------------KEARERIDELLELFGLTDaaDRKVGTLSGG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287 161 WLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG1131 136 MKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAegkTVLLSTHYLEEAERLCDRVAIIDKGRIV 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-230 |
1.88e-31 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 121.42 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFS----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVeGSVYDF 86
Cdd:cd03225 5 LSFSypdgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKV-GLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 87 VaegiEEQaeylkryhdisrLVMNDPSEknlnELA--KVQEQLDHHnlwQLENRINEVLAQLGLDP--NVALSSLSGGWL 162
Cdd:cd03225 84 P----DDQ------------FFGPTVEE----EVAfgLENLGLPEE---EIEERVEEALELVGLEGlrDRSPFTLSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 163 RKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-232 |
2.09e-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: 119.36 E-value: 2.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFS---DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYE-QDLIVARLQ----------Q 73
Cdd:COG1122 6 LSFSypgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN---GLlkpTSGEVLVDgKDITKKNLRelrrkvglvfQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 74 DpPRN--VEGSVYDFVAEGIEEQAeylkryhdISRlvmndpseknlnelAKVQEqldhhnlwqlenRINEVLAQLGLDP- 150
Cdd:COG1122 83 N-PDDqlFAPTVEEDVAFGPENLG--------LPR--------------EEIRE------------RVEEALELVGLEHl 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 151 -NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDL 226
Cdd:COG1122 128 aDRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVL 207
|
....*.
gi 15830287 227 DRGKLV 232
Cdd:COG1122 208 DDGRIV 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-504 |
4.46e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 118.65 E-value: 4.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLE-----VAYFDQhRA 392
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfGKPPRrarrrIGYVPQ-RA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 393 ELDPDK--TVMDnlaegkqeVMVNGKPRHvLGylqdFLFHPKRA-------------MT-----PVRALSGGERNRLLLA 452
Cdd:COG1121 85 EVDWDFpiTVRD--------VVLMGRYGR-RG----LFRRPSRAdreavdealervgLEdladrPIGELSGGQQQRVLLA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 453 RLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQG---TVLLVSHD----RQFVDNTV 504
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDlgavREYFDRVL 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
323-503 |
9.21e-30 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 116.42 E-value: 9.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 323 EDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQ-----HRAE 393
Cdd:COG4133 6 ENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgepiRDAREDYRRRlaylgHADG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 394 LDPDKTVMDNL---AEGKQEVMVNGKPRHVLGYLQdfLfhPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTND 470
Cdd:COG4133 86 LKPELTVRENLrfwAALYGLRADREAIDEALEAVG--L--AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 15830287 471 LDVETLELLEELIDSY---QGTVLLVSHDRQFVDNT 503
Cdd:COG4133 162 LDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAA 197
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-231 |
9.39e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 116.84 E-value: 9.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLI-----------VARLQ 72
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLsampppewrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 73 QDPPRnVEGSVYDfvaegieeqaeYLKRYHDISRLVMNDPseknlnelakvqeqldhhnlwqlenRINEVLAQLGLDPNV 152
Cdd:COG4619 81 QEPAL-WGGTVRD-----------NLPFPFQLRERKFDRE-------------------------RALELLERLGLPPDI 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 153 A---LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVD 225
Cdd:COG4619 124 LdkpVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLT 203
|
....*.
gi 15830287 226 LDRGKL 231
Cdd:COG4619 204 LEAGRL 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
17-232 |
1.00e-29 |
|
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: 117.98 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVegsvydfvaegieeqae 96
Cdd:COG1124 19 PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV----------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 97 ylkryhdisRLVMNDPsEKNLNELAKVQEQLD----HHNLWQLENRINEVLAQLGLDPNVAL---SSLSGGWLRKAALGR 169
Cdd:COG1124 82 ---------QMVFQDP-YASLHPRHTVDRILAeplrIHGLPDREERIAELLEQVGLPPSFLDrypHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 170 ALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
335-469 |
1.53e-29 |
|
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: 114.28 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG-----------TKLEVAYFDQHrAELDPDKTVMDN 403
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQD-PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 404 LAEGKQEVMVNGKPR-----HVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTN 469
Cdd:pfam00005 80 LRLGLLLKGLSKREKdaraeEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-232 |
1.83e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 116.31 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSFS-DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIY-EQDLivARLQQD--PP--R 77
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVnGQDL--SRLKRReiPYlrR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 78 NVeGSVY-DFvaegieeqaeylkryhdisRLVMNDPSEKNLnELA-KVQEQLDHhnlwQLENRINEVLAQLGLD------ 149
Cdd:COG2884 80 RI-GVVFqDF-------------------RLLPDRTVYENV-ALPlRVTGKSRK----EIRRRVREVLDLVGLSdkakal 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 150 PNValssLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFN--G-TIIFISHDRSFIRNMATRIVDL 226
Cdd:COG2884 135 PHE----LSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINrrGtTVLIATHDLELVDRMPKRVLEL 210
|
....*.
gi 15830287 227 DRGKLV 232
Cdd:COG2884 211 EDGRLV 216
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
321-500 |
4.68e-29 |
|
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: 114.94 E-value: 4.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLE-----VAYFDQHRaEL 394
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLEkerkrIGYVPQRR-SI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 DPDK--TVMDnlaegkqeVMVNGKPRHVlgylqDFLFHPKRA-------------MT-----PVRALSGGERNRLLLARL 454
Cdd:cd03235 80 DRDFpiSVRD--------VVLMGLYGHK-----GLFRRLSKAdkakvdealervgLSeladrQIGELSGGQQQRVLLARA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15830287 455 FLKPSNLLILDEPTNDLDVETLELLEELIDSYQG---TVLLVSHDRQFV 500
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLV 195
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-242 |
9.56e-29 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 120.77 E-value: 9.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDpprnvegSVYDFvAEGI 91
Cdd:PRK15064 328 GFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQD-------HAYDF-ENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 92 ---EEQAEYLKRYHDisrlvmndpseknlnelakvqEQLdhhnlwqlenrINEVLAQL---GLDPNVALSSLSGGWLRKA 165
Cdd:PRK15064 400 tlfDWMSQWRQEGDD---------------------EQA-----------VRGTLGRLlfsQDDIKKSVKVLSGGEKGRM 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 166 ALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYL 242
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYL 524
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
317-511 |
1.37e-28 |
|
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: 120.43 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 317 KIVFEMEDVCYQVD-GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQhRAELD 395
Cdd:TIGR03719 2 QYIYTMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQ-EPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 396 PDKTVMDNLAEGKQEVmvngkpRHVL------------------------GYLQDFLFHPK---------RAM------- 435
Cdd:TIGR03719 81 PTKTVRENVEEGVAEI------KDALdrfneisakyaepdadfdklaaeqAELQEIIDAADawdldsqleIAMdalrcpp 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287 436 --TPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVDNtVTEcWIFE 511
Cdd:TIGR03719 155 wdADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDN-VAG-WILE 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
12-231 |
4.67e-28 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 110.57 E-value: 4.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLddgriiyeqdlivarLQQDpprnvEGSVYDFVAEGI 91
Cdd:cd03230 9 RYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIL---GL---------------LKPD-----SGEIKVLGKDIK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 92 EEQAEYLKRyhdISRLVMNDPSEKNLNelakVQEQLDhhnlwqlenrinevlaqlgldpnvalssLSGGWLRKAALGRAL 171
Cdd:cd03230 66 KEPEEVKRR---IGYLPEEPSLYENLT----VRENLK----------------------------LSGGMKQRLALAQAL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830287 172 VSNPRVLLLDEPTNHLDIETIDWLEGFLKTFN---GTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
321-495 |
5.02e-28 |
|
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: 110.55 E-value: 5.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVC--YQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklevaYFDQHraeldpdk 398
Cdd:cd03228 2 EFKNVSfsYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI---------LIDGV-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 399 tvmdNLAEGKQEVMvngkpRHVLGYL-QD-FLFHpkraMTpVRA--LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
Cdd:cd03228 65 ----DLRDLDLESL-----RKNIAYVpQDpFLFS----GT-IREniLSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180
....*....|....*....|...
gi 15830287 475 TLELLEELIDSYQG--TVLLVSH 495
Cdd:cd03228 131 TEALILEALRALAKgkTVIVIAH 153
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
310-538 |
7.10e-28 |
|
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: 118.33 E-value: 7.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 310 EEASRSGKIVFEMEDVC--YQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLE--- 383
Cdd:COG4987 324 EPAPAPGGPSLELEDVSfrYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLgGVDLRdld 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 384 -------VAYFDQhraelDP---DKTVMDNLAEGKQEV----MvngkpRHVLG--YLQDFLFH-PKRAMTPV----RALS 442
Cdd:COG4987 404 eddlrrrIAVVPQ-----RPhlfDTTLRENLRLARPDAtdeeL-----WAALErvGLGDWLAAlPDGLDTWLgeggRRLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 443 GGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQG--TVLLVSHDRQFVDNtVTECWIFEGGGKIGRyv 520
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAgrTVLLITHRLAGLER-MDRILVLEDGRIVEQ-- 550
|
250
....*....|....*...
gi 15830287 521 GGYHDARGQQEQYVALKQ 538
Cdd:COG4987 551 GTHEELLAQNGRYRQLYQ 568
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
310-513 |
1.03e-27 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 117.94 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 310 EEASRSGKIVFEMEDVCYQ-VDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLE---- 383
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILInGVDLSdldp 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 384 ------VAYFDQHrAELdPDKTVMDNLAEGK-----QEVmvngkpRHVLG--YLQDFLfhpkRAM-----TPV----RAL 441
Cdd:COG4988 407 aswrrqIAWVPQN-PYL-FAGTIRENLRLGRpdasdEEL------EAALEaaGLDEFV----AALpdgldTPLgeggRGL 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY-QG-TVLLVSHDRQFVDNtVTECWIFEGG 513
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLaKGrTVILITHRLALLAQ-ADRILVLDDG 547
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
17-232 |
1.26e-27 |
|
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: 111.06 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqdlivarlqqdpPRNVEGSVydfvaegieeQAE 96
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFD------------GKDLLKLS----------RRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 97 YLKRYHDISrLVMNDPSEkNLNELAKVQEQL--------DHHNLWQLENRINEVLAQLGLDPNVALS---SLSGGWLRKA 165
Cdd:cd03257 77 RKIRRKEIQ-MVFQDPMS-SLNPRMTIGEQIaeplrihgKLSKKEARKEAVLLLLVGVGLPEEVLNRyphELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 166 ALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDvsvqAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-232 |
1.91e-27 |
|
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: 116.54 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDL----------IVARLQ---QDP-----PRNv 79
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgKDLtklsrrslreLRRRVQmvfQDPysslnPRM- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 80 egSVYDFVAEGieeqaeyLKRYHDISRlvmndpseknlnelakvqeqldhhnlWQLENRINEVLAQLGLDPNVAL---SS 156
Cdd:COG1123 360 --TVGDIIAEP-------LRLHGLLSR--------------------------AERRERVAELLERVGLPPDLADrypHE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 157 LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVqaqiLNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
317-511 |
2.06e-27 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 116.76 E-value: 2.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 317 KIVFEMEDVCYQVDG-KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQhRAELD 395
Cdd:PRK11819 4 QYIYTMNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQ-EPQLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 396 PDKTVMDNLAEGKQEVM--------VN---GKPRHVL-------GYLQDFLFHP---------KRAM---------TPVR 439
Cdd:PRK11819 83 PEKTVRENVEEGVAEVKaaldrfneIYaayAEPDADFdalaaeqGELQEIIDAAdawdldsqlEIAMdalrcppwdAKVT 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 440 ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVDNtVTEcWIFE 511
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDN-VAG-WILE 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-230 |
2.89e-27 |
|
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: 109.49 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIiyeqdlivaRLQQDPPRNV 79
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRIL---AGLlppSAGEV---------LWNGEPIRDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 80 EGSVYDFVAegieeqaeYLkrYHDISrlvmndpseknLNELAKVQEQLDH----HNLWQLENRINEVLAQLGLDP--NVA 153
Cdd:COG4133 70 REDYRRRLA--------YL--GHADG-----------LKPELTVRENLRFwaalYGLRADREAIDEALEAVGLAGlaDLP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 154 LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFN---GTIIFISHDRSFIRnmATRIVDLDRGK 230
Cdd:COG4133 129 VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-230 |
9.11e-27 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 106.56 E-value: 9.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 5 SMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlivarlqqdpprnvegsvy 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 85 dfvaegieeqaeylkryhdisrlvmndpseknlnelakvqeQLDHHNLWQLENRinEVLAQLGLdpnvaLSSLSGGWLRK 164
Cdd:cd00267 57 -----------------------------------------LIDGKDIAKLPLE--ELRRRIGY-----VPQLSGGQRQR 88
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 165 AALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd00267 89 VALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
321-496 |
4.78e-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: 105.21 E-value: 4.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLE----------VAYFDQ 389
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLdGKDLAslspkelarkIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 390 HRAELDpdktvMDNLAEgkqevmvngkpRhvlgylqdflfhpkramtPVRALSGGERNRLLLARLFLKPSNLLILDEPTN 469
Cdd:cd03214 81 ALELLG-----LAHLAD-----------R------------------PFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190
....*....|....*....|....*....|.
gi 15830287 470 DLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:cd03214 127 HLDIAHQIELLELLrrlaRERGKTVVMVLHD 157
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-473 |
1.32e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.88 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlivarlqqdpprnVEGS 82
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIL-----------------LDGE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 83 VYDF-------------------------VAEGIeeqaeYLKRYHDISRLVmndpSEKNLNELAKvqeqldhhnlwqlen 137
Cdd:COG1129 67 PVRFrsprdaqaagiaiihqelnlvpnlsVAENI-----FLGREPRRGGLI----DWRAMRRRAR--------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 138 rinEVLAQLGL--DPNVALSSLSGGwlRKA--ALGRALVSNPRVLLLDEPTNHLDIETIDWLegF-----LKTFNGTIIF 208
Cdd:COG1129 123 ---ELLARLGLdiDPDTPVGDLSVA--QQQlvEIARALSRDARVLILDEPTASLTEREVERL--FriirrLKAQGVAIIY 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 209 ISHDRSFIRNMATRIVDLDRGKLvtypgnydqyllekeealrVEELQNAEFDRklaqEEVwIRQ--GikarrtrnegrvR 286
Cdd:COG1129 196 ISHRLDEVFEIADRVTVLRDGRL-------------------VGTGPVAELTE----DEL-VRLmvG------------R 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 287 ALKAMRRergerrevmgtakmqvEEASRSGKIVFEMEDVCyqvdGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLML 366
Cdd:COG1129 240 ELEDLFP----------------KRAAAPGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALF 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 367 GQLQADSGRIHV-GTKLE-----------VAYF--DQHRAELDPDKTVMDNLAEGKQEVMVNGKP-------RHVLGYLQ 425
Cdd:COG1129 300 GADPADSGEIRLdGKPVRirsprdairagIAYVpeDRKGEGLVLDLSIRENITLASLDRLSRGGLldrrrerALAEEYIK 379
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15830287 426 DFLFHPKRAMTPVRALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG1129 380 RLRIKTPSPEQPVGNLSGGNQQKVVLAKwLATDPK-VLILDEPTRGIDV 427
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
320-513 |
1.64e-25 |
|
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: 105.11 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQV-DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAEL--- 394
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdGKDITKKNLRELRRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 --DPD-----KTVMD-------NLAEGKQEV---------MVNgkprhvlgyLQDFLFHpkramtPVRALSGGERNRLLL 451
Cdd:COG1122 81 fqNPDdqlfaPTVEEdvafgpeNLGLPREEIrerveealeLVG---------LEHLADR------PPHELSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287 452 AR-LFLKPSnLLILDEPTNDLDVETLELLEELIDSYQG---TVLLVSHDRQFVDNTVTECWIFEGG 513
Cdd:COG1122 146 AGvLAMEPE-VLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDG 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
321-513 |
2.28e-25 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 102.32 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklevaYFDQHRAELDPDKTV 400
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI---------LIDGKDIAKLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 MDNLAegkqevmvngkprhvlgylqdFLFHpkramtpvraLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:cd00267 72 RRRIG---------------------YVPQ----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180 190
....*....|....*....|....*....|....*.
gi 15830287 481 ELIDSYQG---TVLLVSHDRQFVDNTVTECWIFEGG 513
Cdd:cd00267 121 ELLRELAEegrTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
321-496 |
3.50e-25 |
|
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: 102.48 E-value: 3.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV----------GTKLEVAYFDQH 390
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkdikkepeEVKRRIGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 rAELDPDKTVMDNLaegkqevmvngkprhvlgylqdflfhpkramtpvrALSGGERNRLLLARLFLKPSNLLILDEPTND 470
Cdd:cd03230 82 -PSLYENLTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180
....*....|....*....|....*....
gi 15830287 471 LDVETLELLEELIDSY---QGTVLLVSHD 496
Cdd:cd03230 126 LDPESRREFWELLRELkkeGKTILLSSHI 154
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-231 |
4.88e-25 |
|
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: 103.38 E-value: 4.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 5 SMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRI------IYEQDLIVARLQQ-- 73
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAI---LGLlkpTSGSIrvfgkpLEKERKRIGYVPQrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 74 DPPRNVEGSVYDFVAEGIEEQAEYLKRYHDISRlvmndpseknlnelAKVQEQLDHHNLWQLENRinevlaqlgldpnvA 153
Cdd:cd03235 78 SIDRDFPISVRDVVLMGLYGHKGLFRRLSKADK--------------AKVDEALERVGLSELADR--------------Q 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 154 LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd03235 130 IGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLLNRTV 209
|
.
gi 15830287 231 L 231
Cdd:cd03235 210 V 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
321-496 |
4.94e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 103.99 E-value: 4.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----------TKLEVAYFDQH 390
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLgedvardpaeVRRRIGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 rAELDPDKTVMDNLaegkqEVM--VNGKPRHVLG-----YLQDF-LfhPKRAMTPVRALSGGERNRLLLARLFLKPSNLL 462
Cdd:COG1131 82 -PALYPDLTVRENL-----RFFarLYGLPRKEARerideLLELFgL--TDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 15830287 463 ILDEPTNDLDVETLELLEELIDSY--QG-TVLLVSHD 496
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELaaEGkTVLLSTHY 190
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
12-232 |
5.99e-25 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 103.07 E-value: 5.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIiyeQDLIVARLQQDPPRNVEGSVydfva 88
Cdd:cd03268 9 TYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKII---LGLikpDSGEI---TFDGKSYQKNIEALRRIGAL----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 89 egIEEQAeylkryhdisrLVMNDPSEKNLNELAKVqeqldhhnLWQLENRINEVLAQLGLD--PNVALSSLSGGWLRKAA 166
Cdd:cd03268 78 --IEAPG-----------FYPNLTARENLRLLARL--------LGIRKKRIDEVLDVVGLKdsAKKKVKGFSLGMKQRLG 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 167 LGRALVSNPRVLLLDEPTNHLDIETIDWLEGF---LKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELilsLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
11-234 |
6.80e-25 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 101.74 E-value: 6.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQdlivarlqqdpprnvegsvydfvaeg 90
Cdd:cd03214 7 VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG-------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 91 ieeqaeylkryHDISRLvmndpSEKnlnELAK----VQEQLDHHNLWQLENRInevlaqlgldpnvaLSSLSGGWLRKAA 166
Cdd:cd03214 61 -----------KDLASL-----SPK---ELARkiayVPQALELLGLAHLADRP--------------FNELSGGERQRVL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 167 LGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTY 234
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-246 |
8.59e-25 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 109.54 E-value: 8.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFS----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIIY-EQDLivarlQQDPPRNV--- 79
Cdd:COG2274 479 VSFRypgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL---LGLyepTSGRILIdGIDL-----RQIDPASLrrq 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 80 -----------EGSVYD---FVAEGIEEQaeylkRYHDISRLVmndpsekNLNELAKvqeqldhhnlwQLENRINEVLAQ 145
Cdd:COG2274 551 igvvlqdvflfSGTIREnitLGDPDATDE-----EIIEAARLA-------GLHDFIE-----------ALPMGYDTVVGE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 146 LGldpnvalSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKtfNGTIIFISHDRSFIRNmAT 221
Cdd:COG2274 608 GG-------SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETeaiiLENLRRLLK--GRTVIIIAHRLSTIRL-AD 677
|
250 260
....*....|....*....|....*
gi 15830287 222 RIVDLDRGKLVTYpGNYDQyLLEKE 246
Cdd:COG2274 678 RIIVLDKGRIVED-GTHEE-LLARK 700
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
315-502 |
1.29e-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: 109.15 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 315 SGKIvfEMEDVC--YQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGtklevayfDQHRA 392
Cdd:COG2274 471 KGDI--ELENVSfrYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID--------GIDLR 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 393 ELDPDK-----------------TVMDNLAEGKQEV----------MVNgkprhvlgyLQDFL-FHPKRAMTPV----RA 440
Cdd:COG2274 541 QIDPASlrrqigvvlqdvflfsgTIRENITLGDPDAtdeeiieaarLAG---------LHDFIeALPMGYDTVVgeggSN 611
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQG--TVLLVSHDRQFVDN 502
Cdd:COG2274 612 LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL 675
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-230 |
1.95e-24 |
|
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: 100.34 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLDdgriiyeqdlivarlqqdppRNVEGSV 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIA---GLE--------------------EPDSGSI 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 84 YdfvAEGIeeqaeylkryhDISRLVMNDPseknlnelakvqeqldhhnlwQLENRINEVLAQLGLDP------NVALSsL 157
Cdd:cd03229 58 L---IDGE-----------DLTDLEDELP---------------------PLRRRIGMVFQDFALFPhltvleNIALG-L 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 158 SGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKT----FNGTIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd03229 102 SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
321-513 |
4.21e-24 |
|
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: 100.62 E-value: 4.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDG--KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAEL---- 394
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 --DPD-----KTVMDNLAEGkqevMVN-GKPRH-----VLGYLQDFLFHPKRAmTPVRALSGGERNRLLLAR-LFLKPsN 460
Cdd:cd03225 81 fqNPDdqffgPTVEEEVAFG----LENlGLPEEeieerVEEALELVGLEGLRD-RSPFTLSGGQKQRVAIAGvLAMDP-D 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287 461 LLILDEPTNDLDVETLELLEELIDSYQG---TVLLVSHDRQFVDNTVTECWIFEGG 513
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-517 |
4.84e-24 |
|
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: 106.43 E-value: 4.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGLDD-----GRIIYEQDLIVARLQQDPPRNV-------- 79
Cdd:TIGR03269 10 FDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVL---RGMDQyeptsGRIIYHVALCEKCGYVERPSKVgepcpvcg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 80 ---EGSVYDFVAEGIEEQAEYLKR-----------YHDISRL--VMNDPSEKNLNELAKVQEQLDHHNLWQLENRINEVL 143
Cdd:TIGR03269 87 gtlEPEEVDFWNLSDKLRRRIRKRiaimlqrtfalYGDDTVLdnVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 144 aqlgldpnvalSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDW----LEGFLKTFNGTIIFISHDRSFIRNM 219
Cdd:TIGR03269 167 -----------RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 220 ATRIVDLDRGKLVTyPGNYDQYLlekeeALRVEELQNAEFDRKLAQEEVWIR-QGIKARRTRNE-GRVRAlkamrrerge 297
Cdd:TIGR03269 236 SDKAIWLENGEIKE-EGTPDEVV-----AVFMEGVSEVEKECEVEVGEPIIKvRNVSKRYISVDrGVVKA---------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 298 rrevmgtakmqveeasrsgkivfemedvcyqVDGKQLvkdfsaQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH 377
Cdd:TIGR03269 300 -------------------------------VDNVSL------EVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVN 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 378 VG--------TKLEVayFDQHRAE-----------LDPDKTVMDNLAEG-KQEVMVNGKPRHVLGYLQDFLFHPKRAMTP 437
Cdd:TIGR03269 343 VRvgdewvdmTKPGP--DGRGRAKryigilhqeydLYPHRTVLDNLTEAiGLELPDELARMKAVITLKMVGFDEEKAEEI 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 438 VR----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHDRQFVDNTVTECWI 509
Cdd:TIGR03269 421 LDkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQTFIIVSHDMDFVLDVCDRAAL 500
|
570
....*....|
gi 15830287 510 FEGGG--KIG 517
Cdd:TIGR03269 501 MRDGKivKIG 510
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-232 |
8.36e-24 |
|
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: 99.90 E-value: 8.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDliVARLqqdPPRnvegs 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlIDGRD--VTGV---PPE----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 83 vydfvaegieeqaeylKRyhDISrLVMNDPS-------EKNLN---ELAKVQEQldhhnlwQLENRINEVLAQLGLDP-- 150
Cdd:cd03259 71 ----------------RR--NIG-MVFQDYAlfphltvAENIAfglKLRGVPKA-------EIRARVRELLELVGLEGll 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 151 NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKT----FNGTIIFISHDRSFIRNMATRIVDL 226
Cdd:cd03259 125 NRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKElqreLGITTIYVTHDQEEALALADRIAVM 204
|
....*.
gi 15830287 227 DRGKLV 232
Cdd:cd03259 205 NEGRIV 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-496 |
9.37e-24 |
|
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: 100.89 E-value: 9.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLE----------VAYF 387
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLAslsrrelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 388 DQHRaELDPDKTVMDNLAEGK------------------QEVMvngkprHVLGyLQDFlfhpkrAMTPVRALSGGERNRL 449
Cdd:COG1120 81 PQEP-PAPFGLTVRELVALGRyphlglfgrpsaedreavEEAL------ERTG-LEHL------ADRPVDELSGGERQRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 450 LLARLFLKPSNLLILDEPTNDLDVetlelleelidSYQ---------------GTVLLVSHD 496
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDL-----------AHQlevlellrrlarergRTVVMVLHD 197
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
11-246 |
1.15e-22 |
|
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: 102.14 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFS---DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLivARLQQDPPRN-------- 78
Cdd:COG4988 342 VSFSypgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlINGVDL--SDLDPASWRRqiawvpqn 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 79 ---VEGSVYDFVaegieeqaeylkryhdisRLVMNDPSEknlnelAKVQEQLDHHNLWqlenrinEVLAQL--GLDPNVA 153
Cdd:COG4988 420 pylFAGTIRENL------------------RLGRPDASD------EELEAALEAAGLD-------EFVAALpdGLDTPLG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 154 L--SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET---IdwLEGFLKTFNG-TIIFISHDRSFIRNmATRIVDLD 227
Cdd:COG4988 469 EggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETeaeI--LQALRRLAKGrTVILITHRLALLAQ-ADRILVLD 545
|
250
....*....|....*....
gi 15830287 228 RGKLVTYpGNYDQyLLEKE 246
Cdd:COG4988 546 DGRIVEQ-GTHEE-LLAKN 562
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
11-250 |
1.46e-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: 102.15 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFS----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI---------IYEQDL--IVARLQQDP 75
Cdd:COG4987 339 VSFRypgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvdlrdLDEDDLrrRIAVVPQRP 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 76 prnvegsvYDF---VAEGIeeqaeylkryhdisRLVMNDPSEKNLNE-LAKVQeqLDhhnlwqlenrinEVLAQL--GLD 149
Cdd:COG4987 419 --------HLFdttLRENL--------------RLARPDATDEELWAaLERVG--LG------------DWLAALpdGLD 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 150 PNV--ALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETID-WLEGFLKTFNG-TIIFISHDRSFIRNMaTRIVD 225
Cdd:COG4987 463 TWLgeGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQaLLADLLEALAGrTVLLITHRLAGLERM-DRILV 541
|
250 260
....*....|....*....|....*
gi 15830287 226 LDRGKLVTyPGNYDQyLLEKEEALR 250
Cdd:COG4987 542 LEDGRIVE-QGTHEE-LLAQNGRYR 564
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
19-232 |
2.31e-22 |
|
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: 96.65 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLI------VARL------QQdpPRNVEG-SVY 84
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDgRDITglpphrIARLgiartfQN--PRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 85 DFVAEGIEEQAEYlKRYHDISRLVMNDPSEKNLNElakvqeqldhhnlwqlenRINEVLAQLGLDP--NVALSSLSGGWL 162
Cdd:COG0411 98 ENVLVAAHARLGR-GLLAALLRLPRARREEREARE------------------RAEELLERVGLADraDEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 163 RKAALGRALVSNPRVLLLDEPT---NHLDI-ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAaglNPEETeELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
19-232 |
3.45e-22 |
|
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: 95.58 E-value: 3.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDliVARLqqdpprnvegSVYDFVAEGIeeqaey 97
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgED--ITGL----------PPHEIARLGI------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 98 lKRYHDISRLVMNDPSEKNLneLAKVQEQLDHHNLW--------QLENRINEVLAQLGLDP--NVALSSLSGGWLRKAAL 167
Cdd:cd03219 78 -GRTFQIPRLFPELTVLENV--MVAAQARTGSGLLLararreerEARERAEELLERVGLADlaDRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 168 GRALVSNPRVLLLDEPT---NHLDIE-TIDWLEGfLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03219 155 ARALATDPKLLLLDEPAaglNPEETEeLAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-232 |
3.81e-22 |
|
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: 95.92 E-value: 3.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNRE--QGLDDGRIIYEQDL------------ 66
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlpPTYGNDVRLFGERRggedvwelrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 67 -IV-ARLQQDPPRNVegSVYDFVAEGieeqaeylkrYHDISRLvMNDPSEknlnelakvqEQldhhnlwqlENRINEVLA 144
Cdd:COG1119 81 gLVsPALQLRFPRDE--TVLDVVLSG----------FFDSIGL-YREPTD----------EQ---------RERARELLE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 145 QLGLDP--NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRN 218
Cdd:COG1119 129 LLGLAHlaDRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTHHVEEIPP 208
|
250
....*....|....
gi 15830287 219 MATRIVDLDRGKLV 232
Cdd:COG1119 209 GITHVLLLKDGRVV 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
17-231 |
3.95e-22 |
|
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: 95.25 E-value: 3.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLDD---GRIIyeqdlivarlqqdpprnVEGSvyDFVAEGIEE 93
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILG---GLDRptsGEVR-----------------VDGT--DISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 94 QAEYLKR--------YHDISRLvmndPSEKNLnELAKVqeqLDHHNLWQLENRINEVLAQLGLD------PnvalSSLSG 159
Cdd:cd03255 76 LAAFRRRhigfvfqsFNLLPDL----TALENV-ELPLL---LAGVPKKERRERAEELLERVGLGdrlnhyP----SELSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287 160 GWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRnMATRIVDLDRGKL 231
Cdd:cd03255 144 GQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-232 |
5.89e-22 |
|
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: 95.05 E-value: 5.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIY---------EQDLIVAR 70
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLII---GLlrpDSGEILVdgqditglsEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 71 LQ-----QDpprnveGSVYDF--VAEGIeeqAEYLKRYHDISRlvmndpseknlnelakvqeqldhhnlWQLENRINEVL 143
Cdd:COG1127 82 RRigmlfQG------GALFDSltVFENV---AFPLREHTDLSE--------------------------AEIRELVLEKL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 144 AQLGLDPNVAL--SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET---IDWLEGFL-KTFNGTIIFISHDRSFIR 217
Cdd:COG1127 127 ELVGLPGAADKmpSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITsavIDELIRELrDELGLTSVVVTHDLDSAF 206
|
250
....*....|....*
gi 15830287 218 NMATRIVDLDRGKLV 232
Cdd:COG1127 207 AIADRVAVLADGKII 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
312-497 |
8.35e-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: 99.28 E-value: 8.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 312 ASRSGKIVFEMEDVCYQvDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGtklevayfDQHR 391
Cdd:TIGR02857 316 AAPASSLEFSGVSVAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN--------GVPL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 392 AELDPD-----------------KTVMDNLAEGKQEV---MVNGKPRHVlgYLQDFLFH-PKRAMTPV----RALSGGER 446
Cdd:TIGR02857 387 ADADADswrdqiawvpqhpflfaGTIAENIRLARPDAsdaEIREALERA--GLDEFVAAlPQGLDTPIgeggAGLSGGQA 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15830287 447 NRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY-QG-TVLLVSHDR 497
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaQGrTVLLVTHRL 517
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
321-517 |
1.52e-21 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 93.09 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQV-DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlevayfDQHRAEL----- 394
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK------PIKAKERrksig 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 ----DPD-----KTVMDNLAEGKQEV-MVNGKPRHVLGYLQDFLF---HPkramtpvRALSGGERNRLLLARLFLKPSNL 461
Cdd:cd03226 75 yvmqDVDyqlftDSVREELLLGLKELdAGNEQAETVLKDLDLYALkerHP-------LSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 462 LILDEPTNDLDVETLELLEELIDSYQG---TVLLVSHDRQFVDNTVTECwIFEGGGKIG 517
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRV-LLLANGAIV 205
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
561-630 |
1.97e-21 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 88.29 E-value: 1.97e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 561 KLSYKLQRELEQLPQLLEDLEAKLEALQTQVADASFFSQpHEQTQKVLADMAAAEQELEQAFERWEYLEA 630
Cdd:pfam16326 1 KLSYKEQRELEELEAEIEKLEEEIAELEAQLADPELYSD-YEKLQELSAELEELEAELEELYERWEELEE 69
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
321-502 |
2.69e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 92.81 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCY-QVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKL---EVAY------ 386
Cdd:COG2884 3 RFENVSKrYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNgqdlSRLkrrEIPYlrrrig 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 387 --FDQHRaeLDPDKTVMDNLA-----EGKQEVMVNGKPRHVLGYLQdfLFHPKRAMtpVRALSGGERNRLLLARLFL-KP 458
Cdd:COG2884 83 vvFQDFR--LLPDRTVYENVAlplrvTGKSRKEIRRRVREVLDLVG--LSDKAKAL--PHELSGGEQQRVAIARALVnRP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15830287 459 SnLLILDEPTNDLDVETLELLEELIDSY--QG-TVLLVSHDRQFVDN 502
Cdd:COG2884 157 E-LLLADEPTGNLDPETSWEIMELLEEInrRGtTVLIATHDLELVDR 202
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
333-496 |
2.74e-21 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 92.95 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HVGTKLEVAYFDQHRAE-----------LDPD 397
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgKDLLKLSRRLRKIRRKEiqmvfqdpmssLNPR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 398 KTVMDNLAEG--KQEVMVNGKPRHVLGYLQDFLFH-PKRAMT--PvRALSGGERNRLLLAR-LFLKPSnLLILDEPTNDL 471
Cdd:cd03257 99 MTIGEQIAEPlrIHGKLSKKEARKEAVLLLLVGVGlPEEVLNryP-HELSGGQRQRVAIARaLALNPK-LLIADEPTSAL 176
|
170 180
....*....|....*....|....*....
gi 15830287 472 DVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:cd03257 177 DVSVQAQILDLLkklqEELGLTLLFITHD 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-230 |
3.48e-21 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 90.91 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFS----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDL----------IVARLQQDP 75
Cdd:cd03228 6 VSFSypgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlIDGVDLrdldleslrkNIAYVPQDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 76 PRnVEGSVYDfvaegieeqaeylkryhdisrlvmndpseknlnelakvqeqldhhNLwqlenrinevlaqlgldpnvals 155
Cdd:cd03228 86 FL-FSGTIRE---------------------------------------------NI----------------------- 96
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 156 sLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET-IDWLEGFLKTFNG-TIIFISHDRSFIRnMATRIVDLDRGK 230
Cdd:cd03228 97 -LSGGQRQRIAIARALLRDPPILILDEATSALDPETeALILEALRALAKGkTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-232 |
7.18e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 91.64 E-value: 7.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 2 SLISMHGAWLSFSDA----PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLD---DGRIIYE-QDliVARLQQ 73
Cdd:COG1136 3 PLLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILG---GLDrptSGEVLIDgQD--ISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 74 DpprnvegsvydfvaegieEQAEYlkRYHDISrLVMNDPsekNL-NELaKVQE------QLDHHNLWQLENRINEVLAQL 146
Cdd:COG1136 78 R------------------ELARL--RRRHIG-FVFQFF---NLlPEL-TALEnvalplLLAGVSRKERRERARELLERV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 147 GLD------PNvalsSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRsFI 216
Cdd:COG1136 133 GLGdrldhrPS----QLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDP-EL 207
|
250
....*....|....*.
gi 15830287 217 RNMATRIVDLDRGKLV 232
Cdd:COG1136 208 AARADRVIRLRDGRIV 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-232 |
8.43e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 94.39 E-value: 8.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRI-IYEQDliVARLqqdPP 76
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIA---GFetpDSGRIlLDGRD--VTGL---PP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 77 --RNVeG------------SVYDFVAEGIeeqaeylkRYHDISRlvmndpseknlnelAKVQEqldhhnlwqlenRINEV 142
Cdd:COG3842 75 ekRNV-GmvfqdyalfphlTVAENVAFGL--------RMRGVPK--------------AEIRA------------RVAEL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 143 LAQLGLD------PnvalSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHD 212
Cdd:COG3842 120 LELVGLEgladryP----HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHD 195
|
250 260
....*....|....*....|..
gi 15830287 213 RS--FIrnMATRIVDLDRGKLV 232
Cdd:COG3842 196 QEeaLA--LADRIAVMNDGRIE 215
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
327-496 |
9.10e-21 |
|
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: 91.03 E-value: 9.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 327 YQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----------TKLEVAYFDQHRAeLDP 396
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINgysirtdrkaARQSLGYCPQFDA-LFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 397 DKTVMDNL---AegkqevMVNGKPRH-----VLGYLQDFLFHPKRAmTPVRALSGGERNRLLLARLFLKPSNLLILDEPT 468
Cdd:cd03263 89 ELTVREHLrfyA------RLKGLPKSeikeeVELLLRVLGLTDKAN-KRARTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190
....*....|....*....|....*....|
gi 15830287 469 NDLDVETLELLEELIDSYQG--TVLLVSHD 496
Cdd:cd03263 162 SGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
319-495 |
9.42e-21 |
|
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: 92.07 E-value: 9.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQL-QADSGRIHV-GTKLE------------- 383
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLfGERRGgedvwelrkrigl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 384 VAYFDQHRaeLDPDKTVMDNLAEGK----------QEVMVNgKPRHVLGYLQdfLFHpkRAMTPVRALSGGERNRLLLAR 453
Cdd:COG1119 83 VSPALQLR--FPRDETVLDVVLSGFfdsiglyrepTDEQRE-RARELLELLG--LAH--LADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15830287 454 LFLKPSNLLILDEPTNDLDVETLELLEELIDSY--QG--TVLLVSH 495
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGapTLVLVTH 201
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-185 |
1.20e-20 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 88.86 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVeGSVYDFVaegieeqaeyl 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEI-GYVFQDP----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 99 kryHDISRLVMndpsEKNLNELAKVQEQLDHHnlwqLENRINEVLAQLGLD------PNVALSSLSGGWLRKAALGRALV 172
Cdd:pfam00005 69 ---QLFPRLTV----RENLRLGLLLKGLSKRE----KDARAEEALEKLGLGdladrpVGERPGTLSGGQRQRVAIARALL 137
|
170
....*....|...
gi 15830287 173 SNPRVLLLDEPTN 185
Cdd:pfam00005 138 TKPKLLLLDEPTA 150
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
321-516 |
1.72e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.56 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSG----------------RIHVGTkleV 384
Cdd:PRK13537 9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGsislcgepvpsrarhaRQRVGV---V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 385 AYFDQhraeLDPDKTVMDNL-AEGKQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK13537 86 PQFDN----LDPDFTVRENLlVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287 464 LDEPTNDLDVETLELLEELIDSYQG---TVLLVSHDRQFVDNTVTECWIFEGGGKI 516
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLArgkTILLTTHFMEEAERLCDRLCVIEEGRKI 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-232 |
1.83e-20 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 90.64 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKilnreqglddgriiyeqdLIVARLQQDpprnvEGSV 83
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLR------------------LIVGLLRPD-----SGEV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 84 YdfvAEGieeqaeylkryHDISRLvmndpSEKNLNELAK---VQEQ------------------LDHHNL--WQLENRIN 140
Cdd:cd03261 58 L---IDG-----------EDISGL-----SEAELYRLRRrmgMLFQsgalfdsltvfenvafplREHTRLseEEIREIVL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 141 EVLAQLGLDPNVAL--SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD-------IETIDWLEgflKTFNGTIIFISH 211
Cdd:cd03261 119 EKLEAVGLRGAEDLypAELSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLK---KELGLTSIMVTH 195
|
250 260
....*....|....*....|.
gi 15830287 212 DRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03261 196 DLDTAFAIADRIAVLYDGKIV 216
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-232 |
2.01e-20 |
|
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: 88.64 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlivarlqqdpprnVEGSV 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL-----------------VDGKE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 84 YDFvaegieeqaeylkryhdisrlvmNDPSEKnlnelakvqeqldhhnlwqLENRINEVlaqlgldpnvalSSLSGGWLR 163
Cdd:cd03216 64 VSF-----------------------ASPRDA-------------------RRAGIAMV------------YQLSVGERQ 89
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 164 KAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NG-TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03216 90 MVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraQGvAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-500 |
2.15e-20 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 88.78 E-value: 2.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAE------ 393
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrrrigm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 394 ------LDPDKTVMDNLAEGkqevmvngkprhvlgylqdflfhpkramtpvraLSGGERNRLLLAR-LFLKPsNLLILDE 466
Cdd:cd03229 81 vfqdfaLFPHLTVLENIALG---------------------------------LSGGQQQRVALARaLAMDP-DVLLLDE 126
|
170 180 190
....*....|....*....|....*....|....*...
gi 15830287 467 PTNDLDVETLELLEELI----DSYQGTVLLVSHDRQFV 500
Cdd:cd03229 127 PTSALDPITRREVRALLkslqAQLGITVVLVTHDLDEA 164
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
321-497 |
2.17e-20 |
|
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: 89.89 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKL---------EVAYFDQHR 391
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgvpperrNIGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 392 AeLDPDKTVMDNLAEG--KQEVMVNGKPRHVLGYLQ--DFLFHPKRamtPVRALSGGERNRLLLAR-LFLKPSnLLILDE 466
Cdd:cd03259 82 A-LFPHLTVAENIAFGlkLRGVPKAEIRARVRELLElvGLEGLLNR---YPHELSGGQQQRVALARaLAREPS-LLLLDE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 15830287 467 PTNDLDVETLELLEELIDSYQG----TVLLVSHDR 497
Cdd:cd03259 157 PLSALDAKLREELREELKELQRelgiTTIYVTHDQ 191
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-231 |
2.69e-20 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 89.77 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLIVARLqqdpPRNvegsvydfvaegieeQ 94
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVN-GQDVSDL----RGR---------------A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 95 AEYLKR-----YHDiSRLVMNDPSEKNLnelAKVQEQLDH-HNLWQleNRINEVLAQLGLD--PNVALSSLSGGWLRKAA 166
Cdd:cd03292 73 IPYLRRkigvvFQD-FRLLPDRNVYENV---AFALEVTGVpPREIR--KRVPAALELVGLShkHRALPAELSGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287 167 LGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFN---GTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
330-503 |
4.51e-20 |
|
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: 89.92 E-value: 4.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV----------GTKLEVAYFDQHRaELDPDKT 399
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdgedvrkeprEARRQIGVLPDER-GLYDRLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 400 VMDNL---AEGKQEVMVNGKPR-----HVLGyLQDFLfhpKRamtPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
Cdd:COG4555 91 VRENIryfAELYGLFDEELKKRieeliELLG-LEEFL---DR---RVGELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190
....*....|....*....|....*....|....*
gi 15830287 472 DVETLELLEELIDSY--QG-TVLLVSHDRQFVDNT 503
Cdd:COG4555 164 DVMARRLLREILRALkkEGkTVLFSSHIMQEVEAL 198
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
12-232 |
4.57e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 92.13 E-value: 4.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIIY-EQDLIVARLQQDppRNVeG------ 81
Cdd:COG1118 11 RFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRII---AGLetpDSGRIVLnGRDLFTNLPPRE--RRV-Gfvfqhy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 82 ------SVYDFVAEGIEeqaeylkryhdisrlvMNDPSEKNLNelAKVQEQLDHHNLWQLENRInevlaqlgldPnvalS 155
Cdd:COG1118 85 alfphmTVAENIAFGLR----------------VRPPSKAEIR--ARVEELLELVQLEGLADRY----------P----S 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 156 SLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:COG1118 133 QLSGGQRQRVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
.
gi 15830287 232 V 232
Cdd:COG1118 213 E 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
321-496 |
6.14e-20 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 89.10 E-value: 6.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTK--------------LEVAY 386
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 387 FDQHRAELDpDKTVMDNLA------EGKQEVMVNGKprhVLGYLQDFLFHPKRAMTPvRALSGGERNRLLLAR-LFLKPS 459
Cdd:cd03261 82 LFQSGALFD-SLTVFENVAfplrehTRLSEEEIREI---VLEKLEAVGLRGAEDLYP-AELSGGMKKRVALARaLALDPE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15830287 460 nLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:cd03261 157 -LLLYDEPTAGLDPIASGVIDDLIrslkKELGLTSIMVTHD 196
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-232 |
7.26e-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: 88.47 E-value: 7.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLIVARLqqdPP--RNV-- 79
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIG-GRDVTDL---PPkdRDIam 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 80 ---------EGSVYDFVAEGIE----EQAEYLKRYHDISRLVmndpseknlnelaKVQEQLDHHnlwqlenrinevlaql 146
Cdd:cd03301 77 vfqnyalypHMTVYDNIAFGLKlrkvPKDEIDERVREVAELL-------------QIEHLLDRK---------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 147 gldPnvalSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATR 222
Cdd:cd03301 128 ---P----KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADR 200
|
250
....*....|
gi 15830287 223 IVDLDRGKLV 232
Cdd:cd03301 201 IAVMNDGQIQ 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-234 |
8.80e-20 |
|
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: 88.39 E-value: 8.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLD-----------DGRIIYEQDLIVARL- 71
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdegevllDGKDIYDLDVDVLELr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 72 -------QQDPPrnVEGSVYDFVAegieeqaeYLKRYHDISRlvmndpsEKNLNELakVQEQLDHHNLWqlenriNEVLA 144
Cdd:cd03260 81 rrvgmvfQKPNP--FPGSIYDNVA--------YGLRLHGIKL-------KEELDER--VEEALRKAALW------DEVKD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 145 QLgldpnvALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG--TIIFISHDRSFIRNMATR 222
Cdd:cd03260 136 RL------HALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHNMQQAARVADR 209
|
250
....*....|..
gi 15830287 223 IVDLDRGKLVTY 234
Cdd:cd03260 210 TAFLLNGRLVEF 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
320-495 |
9.48e-20 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 86.89 E-value: 9.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQ--LVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRaeldp 396
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADISQWDPNELG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 397 dktvmdnlaegkqevmvngkpRHVlGYL-QDFLFHPKRAMTPVraLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03246 76 ---------------------DHV-GYLpQDDELFSGSIAENI--LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180
....*....|....*....|...
gi 15830287 476 LELLEELIDSYQ---GTVLLVSH 495
Cdd:cd03246 132 ERALNQAIAALKaagATRIVIAH 154
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-224 |
9.55e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 89.38 E-value: 9.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSFSDA----PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLDD---GRIIYE--------QD 65
Cdd:COG1116 5 APALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA---GLEKptsGEVLVDgkpvtgpgPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 66 LIVArLQQD---PPRNVEGSVydfvaegieeqaeylkryhdisRLVMndpseknlnELAKVQEQldhhnlwQLENRINEV 142
Cdd:COG1116 82 RGVV-FQEPallPWLTVLDNV----------------------ALGL---------ELRGVPKA-------ERRERAREL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 143 LAQLGLD------PnvalSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETI----DWLEGFLKTFNGTIIFISHD 212
Cdd:COG1116 123 LELVGLAgfedayP----HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRerlqDELLRLWQETGKTVLFVTHD 198
|
250
....*....|....*
gi 15830287 213 rsfIRN---MATRIV 224
Cdd:COG1116 199 ---VDEavfLADRVV 210
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
330-496 |
1.06e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 87.29 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAelDPDK---TVMDNLAE 406
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSE--VPDSlplTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 407 GK-QEVMVNGKPRHV-----------LGyLQDFLfhpKRamtPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
Cdd:NF040873 81 GRwARRGLWRRLTRDdraavddalerVG-LADLA---GR---QLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180
....*....|....*....|....*
gi 15830287 475 TLELLEELIDSYQG---TVLLVSHD 496
Cdd:NF040873 154 SRERIIALLAEEHArgaTVVVVTHD 178
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
310-496 |
1.22e-19 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 92.81 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 310 EEASRSGKIVFEMEDVCYQVDGKQLV-KDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYF 387
Cdd:TIGR02868 325 AGAVGLGKPTLELRDLSAGYPGAPPVlDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLdGVPVSSLDQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 388 DQHRAEL-----DP---DKTVMDNLAEGKQEV----MVNGKPRHVLGYLQDFLfhPKRAMTPV----RALSGGERNRLLL 451
Cdd:TIGR02868 405 DEVRRRVsvcaqDAhlfDTTVRENLRLARPDAtdeeLWAALERVGLADWLRAL--PDGLDTVLgeggARLSGGERQRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15830287 452 ARLFLKPSNLLILDEPTNDLDVETLELLEELI-DSYQG-TVLLVSHD 496
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLEDLlAALSGrTVVLITHH 529
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
327-472 |
1.39e-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: 86.60 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 327 YQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAELdpdkTVMDnlae 406
Cdd:cd03247 10 YPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLI----SVLN---- 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 407 gkQEVMV-NGKPRHVLGylqdflfhpkramtpvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03247 82 --QRPYLfDTTLRNNLG----------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
320-513 |
1.45e-19 |
|
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: 87.65 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQL--VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklevaYFDQHRA-ELDP 396
Cdd:cd03245 3 IEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV---------LLDGTDIrQLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 397 DK-----------------TVMDNLAEGK-----QEVMVNGKprhvLGYLQDFL-FHPKRAMTPV----RALSGGERNRL 449
Cdd:cd03245 74 ADlrrnigyvpqdvtlfygTLRDNITLGApladdERILRAAE----LAGVTDFVnKHPNGLDLQIgergRGLSGGQRQAV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287 450 LLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQG--TVLLVSHdRQFVDNTVTECWIFEGG 513
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSG 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-232 |
1.52e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 90.52 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGLDD---GRIIYEqDLIVARLqqdPP- 76
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMI---AGLEDptsGEILIG-GRDVTDL---PPk 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 77 -RNVeGSV------YDF--VAEGIeeqAEYLKryhdisrlvmndpseknlneLAKVQEQldhhnlwQLENRINEVLAQLG 147
Cdd:COG3839 74 dRNI-AMVfqsyalYPHmtVYENI---AFPLK--------------------LRKVPKA-------EIDRRVREAAELLG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 148 LDPnvaL-----SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRN 218
Cdd:COG3839 123 LED---LldrkpKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHDQVEAMT 199
|
250
....*....|....
gi 15830287 219 MATRIVDLDRGKLV 232
Cdd:COG3839 200 LADRIAVMNDGRIQ 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-232 |
2.34e-19 |
|
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: 89.34 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKI---LNREQGLDDGRIIYE-QDLivARLQQDPPRNVegsvydfvaegieeq 94
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAilgLLPPPGITSGEILFDgEDL--LKLSEKELRKI--------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 95 aeylkRYHDISrLVMNDP--SeknLNELAKVQEQ----LDHHNLW---QLENRINEVLAQLGL-DPNVALSS----LSGG 160
Cdd:COG0444 84 -----RGREIQ-MIFQDPmtS---LNPVMTVGDQiaepLRIHGGLskaEARERAIELLERVGLpDPERRLDRypheLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287 161 WLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVtiqaQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-232 |
2.39e-19 |
|
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: 87.26 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQ------DLIVAR-----LQQDPpRNVEGS 82
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqlDPADLRrnigyVPQDV-TLFYGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 83 VYDFVAEGieeqaeylKRYHDISRLVmndpsekNLNELAKVQEQLDHHnlwqlenrinevlaQLGLDPNVAL--SSLSGG 160
Cdd:cd03245 94 LRDNITLG--------APLADDERIL-------RAAELAGVTDFVNKH--------------PNGLDLQIGErgRGLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 161 WLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG--TIIFISHDRSFIrNMATRIVDLDRGKLV 232
Cdd:cd03245 145 QRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-224 |
4.34e-19 |
|
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: 86.37 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSFSDA----PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVAR-------LQ 72
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPgpdrgyvFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 73 QD---PPRnvegSVYDFVAEGIEeqaeylkryhdisrlvmndpseknlneLAKVQEQldhhnlwQLENRINEVLAQLGLD 149
Cdd:cd03293 81 QDallPWL----TVLDNVALGLE---------------------------LQGVPKA-------EARERAEELLELVGLS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 150 ------PnvalSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDrsfIRN- 218
Cdd:cd03293 123 gfenayP----HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTreqlQEELLDIWRETGKTVLLVTHD---IDEa 195
|
....*...
gi 15830287 219 --MATRIV 224
Cdd:cd03293 196 vfLADRVV 203
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
321-496 |
5.84e-19 |
|
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: 85.99 E-value: 5.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQL----VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKL-----EVAY-FDQ 389
Cdd:cd03293 2 EVRNVSKTYGGGGGavtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdGEPVtgpgpDRGYvFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 390 HRaeLDPDKTVMDNLAEGkqeVMVNGKPR-----HVLGY-----LQDFLFH-PKramtpvrALSGGERNRLLLAR-LFLK 457
Cdd:cd03293 82 DA--LLPWLTVLDNVALG---LELQGVPKaeareRAEELlelvgLSGFENAyPH-------QLSGGMRQRVALARaLAVD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15830287 458 PsNLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:cd03293 150 P-DVLLLDEPFSALDALTREQLQEELldiwRETGKTVLLVTHD 191
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-473 |
9.98e-19 |
|
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: 89.74 E-value: 9.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSFSDA----PLLDNAELHIEDNERVCLVGRNGAGKS----TLMKILNREQGLDDGRIIYE-QDLivarL 71
Cdd:COG4172 4 MPLLSVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDgQDL----L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 72 QQDPP--RNVEGSvydfvaegieeqaeylkryhDISrLVMNDP--SeknLNELAKVQEQLD-----HHNLW--QLENRIN 140
Cdd:COG4172 80 GLSERelRRIRGN--------------------RIA-MIFQEPmtS---LNPLHTIGKQIAevlrlHRGLSgaAARARAL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 141 EVLAQLGL-DPNVALSS----LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIeTI-----DWLEGFLKTFNGTIIFIS 210
Cdd:COG4172 136 ELLERVGIpDPERRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVqaqilDLLKDLQRELGMALLLIT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 211 HDRSFIRNMATRIVDLDRGKLV---------TYPGN-YDQYLLEKE-------------EALRVEELQnaefdrklaqee 267
Cdd:COG4172 215 HDLGVVRRFADRVAVMRQGEIVeqgptaelfAAPQHpYTRKLLAAEprgdprpvppdapPLLEARDLK------------ 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 268 VW--IRQGIKARRTrneGRVRAlkamrrergerrevmgtakmqveeasrsgkivfemedvcyqvdgkqlVKDFSAQVLRG 345
Cdd:COG4172 283 VWfpIKRGLFRRTV---GHVKA-----------------------------------------------VDGVSLTLRRG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 346 DKIALIGPNGCGKTTLLKLMLGqLQADSGRIHV-GTKLEVAYFDQHR--------------AELDPDKTVMDNLAEG--K 408
Cdd:COG4172 313 ETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFdGQDLDGLSRRALRplrrrmqvvfqdpfGSLSPRMTVGQIIAEGlrV 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 409 QEVMVNGKPRHvlgylqdflfhpKRAmtpVRAL-----------------SGGERNRLLLAR-LFLKPSnLLILDEPTND 470
Cdd:COG4172 392 HGPGLSAAERR------------ARV---AEALeevgldpaarhryphefSGGQRQRIAIARaLILEPK-LLVLDEPTSA 455
|
...
gi 15830287 471 LDV 473
Cdd:COG4172 456 LDV 458
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-473 |
1.10e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.32 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIyeqdlivarlqqdpprnVEGSVYDF--------- 86
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILY---GLyqpDSGEIL-----------------IDGKPVRIrsprdaial 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 87 ----------------VAEGIeeqaeylkryhdisrlVM-NDPSEKNLNELAKVQEqldhhnlwqlenRINEVLAQLGL- 148
Cdd:COG3845 81 gigmvhqhfmlvpnltVAENI----------------VLgLEPTKGGRLDRKAARA------------RIRELSERYGLd 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 149 -DPNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NG-TIIFISHDRSFIRNMATRIV 224
Cdd:COG3845 133 vDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLaaEGkSIIFITHKLREVMAIADRVT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 225 DLDRGKLVtypgnydqyllekeEALRVEELQNAEfdrkLAQEEVwirqgikarrtrneGRVRALKAmrrergerrevmgt 304
Cdd:COG3845 213 VLRRGKVV--------------GTVDTAETSEEE----LAELMV--------------GREVLLRV-------------- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 305 akmqVEEASRSGKIVFEMEDVCYQVD-GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG---- 379
Cdd:COG3845 247 ----EKAPAEPGEVVLEVENLSVRDDrGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDgedi 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 380 --------TKLEVAYF--DQHRAELDPDKTVMDNLAEGKQE-------VMVNGKP--RHVLGYLQDFLFHPKRAMTPVRA 440
Cdd:COG3845 323 tglsprerRRLGVAYIpeDRLGRGLVPDMSVAENLILGRYRrppfsrgGFLDRKAirAFAEELIEEFDVRTPGPDTPARS 402
|
490 500 510
....*....|....*....|....*....|...
gi 15830287 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDV 435
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
321-496 |
1.87e-18 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 85.03 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVgtklevayFDQHRAELDPDK-- 398
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV--------DGQDITGLSEKEly 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 399 -------------------TVMDNLA----E----GKQEV--MVNGKPRHVlGyLQDFlfhpkRAMTPvRALSGGERNRL 449
Cdd:COG1127 79 elrrrigmlfqggalfdslTVFENVAfplrEhtdlSEAEIreLVLEKLELV-G-LPGA-----ADKMP-SELSGGMRKRV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15830287 450 LLAR-LFLKPSnLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:COG1127 151 ALARaLALDPE-ILLYDEPTAGLDPITSAVIDELIrelrDELGLTSVVVTHD 201
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
331-495 |
2.73e-18 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 83.81 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 331 GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgTKLEVAYFDQHRA-----------ELDPDKT 399
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI---TFDGKSYQKNIEAlrrigalieapGFYPNLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 400 VMDNLAEGKQEVMVNGKPRH-VLGY--LQDflfHPKRamtPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETL 476
Cdd:cd03268 89 ARENLRLLARLLGIRKKRIDeVLDVvgLKD---SAKK---KVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180
....*....|....*....|..
gi 15830287 477 ELLEELIDSYQ---GTVLLVSH 495
Cdd:cd03268 163 KELRELILSLRdqgITVLISSH 184
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
321-501 |
2.91e-18 |
|
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: 84.08 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDG----KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKL------------- 382
Cdd:cd03255 2 ELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdGTDIsklsekelaafrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 383 -EVAY-FDQHRaeLDPDKTVMDNLA-----EGKQEVMVNGKPRHVLGYLQdfLfhPKRAMTPVRALSGGERNRLLLARLF 455
Cdd:cd03255 82 rHIGFvFQSFN--LLPDLTALENVElplllAGVPKKERRERAEELLERVG--L--GDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15830287 456 LKPSNLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHDRQFVD 501
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLrelnKEAGTTIVVVTHDPELAE 205
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-232 |
3.23e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 84.58 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNR-----------EQGLDDGRIIYEQDLIVA 69
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielypearvsGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 70 RLQ-----QDPPRNVEGSVYDFVAEGIEeqaeylkryhdISRLVmndpseKNLNEL-AKVQEQLDHHNLW-QLENRInev 142
Cdd:PRK14247 81 RRRvqmvfQIPNPIPNLSIFENVALGLK-----------LNRLV------KSKKELqERVRWALEKAQLWdEVKDRL--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 143 laqlgldpNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG--TIIFISHdrsfIRNMA 220
Cdd:PRK14247 141 --------DAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH----FPQQA 208
|
250
....*....|....*.
gi 15830287 221 TRIVD----LDRGKLV 232
Cdd:PRK14247 209 ARISDyvafLYKGQIV 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-241 |
3.29e-18 |
|
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: 88.45 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQ-----DPPRNvegsVYDF 86
Cdd:TIGR03719 331 AFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQsrdalDPNKT----VWEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 87 VAEGieeqaeylkryHDISRLvmndpSEKNLNELAKVqeqldhhnlwqleNRINEVlaqlGLDPNVALSSLSGGWLRKAA 166
Cdd:TIGR03719 407 ISGG-----------LDIIKL-----GKREIPSRAYV-------------GRFNFK----GSDQQKKVGQLSGGERNRVH 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287 167 LGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLD-RGKLVTYPGNYDQY 241
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEY 529
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
335-496 |
3.93e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 83.92 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQH----------RAELDPDKTVMDNL 404
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFlrrigvvfgqKTQLWWDLPVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 405 AEGKQevMVNGKPRHV---LGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEE 481
Cdd:cd03267 117 YLLAA--IYDLPPARFkkrLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170
....*....|....*....
gi 15830287 482 LIDSY----QGTVLLVSHD 496
Cdd:cd03267 195 FLKEYnrerGTTVLLTSHY 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-501 |
4.33e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 87.94 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 34 LVGRNGAGKSTLMKILNreqglddGRIIyeqdlivarlqqdpPR--NVEGSV-YDFVAE---GIEEQaEYLKR------- 100
Cdd:PRK13409 104 ILGPNGIGKTTAVKILS-------GELI--------------PNlgDYEEEPsWDEVLKrfrGTELQ-NYFKKlyngeik 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 101 ------YHD-ISRLVMNDPSEknlnELAKVQEqldhhnlwqlENRINEVLAQLGLDP--NVALSSLSGGWLRKAALGRAL 171
Cdd:PRK13409 162 vvhkpqYVDlIPKVFKGKVRE----LLKKVDE----------RGKLDEVVERLGLENilDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 172 VSNPRVLLLDEPTNHLDI-------ETIDWLegflkTFNGTIIFISHDRSFIRNMATRIVdldrgklVTY--PGNY---- 238
Cdd:PRK13409 228 LRDADFYFFDEPTSYLDIrqrlnvaRLIREL-----AEGKYVLVVEHDLAVLDYLADNVH-------IAYgePGAYgvvs 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 239 ---------DQYLlekeealrveelqnaefDRKLAQEEVWIRQgikarrTRNEGRVRAlkamrrergerrevmgtakmqv 309
Cdd:PRK13409 296 kpkgvrvgiNEYL-----------------KGYLPEENMRIRP------EPIEFEERP---------------------- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 310 EEASRSGKIVFEMEDVCYQVDGKQLVKDfSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRihVGTKLEVAYFDQ 389
Cdd:PRK13409 331 PRDESERETLVEYPDLTKKLGDFSLEVE-GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE--VDPELKISYKPQ 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 390 hRAELDPDKTVMDNLAEGKQEVMVNgkprhvlgYLQDFLFHP---KRAMT-PVRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:PRK13409 408 -YIKPDYDGTVEDLLRSITDDLGSS--------YYKSEIIKPlqlERLLDkNVKDLSGGELQRVAIAACLSRDADLYLLD 478
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15830287 466 EPTNDLDVETLELLEELI----DSYQGTVLLVSHDRQFVD 501
Cdd:PRK13409 479 EPSAHLDVEQRLAVAKAIrriaEEREATALVVDHDIYMID 518
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
14-232 |
4.61e-18 |
|
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: 83.78 E-value: 4.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYeQDLIVARLQQDPPRNV-------------- 79
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLV-DGTDLTLLSGKELRKArrrigmifqhfnll 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 80 -EGSVYDFVAEGIEeqaeylkryhdisrlvmndpseknlneLAKVQEQldhhnlwQLENRINEVLAQLGLD------Pnv 152
Cdd:cd03258 95 sSRTVFENVALPLE---------------------------IAGVPKA-------EIEERVLELLELVGLEdkadayP-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 153 alSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDR 228
Cdd:cd03258 139 --AQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsiLALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK 216
|
....
gi 15830287 229 GKLV 232
Cdd:cd03258 217 GEVV 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
34-232 |
5.57e-18 |
|
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: 83.01 E-value: 5.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 34 LVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDL---------IVARLQQDPPRNVEGSVYDFVAegieeqaeYLKRYHD 103
Cdd:cd03264 30 LLGPNGAGKTTLMRILATLTPPSSGTIrIDGQDVlkqpqklrrRIGYLPQEFGVYPNFTVREFLD--------YIAWLKG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 104 ISrlvmnDPSEKnlnelAKVQEQLDHHNLWQLENRinevlaqlgldpnvALSSLSGGWLRKAALGRALVSNPRVLLLDEP 183
Cdd:cd03264 102 IP-----SKEVK-----ARVDEVLELVNLGDRAKK--------------KIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15830287 184 TNHLDIETIDWLEGFLKTF--NGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELgeDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
335-496 |
6.37e-18 |
|
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: 83.54 E-value: 6.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GT--------KLEVAYFDQHRAeLDPDKTVMDNLA 405
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKditnlppeKRDISYVPQNYA-LFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 406 EG--KQEVMVNGKPRHVL---GYLQ-DFLFHPKramtpVRALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLEL 478
Cdd:cd03299 94 YGlkKRKVDKKEIERKVLeiaEMLGiDHLLNRK-----PETLSGGEQQRVAIARaLVVNPK-ILLLDEPFSALDVRTKEK 167
|
170 180
....*....|....*....|..
gi 15830287 479 LEELI----DSYQGTVLLVSHD 496
Cdd:cd03299 168 LREELkkirKEFGVTVLHVTHD 189
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-231 |
7.48e-18 |
|
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: 83.16 E-value: 7.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDppRNV-----------EG 81
Cdd:cd03296 12 FGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVgfvfqhyalfrHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 82 SVYDFVAEGIEEqaeylkryhdisRLVMNDPSEKNLNElaKVQEQLDhhnLWQLENRINEVLAQLgldpnvalsslSGGW 161
Cdd:cd03296 90 TVFDNVAFGLRV------------KPRSERPPEAEIRA--KVHELLK---LVQLDWLADRYPAQL-----------SGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 162 LRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:cd03296 142 RQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
312-516 |
7.53e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 85.27 E-value: 7.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 312 ASRSGK---IVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVgtkLEVAYFD 388
Cdd:PRK13536 31 ASIPGSmstVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV---LGVPVPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 389 QHRA------------ELDPDKTVMDNL-AEGKQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLF 455
Cdd:PRK13536 108 RARLararigvvpqfdNLDLEFTVRENLlVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 456 LKPSNLLILDEPTNDLDVETLELLEELIDSY--QG-TVLLVSHDRQFVDNTVTECWIFEGGGKI 516
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLlaRGkTILLTTHFMEEAERLCDRLCVLEAGRKI 251
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-234 |
8.47e-18 |
|
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: 83.15 E-value: 8.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQdlivARLQQDPP--RNVeGSVYD----FVAEGIE 92
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG----KDITNLPPekRDI-SYVPQnyalFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 93 EQAEY-LKRyhdisRLVMNDPSEKNLNELAKVQeQLDHhnlwqLENRinevlaqlglDPnvalSSLSGGWLRKAALGRAL 171
Cdd:cd03299 90 KNIAYgLKK-----RKVDKKEIERKVLEIAEML-GIDH-----LLNR----------KP----ETLSGGEQQRVAIARAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 172 VSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTY 234
Cdd:cd03299 145 VVNPKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
12-232 |
1.12e-17 |
|
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: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLIVARLqqdPP--RNVEG-------- 81
Cdd:cd03300 9 FYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD-GKDITNL---PPhkRPVNTvfqnyalf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 82 ---SVYDFVAEGieeqaeylkryhdisrLVMNDPSEKNLNElaKVQEQLDHHNLWQLENRinevlaqlglDPnvalSSLS 158
Cdd:cd03300 85 phlTVFENIAFG----------------LRLKKLPKAEIKE--RVAEALDLVQLEGYANR----------KP----SQLS 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287 159 GGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG----TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03300 133 GGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
315-472 |
1.15e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 86.76 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 315 SGKIVFEmeDVCYQ-VDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFDQH--R 391
Cdd:COG1132 337 RGEIEFE--NVSFSyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV-DIRDLTLEslR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 392 AEL-----DP---DKTVMDNLAEGK-----QEVM-----------VNGKPRhvlGYlqDflfhpkramTPV----RALSG 443
Cdd:COG1132 414 RQIgvvpqDTflfSGTIRENIRYGRpdatdEEVEeaakaaqahefIEALPD---GY--D---------TVVgergVNLSG 479
|
170 180
....*....|....*....|....*....
gi 15830287 444 GERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALD 508
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
17-242 |
1.38e-17 |
|
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: 82.73 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI------IYEQDLIVARlqqdppRNVeGSVYdfvaeg 90
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedIREQDPVELR------RKI-GYVI------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 91 ieeQAEYLKRYHDISRLVMNDPSeknlneLAKVQEQldhhnlwQLENRINEVLAQLGLDPNVAL----SSLSGGWLRKAA 166
Cdd:cd03295 82 ---QQIGLFPHMTVEENIALVPK------LLKWPKE-------KIRERADELLALVGLDPAEFAdrypHELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 167 LGRALVSNPRVLLLDEPTNHLDIETIDWL-EGFLK---TFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYpGNYDQYL 242
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLqEEFKRlqqELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQV-GTPDEIL 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
321-496 |
1.47e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 82.83 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVC--YQVDGKQL--VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV------GTKLEVAY-FDQ 389
Cdd:COG1116 9 ELRGVSkrFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDRGVvFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 390 HRaeLDPDKTVMDNLAEGkqeVMVNGKPR-----HVLGY-----LQDFL-FHPkramtpvRALSGGERNRLLLAR-LFLK 457
Cdd:COG1116 89 PA--LLPWLTVLDNVALG---LELRGVPKaerreRARELlelvgLAGFEdAYP-------HQLSGGMRQRVAIARaLAND 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15830287 458 PSnLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:COG1116 157 PE-VLLMDEPFGALDALTRERLQDELlrlwQETGKTVLFVTHD 198
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
19-232 |
1.66e-17 |
|
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: 82.23 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLIVARLQQDPPRNVEGSVydfvaegieeqAEYL 98
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLID-GTDINKLKGKALRQLRRQI-----------GMIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 99 KRYHDISRL-VMndpseKNLNELAkvqeqLDHHNLWQ-------LENRIN--EVLAQLGLDP--NVALSSLSGGWLRKAA 166
Cdd:cd03256 85 QQFNLIERLsVL-----ENVLSGR-----LGRRSTWRslfglfpKEEKQRalAALERVGLLDkaYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 167 LGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASsrqvMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
321-496 |
1.67e-17 |
|
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: 81.53 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLE-----VAYFDQHR 391
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvTDLPpkdrdIAMVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 392 AeLDPDKTVMDNLAEG-----KQEVMVNGKPRHVLGYLQ-DFLFHPKramtpVRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:cd03301 82 A-LYPHMTVYDNIAFGlklrkVPKDEIDERVREVAELLQiEHLLDRK-----PKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190
....*....|....*....|....*....|....*
gi 15830287 466 EPTNDLDVETLELLEELIDSYQ----GTVLLVSHD 496
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQqrlgTTTIYVTHD 190
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
335-500 |
2.77e-17 |
|
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: 82.01 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFDQHR------------AELDPDKTVMD 402
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGR-DITGLPPHRiarlgiartfqnPRLFPELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 403 NlaegkqeVMVNGKPRHVLGYLQDFLFHPK----------RAM-------------TPVRALSGGERNRLLLAR-LFLKP 458
Cdd:COG0411 99 N-------VLVAAHARLGRGLLAALLRLPRarreereareRAEellervgladradEPAGNLSYGQQRRLEIARaLATEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15830287 459 SnLLILDEPT---NDLDVETLELLEELIDSYQG-TVLLVSHDRQFV 500
Cdd:COG0411 172 K-LLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLV 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-232 |
2.88e-17 |
|
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: 80.76 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIIYEQDLIVAR--------LQQDPPRNV-EGSVYD 85
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKIL---AGLikeSSGSILLNGKPIKAKerrksigyVMQDVDYQLfTDSVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 86 FVAEGIEEQAEYlkryhdisrlvmndpseknlneLAKVQEQLDHHNLWQLENRinevlaqlglDPnvalSSLSGGWLRKA 165
Cdd:cd03226 92 ELLLGLKELDAG----------------------NEQAETVLKDLDLYALKER----------HP----LSLSGGQKQRL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 166 ALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03226 136 AIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
321-500 |
3.04e-17 |
|
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: 81.33 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFDQHR--------- 391
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGE-DITGLPPHEiarlgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 392 ---AELDPDKTVMDNlaegkqeVMVNGKPRHVLGYLQDFLFHPKRAM------------------TPVRALSGGERNRLL 450
Cdd:cd03219 81 fqiPRLFPELTVLEN-------VMVAAQARTGSGLLLARARREEREAreraeellervgladladRPAGELSYGQQRRLE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15830287 451 LAR-LFLKPSnLLILDEPT---NDLDVETLELLEELIDSYQGTVLLVSHDRQFV 500
Cdd:cd03219 154 IARaLATDPK-LLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVV 206
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
10-245 |
3.10e-17 |
|
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: 81.12 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 10 WLSF-SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNR----EQG--LDDGRIIYEQDLIVAR-----LQQDPpr 77
Cdd:cd03254 9 NFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfydpQKGqiLIDGIDIRDISRKSLRsmigvVLQDT-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 78 nvegsvYDF---VAEGIeeqaeylkryhdisRLVMNDPSEKNLNELAKvQEQLdHHNLWQLENRINEVLAQLGldpnval 154
Cdd:cd03254 87 ------FLFsgtIMENI--------------RLGRPNATDEEVIEAAK-EAGA-HDFIMKLPNGYDTVLGENG------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 155 SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWL-EGFLKTFNG-TIIFISHDRSFIRNmATRIVDLDRGKLV 232
Cdd:cd03254 138 GNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIqEALEKLMKGrTSIIIAHRLSTIKN-ADKILVLDDGKII 216
|
250
....*....|...
gi 15830287 233 TyPGNYDQyLLEK 245
Cdd:cd03254 217 E-EGTHDE-LLAK 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-255 |
3.72e-17 |
|
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: 81.38 E-value: 3.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 15 DAPL-LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLIVArlqqDPP---RNVegsvydfvae 89
Cdd:cd03252 13 DGPViLDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDgHDLALA----DPAwlrRQV---------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 90 GIEEQAEYLKRYHDISRLVMNDP--SEKNLNELAKVQEQldHHNLWQLENRINEVLAQLGldpnvalSSLSGGWLRKAAL 167
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPgmSMERVIEAAKLAGA--HDFISELPEGYDTIVGEQG-------AGLSGGQRQRIAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 168 GRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NGTIIFISHDRSFIRNmATRIVDLDRGKLVTyPGNYDQYLLEK 245
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAIMRNMHDIcaGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVE-QGSHDELLAEN 227
|
250
....*....|
gi 15830287 246 EEALRVEELQ 255
Cdd:cd03252 228 GLYAYLYQLQ 237
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-473 |
4.00e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.84 E-value: 4.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlivarlqqdpprNVEGS 82
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI-----------------TINNI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 83 VYDFVAEGIEEQAEYLKRYHDISrlVMNDPS-EKNL---NELAKVQEQLDHHNLWQLENRINEVLAQLGL--DPNVALSS 156
Cdd:PRK09700 68 NYNKLDHKLAAQLGIGIIYQELS--VIDELTvLENLyigRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLkvDLDEKVAN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 157 LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGF---LKTFNGTIIFISHDRSFIRNMATRIVDLDRGklvT 233
Cdd:PRK09700 146 LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLImnqLRKEGTAIVYISHKLAEIRRICDRYTVMKDG---S 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 234 YPGNYDqyllekeealrVEELQNAEFDRKLAQEEvwirqgIKARRTRNEGRVRALkamrrergerrevmgtakmqveeas 313
Cdd:PRK09700 223 SVCSGM-----------VSDVSNDDIVRLMVGRE------LQNRFNAMKENVSNL------------------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 314 rSGKIVFEMEDVCYQVDGKqlVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLE--------- 383
Cdd:PRK09700 261 -AHETVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLnGKDISprspldavk 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 384 --VAYFDQHRAE--LDPDKTVMDNLAEGKQevMVNGKPRHVLGylqdfLFHPK---------RAMTPVRA---------L 441
Cdd:PRK09700 338 kgMAYITESRRDngFFPNFSIAQNMAISRS--LKDGGYKGAMG-----LFHEVdeqrtaenqRELLALKChsvnqniteL 410
|
490 500 510
....*....|....*....|....*....|..
gi 15830287 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK09700 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
321-495 |
4.38e-17 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 80.10 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTK---------LEVAYFDQHR 391
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdepHENILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 392 AELDPDKTVMDNLAEGkqevmvngkpRHVLGYLQDFLFHPKRAM-------TPVRALSGGERNRLLLARLFLKPSNLLIL 464
Cdd:TIGR01189 82 PGLKPELSALENLHFW----------AAIHGGAQRTIEDALAAVgltgfedLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 15830287 465 DEPTNDLDVETLELLEELIDSY---QGTVLLVSH 495
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-234 |
4.55e-17 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 80.42 E-value: 4.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 28 DNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlivarlqqdpprnVEGSVYDfvaegieeqaeylkryhDiSRL 107
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIV-----------------LNGTVLF-----------------D-SRK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 108 VMNDPSEK--------------NLNELAKVQEQLDHHNLWQLENRINEVLAQLGLDP--NVALSSLSGGWLRKAALGRAL 171
Cdd:cd03297 67 KINLPPQQrkiglvfqqyalfpHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHllNRYPAQLSGGEKQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 172 VSNPRVLLLDEPTNHLDIETIDWLEGFL----KTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTY 234
Cdd:cd03297 147 AAQPELLLLDEPFSALDRALRLQLLPELkqikKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-232 |
5.45e-17 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 79.52 E-value: 5.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 10 WLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqglddGRIIYEQdlivarlqqdpprnVEGSVYdfvae 89
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALA-------GRRTGLG--------------VSGEVL----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 90 gIEEQAEYLKRYHDISRLVMndpseknlnelakvQEQLDHHNLWQLENrinevlaqlgLDPNVALSSLSGGWLRKAALGR 169
Cdd:cd03213 70 -INGRPLDKRSFRKIIGYVP--------------QDDILHPTLTVRET----------LMFAAKLRGLSGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287 170 ALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTfNGTIIFISHD-RSFIRNMATRIVDLDRGKLV 232
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSalqvMSLLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
345-495 |
5.73e-17 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 79.89 E-value: 5.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 345 GDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTK--------LEVAYFDqHRAELDPDKTVMDNLaegkqevmvngk 416
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsRFMAYLG-HLPGLKADLSTLENL------------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 417 prHVLGYLQDFlfHPKR--------------AMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEEL 482
Cdd:PRK13543 104 --HFLCGLHGR--RAKQmpgsalaivglagyEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRM 179
|
170
....*....|....*.
gi 15830287 483 IDSY---QGTVLLVSH 495
Cdd:PRK13543 180 ISAHlrgGGAALVTTH 195
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-287 |
6.59e-17 |
|
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: 82.47 E-value: 6.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 22 AELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIV---ARLQQDPPRNVEGSVYD----FVAEGIEEQ 94
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdsrKGIFLPPEKRRIGYVFQearlFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 95 AEY-LKRyhdisrlvmNDPSEKNLNElakvqeqldhhnlwqlenriNEVLAQLGLDPNVA--LSSLSGGWLRKAALGRAL 171
Cdd:TIGR02142 96 LRYgMKR---------ARPSERRISF--------------------ERVIELLGIGHLLGrlPGRLSGGEKQRVAIGRAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 172 VSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKlVTYPGNYDQY------ 241
Cdd:TIGR02142 147 LSSPRLLLMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGR-VAAAGPIAEVwaspdl 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 15830287 242 -LLEKEEALRVEELQNAEFDRK-------LAQEEVWIRQGIKARRTRNEGRVRA 287
Cdd:TIGR02142 226 pWLAREDQGSLIEGVVAEHDQHygltalrLGGGHLWVPENLGPTGARLRLRVPA 279
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-232 |
7.21e-17 |
|
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: 84.00 E-value: 7.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE----QDLIVARLqqdppRN----VEGSVY-- 84
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDghdlADYTLASL-----RRqvalVSQDVVlf 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 85 -DFVAEGIeeqaeylkRYHDISRLVMndpseknlnelAKVQEQLDHHNLWQLENRInevlaQLGLDPNVAL--SSLSGGW 161
Cdd:TIGR02203 419 nDTIANNI--------AYGRTEQADR-----------AEIERALAAAYAQDFVDKL-----PLGLDTPIGEngVLLSGGQ 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287 162 LRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKtfNGTIIFISHDRSFIRNmATRIVDLDRGKLV 232
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALDNESerlvQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIV 546
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-501 |
8.14e-17 |
|
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: 84.07 E-value: 8.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 34 LVGRNGAGKSTLMKILNreqglddGRII-----YEqdlivarlqqDPPRnvegsvYDFVAE---GIEEQaEYLKR----- 100
Cdd:COG1245 104 ILGPNGIGKSTALKILS-------GELKpnlgdYD----------EEPS------WDEVLKrfrGTELQ-DYFKKlange 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 101 --------YHD-ISRLVMNDPSEknLneLAKVQEqldhhnlwqlENRINEVLAQLGLDP--NVALSSLSGGWLRKAALGR 169
Cdd:COG1245 160 ikvahkpqYVDlIPKVFKGTVRE--L--LEKVDE----------RGKLDELAEKLGLENilDRDISELSGGELQRVAIAA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 170 ALVSNPRVLLLDEPTNHLDI-------ETIDWLEGFLKTfngtIIFISHDRSFIRNMATRIVdldrgklVTY--PGNY-- 238
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLDIyqrlnvaRLIRELAEEGKY----VLVVEHDLAILDYLADYVH-------ILYgePGVYgv 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 239 -----------DQYL---LeKEEALRVeelqnaefdrklaqeevwirqgikaRRTRNEGRVRALkamrrergerrevmgt 304
Cdd:COG1245 295 vskpksvrvgiNQYLdgyL-PEENVRI-------------------------RDEPIEFEVHAP---------------- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 305 akmqveEASRSGKIVFEMEDVCYQVDGKQLVKDfSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHvgTKLEV 384
Cdd:COG1245 333 ------RREKEEETLVEYPDLTKSYGGFSLEVE-GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--EDLKI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 385 AYFDQhRAELDPDKTVMDNLAEgkqevmVNGKPrhvLG--YLQDFLFHP---KRAMT-PVRALSGGERNRLLLARLFLKP 458
Cdd:COG1245 404 SYKPQ-YISPDYDGTVEEFLRS------ANTDD---FGssYYKTEIIKPlglEKLLDkNVKDLSGGELQRVAIAACLSRD 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15830287 459 SNLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHDRQFVD 501
Cdd:COG1245 474 ADLYLLDEPSAHLDVEQRLAVAKAIrrfaENRGKTAMVVDHDIYLID 520
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
332-500 |
9.29e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.16 E-value: 9.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQhRAELDPD-----KTVMDNLAE 406
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ-KLYLDTTlpltvNRFLRLRPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 407 GKQEVMVNGKPRHVLGYLQDFlfhpkramtPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY 486
Cdd:PRK09544 96 TKKEDILPALKRVQAGHLIDA---------PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQL 166
|
170
....*....|....*...
gi 15830287 487 QGT----VLLVSHDRQFV 500
Cdd:PRK09544 167 RREldcaVLMVSHDLHLV 184
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-246 |
1.13e-16 |
|
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: 79.58 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE----QDLIVARLqqdppRN----VEGSVYDFvA 88
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghdvRDYTLASL-----RRqiglVSQDVFLF-N 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 89 EGIEEQAEYLKRyhdisrlvmnDPSEKNLNELAKVQEQldHHNLWQLENRINEVLAQLGldpnvalSSLSGGWLRKAALG 168
Cdd:cd03251 90 DTVAENIAYGRP----------GATREEVEEAARAANA--HEFIMELPEGYDTVIGERG-------VKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 169 RALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKtfNGTIIFISHDRSFIRNmATRIVDLDRGKLVTYpGNYDQyLLE 244
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESerlvQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVER-GTHEE-LLA 225
|
..
gi 15830287 245 KE 246
Cdd:cd03251 226 QG 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-226 |
1.22e-16 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 83.10 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSFSDA-PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLI----------VARL 71
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIaVNGVPLAdadadswrdqIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 72 QQDPprnveGSVYDFVAEGIeeqaeylkryhdisRLVMNDPSEknlnelAKVQEQLDHHNLWQLENRINEVLA-QLGLDP 150
Cdd:TIGR02857 402 PQHP-----FLFAGTIAENI--------------RLARPDASD------AEIREALERAGLDEFVAALPQGLDtPIGEGG 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287 151 nvalSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET-IDWLEGFLKTFNG-TIIFISHDRSFIRNmATRIVDL 226
Cdd:TIGR02857 457 ----AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETeAEVLEALRALAQGrTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-231 |
1.50e-16 |
|
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: 78.73 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlivarlqqdpprnVEGSV 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTII-----------------IDGLK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 84 YDFvaegieeqaeylkryhdisrlvmndpSEKNLNEL-AKVQEQLDHHNLWQ----LEN------------------RIN 140
Cdd:cd03262 64 LTD--------------------------DKKNINELrQKVGMVFQQFNLFPhltvLENitlapikvkgmskaeaeeRAL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 141 EVLAQLGLDP--NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISHDRSF 215
Cdd:cd03262 118 ELLEKVGLADkaDAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaeeGMTMVVVTHEMGF 197
|
250
....*....|....*.
gi 15830287 216 IRNMATRIVDLDRGKL 231
Cdd:cd03262 198 AREVADRVIFMDDGRI 213
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
320-495 |
1.81e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 77.19 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQV-DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQhraeldpdk 398
Cdd:cd03223 1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQ--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 399 tvmdnlaegkqevmvngKPRHVLGYLQDFLFHPKRamtpvRALSGGERNRLLLARLFL-KPSnLLILDEPTNDLDVETLE 477
Cdd:cd03223 72 -----------------RPYLPLGTLREQLIYPWD-----DVLSGGEQQRLAFARLLLhKPK-FVFLDEATSALDEESED 128
|
170
....*....|....*...
gi 15830287 478 LLEELIDSYQGTVLLVSH 495
Cdd:cd03223 129 RLYQLLKELGITVISVGH 146
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
320-498 |
1.98e-16 |
|
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: 78.76 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGtklEVAYFDQHRAELDPD-- 397
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEG---EVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 398 -----------------KTVMDNLAEGKQevmVNG-KPRHVLGYLqdflfhPKRAMTPV------------RALSGGERN 447
Cdd:cd03260 78 elrrrvgmvfqkpnpfpGSIYDNVAYGLR---LHGiKLKEELDER------VEEALRKAalwdevkdrlhaLGLSGGQQQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15830287 448 RLLLAR-LFLKPSNLLiLDEPTNDLDVETLELLEELIDSYQG--TVLLVSHDRQ 498
Cdd:cd03260 149 RLCLARaLANEPEVLL-LDEPTSALDPISTAKIEELIAELKKeyTIVIVTHNMQ 201
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-232 |
2.12e-16 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 78.88 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIvarlqqdpprnvegs 82
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 83 vydfvaegieeqaeylkryhdisrlvmnDPSEKNLNEL-AKV----QeqldHHNLWQ----LEN---------------- 137
Cdd:COG1126 66 ----------------------------TDSKKDINKLrRKVgmvfQ----QFNLFPhltvLENvtlapikvkkmskaea 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 138 --RINEVLAQLGLD------PnvalSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NG-TI 206
Cdd:COG1126 114 eeRAMELLERVGLAdkadayP----AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLakEGmTM 189
|
250 260
....*....|....*....|....*.
gi 15830287 207 IFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG1126 190 VVVTHEMGFAREVADRVVFMDGGRIV 215
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
338-496 |
2.54e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.82 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 338 FSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQAdSGRIHV-GTKLE---VAYFDQHRAEL---DPDKTVMD---NLAEG 407
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFaGQPLEawsAAELARHRAYLsqqQTPPFAMPvfqYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 408 KQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLK------P-SNLLILDEPTNDLDVETLELLE 480
Cdd:PRK03695 94 QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinPaGQLLLLDEPMNSLDVAQQAALD 173
|
170
....*....|....*....
gi 15830287 481 ELID--SYQG-TVLLVSHD 496
Cdd:PRK03695 174 RLLSelCQQGiAVVMSSHD 192
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-232 |
2.72e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 79.35 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSFSDAPL---------LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYeQDLIVARL 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGLsgkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW-RGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 72 QQdpprnvegsvydfvaegieEQAEYLKRyhDIsRLVMND-PSEKNLNEL--AKVQEQLDHhnLWQL-----ENRINEVL 143
Cdd:PRK10419 80 NR-------------------AQRKAFRR--DI-QMVFQDsISAVNPRKTvrEIIREPLRH--LLSLdkaerLARASEML 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 144 AQLGLDPNVA---LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFI 216
Cdd:PRK10419 136 RAVDLDDSVLdkrPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLV 215
|
250
....*....|....*.
gi 15830287 217 RNMATRIVDLDRGKLV 232
Cdd:PRK10419 216 ERFCQRVMVMDNGQIV 231
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-234 |
2.82e-16 |
|
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: 78.32 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLIVARLQQDPPRNVegsvydfvaeGIEEQaeyl 98
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN-GYSIRTDRKAARQSL----------GYCPQ---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 99 kryHDIsrlvmNDPsekNLN--ELAKVQEQLDHHNLWQLENRINEVLAQLGLDP--NVALSSLSGGWLRKAALGRALVSN 174
Cdd:cd03263 83 ---FDA-----LFD---ELTvrEHLRFYARLKGLPKSEIKEEVELLLRVLGLTDkaNKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 175 PRVLLLDEPTNHLDI-------ETIDWLEGflktfNGTIIFISHDRSFIRNMATRIVDLDRGKLVTY 234
Cdd:cd03263 152 PSVLLLDEPTSGLDPasrraiwDLILEVRK-----GRSIILTTHSMDEAEALCDRIAIMSDGKLRCI 213
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-229 |
4.26e-16 |
|
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: 77.86 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVE-------GSV------ 83
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQASPREILalrrrtiGYVsqflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 84 ------YDFVAEGIEEQAEylkryhdisrlvmnDPSEKnlneLAKVQEQLDHHN----LWQLenrinevlaqlgldpnvA 153
Cdd:COG4778 105 iprvsaLDVVAEPLLERGV--------------DREEA----RARARELLARLNlperLWDL-----------------P 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 154 LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGfLKTFNGTIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:COG4778 150 PATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEE-AKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
318-472 |
4.43e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 78.27 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 318 IVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTK-------LEVAyfdQH 390
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwspAELA---RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 RAELdPDKTVMdNLAEGKQEVMVNGKPRHVLGYLQDFLfHPKRAMTPV----------RALSGGERNRLLLARLFL---- 456
Cdd:PRK13548 78 RAVL-PQHSSL-SFPFTVEEVVAMGRAPHGLSRAEDDA-LVAAALAQVdlahlagrdyPQLSGGEQQRVQLARVLAqlwe 154
|
170
....*....|....*...
gi 15830287 457 --KPSNLLILDEPTNDLD 472
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALD 172
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
16-232 |
4.65e-16 |
|
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: 78.69 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 16 APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLIvarlQQDPprnvegsvydfvaegieEQ 94
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgQDLY----QLDR-----------------KQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 95 AEYLKRyhDISRLVMNDPSEKNLNELAK--VQEQLDHhnLWQL-----ENRINEVLAQLGLDPNVAL---SSLSGGWLRK 164
Cdd:TIGR02769 83 RRAFRR--DVQLVFQDSPSAVNPRMTVRqiIGEPLRH--LTSLdeseqKARIAELLDMVGLRSEDADklpRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 165 AALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
338-496 |
5.25e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.96 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 338 FSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQAdSGRIHV-GTKLE---VAYFDQHRAEL---DPDKTVMD-------N 403
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLnGRPLSdwsAAELARHRAYLsqqQSPPFAMPvfqylalH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 404 LAEGKQEVMVNGKPRHVLGYLQ--DFLfhpkraMTPVRALSGGERNRLLLARLFLK-------PSNLLILDEPTNDLDVE 474
Cdd:COG4138 94 QPAGASSEAVEQLLAQLAEALGleDKL------SRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVA 167
|
170 180
....*....|....*....|....*
gi 15830287 475 TLELLEELIDSY---QGTVLLVSHD 496
Cdd:COG4138 168 QQAALDRLLRELcqqGITVVMSSHD 192
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
321-472 |
7.42e-16 |
|
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: 77.27 E-value: 7.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVC--YQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAEL--- 394
Cdd:cd03251 2 EFKNVTfrYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDVRDYTLASLRRQIglv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 --DP---DKTVMDNLAEGK-----QEVMVNGKprhvLGYLQDFLFH-PKRAMTPV--RA--LSGGERNRLLLARLFLKPS 459
Cdd:cd03251 82 sqDVflfNDTVAENIAYGRpgatrEEVEEAAR----AANAHEFIMElPEGYDTVIgeRGvkLSGGQRQRIAIARALLKDP 157
|
170
....*....|...
gi 15830287 460 NLLILDEPTNDLD 472
Cdd:cd03251 158 PILILDEATSALD 170
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-245 |
8.88e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 80.59 E-value: 8.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFS---DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDL-------------IVarlQQ 73
Cdd:COG1132 345 VSFSypgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlIDGVDIrdltleslrrqigVV---PQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 74 DPPRnVEGSVYDFVAEGIEeqaeylkryhDISRlvmndpseknlnelAKVQEQLDHHNLW----QLENRINEVLAQLGld 149
Cdd:COG1132 422 DTFL-FSGTIRENIRYGRP----------DATD--------------EEVEEAAKAAQAHefieALPDGYDTVVGERG-- 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 150 pnvalSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKtfNGTIIFISHDRSFIRNmATRIVD 225
Cdd:COG1132 475 -----VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETealiQEALERLMK--GRTTIVIAHRLSTIRN-ADRILV 546
|
250 260
....*....|....*....|
gi 15830287 226 LDRGKLVTYpGNYDQyLLEK 245
Cdd:COG1132 547 LDDGRIVEQ-GTHEE-LLAR 564
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
321-503 |
9.77e-16 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 76.29 E-value: 9.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQL-VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKL------EVAYFDQHRA 392
Cdd:cd03292 2 EFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVsdlrgrAIPYLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 393 ------ELDPDKTVMDNLAEGKQEVMVNGK--PRHVLGYLQDF-LFHPKRAMTpvRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:cd03292 82 vvfqdfRLLPDRNVYENVAFALEVTGVPPReiRKRVPAALELVgLSHKHRALP--AELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15830287 464 LDEPTNDLDVETLELLEELIDSYQ---GTVLLVSHDRQFVDNT 503
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDTT 202
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
321-473 |
1.53e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 76.69 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG-------TKLEVAyfdQHRAE 393
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgrplaawSPWELA---RRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 394 LdPDKTVMdNLAEGKQEVMVNGKPRHVLGYLQDfLFHPKRAMTPV----------RALSGGERNRLLLARLFL------- 456
Cdd:COG4559 80 L-PQHSSL-AFPFTVEEVVALGRAPHGSSAAQD-RQIVREALALVglahlagrsyQTLSGGEQQRVQLARVLAqlwepvd 156
|
170
....*....|....*..
gi 15830287 457 KPSNLLILDEPTNDLDV 473
Cdd:COG4559 157 GGPRWLFLDEPTSALDL 173
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
15-232 |
1.59e-15 |
|
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: 75.93 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIIYE-QDLIVARLQQdppRNVEGSVYdfVAEG 90
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTI---MGLlppRSGSIRFDgRDITGLPPHE---RARAGIGY--VPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 91 ieeqaeylkryhdisRLVMNDPS-EKNL------NELAKVQEQLDHhnLWQLENRINEVLAQLGldpnvalSSLSGGWLR 163
Cdd:cd03224 84 ---------------RRIFPELTvEENLllgayaRRRAKRKARLER--VYELFPRLKERRKQLA-------GTLSGGEQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 164 KAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03224 140 MLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDegvTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
321-495 |
1.66e-15 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 76.50 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVD-GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQHRAELD 395
Cdd:cd03253 2 EFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdiREVTLDSLRRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 396 PD-----KTVMDNLAEGK-----QEVMVNGKPRHVLGYLQDFlfhPKRAMTPV--RA--LSGGERNRLLLARLFLKPSNL 461
Cdd:cd03253 82 QDtvlfnDTIGYNIRYGRpdatdEEVIEAAKAAQIHDKIMRF---PDGYDTIVgeRGlkLSGGEKQRVAIARAILKNPPI 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 15830287 462 LILDEPTNDLDVETLELLEELIDSYQG--TVLLVSH 495
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKgrTTIVIAH 194
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
324-496 |
1.87e-15 |
|
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: 75.79 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 324 DVCYQVDGKQlvKDFSAQV---LRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG---------------TKLEVA 385
Cdd:cd03297 1 MLCVDIEKRL--PDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsrkkinlppQQRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 386 YFDQHRAeLDPDKTVMDNLAEGKQEVMVNGK---PRHVLGYLQdfLFHPKRAmtPVRALSGGERNRLLLARLFLKPSNLL 462
Cdd:cd03297 79 LVFQQYA-LFPHLNVRENLAFGLKRKRNREDrisVDELLDLLG--LDHLLNR--YPAQLSGGEKQRVALARALAAQPELL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 15830287 463 ILDEPTNDLDVETLELLEELIDS----YQGTVLLVSHD 496
Cdd:cd03297 154 LLDEPFSALDRALRLQLLPELKQikknLNIPVIFVTHD 191
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
316-472 |
1.91e-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: 79.76 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 316 GKIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAEL 394
Cdd:TIGR02203 329 GDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLdGHDLADYTLASLRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 DP--------DKTVMDNLAEGKQEVMVNGKPRHVL--GYLQDFLFH-PKRAMTPVRA----LSGGERNRLLLARLFLKPS 459
Cdd:TIGR02203 409 ALvsqdvvlfNDTIANNIAYGRTEQADRAEIERALaaAYAQDFVDKlPLGLDTPIGEngvlLSGGQRQRLAIARALLKDA 488
|
170
....*....|...
gi 15830287 460 NLLILDEPTNDLD 472
Cdd:TIGR02203 489 PILILDEATSALD 501
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
317-472 |
2.11e-15 |
|
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: 74.89 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 317 KIVFEMEDVCYQVDG------KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQL--QADSGrihvgtklevayfd 388
Cdd:cd03213 1 GVTLSFRNLTVTVKSspsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 389 qhraeldpdktvmdnlaegkqEVMVNGKPRH------VLGY-LQDFLFHPKraMTP---------VRALSGGERNRLLLA 452
Cdd:cd03213 67 ---------------------EVLINGRPLDkrsfrkIIGYvPQDDILHPT--LTVretlmfaakLRGLSGGERKRVSIA 123
|
170 180
....*....|....*....|.
gi 15830287 453 R-LFLKPSnLLILDEPTNDLD 472
Cdd:cd03213 124 LeLVSNPS-LLFLDEPTSGLD 143
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-237 |
3.53e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 77.38 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGLDDgriIYEQDLIVA--RLQQDPP-- 76
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMI---AGLED---ITSGDLFIGekRMNDVPPae 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 77 RNVeGSVYdfvaegiEEQAEY--LKRYHDIS---RLVMNDPSE--KNLNELAKVQeQLDHhnlwQLENRinevlaqlgld 149
Cdd:PRK11000 75 RGV-GMVF-------QSYALYphLSVAENMSfglKLAGAKKEEinQRVNQVAEVL-QLAH----LLDRK----------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 150 PNvalsSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD--------IEtIDWLEgflKTFNGTIIFISHDRSFIRNMAT 221
Cdd:PRK11000 131 PK----ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqmrIE-ISRLH---KRLGRTMIYVTHDQVEAMTLAD 202
|
250 260
....*....|....*....|....*
gi 15830287 222 RIVDLDRGK---------LVTYPGN 237
Cdd:PRK11000 203 KIVVLDAGRvaqvgkpleLYHYPAN 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
319-473 |
3.60e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.53 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-------HVGTKLEVAYFDQHR 391
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIkldggdiDDPDVAEACHYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 392 AELDPDKTVMDNLaEGKQEVMvNGKPRHVLGYLQDF----LFHpkramTPVRALSGGERNRLLLARLFLKPSNLLILDEP 467
Cdd:PRK13539 82 NAMKPALTVAENL-EFWAAFL-GGEELDIAAALEAVglapLAH-----LPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
....*.
gi 15830287 468 TNDLDV 473
Cdd:PRK13539 155 TAALDA 160
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-234 |
5.12e-15 |
|
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: 74.24 E-value: 5.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlivarlqqdpprnVEGSV 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVL-----------------FDGKP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 84 YDFVAegieeqaeylkrYHDISRLvmndPSEKNLNELAKVQEQLDHhnLWQLEN--------RINEVLAQLGLDP--NVA 153
Cdd:cd03269 64 LDIAA------------RNRIGYL----PEERGLYPKMKVIDQLVY--LAQLKGlkkeearrRIDEWLERLELSEyaNKR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 154 LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGF---LKTFNGTIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd03269 126 VEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVireLARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
....
gi 15830287 231 LVTY 234
Cdd:cd03269 206 AVLY 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
321-497 |
5.70e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 76.68 E-value: 5.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLE-----VAYFDQHR 391
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvTGLPpekrnVGMVFQDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 392 AeLDPDKTVMDNLAEG-------KQEV---------MVNgkprhvlgyLQDFLfhpKRAmtpVRALSGGERNRLLLAR-L 454
Cdd:COG3842 87 A-LFPHLTVAENVAFGlrmrgvpKAEIrarvaelleLVG---------LEGLA---DRY---PHQLSGGQQQRVALARaL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15830287 455 FLKPSnLLILDEPTNDLDVETLELLEELIDSYQ----GTVLLVSHDR 497
Cdd:COG3842 151 APEPR-VLLLDEPLSALDAKLREEMREELRRLQrelgITFIYVTHDQ 196
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
335-496 |
5.84e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 76.28 E-value: 5.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAY-------FDQhRAELDPDKTVMDN 403
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLgyvpFKRRKEFarrigvvFGQ-RSQLWWDLPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 404 L-----------AEGKQ--EVMVNgkprhVLGyLQDFLfhpkraMTPVRALSGGERNRL-LLARLFLKPSnLLILDEPTN 469
Cdd:COG4586 117 FrllkaiyripdAEYKKrlDELVE-----LLD-LGELL------DTPVRQLSLGQRMRCeLAAALLHRPK-ILFLDEPTI 183
|
170 180 190
....*....|....*....|....*....|.
gi 15830287 470 DLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:COG4586 184 GLDVVSKEAIREFLkeynRERGTTILLTSHD 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
323-497 |
6.43e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 76.34 E-value: 6.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 323 EDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTklEVAYFD------------QH 390
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG--RDLFTNlpprerrvgfvfQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 RAeLDPDKTVMDNLAEGKQevmVNGKPRH-----VLGYLQdfLFH--------PKRamtpvraLSGGERNRLLLAR-LFL 456
Cdd:COG1118 84 YA-LFPHMTVAENIAFGLR---VRPPSKAeirarVEELLE--LVQlegladryPSQ-------LSGGQRQRVALARaLAV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15830287 457 KPSnLLILDEPTNDLDVETLELL----EELIDSYQGTVLLVSHDR 497
Cdd:COG1118 151 EPE-VLLLDEPFGALDAKVRKELrrwlRRLHDELGGTTVFVTHDQ 194
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
321-496 |
6.78e-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: 74.33 E-value: 6.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV----------GTKLEVAYFDQH 390
Cdd:cd03265 2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghdvvreprEVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 RAeLDPDKTVMDNLA-EGKQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTN 469
Cdd:cd03265 82 LS-VDDELTGWENLYiHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190
....*....|....*....|....*....|.
gi 15830287 470 DLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:cd03265 161 GLDPQTRAHVWEYIeklkEEFGMTILLTTHY 191
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
323-496 |
7.09e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.41 E-value: 7.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 323 EDVCYQVDGKQLvkDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVA------YFDQHra 392
Cdd:COG3840 5 DDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgqdlTALPPAerpvsmLFQEN-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 393 ELDPDKTVMDNLAEG-----------KQEVM-----VNgkprhvLGYLQDFLfhpkramtPvRALSGGERNRLLLARLFL 456
Cdd:COG3840 81 NLFPHLTVAQNIGLGlrpglkltaeqRAQVEqalerVG------LAGLLDRL--------P-GQLSGGQRQRVALARCLV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15830287 457 KPSNLLILDEPTNDLDVETLELLEELID----SYQGTVLLVSHD 496
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDelcrERGLTVLMVTHD 189
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-250 |
8.96e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.84 E-value: 8.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFS-----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNR------EQGLDDGRII--YEQDLI---VARLQQDP 75
Cdd:TIGR00958 485 SFSypnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNlyqptgGQVLLDGVPLvqYDHHYLhrqVALVGQEP 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 76 PRnVEGSVYDFVAEGieeqaeyLKRYHDisRLVMndpseknlnelAKVQEQLDHHNLWQLENRINEVLAQLGldpnvalS 155
Cdd:TIGR00958 565 VL-FSGSVRENIAYG-------LTDTPD--EEIM-----------AAAKAANAHDFIMEFPNGYDTEVGEKG-------S 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 156 SLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIEtIDWLEGFLKTFNG-TIIFISHDRSFIRNmATRIVDLDRGKLVTY 234
Cdd:TIGR00958 617 QLSGGQKQRIAIARALVRKPRVLILDEATSALDAE-CEQLLQESRSRASrTVLLIAHRLSTVER-ADQILVLKKGSVVEM 694
|
250
....*....|....*.
gi 15830287 235 pGNYDQyLLEKEEALR 250
Cdd:TIGR00958 695 -GTHKQ-LMEDQGCYK 708
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
19-232 |
8.99e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 75.88 E-value: 8.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIY---------EQDLIVAR------------LQQdppR 77
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVdgvdltalsERELRAARrkigmifqhfnlLSS---R 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 78 NVegsvYDFVAegieeqaeylkryhdisrLVMndpseknlnELAKVQEQldhhnlwQLENRINEVLAQLGLDP--NVALS 155
Cdd:COG1135 98 TV----AENVA------------------LPL---------EIAGVPKA-------EIRKRVAELLELVGLSDkaDAYPS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 156 SLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET---IdwLEgFLKTFNG----TIIFISHDRSFIRNMATRIVDLDR 228
Cdd:COG1135 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtrsI--LD-LLKDINRelglTIVLITHEMDVVRRICDRVAVLEN 216
|
....
gi 15830287 229 GKLV 232
Cdd:COG1135 217 GRIV 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-495 |
9.60e-15 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 72.08 E-value: 9.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHvgtklevayfdqhraeldpdkt 399
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 400 vmdnlaegkqevmVNGKPRHVLGylqdflfhPKRAM----TPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03216 59 -------------VDGKEVSFAS--------PRDARragiAMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAE 117
|
170 180
....*....|....*....|...
gi 15830287 476 LELLEELIDSY--QG-TVLLVSH 495
Cdd:cd03216 118 VERLFKVIRRLraQGvAVIFISH 140
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-232 |
1.17e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 74.70 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYEQ-DLIVARLQQDPPRNVEGSV-----YDFVAE 89
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLN---GLlkpTSGKIIIDGvDITDKKVKLSDIRKKVGLVfqypeYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 90 GIEEQAEYlkryhdisrlvmnDPSEKNLNELakvqeqldhhnlwQLENRINEVLAQLGLDPNVALS----SLSGGWLRKA 165
Cdd:PRK13637 100 TIEKDIAF-------------GPINLGLSEE-------------EIENRVKRAMNIVGLDYEDYKDkspfELSGGQKRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 166 ALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKT----FNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKElhkeYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
332-495 |
1.19e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 73.08 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-------GTKLEVAYFDQHRAeLDPDKTVMDNL 404
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgkpldiAARNRIGYLPEERG-LYPKMKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 405 ---AE----GKQEVMvngkpRHVLGYLQDFLFHPKRAmTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLE 477
Cdd:cd03269 92 vylAQlkglKKEEAR-----RRIDEWLERLELSEYAN-KRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVE 165
|
170 180
....*....|....*....|.
gi 15830287 478 LLEELIDSYQG---TVLLVSH 495
Cdd:cd03269 166 LLKDVIRELARagkTVILSTH 186
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-248 |
1.39e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.98 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE----QDLIVARLqqdppRN----VEGSVY-- 84
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDghdlRDYTLASL-----RNqvalVSQNVHlf 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 85 -DFVAEGIEEQAEylKRYhdisrlvmndpSEKNLNELAKVQEQLDHHNlwQLENRINEVLAQLGLdpnvalsSLSGGWLR 163
Cdd:PRK11176 430 nDTIANNIAYART--EQY-----------SREQIEEAARMAYAMDFIN--KMDNGLDTVIGENGV-------LLSGGQRQ 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 164 KAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NGTIIFISHDRSFIRNmATRIVDLDRGKLVTYpGNYDQy 241
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELqkNRTSLVIAHRLSTIEK-ADEILVVEDGEIVER-GTHAE- 564
|
....*..
gi 15830287 242 LLEKEEA 248
Cdd:PRK11176 565 LLAQNGV 571
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-232 |
1.41e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 73.96 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDL----------IVARLQ 72
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVlVDGLDVattpsrelakRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 73 QDPPRNVEGSVYDFVAEGieeqaeylkRY-HDISRLVMNDpseknlneLAKVQEQLDHHNLWQLENRInevlaqlgldpn 151
Cdd:COG4604 82 QENHINSRLTVRELVAFG---------RFpYSKGRLTAED--------REIIDEAIAYLDLEDLADRY------------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 152 vaLSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLD 227
Cdd:COG4604 133 --LDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMK 210
|
....*
gi 15830287 228 RGKLV 232
Cdd:COG4604 211 DGRVV 215
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
11-245 |
1.45e-14 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 77.09 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFS---DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL----NREQG--LDDGRIIYEQDLIVAR-----LQQDPp 76
Cdd:TIGR01193 479 VSYSygyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLvgffQARSGeiLLNGFSLKDIDRHTLRqfinyLPQEP- 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 77 RNVEGSVYDFVAEGIEEQAEYlkryHDISRLVmndpseknlnELAKVQEQLDHhnlwqlenrinevlAQLGLDPNVAL-- 154
Cdd:TIGR01193 558 YIFSGSILENLLLGAKENVSQ----DEIWAAC----------EIAEIKDDIEN--------------MPLGYQTELSEeg 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 155 SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET---IdwLEGFLKTFNGTIIFISHdRSFIRNMATRIVDLDRGKL 231
Cdd:TIGR01193 610 SSISGGQKQRIALARALLTDSKVLILDESTSNLDTITekkI--VNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKI 686
|
250
....*....|....
gi 15830287 232 VTyPGNYDQYLLEK 245
Cdd:TIGR01193 687 IE-QGSHDELLDRN 699
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
321-473 |
1.60e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQHRAELDP 396
Cdd:PRK09536 5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvEALSARAASRRVASVPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 397 DKTVMDNLaEGKQEVMVNGKPrhvlgYLQDFLFHP-------KRAMT----------PVRALSGGERNRLLLARLFLKPS 459
Cdd:PRK09536 85 DTSLSFEF-DVRQVVEMGRTP-----HRSRFDTWTetdraavERAMErtgvaqfadrPVTSLSGGERQRVLLARALAQAT 158
|
170
....*....|....
gi 15830287 460 NLLILDEPTNDLDV 473
Cdd:PRK09536 159 PVLLLDEPTASLDI 172
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
34-232 |
1.65e-14 |
|
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: 73.70 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 34 LVGRNGAGKSTLMKILNREQGLDDGRIIY-----------EQDLIVARLQQDPPRNVEGSVYDFVAEGieeqaeylkryh 102
Cdd:TIGR03873 32 LLGPNGSGKSTLLRLLAGALRPDAGTVDLagvdlhglsrrARARRVALVEQDSDTAVPLTVRDVVALG------------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 103 disrlvmndpseknlnelakvqeQLDHHNLWQLENR-----INEVLAQLGLD--PNVALSSLSGGWLRKAALGRALVSNP 175
Cdd:TIGR03873 100 -----------------------RIPHRSLWAGDSPhdaavVDRALARTELShlADRDMSTLSGGERQRVHVARALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 176 RVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:TIGR03873 157 KLLLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHDLNLAASYCDHVVVLDGGRVV 216
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-223 |
1.71e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 74.77 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLIVA----------RLQ---QDP-----PRNv 79
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgQDITGLsgrelrplrrRMQmvfQDPyaslnPRM- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 80 egSVYDFVAEGIEeqaeylkryhdisrlvmndpseknLNELAKVQEQLDhhnlwqlenRINEVLAQLGLDPNVALS---S 156
Cdd:COG4608 113 --TVGDIIAEPLR------------------------IHGLASKAERRE---------RVAELLELVGLRPEHADRyphE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 157 LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRI 223
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDVsiqaQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRV 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-258 |
1.73e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 73.59 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGriiyeqDLIVARLQQDPPRNVE-------GSVY 84
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSG------DLIVDGLKVNDPKVDErlirqeaGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 85 dfvaegieeQAEYLkrYHDISRL--VMNDP------SEKNLNELAKvqeqldhhnlwqlenrinEVLAQLGLDP--NVAL 154
Cdd:PRK09493 84 ---------QQFYL--FPHLTALenVMFGPlrvrgaSKEEAEKQAR------------------ELLAKVGLAEraHHYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 155 SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NG-TIIFISHDRSFIRNMATRIVDLDRGKl 231
Cdd:PRK09493 135 SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLaeEGmTMVIVTHEIGFAEKVASRLIFIDKGR- 213
|
250 260
....*....|....*....|....*...
gi 15830287 232 VTYPGNYDQyLLEKEEALRVEE-LQNAE 258
Cdd:PRK09493 214 IAEDGDPQV-LIKNPPSQRLQEfLQHVS 240
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
315-497 |
1.74e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 76.54 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 315 SGKIVFEmeDVCYQVDGK-QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEvayfDQHRA 392
Cdd:PRK13657 332 KGAVEFD--DVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTDIR----TVTRA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 393 EL---------DP---DKTVMDNLAEGK-----QEVMVNGKPRHVLgylqDFLF-HPKRAMTPV----RALSGGERNRLL 450
Cdd:PRK13657 406 SLrrniavvfqDAglfNRSIEDNIRVGRpdatdEEMRAAAERAQAH----DFIErKPDGYDTVVgergRQLSGGERQRLA 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15830287 451 LARLFLKPSNLLILDEPTNDLDVETLELLEELIDSyqgtvllVSHDR 497
Cdd:PRK13657 482 IARALLKDPPILILDEATSALDVETEAKVKAALDE-------LMKGR 521
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
321-498 |
1.79e-14 |
|
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: 73.04 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFD----------QH 390
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK-DITNLPphkrpvntvfQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 RAeLDPDKTVMDNLAEG-----------KQEVMVNGKPRHVLGYLQDFlfhpkramtpVRALSGGERNRLLLAR-LFLKP 458
Cdd:cd03300 81 YA-LFPHLTVFENIAFGlrlkklpkaeiKERVAEALDLVQLEGYANRK----------PSQLSGGQQQRVAIARaLVNEP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15830287 459 SnLLILDEPTNDLDVETLELLEELIDSYQG----TVLLVSHDRQ 498
Cdd:cd03300 150 K-VLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQE 192
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
321-473 |
2.12e-14 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 76.70 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVD-GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLeVAYFDQH--RAEL--- 394
Cdd:TIGR01193 475 VINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS-LKDIDRHtlRQFInyl 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 --DP---DKTVMDNLAEGKQEVMVNGKPRHV--------------LGYLQDFLFHPKramtpvrALSGGERNRLLLARLF 455
Cdd:TIGR01193 554 pqEPyifSGSILENLLLGAKENVSQDEIWAAceiaeikddienmpLGYQTELSEEGS-------SISGGQKQRIALARAL 626
|
170
....*....|....*...
gi 15830287 456 LKPSNLLILDEPTNDLDV 473
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDT 644
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-234 |
2.25e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 73.12 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSlISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlivarlqqdpprNVE 80
Cdd:COG4161 1 MS-IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL-----------------NIA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 81 GSVYDFVAEGIEEQAEYLKR--------YHDISRL-VMNDPSEKNLNELAKVQEQLdhhnlwqlENRINEVLAQLGLDP- 150
Cdd:COG4161 63 GHQFDFSQKPSEKAIRLLRQkvgmvfqqYNLWPHLtVMENLIEAPCKVLGLSKEQA--------REKAMKLLARLRLTDk 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 151 -NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTII---FISHDRSFIRNMATRIVDL 226
Cdd:COG4161 135 aDRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGItqvIVTHEVEFARKVASQVVYM 214
|
....*...
gi 15830287 227 DRGKLVTY 234
Cdd:COG4161 215 EKGRIIEQ 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
157-500 |
2.30e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.90 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 157 LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVsvqaQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 233 ------------TYPgnYDQYLLEKEEA-------------LRVEELQNAeFDrklaqeevwIRQGIKARRtrnegrvra 287
Cdd:PRK15134 237 eqnraatlfsapTHP--YTQKLLNSEPSgdpvplpepasplLDVEQLQVA-FP---------IRKGILKRT--------- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 288 lkamrrergerrevmgtakmqveeasrsgkivfemedvcyqVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTT----LLK 363
Cdd:PRK15134 296 -----------------------------------------VDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLR 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 364 LML--GQLQADSGRIH---------VGTKLEVAYFDQHRAeLDPDKTVMDNLAEGKQ--EVMVNGKPR--HVLGYLQDFL 428
Cdd:PRK15134 335 LINsqGEIWFDGQPLHnlnrrqllpVRHRIQVVFQDPNSS-LNPRLNVLQIIEEGLRvhQPTLSAAQReqQVIAVMEEVG 413
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287 429 FHPK-RAMTPVrALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLELLEELIDSYQGT----VLLVSHDRQFV 500
Cdd:PRK15134 414 LDPEtRHRYPA-EFSGGQRQRIAIARaLILKPS-LIILDEPTSSLDKTVQAQILALLKSLQQKhqlaYLFISHDLHVV 489
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-473 |
2.32e-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: 76.02 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN--REQGLDDGRIIYEQDLIVARlqqdpprnve 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSgvYPHGTWDGEIYWSGSPLKAS---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 81 gSVYDFVAEGIEEQAEYLKRYHDISRLvmndpseKNL---NELAKVQEQLDHHNLWQlenRINEVLAQLGLDP-NVAL-- 154
Cdd:TIGR02633 71 -NIRDTERAGIVIIHQELTLVPELSVA-------ENIflgNEITLPGGRMAYNAMYL---RAKNLLRELQLDAdNVTRpv 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 155 SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGF---LKTFNGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:TIGR02633 140 GDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIirdLKAHGVACVYISHKLNEVKAVCDTICVIRDGQH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 232 VTypgnydqyllekeealrVEELQNAEFDRKLAQeevwirqgIKARRTRNegrvralkamrrergerrevmgtakMQVEE 311
Cdd:TIGR02633 220 VA-----------------TKDMSTMSEDDIITM--------MVGREITS-------------------------LYPHE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 312 ASRSGKIVFEMEDV-CYQVDGKQL--VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLG---------------QLQADS 373
Cdd:TIGR02633 250 PHEIGDVILEARNLtCWDVINPHRkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaypgkfegnvfingkPVDIRN 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 374 GRIHVGTKLEVAYFDQHRAELDPDKTVMDNL---------------AEGKQEVMVNGKPRhvlgyLQDFLFHPkraMTPV 438
Cdd:TIGR02633 330 PAQAIRAGIAMVPEDRKRHGIVPILGVGKNItlsvlksfcfkmridAAAELQIIGSAIQR-----LKVKTASP---FLPI 401
|
490 500 510
....*....|....*....|....*....|....*
gi 15830287 439 RALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-246 |
2.66e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.02 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFS----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIvARLQQDPPRN----VEGS 82
Cdd:PRK11160 344 VSFTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI-ADYSEAALRQaisvVSQR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 83 VYDFVAEgieeqaeyLKryhdiSRLVMNDPsEKNLNELAKVQEQLDHHNLWQLENRINEVLAQLGldpnvalSSLSGGWL 162
Cdd:PRK11160 423 VHLFSAT--------LR-----DNLLLAAP-NASDEALIEVLQQVGLEKLLEDDKGLNAWLGEGG-------RQLSGGEQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 163 RKAALGRALVSNPRVLLLDEPTNHLDIET---IdwLEGFLKTFNG-TIIFISHDRSFIRNMaTRIVDLDRGKLVTYpGNY 238
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETerqI--LELLAEHAQNkTVLMITHRLTGLEQF-DRICVMDNGQIIEQ-GTH 557
|
....*...
gi 15830287 239 DQyLLEKE 246
Cdd:PRK11160 558 QE-LLAQQ 564
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-232 |
2.88e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 72.75 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLddgriiyeqdlivarLQqdpPRNVEGSVYDFVAegIE 92
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILS---GL---------------LQ---PTSGEVRVAGLVP--WK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 93 EQAEYLKRyhdISrLVMNDPSEKNLNeLAKVQEQLDHHNLWQLE-----NRINEVLAQLGLDP--NVALSSLSGGWLRKA 165
Cdd:cd03267 88 RRKKFLRR---IG-VVFGQKTQLWWD-LPVIDSFYLLAAIYDLPparfkKRLDELSELLDLEEllDTPVRQLSLGQRMRA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 166 ALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFN----GTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNrergTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-232 |
3.51e-14 |
|
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: 72.02 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLIVARLQQDPPRN---VEGS--VYDFVAegIEE 93
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVD-GFDVVKEPAEARRRlgfVSDStgLYDRLT--ARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 94 QAEYLKRYHDISRLvmndpseknlnelakvqeqldhhnlwQLENRINEVLAQLGLDP--NVALSSLSGGWLRKAALGRAL 171
Cdd:cd03266 98 NLEYFAGLYGLKGD--------------------------ELTARLEELADRLGMEEllDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 172 VSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
335-500 |
3.86e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.42 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTK----LEVAyfdqhrAELDPDKTVMDNlaegkqe 410
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsalLELG------AGFHPELTGREN------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 411 VMVNGkprHVLGY-----------------LQDFLfhpkraMTPVRALSGGERNRLLLA-RLFLKPsNLLILDEPTNDLD 472
Cdd:COG1134 109 IYLNG---RLLGLsrkeidekfdeivefaeLGDFI------DQPVKTYSSGMRARLAFAvATAVDP-DILLVDEVLAVGD 178
|
170 180 190
....*....|....*....|....*....|.
gi 15830287 473 VETLELLEELIDSYQ---GTVLLVSHDRQFV 500
Cdd:COG1134 179 AAFQKKCLARIRELResgRTVIFVSHSMGAV 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
330-472 |
3.93e-14 |
|
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: 72.22 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQHRAE---------LDP 396
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdiNKLKGKALRQLRRQigmifqqfnLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 397 DKTVMDNLAEGKqevmvngkprhvLGYLQDF-----LFHP----------------KRAMTPVRALSGGERNRLLLARLF 455
Cdd:cd03256 92 RLSVLENVLSGR------------LGRRSTWrslfgLFPKeekqralaalervgllDKAYQRADQLSGGQQQRVAIARAL 159
|
170
....*....|....*..
gi 15830287 456 LKPSNLLILDEPTNDLD 472
Cdd:cd03256 160 MQQPKLILADEPVASLD 176
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
321-472 |
5.74e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 73.57 E-value: 5.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLE-----VAY-FdQH 390
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGgrdvTDLPpkdrnIAMvF-QS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 RAeLDPDKTVMDNLAEG-------KQEvmVNGKPRHVLGYLQ--DFLfhpKRamtPVRALSGGERNRLLLARLFLKPSNL 461
Cdd:COG3839 84 YA-LYPHMTVYENIAFPlklrkvpKAE--IDRRVREAAELLGleDLL---DR---KPKQLSGGQRQRVALGRALVREPKV 154
|
170
....*....|.
gi 15830287 462 LILDEPTNDLD 472
Cdd:COG3839 155 FLLDEPLSNLD 165
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
321-472 |
6.41e-14 |
|
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: 71.60 E-value: 6.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTK---------LEVAYFDQHR 391
Cdd:cd03296 4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqeRNVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 392 AeLDPDKTVMDNLAEG---------KQEVMVNGKPRHVLGYLQ-DFLF--HPKRamtpvraLSGGERNRLLLARLFLKPS 459
Cdd:cd03296 84 A-LFRHMTVFDNVAFGlrvkprserPPEAEIRAKVHELLKLVQlDWLAdrYPAQ-------LSGGQRQRVALARALAVEP 155
|
170
....*....|...
gi 15830287 460 NLLILDEPTNDLD 472
Cdd:cd03296 156 KVLLLDEPFGALD 168
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
320-516 |
6.60e-14 |
|
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: 71.02 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKL------------EVAY 386
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdGLKLtddkkninelrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 387 FDQHrAELDPDKTVMDNLAEGkqEVMVNGKPR-----HVLGYLQDFLFHPKRAMTPvRALSGGERNRLLLAR-LFLKPSn 460
Cdd:cd03262 81 VFQQ-FNLFPHLTVLENITLA--PIKVKGMSKaeaeeRALELLEKVGLADKADAYP-AQLSGGQQQRVAIARaLAMNPK- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 461 LLILDEPTNDLD---VETLELLEELIDSYQGTVLLVSHDRQFVDNtVTECWIFEGGGKI 516
Cdd:cd03262 156 VMLFDEPTSALDpelVGEVLDVMKDLAEEGMTMVVVTHEMGFARE-VADRVIFMDDGRI 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-232 |
6.95e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 74.72 E-value: 6.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMK-ILnreqGLDD--GRIIYE-QDL----------IVARLQ---QDP-----P 76
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLaLL----RLIPseGEIRFDgQDLdglsrralrpLRRRMQvvfQDPfgslsP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 77 RNvegSVYDFVAEGIeeqaeylkRYHDIsrlvmnDPSEKnlnelakvqeqldhhnlwQLENRINEVLAQLGLDPNVAL-- 154
Cdd:COG4172 378 RM---TVGQIIAEGL--------RVHGP------GLSAA------------------ERRARVAEALEEVGLDPAARHry 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 155 -SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:COG4172 423 pHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVsvqaQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDG 502
|
...
gi 15830287 230 KLV 232
Cdd:COG4172 503 KVV 505
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-232 |
7.21e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 71.58 E-value: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSlISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlivarlqqdpprNVE 80
Cdd:PRK11124 1 MS-IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL-----------------NIA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 81 GSVYDFVAEgieeqaeylkryhdisrlvmndPSEKNLNEL-AKVQEQLDHHNLWQ----LENRINEVLAQLGLDPNVALS 155
Cdd:PRK11124 63 GNHFDFSKT----------------------PSDKAIRELrRNVGMVFQQYNLWPhltvQQNLIEAPCRVLGLSKDQALA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 156 S--------------------LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTII---FISHD 212
Cdd:PRK11124 121 RaekllerlrlkpyadrfplhLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHE 200
|
250 260
....*....|....*....|
gi 15830287 213 RSFIRNMATRIVDLDRGKLV 232
Cdd:PRK11124 201 VEVARKTASRVVYMENGHIV 220
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
344-512 |
7.31e-14 |
|
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: 71.67 E-value: 7.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 344 RGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvGTKLE-VAYFDQHrAELDPDKTVMDNLAEG----------KQEVM 412
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--EIELDtVSYKPQY-IKADYEGTVRDLLSSItkdfythpyfKTEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 413 vngKPRHVLGYLQdflfhpkramTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY----QG 488
Cdd:cd03237 101 ---KPLQIEQILD----------REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEK 167
|
170 180
....*....|....*....|....
gi 15830287 489 TVLLVSHDRQFVDNTVTECWIFEG 512
Cdd:cd03237 168 TAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-247 |
7.55e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.00 E-value: 7.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 10 WLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI------------IYEQDLIVARLQ----- 72
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIkvdgkvlyfgkdIFQIDAIKLRKEvgmvf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 73 QDPPRNVEGSVYDFVAegieeqaeYLKRYHDIsrlvmndpseKNLNELAK-VQEQLDHHNLWQlenrinEVLAQLgldpN 151
Cdd:PRK14246 97 QQPNPFPHLSIYDNIA--------YPLKSHGI----------KEKREIKKiVEECLRKVGLWK------EVYDRL----N 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 152 VALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG--TIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:PRK14246 149 SPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNG 228
|
250
....*....|....*...
gi 15830287 230 KLVTYPGNYDQYLLEKEE 247
Cdd:PRK14246 229 ELVEWGSSNEIFTSPKNE 246
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
322-496 |
8.88e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.63 E-value: 8.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 322 MEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHR-----AELDP 396
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRlmfqdARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 397 DKTVMDNLAEGkqevmVNGKPR-------HVLGyLQDflfhpkRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTN 469
Cdd:PRK11247 95 WKKVIDNVGLG-----LKGQWRdaalqalAAVG-LAD------RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190
....*....|....*....|....*....|.
gi 15830287 470 DLDVETLELLEELIDS----YQGTVLLVSHD 496
Cdd:PRK11247 163 ALDALTRIEMQDLIESlwqqHGFTVLLVTHD 193
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-212 |
8.95e-14 |
|
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: 74.32 E-value: 8.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFS---DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLIVARLQQDPPRNVEGsvydFV 87
Cdd:TIGR02868 340 LSAGypgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD-GVPVSSLDQDEVRRRVS----VC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 88 AEgieeqaeylkRYH-------DISRLVMNDPSEKnlnELAKVQEQLDHHNLWQ-LENRINEVLAQLGldpnvalSSLSG 159
Cdd:TIGR02868 415 AQ----------DAHlfdttvrENLRLARPDATDE---ELWAALERVGLADWLRaLPDGLDTVLGEGG-------ARLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15830287 160 GWLRKAALGRALVSNPRVLLLDEPTNHLDIETID-WLEGFLKTFNG-TIIFISHD 212
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADeLLEDLLAALSGrTVVLITHH 529
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
317-498 |
9.52e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 70.84 E-value: 9.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 317 KIVFEMEDVC--YQVDGKQLV--KDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFD 388
Cdd:COG1136 2 SPLLELRNLTksYGTGEGEVTalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDgqdiSSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 389 QHRAE----------LDPDKTVMDNLA-----EGKQEVMVNGKPRHVLGYLQdfLFHpkRAMTPVRALSGGERNRLLLAR 453
Cdd:COG1136 82 RLRRRhigfvfqffnLLPELTALENVAlplllAGVSRKERRERARELLERVG--LGD--RLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15830287 454 -LFLKPSnLLILDEPTNDLDvetlELLEELI--------DSYQGTVLLVSHDRQ 498
Cdd:COG1136 158 aLVNRPK-LILADEPTGNLD----SKTGEEVlellrelnRELGTTIVMVTHDPE 206
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
330-495 |
9.96e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.11 E-value: 9.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLqADSGRIHVG----TKLEVAYFDQHRAELD-----PDKTV 400
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINgielRELDPESWRKHLSWVGqnpqlPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 MDNLAEGKQEvMVNGKPRHVL--GYLQDFLF-HPKRAMTPVR----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK11174 440 RDNVLLGNPD-ASDEQLQQALenAWVSEFLPlLPQGLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180
....*....|....*....|....
gi 15830287 474 ETLELLEELIDSY--QGTVLLVSH 495
Cdd:PRK11174 519 HSEQLVMQALNAAsrRQTTLMVTH 542
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-226 |
1.01e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 69.96 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQ--DPPRNVEGSVYDFVAE 89
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsEVPDSLPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 90 GIEEQAEYLKRYHDISRLVmndpseknlnelakVQEQLDHHNLWQLENRinevlaqlgldpnvALSSLSGGWLRKAALGR 169
Cdd:NF040873 81 GRWARRGLWRRLTRDDRAA--------------VDDALERVGLADLAGR--------------QLGELSGGQRQRALLAQ 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 170 ALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNmATRIVDL 226
Cdd:NF040873 133 GLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLELVRR-ADPCVLL 191
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-189 |
1.05e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.34 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNV- 79
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 80 ----EGSV-YDFVAEGIEEqaeyLKRYHDISRLVMNDPSEKnlnelAKVQEQLDHHNLWQLENRinevlaqlgldpnvAL 154
Cdd:PRK09536 81 svpqDTSLsFEFDVRQVVE----MGRTPHRSRFDTWTETDR-----AAVERAMERTGVAQFADR--------------PV 137
|
170 180 190
....*....|....*....|....*....|....*
gi 15830287 155 SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI 189
Cdd:PRK09536 138 TSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-230 |
1.19e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.06 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDliVARLqqdPP--R 77
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgQD--ITHV---PAenR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 78 NVEG-----------SVYDFVAEGIEEQ----AEYLKRYHDISRLVmndpseknlnelakvqeqldhhnlwQLENRINEV 142
Cdd:PRK09452 87 HVNTvfqsyalfphmTVFENVAFGLRMQktpaAEITPRVMEALRMV-------------------------QLEEFAQRK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 143 LAQLgldpnvalsslSGGWLRKAALGRALVSNPRVLLLDEPTNHLD--------IEtidwLEGFLKTFNGTIIFISHDRS 214
Cdd:PRK09452 142 PHQL-----------SGGQQQRVAIARAVVNKPKVLLLDESLSALDyklrkqmqNE----LKALQRKLGITFVFVTHDQE 206
|
250
....*....|....*.
gi 15830287 215 FIRNMATRIVDLDRGK 230
Cdd:PRK09452 207 EALTMSDRIVVMRDGR 222
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-234 |
1.35e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 70.25 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlivarlqqdpprnVEGSVYDFVAEGI------- 91
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT-----------------VRGRVSSLLGLGGgfnpelt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 92 -EEQAEYLKRYHDISRlvmndpseknlnelakvqEQLDhhnlwQLENRINEvLAQLGLDPNVALSSLSGGWLRKAALGRA 170
Cdd:cd03220 101 gRENIYLNGRLLGLSR------------------KEID-----EKIDEIIE-FSELGDFIDLPVKTYSSGMKARLAFAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287 171 LVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTfNGTIIFISHDRSFIRNMATRIVDLDRGKLVTY 234
Cdd:cd03220 157 TALEPDILLIDEVLAVGDAAFqekcQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
319-472 |
1.53e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 72.56 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI--------HVGTKLEVAYFDQH 390
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvdlsHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 RAELDPDKTVMDNLAEG-KQEVM----VNGKPRHVLG--YLQDFlfhpkrAMTPVRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGlKQDKLpkaeIASRVNEMLGlvHMQEF------AKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
....*....
gi 15830287 464 LDEPTNDLD 472
Cdd:PRK11607 173 LDEPMGALD 181
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-245 |
1.58e-13 |
|
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: 70.34 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDliVARLQQDPPRNVEGSV-------YDFVA 88
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIlIDGQD--IREVTLDSLRRAIGVVpqdtvlfNDTIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 89 EGIeeqaeylkRYHDIsrlvmnDPSEKNLNELAKVQEQldHHNLWQLENRINEVLAQLGLdpnvalsSLSGGWLRKAALG 168
Cdd:cd03253 93 YNI--------RYGRP------DATDEEVIEAAKAAQI--HDKIMRFPDGYDTIVGERGL-------KLSGGEKQRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 169 RALVSNPRVLLLDEPTNHLDIET---IdwLEGFLKTFNG-TIIFISHDRSFIRNmATRIVDLDRGKLVTyPGNYDQYLLE 244
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTereI--QAALRDVSKGrTTIVIAHRLSTIVN-ADKIIVLKDGRIVE-RGTHEELLAK 225
|
.
gi 15830287 245 K 245
Cdd:cd03253 226 G 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
320-467 |
1.65e-13 |
|
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: 70.26 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEV--------AYF 387
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqdiTKLPMhkrarlgiGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 388 DQhRAELDPDKTVMDNLAEGKQEVMVNGKPRH-VLGYLQDfLFHPKR-AMTPVRALSGGERNRLLLAR-LFLKPSNLLiL 464
Cdd:cd03218 81 PQ-EASIFRKLTVEENILAVLEIRGLSKKEREeKLEELLE-EFHITHlRKSKASSLSGGERRRVEIARaLATNPKFLL-L 157
|
...
gi 15830287 465 DEP 467
Cdd:cd03218 158 DEP 160
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-241 |
1.69e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 73.67 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQdpprnvegs 82
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQ--------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 83 vydfvaegieEQAEYLKryhdisrlvmndPSEKNLNELAKVQEQldhhnlwQLENRINEVLAQLGLDPNV---ALSSLSG 159
Cdd:PRK10636 383 ----------HQLEFLR------------ADESPLQHLARLAPQ-------ELEQKLRDYLGGFGFQGDKvteETRRFSG 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 160 GwlRKAALGRALV--SNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGN 237
Cdd:PRK10636 434 G--EKARLVLALIvwQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGD 511
|
....
gi 15830287 238 YDQY 241
Cdd:PRK10636 512 LEDY 515
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-248 |
1.94e-13 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 70.26 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLI-----------VARLQQDPprnV--EG 81
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrdlnlrwlrsqIGLVSQEP---VlfDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 82 SVYDFVAEG----IEEQAEYLKRYHDISRLVMNDPseknlnelakvqeqldhhnlwqleNRINEVLAQLGldpnvalSSL 157
Cdd:cd03249 92 TIAENIRYGkpdaTDEEVEEAAKKANIHDFIMSLP------------------------DGYDTLVGERG-------SQL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 158 SGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKtfNGTIIFISHDRSFIRNmATRIVDLDRGKLVT 233
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESeklvQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVE 217
|
250
....*....|....*
gi 15830287 234 YpGNYDQyLLEKEEA 248
Cdd:cd03249 218 Q-GTHDE-LMAQKGV 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
333-468 |
2.22e-13 |
|
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: 69.77 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLE--------VAYFDQHRaELDPDKTV 400
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrdiTGLPpheraragIGYVPEGR-RIFPELTV 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 401 MDNLAEGKQeVMVNGKPRHVLGYLQDfLFhPK---RAMTPVRALSGGERNRLLLAR-LFLKPSnLLILDEPT 468
Cdd:cd03224 93 EENLLLGAY-ARRRAKRKARLERVYE-LF-PRlkeRRKQLAGTLSGGEQQMLAIARaLMSRPK-LLLLDEPS 160
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-277 |
2.30e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 71.29 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYEQdlivARLQQDPPRNV-----EGSV 83
Cdd:COG4152 10 RFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIIL---GIlapDSGEVLWDG----EPLDPEDRRRIgylpeERGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 84 YDfvAEGIEEQAEYLKRYHDISRlvmndpseknlnelAKVQEQLDHhnlWqlenrinevLAQLGLDP--NVALSSLSGGW 161
Cdd:COG4152 83 YP--KMKVGEQLVYLARLKGLSK--------------AEAKRRADE---W---------LERLGLGDraNKKVEELSKGN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 162 LRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NG-TIIFISHDRSFIRNMATRIVDLDRGKLVTYpGN- 237
Cdd:COG4152 135 QQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaaKGtTVIFSSHQMELVEELCDRIVIINKGRKVLS-GSv 213
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15830287 238 ---YDQYlleKEEALRVEELQNAEFDRKLAQEEVWIRQGIKAR 277
Cdd:COG4152 214 deiRRQF---GRNTLRLEADGDAGWLRALPGVTVVEEDGDGAE 253
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-233 |
2.39e-13 |
|
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: 69.77 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 2 SLISMHGAWLSFSDA--PL--LDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGLD---DGRI-IYEQDLivARLQQ 73
Cdd:COG4181 7 PIIELRGLTKTVGTGagELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLL---AGLDrptSGTVrLAGQDL--FALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 74 DP-----PRNVegsvydfvaeGIEEQAEYLkryhdISRL-----VM--------NDPSEKNLNELAKV--QEQLDHHnlw 133
Cdd:COG4181 82 DArarlrARHV----------GFVFQSFQL-----LPTLtalenVMlplelagrRDARARARALLERVglGHRLDHY--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 134 qlenrinevlaqlgldPNValssLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFI 209
Cdd:COG4181 144 ----------------PAQ----LSGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRERGTTLVLV 203
|
250 260
....*....|....*....|....
gi 15830287 210 SHDRSFIRnMATRIVDLDRGKLVT 233
Cdd:COG4181 204 THDPALAA-RCDRVLRLRAGRLVE 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
310-472 |
2.68e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 72.94 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 310 EEASRSGKIVFEMEDVC--YQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYF 387
Cdd:PRK11160 329 TSTAAADQVSLTLNNVSftYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 388 DQ----------HRAELDPDkTVMDNLAEGK----QEVMVngkprHVL---GyLQDFLFHPKRAMTPV----RALSGGER 446
Cdd:PRK11160 409 EAalrqaisvvsQRVHLFSA-TLRDNLLLAApnasDEALI-----EVLqqvG-LEKLLEDDKGLNAWLgeggRQLSGGEQ 481
|
170 180
....*....|....*....|....*.
gi 15830287 447 NRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLD 507
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
329-513 |
3.35e-13 |
|
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: 69.10 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 329 VDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTK----LEVAYFdqhraeLDPDKTVMDNl 404
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsslLGLGGG------FNPELTGREN- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 405 aegkqeVMVNGKprhVLGYLQDFLfhpkRAM---------------TPVRALSGGERNRLLLA-RLFLKPsNLLILDEPT 468
Cdd:cd03220 105 ------IYLNGR---LLGLSRKEI----DEKideiiefselgdfidLPVKTYSSGMKARLAFAiATALEP-DILLIDEVL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15830287 469 NDLDVETLELLEELIDSYQ---GTVLLVSHDRQFVDNTVTECWIFEGG 513
Cdd:cd03220 171 AVGDAAFQEKCQRRLRELLkqgKTVILVSHDPSSIKRLCDRALVLEKG 218
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
277-545 |
3.40e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 72.59 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 277 RRTRNEGRVRALKAMRRERGERREVMGTAKMQVEEASRSGKIV---FEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGP 353
Cdd:PLN03073 132 RRKRKEERQREVQYQAHVAEMEAAKAGMPGVYVNHDGNGGGPAikdIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGR 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 354 NGCGKTTLLKLMlgQLQADSGR------IHVG---------------------TKL--EVAYFDQHRAELD--------- 395
Cdd:PLN03073 212 NGTGKTTFLRYM--AMHAIDGIpkncqiLHVEqevvgddttalqcvlntdierTQLleEEAQLVAQQRELEfetetgkgk 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 396 -PDKTVMDNLAEGKQEVMVNGKPRHVLGY---------LQDFLFHPKRAMTPVRALSGGERNRLLLAR-LFLKPsNLLIL 464
Cdd:PLN03073 290 gANKDGVDKDAVSQRLEEIYKRLELIDAYtaearaasiLAGLSFTPEMQVKATKTFSGGWRMRIALARaLFIEP-DLLLL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 465 DEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVDNTVTECWIFEGGgKIGRYVGGYHDARGQQEQYVALKQPAVKKN 544
Cdd:PLN03073 369 DEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQ-KLVTYKGDYDTFERTREEQLKNQQKAFESN 447
|
.
gi 15830287 545 E 545
Cdd:PLN03073 448 E 448
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
317-505 |
3.85e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.97 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 317 KIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKL----------EVA 385
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDIstlkpeiyrqQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 386 YFDQHRAeLDPDkTVMDNLAEGKQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:PRK10247 85 YCAQTPT-LFGD-TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15830287 466 EPTNDLDVETLELLEELIDSY----QGTVLLVSHDR---QFVDNTVT 505
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYvreqNIAVLWVTHDKdeiNHADKVIT 209
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-266 |
3.87e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.73 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDlivarlqqdpprnvegsvydfvaegIEEQAE 96
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlIDGKD-------------------------VTKLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 97 YlKRYHDISRlVMNDPS---------EKNL------------------NELAKVQEQLDHHNLwQLENRINevlAQLGLd 149
Cdd:COG1101 76 Y-KRAKYIGR-VFQDPMmgtapsmtiEENLalayrrgkrrglrrgltkKRRELFRELLATLGL-GLENRLD---TKVGL- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 150 pnvalssLSGGWlRKA-ALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIV 224
Cdd:COG1101 149 -------LSGGQ-RQAlSLLMATLTKPKLLLLDEHTAALDPKTaalvLELTEKIVEENNLTTLMVTHNMEQALDYGNRLI 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15830287 225 DLDRGKLVtypgnYDqylLEKEE--ALRVEELQnAEFDRKLAQE 266
Cdd:COG1101 221 MMHEGRII-----LD---VSGEEkkKLTVEDLL-ELFEEIRGEE 255
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
321-472 |
3.95e-13 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 68.76 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGdKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklevaYFDQHRAELDPDKTv 400
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTI---------RIDGQDVLKQPQKL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 mdnlaegkqevmvngkpRHVLGYL-QDFLFHPK------------------------------------RAMTPVRALSG 443
Cdd:cd03264 71 -----------------RRRIGYLpQEFGVYPNftvrefldyiawlkgipskevkarvdevlelvnlgdRAKKKIGSLSG 133
|
170 180
....*....|....*....|....*....
gi 15830287 444 GERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03264 134 GMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
311-472 |
4.16e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 71.13 E-value: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 311 EASRSGKIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-------------- 376
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgqdithvpaen 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 377 -HVGTKLevayfdQHRAeLDPDKTVMDNLAEG-------KQEVmvngKPRhVLG-----YLQDFlfhpkrAMTPVRALSG 443
Cdd:PRK09452 86 rHVNTVF------QSYA-LFPHMTVFENVAFGlrmqktpAAEI----TPR-VMEalrmvQLEEF------AQRKPHQLSG 147
|
170 180
....*....|....*....|....*....
gi 15830287 444 GERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
332-472 |
4.47e-13 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 68.84 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQAD---SGRIHVG--------TKLEVAYFDQHRAELdPDKTV 400
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNgqprkpdqFQKCVAYVRQDDILL-PGLTV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 401 MDNLAEGKQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVR-----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03234 99 RETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGgnlvkGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-234 |
5.10e-13 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 68.67 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSFSD--APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIY-EQDLIVARLQ-------- 72
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdGVDISKIGLHdlrsrisi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 73 --QDPprnvegsvydFVAEG-IEEQAEYLKRYHDisrlvmndpsEKNLNELAKVQeqldhhnlwqLENRINEVLAQLGLD 149
Cdd:cd03244 83 ipQDP----------VLFSGtIRSNLDPFGEYSD----------EELWQALERVG----------LKEFVESLPGGLDTV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 150 PNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NGTIIFISHdRsfIRNMAT--RIVD 225
Cdd:cd03244 133 VEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAH-R--LDTIIDsdRILV 209
|
....*....
gi 15830287 226 LDRGKLVTY 234
Cdd:cd03244 210 LDKGRVVEF 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-232 |
5.41e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 69.81 E-value: 5.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLIVARLQQD----PPRNVEGSVYDFVAEGIEEQ 94
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-DITITHKTKDkyirPVRKRIGMVFQFPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 95 aeylkryhDISRLVMNDPseKNLNelakvqeqldhHNLWQLENRINEVLAQLGLDPNVALSS---LSGGWLRKAALGRAL 171
Cdd:PRK13646 102 --------TVEREIIFGP--KNFK-----------MNLDEVKNYAHRLLMDLGFSRDVMSQSpfqMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287 172 VSNPRVLLLDEPTNHLDIETIDWLEGFLKTF----NGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqtdeNKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
316-473 |
5.64e-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: 68.79 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 316 GKIVFEmeDVCYQVDGKQLV-KDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGtklEVAYFDQHRAEL 394
Cdd:cd03254 1 GEIEFE--NVNFSYDEKKPVlKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILID---GIDIRDISRKSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 ---------DP---DKTVMDNLAEGKQ-----EVMVNGKPRHvlgyLQDFLFH-PKRAMTPVR----ALSGGERNRLLLA 452
Cdd:cd03254 76 rsmigvvlqDTflfSGTIMENIRLGRPnatdeEVIEAAKEAG----AHDFIMKlPNGYDTVLGenggNLSQGERQLLAIA 151
|
170 180
....*....|....*....|.
gi 15830287 453 RLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDT 172
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-232 |
5.97e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.60 E-value: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIY---------EQDLIVARlqqdppRNVeG-------- 81
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVdgqdltalsEKELRKAR------RQI-Gmifqhfnl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 82 ----SVYDFVAegieeqaeylkryhdisrLVMndpseknlnELAKVQEQldhhnlwQLENRINEVLAQLGLDP--NVALS 155
Cdd:PRK11153 94 lssrTVFDNVA------------------LPL---------ELAGTPKA-------EIKARVTELLELVGLSDkaDRYPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 156 SLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATtrsiLELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
.
gi 15830287 232 V 232
Cdd:PRK11153 220 V 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
330-473 |
6.68e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.91 E-value: 6.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQ-----HRAELDPDKTV 400
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQgepiRRQRDEYHQDllylgHQPGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 MDNLA-------EGKQEVMVNGKPRHVLGylqdflfhpKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK13538 92 LENLRfyqrlhgPGDDEALWEALAQVGLA---------GFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
15-231 |
7.09e-13 |
|
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: 67.24 E-value: 7.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreqglddgriiyeqdlivARLQQDpprnVEGSVYdfvAEGIEEQ 94
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLI-------------------LGLLRP----TSGRVR---LDGADIS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 95 AEYLKRYHDISRLVMNDpseknlNELakvqeqldhhnlwqLENRINEvlaqlgldpNValssLSGGWLRKAALGRALVSN 174
Cdd:cd03246 68 QWDPNELGDHVGYLPQD------DEL--------------FSGSIAE---------NI----LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 175 PRVLLLDEPTNHLDIETIDWLE---GFLKTFNGTIIFISHDRSFIRnMATRIVDLDRGKL 231
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNqaiAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
304-513 |
7.14e-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: 7.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 304 TAKMQVEEASRSgkivFEMedvcYQVDGKQL--VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV--- 378
Cdd:COG4778 2 TTLLEVENLSKT----FTL----HLQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 379 GTKLEVAyfdqhRAeldPDKTVMDNLaegkqevmvngkpRHVLGYLQDFLfhpkRAMTPVRAL----------------- 441
Cdd:COG4778 74 GGWVDLA-----QA---SPREILALR-------------RRTIGYVSQFL----RVIPRVSALdvvaepllergvdreea 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 442 -------------------------SGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY--QGTVLL-V 493
Cdd:COG4778 129 rararellarlnlperlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkaRGTAIIgI 208
|
250 260
....*....|....*....|
gi 15830287 494 SHDRQFVDNTVTECWIFEGG 513
Cdd:COG4778 209 FHDEEVREAVADRVVDVTPF 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-232 |
7.26e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 69.01 E-value: 7.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI------------IYEQDLIV 68
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtarsLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 69 ARLQQD-----------PPRnvegSVYDFVAEGieeqaeylkryhdiSRLVMNDPSEknlnelakvqeqldhhnlwQLEN 137
Cdd:PRK11264 81 RQLRQHvgfvfqnfnlfPHR----TVLENIIEG--------------PVIVKGEPKE-------------------EATA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 138 RINEVLAQLGLD--PNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLegfLKTFNG------TIIFI 209
Cdd:PRK11264 124 RARELLAKVGLAgkETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEV---LNTIRQlaqekrTMVIV 200
|
250 260
....*....|....*....|...
gi 15830287 210 SHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK11264 201 THEMSFARDVADRAIFMDQGRIV 223
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-258 |
7.79e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.73 E-value: 7.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIiyeqdlivarlqqdpprnvegSVYDFVAegIEEQA 95
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLT---GIlvpTSGEV---------------------RVLGYVP--FKRRK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 96 EYLKRyhdISrLVMndpSEKNlnelakvqeQLdhhnLWQL--------------------ENRINEVLAQLGLDP--NVA 153
Cdd:COG4586 92 EFARR---IG-VVF---GQRS---------QL----WWDLpaidsfrllkaiyripdaeyKKRLDELVELLDLGEllDTP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 154 LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFN----GTIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:COG4586 152 VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNrergTTILLTSHDMDDIEALCDRVIVIDHG 231
|
250 260
....*....|....*....|....*....
gi 15830287 230 KLVtYPGNYDQyLLEKEEALRVEELQNAE 258
Cdd:COG4586 232 RII-YDGSLEE-LKERFGPYKTIVLELAE 258
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-520 |
8.74e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 70.81 E-value: 8.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDG----------RIIYEQdlivar 70
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfshitRLSFEQ------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 71 LQQdpprnvegsvydfvaegIEEQaEYLKRYHDisrlvMNDPSEKNLNELAKVQEQLDHHNlwqlENRINEVLAQLGLDP 150
Cdd:PRK10938 75 LQK-----------------LVSD-EWQRNNTD-----MLSPGEDDTGRTTAEIIQDEVKD----PARCEQLAQQFGITA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 151 --NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVD 225
Cdd:PRK10938 128 llDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLVLNRFDEIPDFVQFAGV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 226 LDRGKLvTYPGNYDQYLlekEEALrVEELQNAEfdrKLAQEEVWIRQGIKARRTRNEGRVRalkamrrergerrevmgta 305
Cdd:PRK10938 208 LADCTL-AETGEREEIL---QQAL-VAQLAHSE---QLEGVQLPEPDEPSARHALPANEPR------------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 306 kmqveeasrsgkivFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLG-QLQADSGRIHVgtklev 384
Cdd:PRK10938 261 --------------IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdHPQGYSNDLTL------ 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 385 ayFDQHRAEldpDKTVMDNlaegKQ-----------EVMVNGKPRHVL--GYLQ--------------------DFLFHP 431
Cdd:PRK10938 321 --FGRRRGS---GETIWDI----KKhigyvssslhlDYRVSTSVRNVIlsGFFDsigiyqavsdrqqklaqqwlDILGID 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 432 KR-AMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQG---TVLL-VSHDRQFVDNTVTE 506
Cdd:PRK10938 392 KRtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISegeTQLLfVSHHAEDAPACITH 471
|
570
....*....|....
gi 15830287 507 CWIFEGGGKIGRYV 520
Cdd:PRK10938 472 RLEFVPDGDIYRYV 485
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
11-241 |
1.02e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 71.04 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFSDA-------PLL-DNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQdpprnvegs 82
Cdd:PLN03073 509 ISFSDAsfgypggPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQ--------- 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 83 vydfvaegieeqaeylkryHDISRLvmnDPSEKNLNELAKVQEQLdhhnlwqLENRINEVLAQLGLDPNVALSS---LSG 159
Cdd:PLN03073 580 -------------------HHVDGL---DLSSNPLLYMMRCFPGV-------PEQKLRAHLGSFGVTGNLALQPmytLSG 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 160 GWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYD 239
Cdd:PLN03073 631 GQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFH 710
|
..
gi 15830287 240 QY 241
Cdd:PLN03073 711 DY 712
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-234 |
1.02e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 68.52 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNReqgLDD--------GRIIYEQDLIVARlQQDPP---RNV 79
Cdd:COG1117 19 VYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNR---MNDlipgarveGEILLDGEDIYDP-DVDVVelrRRV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 80 eG-----------SVYDFVAEGIeeqaeylkRYHDISrlvmndpSEKNLNELakVQEQLDHHNLWqlenriNEV---LAQ 145
Cdd:COG1117 95 -GmvfqkpnpfpkSIYDNVAYGL--------RLHGIK-------SKSELDEI--VEESLRKAALW------DEVkdrLKK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 146 LGLdpnvalsSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD------IE-TIDwlEgfLKTfNGTIIFISHdrsfirN 218
Cdd:COG1117 151 SAL-------GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistakIEeLIL--E--LKK-DYTIVIVTH------N 212
|
250 260
....*....|....*....|..
gi 15830287 219 M--ATRIVD----LDRGKLVTY 234
Cdd:COG1117 213 MqqAARVSDytafFYLGELVEF 234
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
31-225 |
1.12e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.66 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 31 RVC-LVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLI-----------VARL-QQDPPrnVEG-SVYDFVAEGieeqae 96
Cdd:PRK10575 38 KVTgLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsskafarkVAYLpQQLPA--AEGmTVRELVAIG------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 97 ylkRYhdisrlvmndPSEKNLNELAKVQEQldhhnlwqlenRINEVLAQLGLDP--NVALSSLSGGWLRKAALGRALVSN 174
Cdd:PRK10575 110 ---RY----------PWHGALGRFGAADRE-----------KVEEAISLVGLKPlaHRLVDSLSGGERQRAWIAMLVAQD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15830287 175 PRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDrsfiRNMATRIVD 225
Cdd:PRK10575 166 SRCLLLDEPTSALDIahqvDVLALVHRLSQERGLTVIAVLHD----INMAARYCD 216
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-231 |
1.23e-12 |
|
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: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRII--------YEQDLI---VARLQQDPPRnVEGS 82
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgkpisqYEHKYLhskVSLVGQEPVL-FARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 83 VYDFVAEGieeqaeylkryhdisrlvMNDPSEKNLNELAkvQEQLDHHNLWQLENRINEVLAQLGldpnvalSSLSGGWL 162
Cdd:cd03248 104 LQDNIAYG------------------LQSCSFECVKEAA--QKAHAHSFISELASGYDTEVGEKG-------SQLSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 163 RKAALGRALVSNPRVLLLDEPTNHLDIET--------IDWLEgflktfNGTIIFISHDRSFIRNmATRIVDLDRGKL 231
Cdd:cd03248 157 QRVAIARALIRNPQVLILDEATSALDAESeqqvqqalYDWPE------RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-231 |
1.30e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 69.34 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDliVARLQ-QDppRNV---------- 79
Cdd:PRK10851 11 SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgTD--VSRLHaRD--RKVgfvfqhyalf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 80 -EGSVYDFVAEGIEeqaeYLKRYHDISRLVMNdpseknlnelAKVQEQLDHHNLWQLENRInevlaqlgldPnvalSSLS 158
Cdd:PRK10851 87 rHMTVFDNIAFGLT----VLPRRERPNAAAIK----------AKVTQLLEMVQLAHLADRY----------P----AQLS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 159 GGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK10851 139 GGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
12-231 |
1.45e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.17 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL-------------------DDGRIIYeQDlivARLQ 72
Cdd:PRK11247 21 RYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLL---AGLetpsagellagtaplaearEDTRLMF-QD---ARLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 73 qdPPRnvegSVYDFVAEGIEeqaeylkryhdisrlvmNDPSEKNLNELAKVQeqldhhnlwqLENRINEVLAqlgldpnv 152
Cdd:PRK11247 94 --PWK----KVIDNVGLGLK-----------------GQWRDAALQALAAVG----------LADRANEWPA-------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 153 alsSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDR 228
Cdd:PRK11247 133 ---ALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEE 209
|
...
gi 15830287 229 GKL 231
Cdd:PRK11247 210 GKI 212
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
24-232 |
1.86e-12 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 67.31 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 24 LHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLivarLQQDPPRNVE-GSVYdfVAEG--------IEE 93
Cdd:COG0410 24 LEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgEDI----TGLPPHRIARlGIGY--VPEGrrifpsltVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 94 qaeylkryhdisrlvmndpsekNLnELAKVQEQLDHHNLWQLEN------RINEVLAQLGldpnvalSSLSGGWLRKAAL 167
Cdd:COG0410 98 ----------------------NL-LLGAYARRDRAEVRADLERvyelfpRLKERRRQRA-------GTLSGGEQQMLAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 168 GRALVSNPRVLLLDEPTNHL------DI-ETIDWL--EGFlktfngTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGLapliveEIfEIIRRLnrEGV------TILLVEQNARFALEIADRAYVLERGRIV 215
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
330-496 |
1.96e-12 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 66.29 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAY----FDQHRAEL-----DPDK-- 398
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGE-PLDYsrkgLLERRQRVglvfqDPDDql 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 399 ---TVMDNLA-----EGKQEVMVNGKPRHVLGYLqDFLFHPKRamtPVRALSGGERNRLLLA-RLFLKPsNLLILDEPTN 469
Cdd:TIGR01166 82 faaDVDQDVAfgplnLGLSEAEVERRVREALTAV-GASGLRER---PTHCLSGGEKKRVAIAgAVAMRP-DVLLLDEPTA 156
|
170 180 190
....*....|....*....|....*....|
gi 15830287 470 DLDVETLELLEELIDSY--QG-TVLLVSHD 496
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLraEGmTVVISTHD 186
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
335-468 |
2.22e-12 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 66.93 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLE--------VAYFDQHRaELDPDKTVMD 402
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgediTGLPphriarlgIGYVPEGR-RIFPSLTVEE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 403 NLAEGKQEVMVNGKPRHVLGYLQDfLFhPK---RAMTPVRALSGGERNRLLLAR-LFLKPSnLLILDEPT 468
Cdd:COG0410 98 NLLLGAYARRDRAEVRADLERVYE-LF-PRlkeRRRQRAGTLSGGEQQMLAIGRaLMSRPK-LLLLDEPS 164
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-232 |
2.40e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 67.71 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFS----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL----NREQG--LDDGRIIYEQDLIVAR-----LQQDP 75
Cdd:PRK13632 13 VSFSypnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILtgllKPQSGeiKIDGITISKENLKEIRkkigiIFQNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 76 PRNVEGS-VYDFVAEGIEEqaeylKRyhdISRLVMNDPseknLNELAKV---QEQLDHhnlwqlenrinevlaqlglDPn 151
Cdd:PRK13632 93 DNQFIGAtVEDDIAFGLEN-----KK---VPPKKMKDI----IDDLAKKvgmEDYLDK-------------------EP- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 152 valSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD-------IETIDWLEgflKTFNGTIIFISHDRSFIRNmATRIV 224
Cdd:PRK13632 141 ---QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgkreiKKIMVDLR---KTRKKTLISITHDMDEAIL-ADKVI 213
|
....*...
gi 15830287 225 DLDRGKLV 232
Cdd:PRK13632 214 VFSEGKLI 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
14-212 |
2.53e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.47 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 14 SDAPL-LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLI-----------VARLQQDPPRNVEG 81
Cdd:PRK13648 19 SDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnfeklrkhIGIVFQNPDNQFVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 82 SVYDF-VAEGIEEQAEylkryhdisrlvmndPSEKNLNELAKVQEQLDhhnlwqlenrineVLAQLGLDPNvalsSLSGG 160
Cdd:PRK13648 99 SIVKYdVAFGLENHAV---------------PYDEMHRRVSEALKQVD-------------MLERADYEPN----ALSGG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287 161 WLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHD 212
Cdd:PRK13648 147 QKQRVAIAGVLALNPSVIILDEATSMLDPDArqnlLDLVRKVKSEHNITIISITHD 202
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-237 |
2.60e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 69.75 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGriIYE---QDliVARLQQDPPRNVEGSVYDFVaegieeqa 95
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSG--TYRvagQD--VATLDADALAQLRREHFGFI-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 96 eyLKRYHDISRLVmndpSEKNLnELAKVQEQLDHHnlwQLENRINEVLAQLGLDPNVAL--SSLSGGWLRKAALGRALVS 173
Cdd:PRK10535 92 --FQRYHLLSHLT----AAQNV-EVPAVYAGLERK---QRLLRAQELLQRLGLEDRVEYqpSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 174 NPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSfIRNMATRIVDLDRGKLVTYPGN 237
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDrghTVIIVTHDPQ-VAAQAERVIEIRDGEIVRNPPA 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
332-472 |
3.33e-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: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV------GTKLEVAYFDQHRAeLDPDKTVMDNLA 405
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdgvpvtGPGADRGVVFQKDA-LLPWLNVLDNVA 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287 406 EGKQevmVNGKPRH-----------VLGyLQDFlfhpkrAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:COG4525 99 FGLR---LRGVPKAerraraeellaLVG-LADF------ARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
320-467 |
3.52e-12 |
|
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: 65.95 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQ-----LVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKleVAY-------- 386
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYvsqepwiq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 387 -------------FDQHRAE-------LDPDktvMDNLAEGKQ-EVMVNGkprhvlgylqdflfhpkramtpvRALSGGE 445
Cdd:cd03250 79 ngtirenilfgkpFDEERYEkvikacaLEPD---LEILPDGDLtEIGEKG-----------------------INLSGGQ 132
|
170 180
....*....|....*....|..
gi 15830287 446 RNRLLLARLFLKPSNLLILDEP 467
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDP 154
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
320-496 |
3.69e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.12 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKlMLGQLQ-ADSGRIHVGTKL-----------EVAYF 387
Cdd:PRK10575 12 FALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQpPSEGEILLDAQPleswsskafarKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 388 DQhraELDPdktvmdnlAEG---KQEVMVNGKPRHvlGYLQDFLFHPKR---------AMTP-----VRALSGGERNRLL 450
Cdd:PRK10575 91 PQ---QLPA--------AEGmtvRELVAIGRYPWH--GALGRFGAADREkveeaislvGLKPlahrlVDSLSGGERQRAW 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15830287 451 LARLFLKPSNLLILDEPTNDLDVETLELLEELID--SYQG--TVLLVSHD 496
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHrlSQERglTVIAVLHD 207
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
321-496 |
3.82e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 66.65 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGtKLEVAYFdqhraeldPDKTV 400
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVD-GLDVATT--------PSREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 MDNLAEGKQEVMVN------------------GKP-----RHV---LGYLQdflfhpkraMTPVRA-----LSGGERNRL 449
Cdd:COG4604 74 AKRLAILRQENHINsrltvrelvafgrfpyskGRLtaedrEIIdeaIAYLD---------LEDLADryldeLSGGQRQRA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15830287 450 LLARLFLKPSNLLILDEPTNDLD----VETLELLEELIDSYQGTVLLVSHD 496
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADELGKTVVIVLHD 195
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-496 |
3.94e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.92 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlivarlqqdpprNVEGS 82
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL-----------------EIGGN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 83 VYdfvAEGIEEQAEYLKRYhdisrLVmndPSEKNLNELAKVQEQ----LDHHNLwqLENRINEVLAQLG--LDPNVALSS 156
Cdd:PRK15439 74 PC---ARLTPAKAHQLGIY-----LV---PQEPLLFPNLSVKENilfgLPKRQA--SMQKMKQLLAALGcqLDLDSSAGS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 157 LSGGWLRKAALGRALVSNPRVLLLDEPTNHLD-IET---IDWLEGFLKTFNGtIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK15439 141 LEVADRQIVEILRGLMRDSRILILDEPTASLTpAETerlFSRIRELLAQGVG-IVFISHKLPEIRQLADRISVMRDGTIA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 233 typgnydqyLLEKEEALRVEELQNAefdrklaqeevwirqgiKARRTRNEGRVRALKA-MRRERGERREVMGTAKMQVEE 311
Cdd:PRK15439 220 ---------LSGKTADLSTDDIIQA-----------------ITPAAREKSLSASQKLwLELPGNRRQQAAGAPVLTVED 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 312 ASRSGkivfemedvcyqvdgkqlVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklevaYFDQHr 391
Cdd:PRK15439 274 LTGEG------------------FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI---------MLNGK- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 392 aELDPDKTVmDNLAEGkqeVMVNGKPRHVLG-YL---------------QDFLFHPKR------------------AMTP 437
Cdd:PRK15439 326 -EINALSTA-QRLARG---LVYLPEDRQSSGlYLdaplawnvcalthnrRGFWIKPARenavleryrralnikfnhAEQA 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 438 VRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY--QGT-VLLVSHD 496
Cdd:PRK15439 401 ARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIaaQNVaVLFISSD 462
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-211 |
4.24e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.67 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQdlivarlqqdpprnvEGSVYDFVAEgieeQAE 96
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---------------GDIDDPDVAE----ACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 97 YLkryhdisrlvmndpSEKN-LNELAKVQEQLDhhnLW-----QLENRINEVLAQLGLDP--NVALSSLSGGWLRKAALG 168
Cdd:PRK13539 77 YL--------------GHRNaMKPALTVAENLE---FWaaflgGEELDIAAALEAVGLAPlaHLPFGYLSAGQKRRVALA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15830287 169 RALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISH 211
Cdd:PRK13539 140 RLLVSNRPIWILDEPTAALDAAAVALFAELIRAHlaqGGIVIAATH 185
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
333-495 |
4.76e-12 |
|
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: 65.85 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklEVAYFDQHRAELD--------PDK------ 398
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA------TVDGFDVVKEPAEarrrlgfvSDStglydr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 399 -TVMDNLA-----EGKQEVMVNGKPRHVLGYLQDFLFHPKRamtpVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03266 93 lTARENLEyfaglYGLKGDELTARLEELADRLGMEELLDRR----VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180
....*....|....*....|....*.
gi 15830287 473 VETLELLEELIDSY---QGTVLLVSH 495
Cdd:cd03266 169 VMATRALREFIRQLralGKCILFSTH 194
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
321-516 |
4.93e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 66.31 E-value: 4.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG------------TKLEVAYFD 388
Cdd:PRK11264 5 EVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtarslsqQKGLIRQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 389 QHRA------ELDPDKTVMDNLAEGKqeVMVNGKPRHVLGYLQDFLFHP-----KRAMTPvRALSGGERNRLLLARLFLK 457
Cdd:PRK11264 85 QHVGfvfqnfNLFPHRTVLENIIEGP--VIVKGEPKEEATARARELLAKvglagKETSYP-RRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 458 PSNLLILDEPTNDLDVETLELLEELIDSY---QGTVLLVSHDRQFVDNtVTECWIFEGGGKI 516
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVIVTHEMSFARD-VADRAIFMDQGRI 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
21-250 |
6.00e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 65.93 E-value: 6.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDliVARLqqdPP--RNV-----EG------SVYDF 86
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgQD--LTAL---PPaeRPVsmlfqENnlfphlTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 87 VAEGIeeqaeylkryhdisrlvmnDPSEKnLNELAKvqeqldhhnlwqleNRINEVLAQLGLD------PnvalSSLSGG 160
Cdd:COG3840 92 IGLGL-------------------RPGLK-LTAEQR--------------AQVEQALERVGLAglldrlP----GQLSGG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 161 WLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKlVTYPG 236
Cdd:COG3840 134 QRQRVALARCLVRKRPILLLDEPFSALDPalrqEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGR-IAADG 212
|
250
....*....|....*
gi 15830287 237 NYDQYL-LEKEEALR 250
Cdd:COG3840 213 PTAALLdGEPPPALA 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
320-498 |
6.22e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 65.20 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQAD---SGRIhvgtklevaYFDQHRaeldp 396
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEV---------LLNGRR----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 397 dktvmdnLAEGKQEvmvngkPRHVlGYL-QDFLFHP----------------KRAMTPVRA------------------- 440
Cdd:COG4136 68 -------LTALPAE------QRRI-GILfQDDLLFPhlsvgenlafalpptiGRAQRRARVeqaleeaglagfadrdpat 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830287 441 LSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLDVETLELLEE----LIDSYQGTVLLVSHDRQ 498
Cdd:COG4136 134 LSGGQRARVALLRaLLAEPRALL-LDEPFSKLDAALRAQFREfvfeQIRQRGIPALLVTHDEE 195
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-473 |
6.46e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.42 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN--REQGLDDGRIIYEQDLIVARlqqdpprnve 80
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSgvYPHGTYEGEIIFEGEELQAS---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 81 gSVYDFVAEGI----EEQAeylkryhdisrLVMNDPSEKNL---NELAKvQEQLDHHNLWQlenRINEVLAQLGLDPNVA 153
Cdd:PRK13549 75 -NIRDTERAGIaiihQELA-----------LVKELSVLENIflgNEITP-GGIMDYDAMYL---RAQKLLAQLKLDINPA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 154 L--SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHL-DIET---IDWLEGfLKTFNGTIIFISHDRSFIRNMATRIVDLD 227
Cdd:PRK13549 139 TpvGNLGLGQQQLVEIAKALNKQARLLILDEPTASLtESETavlLDIIRD-LKAHGIACIYISHKLNEVKAISDTICVIR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 228 RGKLV-TYPGnydqyllekeealrveelqnaefdRKLAQEEVwIRQGIKarrtrnegrvRALKAMRRergerrevmgtak 306
Cdd:PRK13549 218 DGRHIgTRPA------------------------AGMTEDDI-ITMMVG----------RELTALYP------------- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 307 mqvEEASRSGKIVFEMEDV-CYQVD--GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQ-ADSGRIHV-GTK 381
Cdd:PRK13549 250 ---REPHTIGEVILEVRNLtAWDPVnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIdGKP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 382 LEV-----------AYF--DQHRAELDPDKTVMDN--LAEGKQEV---MVNG--KPRHVLGYLQDFLFHPKRAMTPVRAL 441
Cdd:PRK13549 327 VKIrnpqqaiaqgiAMVpeDRKRDGIVPVMGVGKNitLAALDRFTggsRIDDaaELKTILESIQRLKVKTASPELAIARL 406
|
490 500 510
....*....|....*....|....*....|..
gi 15830287 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK13549 407 SGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
12-232 |
6.54e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.55 E-value: 6.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLIVARLQQDPPRNVEGSVYDFVAEG 90
Cdd:PRK11607 28 SFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgVDLSHVPPYQRPINMMFQSYALFPHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 91 IEEQAEYLKRYHDISRLVMNDpseknlnelaKVQEQLDHHNLWQLENRinevlaqlglDPNvalsSLSGGWLRKAALGRA 170
Cdd:PRK11607 108 VEQNIAFGLKQDKLPKAEIAS----------RVNEMLGLVHMQEFAKR----------KPH----QLSGGQRQRVALARS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 171 LVSNPRVLLLDEPTNHLD--------IETIDWLEgflkTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDkklrdrmqLEVVDILE----RVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
319-467 |
6.82e-12 |
|
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: 65.76 E-value: 6.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------------HVGTKLEVAY 386
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKIlidgqdithlpmHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 387 FDQHrAELDPDKTVMDNLA---EGKQEVMVNGKPRHVLGYLQDF-LFHPKRAmtPVRALSGGERNRLLLARLFLKPSNLL 462
Cdd:TIGR04406 81 LPQE-ASIFRKLTVEENIMavlEIRKDLDRAEREERLEALLEEFqISHLRDN--KAMSLSGGERRRVEIARALATNPKFI 157
|
....*
gi 15830287 463 ILDEP 467
Cdd:TIGR04406 158 LLDEP 162
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
12-232 |
7.66e-12 |
|
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: 65.08 E-value: 7.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlivarlqqdpprnVEGsvYDFVAEGI 91
Cdd:cd03265 9 KYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT-----------------VAG--HDVVREPR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 92 EEQAEylkryhdISrLVMNDPSEKNlnELAKVQEQLDHHNLW-----QLENRINEVLAQLGL--DPNVALSSLSGGWLRK 164
Cdd:cd03265 70 EVRRR-------IG-IVFQDLSVDD--ELTGWENLYIHARLYgvpgaERRERIDELLDFVGLleAADRLVKTYSGGMRRR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 165 AALGRALVSNPRVLLLDEPTNHLDIETID--W--LEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03265 140 LEIARSLVHRPEVLFLDEPTIGLDPQTRAhvWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
331-467 |
7.81e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 65.44 E-value: 7.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 331 GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklevaYFDQH---------RAEL------- 394
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI---------FLDGEdithlpmhkRARLgigylpq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 DP----DKTVMDNLAEGKQEVMVNGKPRH--VLGYLQDF-LFHPKRamTPVRALSGGERNRLLLAR-LFLKPSNLLiLDE 466
Cdd:COG1137 86 EAsifrKLTVEDNILAVLELRKLSKKEREerLEELLEEFgITHLRK--SKAYSLSGGERRRVEIARaLATNPKFIL-LDE 162
|
.
gi 15830287 467 P 467
Cdd:COG1137 163 P 163
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-229 |
8.11e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.91 E-value: 8.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYEQDLIVARLQQDP--PrnvEGS-----V 83
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIA---GLwpyGSGRIARPAGARVLFLPQRPylP---LGTlrealL 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 84 YDFVAEGIEEQAeylkrYHDISRLVmndpsekNLNELAkvqEQLDHHNLWQLEnrinevlaqlgldpnvalssLSGGWLR 163
Cdd:COG4178 448 YPATAEAFSDAE-----LREALEAV-------GLGHLA---ERLDEEADWDQV--------------------LSLGEQQ 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287 164 KAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKT--FNGTIIFISHdRSFIRNMATRIVDLDRG 229
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
338-495 |
9.99e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.99 E-value: 9.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 338 FSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------HVGT---KLEVAYFDQHRaELDPDKTVMDNLAEGK 408
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdHTTTppsRRPVSMLFQEN-NLFSHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 409 QE-VMVNGKPRHVLGY------LQDFLfhpkrAMTPvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEE 481
Cdd:PRK10771 97 NPgLKLNAAQREKLHAiarqmgIEDLL-----ARLP-GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170
....*....|....*...
gi 15830287 482 LIDSY----QGTVLLVSH 495
Cdd:PRK10771 171 LVSQVcqerQLTLLMVSH 188
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
311-498 |
1.01e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 65.45 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 311 EASRSGKIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKleVAYFDQH 390
Cdd:PRK14246 2 EAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGK--VLYFGKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 RAELD------------------PDKTVMDNLAEGKQEVMVNGKpRHVLGYLQDFLFHP-------KRAMTPVRALSGGE 445
Cdd:PRK14246 80 IFQIDaiklrkevgmvfqqpnpfPHLSIYDNIAYPLKSHGIKEK-REIKKIVEECLRKVglwkevyDRLNSPASQLSGGQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287 446 RNRLLLAR-LFLKPsNLLILDEPTNDLDVETLELLEELIDSYQG--TVLLVSHDRQ 498
Cdd:PRK14246 159 QQRLTIARaLALKP-KVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQ 213
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
321-496 |
1.01e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 65.49 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV------GTKLEVAYFDQHRAEL 394
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpveGPGAERGVVFQNEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 dPDKTVMDNLAEGKQEVMVNGKPRHVLGylQDFL-------FHPKRamtpVRALSGGERNRLLLARLFLKPSNLLILDEP 467
Cdd:PRK11248 83 -PWRNVQDNVAFGLQLAGVEKMQRLEIA--HQMLkkvglegAEKRY----IWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190
....*....|....*....|....*....|...
gi 15830287 468 TNDLDV-ETLELLEELIDSYQGT---VLLVSHD 496
Cdd:PRK11248 156 FGALDAfTREQMQTLLLKLWQETgkqVLLITHD 188
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
30-240 |
1.15e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 67.68 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 30 ERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE----QDLIVARLqqdppRNVEGSVYdfvaegieEQAEYLKR-YHDI 104
Cdd:PRK13657 362 QTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDgtdiRTVTRASL-----RRNIAVVF--------QDAGLFNRsIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 105 SRLVMNDPSEKNLNELAKVQEQLDHhnlwqLENRINevlaqlGLDPNVAL--SSLSGGWLRKAALGRALVSNPRVLLLDE 182
Cdd:PRK13657 429 IRVGRPDATDEEMRAAAERAQAHDF-----IERKPD------GYDTVVGErgRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 183 PTNHLDIETIDWLEGFLKTF--NGTIIFISHDRSFIRNmATRIVDLDRGKLVTyPGNYDQ 240
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELmkGRTTFIIAHRLSTVRN-ADRILVFDNGRVVE-SGSFDE 555
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-232 |
1.30e-11 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 65.14 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE---------QDLivAR----LQQDPPR 77
Cdd:COG4559 9 VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgrplaawspWEL--ARrravLPQHSSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 78 NVEGSVYDFVAEGIEEQAEYLKRYHDISRLVMndpseknlnelakvqEQLDhhnLWQLENRinevlaqlgldpnvALSSL 157
Cdd:COG4559 87 AFPFTVEEVVALGRAPHGSSAAQDRQIVREAL---------------ALVG---LAHLAGR--------------SYQTL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 158 SGGWLRKAALGRALV-------SNPRVLLLDEPTNHLDI----ETIDWLEGFLKTfNGTIIFISHDrsfiRNMAT----R 222
Cdd:COG4559 135 SGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLahqhAVLRLARQLARR-GGGVVAVLHD----LNLAAqyadR 209
|
250
....*....|
gi 15830287 223 IVDLDRGKLV 232
Cdd:COG4559 210 ILLLHQGRLV 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-232 |
1.73e-11 |
|
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: 63.10 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFS----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlivarLQQDPPRNVEGSVYDF 86
Cdd:cd03247 6 VSFSypeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT---------LDGVPVSDLEKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 87 VaeGIEEQAEYLkryhdisrlvMNDPSEKNLNElakvqeqldhhnlwqlenrinevlaqlgldpnvalsSLSGGWLRKAA 166
Cdd:cd03247 77 I--SVLNQRPYL----------FDTTLRNNLGR------------------------------------RFSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 167 LGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKtfNGTIIFISHDRSFIRNMaTRIVDLDRGKLV 232
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITerqlLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
224-291 |
2.00e-11 |
|
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: 60.28 E-value: 2.00e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 224 VDLDRGKLVTYPGNYDQYLLEKEEALRVEELQNAEFDRKLAQEEVWI-RQGIKARRTR-NEGRVRALKAM 291
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIdRFRAKASKAKqAQSRIKALEKM 70
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
14-234 |
2.04e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.82 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqglddGRIIYEQDLIVARLQQDPPRNVEgSVYDFVAegiee 93
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFN-------GILKPTSGSVLIRGEPITKENIR-EVRKFVG----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 94 qaeylkryhdisrLVMNDPSEKNLNELAKVQEQLDHHNLW----QLENRINEVLAQLGLDP--NVALSSLSGGWLRKAAL 167
Cdd:PRK13652 82 -------------LVFQNPDDQIFSPTVEQDIAFGPINLGldeeTVAHRVSSALHMLGLEElrDRVPHHLSGGEKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 168 GRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTY 234
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDpqgvKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
349-498 |
2.08e-11 |
|
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: 65.90 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 349 ALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLE--------------VAYFDQhRAELDPDKTVMDNLAEGKQEVMV 413
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLnGRTLFdsrkgiflppekrrIGYVFQ-EARLFPHLSVRGNLRYGMKRARP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 414 ---NGKPRHVLGYLQdfLFHPKRamTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELI----DSY 486
Cdd:TIGR02142 106 serRISFERVIELLG--IGHLLG--RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLerlhAEF 181
|
170
....*....|..
gi 15830287 487 QGTVLLVSHDRQ 498
Cdd:TIGR02142 182 GIPILYVSHSLQ 193
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
136-231 |
2.81e-11 |
|
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: 62.83 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 136 ENRINE-VLAQLGLDPNVALSS-LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFIS 210
Cdd:cd03215 82 EDRKREgLVLDLSVAENIALSSlLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELadaGKAVLLIS 161
|
90 100
....*....|....*....|.
gi 15830287 211 HDRSFIRNMATRIVDLDRGKL 231
Cdd:cd03215 162 SELDELLGLCDRILVMYEGRI 182
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
316-473 |
2.94e-11 |
|
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: 62.45 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 316 GKIVFEMEDVCyqvdGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG------------TKLE 383
Cdd:cd03215 1 GEPVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgkpvtrrsprdaIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 384 VAYF--DQHRAELDPDKTVMDNLAegkqevmvngkprhvLGYLqdflfhpkramtpvraLSGGERNRLLLARLFLKPSNL 461
Cdd:cd03215 77 IAYVpeDRKREGLVLDLSVAENIA---------------LSSL----------------LSGGNQQKVVLARWLARDPRV 125
|
170
....*....|..
gi 15830287 462 LILDEPTNDLDV 473
Cdd:cd03215 126 LILDEPTRGVDV 137
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
11-232 |
3.77e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 64.02 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDlivarLQQDPPRnvegsvydfvae 89
Cdd:PRK13548 10 VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrLNGRP-----LADWSPA------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 90 gieEQAeylKRyhdisRLVMndPSEKNLNELAKVQE----QLDHHNLWQLENR--INEVLAQLGLDP--NVALSSLSGGW 161
Cdd:PRK13548 73 ---ELA---RR-----RAVL--PQHSSLSFPFTVEEvvamGRAPHGLSRAEDDalVAAALAQVDLAHlaGRDYPQLSGGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 162 LRKAALGRALV------SNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDrsfiRNMAT----RIVDLD 227
Cdd:PRK13548 140 QQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD----LNLAAryadRIVLLH 215
|
....*
gi 15830287 228 RGKLV 232
Cdd:PRK13548 216 QGRLV 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
319-472 |
3.82e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 64.27 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQVDG--KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAEL- 394
Cdd:PRK13635 5 IIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVgGMVLSEETVWDVRRQVg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 ----DPDK-----TVMDNLAEGKQEvmvNGKPR-----------HVLGyLQDFLFH-PKRamtpvraLSGGERNRLLLAR 453
Cdd:PRK13635 85 mvfqNPDNqfvgaTVQDDVAFGLEN---IGVPReemvervdqalRQVG-MEDFLNRePHR-------LSGGQKQRVAIAG 153
|
170 180
....*....|....*....|
gi 15830287 454 -LFLKPSnLLILDEPTNDLD 472
Cdd:PRK13635 154 vLALQPD-IIILDEATSMLD 172
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-232 |
6.01e-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: 62.51 E-value: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 24 LHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLIVArlqqDPPRNVEGSVY---DFVAEGIEEQAEYLK 99
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlINGVDVTAA----PPADRPVSMLFqenNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 100 RyhdisrlvmnDPSEKnlneLAKVQEQldhhnlwqlenRINEVLAQLGLDPNVAL--SSLSGGWLRKAALGRALVSNPRV 177
Cdd:cd03298 95 L----------SPGLK----LTAEDRQ-----------AIEVALARVGLAGLEKRlpGELSGGERQRVALARVLVRDKPV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 178 LLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03298 150 LLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-226 |
6.02e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.52 E-value: 6.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLD-----DGRI------IYEQDLIVARLQQD----- 74
Cdd:PRK14258 15 FYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVeffnqnIYERRVNLNRLRRQvsmvh 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 75 -PPRNVEGSVYDFVAEGIEeqaeyLKRYHdiSRLVMNDpseknlnelaKVQEQLDHHNLWqleNRINEVLAQLGLDpnva 153
Cdd:PRK14258 95 pKPNLFPMSVYDNVAYGVK-----IVGWR--PKLEIDD----------IVESALKDADLW---DEIKHKIHKSALD---- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 154 lssLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFN----GTIIFISHDRSFIrnmaTRIVDL 226
Cdd:PRK14258 151 ---LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHNLHQV----SRLSDF 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
330-472 |
6.19e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.21 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQ----------------HRAE 393
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQrpylplgtlreallypATAE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 394 LDPDKTVMDNLAEgkqevmVNgkprhvLGYLQDFLFHPKRAMtpvRALSGGERNRLLLARLFL-KPSnLLILDEPTNDLD 472
Cdd:COG4178 454 AFSDAELREALEA------VG------LGHLAERLDEEADWD---QVLSLGEQQRLAFARLLLhKPD-WLFLDEATSALD 517
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
332-473 |
6.28e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.11 E-value: 6.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAE---LDPDKTVMdnlAEG- 407
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARrlaLLPQHHLT---PEGi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 408 -KQEVMVNGKPRHV--LGYL-QDFLFHPKRAMT----------PVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK11231 92 tVRELVAYGRSPWLslWGRLsAEDNARVNQAMEqtrinhladrRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
334-497 |
6.57e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.27 E-value: 6.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 334 LVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV---GTKLEVAYFDQ------HRAELDPDKTVMDNL 404
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFerqSIKKDLCTYQKqlcfvgHRSGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 405 ---------AEGKQEVMVNGKprhvLGYLQDFlfhpkramtPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
Cdd:PRK13540 96 lydihfspgAVGITELCRLFS----LEHLIDY---------PCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|....*
gi 15830287 476 LELLEELIDSYQ---GTVLLVSHDR 497
Cdd:PRK13540 163 LLTIITKIQEHRakgGAVLLTSHQD 187
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-212 |
6.71e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.49 E-value: 6.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGLDDGRIiYEQDLIVARLQQdpprnvegsvydfvaegIEEQAEY 97
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAIL---AGLDDGSS-GEVSLVGQPLHQ-----------------MDEEARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 98 LKRYHDISRLVMNDPSEKNLNELAKVQ--EQLDHHNLWQLENRINEVLAQLGLDPNVAL--SSLSGGWLRKAALGRALVS 173
Cdd:PRK10584 84 KLRAKHVGFVFQSFMLIPTLNALENVElpALLRGESSRQSRNGAKALLEQLGLGKRLDHlpAQLSGGEQQRVALARAFNG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15830287 174 NPRVLLLDEPTNHLDIETIDWLEGFLKTFN----GTIIFISHD 212
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNrehgTTLILVTHD 206
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
329-472 |
8.16e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 62.80 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 329 VDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFDQH-RAEL------DP----- 396
Cdd:COG1101 16 VNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK-DVTKLPEYkRAKYigrvfqDPmmgta 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 397 -DKTVMDNLA----EGKQEVMVNGKPRHVLGYLQDFLFH-----PKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDE 466
Cdd:COG1101 95 pSMTIEENLAlayrRGKRRGLRRGLTKKRRELFRELLATlglglENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDE 174
|
....*.
gi 15830287 467 PTNDLD 472
Cdd:COG1101 175 HTAALD 180
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
319-472 |
9.00e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 61.49 E-value: 9.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQVDG----KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMlgqlqadSGRIHVGTklevayfdqhrael 394
Cdd:cd03232 3 VLTWKNLNYTVPVkggkRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVL-------AGRKTAGV-------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 dpdktvmdnlAEGkqEVMVNGKP-----RHVLGYLQDFLFHPK--------RAMTPVRALSGGERNRLLLA-RLFLKPSn 460
Cdd:cd03232 62 ----------ITG--EILINGRPldknfQRSTGYVEQQDVHSPnltvrealRFSALLRGLSVEQRKRLTIGvELAAKPS- 128
|
170
....*....|..
gi 15830287 461 LLILDEPTNDLD 472
Cdd:cd03232 129 ILFLDEPTSGLD 140
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
138-232 |
9.83e-11 |
|
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: 63.58 E-value: 9.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 138 RINEVLAQLGLDPnvaL-----SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIF 208
Cdd:COG4148 113 SFDEVVELLGIGH---LldrrpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLarkaEILPYLERLRDELDIPILY 189
|
90 100
....*....|....*....|....
gi 15830287 209 ISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG4148 190 VSHSLDEVARLADHVVLLEQGRVV 213
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
344-503 |
1.01e-10 |
|
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: 60.08 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 344 RGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVgtklevayfdqhraeLDPDKTVMDNLAEGKQEVMVNGKprhvlgy 423
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------IDGEDILEEVLDQLLLIIVGGKK------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 424 lqdflfhpkramtpvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVDNT 503
Cdd:smart00382 59 ---------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTT 123
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
321-495 |
1.02e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 61.39 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGqlqadsgriHVG---TKLEVAYFDQHRAELDPD 397
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG---------HPKyevTEGEILFKGEDITDLPPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 398 KTVMDNLAEGKQEvmvngkPRHVLGY-LQDFLfhpkRAMTpvRALSGGERNRL-LLARLFLKPSnLLILDEPTNDLDVET 475
Cdd:cd03217 73 ERARLGIFLAFQY------PPEIPGVkNADFL----RYVN--EGFSGGEKKRNeILQLLLLEPD-LAILDEPDSGLDIDA 139
|
170 180
....*....|....*....|...
gi 15830287 476 LELLEELIDSYQG---TVLLVSH 495
Cdd:cd03217 140 LRLVAEVINKLREegkSVLIITH 162
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
337-495 |
1.13e-10 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 61.74 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 337 DFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVA------YFDQHraELDPDKTVMDNLAE 406
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvdvTAAPPAdrpvsmLFQEN--NLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 407 GKQ-EVMVNGKPRH-VLGYLQDFLFHPKRAMTPvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELID 484
Cdd:cd03298 94 GLSpGLKLTAEDRQaIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170
....*....|....*
gi 15830287 485 SY----QGTVLLVSH 495
Cdd:cd03298 173 DLhaetKMTVLMVTH 187
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
332-537 |
1.17e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 64.74 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQHRAELDPD-----KTVMD 402
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDgvplVQYDHHYLHRQVALVGQEpvlfsGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 403 NLAEG-----KQEVMVNGKPRHVLGYLQDFlfhPKRAMTPV----RALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:TIGR00958 574 NIAYGltdtpDEEIMAAAKAANAHDFIMEF---PNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287 474 ETLELLEELIDSYQGTVLLVSHDRQFVDNtVTECwIFEGGGKIGRyvGGYHDA-RGQQEQYVALK 537
Cdd:TIGR00958 651 ECEQLLQESRSRASRTVLLIAHRLSTVER-ADQI-LVLKKGSVVE--MGTHKQlMEDQGCYKHLV 711
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
331-496 |
1.28e-10 |
|
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: 64.38 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 331 GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-----------------HVGtklevaYFDQH--- 390
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdreelgrHIG------YLPQDvel 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 ----------R-AELDPDKTVMDNLAEGKQEvMVNGKPrhvLGYlqDflfhpkramTPV----RALSGGERNRLLLAR-L 454
Cdd:COG4618 418 fdgtiaeniaRfGDADPEKVVAAAKLAGVHE-MILRLP---DGY--D---------TRIgeggARLSGGQRQRIGLARaL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15830287 455 FLKPSnLLILDEPTNDLDVETLELLEELIDSY---QGTVLLVSHD 496
Cdd:COG4618 483 YGDPR-LVVLDEPNSNLDDEGEAALAAAIRALkarGATVVVITHR 526
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
11-233 |
1.37e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 62.34 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLI----------VARLQQDPPrNV 79
Cdd:PRK11231 10 VGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVfLGDKPISmlssrqlarrLALLPQHHL-TP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 80 EG-SVYDFVAEGieeQAEYLKRYhdiSRLVMNDpseKNLNELAKVQEQLDHhnlwqLENRinevlaqlgldpnvALSSLS 158
Cdd:PRK11231 89 EGiTVRELVAYG---RSPWLSLW---GRLSAED---NARVNQAMEQTRINH-----LADR--------------RLTDLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 159 GGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDwLEGFLKTFNGTIIFISHDrsfiRNMATRIVD----LDRGK 230
Cdd:PRK11231 141 GGQRQRAFLAMVLAQDTPVVLLDEPTTYLDInhqvELMR-LMRELNTQGKTVVTVLHD----LNQASRYCDhlvvLANGH 215
|
...
gi 15830287 231 LVT 233
Cdd:PRK11231 216 VMA 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-236 |
1.38e-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: 61.52 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMK-ILNREQGLD--DGRIIY-EQDL-------IVARLQQDpprnvegs 82
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDaISGRVEGGGttSGQILFnGQPRkpdqfqkCVAYVRQD-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 83 vyDFVAEGIEeQAEYLkRYHDISRLvmndPSEKNLNELAKVQEQldhhnlwqlenrinEVLAQLGLDP--NVALSSLSGG 160
Cdd:cd03234 90 --DILLPGLT-VRETL-TYTAILRL----PRKSSDAIRKKRVED--------------VLLRDLALTRigGNLVKGISGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 161 WLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISHD-RSFIRNMATRIVDLDRGKLVtYPG 236
Cdd:cd03234 148 ERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLarrNRIVILTIHQpRSDLFRLFDRILLLSSGEIV-YSG 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
330-495 |
1.54e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 60.97 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI---------HVGTKLEVAYFDQHRAELDPDKTV 400
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVllnggpldfQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 MDNL----AEGKQEVMVNGKPRHVLGYLQDflfhpkramTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETL 476
Cdd:cd03231 91 LENLrfwhADHSDEQVEEALARVGLNGFED---------RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|..
gi 15830287 477 ELLEELIDSYQ---GTVLLVSH 495
Cdd:cd03231 162 ARFAEAMAGHCargGMVVLTTH 183
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-257 |
1.76e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.97 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFS---DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLI-----------VARLQQDPP 76
Cdd:PRK10790 346 VSFAyrdDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLsslshsvlrqgVAMVQQDPV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 77 RnVEGSVYDFVAEGieeqaeylkryHDISRLVMNDPSEK-NLNELAKvqeqldhhnlwQLENRINEVLAQLGldpnvalS 155
Cdd:PRK10790 426 V-LADTFLANVTLG-----------RDISEEQVWQALETvQLAELAR-----------SLPDGLYTPLGEQG-------N 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 156 SLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NGTIIFISHDRSFIRNmATRIVDLDRGKLVT 233
Cdd:PRK10790 476 NLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHRLSTIVE-ADTILVLHRGQAVE 554
|
250 260
....*....|....*....|....
gi 15830287 234 YpGNYDQYLLEKEEALRVEELQNA 257
Cdd:PRK10790 555 Q-GTHQQLLAAQGRYWQMYQLQLA 577
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
30-232 |
1.85e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.57 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 30 ERVCLVGRNGAGKST----LMKILNREQGLD-DGRIIYEQDlivaRLQQDPPRnvegsvydfvaegieeqaeylkryHDI 104
Cdd:PRK15134 313 ETLGLVGESGSGKSTtglaLLRLINSQGEIWfDGQPLHNLN----RRQLLPVR------------------------HRI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 105 sRLVMNDP-SEKN--LNELAKVQEQLDHH----NLWQLENRINEVLAQLGLDPNVAL---SSLSGGWLRKAALGRALVSN 174
Cdd:PRK15134 365 -QVVFQDPnSSLNprLNVLQIIEEGLRVHqptlSAAQREQQVIAVMEEVGLDPETRHrypAEFSGGQRQRIAIARALILK 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 175 PRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK15134 444 PSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-232 |
2.04e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 61.95 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN----REQGLD--DGRIIYEQDLIVARLQ-----QDPPRNVEGS- 82
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNglllPEAGTItvGGMVLSEETVWDVRRQvgmvfQNPDNQFVGAt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 83 VYDFVAEGIEEQAeylkryhdISRLVMndpseknlneLAKVQEQLDHHNLWQLENRinevlaqlglDPnvalSSLSGGWL 162
Cdd:PRK13635 99 VQDDVAFGLENIG--------VPREEM----------VERVDQALRQVGMEDFLNR----------EP----HRLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 163 RKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNmATRIVDLDRGKLV 232
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
318-472 |
2.19e-10 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 61.35 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 318 IVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAELDP 396
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 397 --------DKTVMDNLAEGKQevmvnGKPRHVLGYL------QDFLFH-PKRAMTPV----RALSGGERNRLLLARLFLK 457
Cdd:cd03252 81 vlqenvlfNRSIRDNIALADP-----GMSMERVIEAaklagaHDFISElPEGYDTIVgeqgAGLSGGQRQRIAIARALIH 155
|
170
....*....|....*
gi 15830287 458 PSNLLILDEPTNDLD 472
Cdd:cd03252 156 NPRILIFDEATSALD 170
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-237 |
2.65e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 61.68 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-----------IYEQDLIVARLQQDPPRNV-EGSVYDF 86
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrevnaenEKWVRSKVGLVFQDPDDQVfSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 87 VAEGIEEQaeylkryhdisRLvmnDPSEKNlnelAKVQEQLDHHNLWQLENRinevlaqlgldpnvALSSLSGGWLRKAA 166
Cdd:PRK13647 101 VAFGPVNM-----------GL---DKDEVE----RRVEEALKAVRMWDFRDK--------------PPYHLSYGQKKRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 167 LGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGKLVTYPGN 237
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNqgkTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
349-467 |
2.83e-10 |
|
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: 62.43 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 349 ALIGPNGCGKTTLLKLMLGQLQADSGRIHVGtklEVAYFDQ--------HR---------AELDPDKTVMDNLAEG-KQE 410
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLG---GEVLQDSargiflppHRrrigyvfqeARLFPHLSVRGNLLYGrKRA 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830287 411 VMVNGKPRH-----VLGyLQDFLfhpKRamtPVRALSGGERNRLLLAR-LFLKPSnLLILDEP 467
Cdd:COG4148 106 PRAERRISFdevveLLG-IGHLL---DR---RPATLSGGERQRVAIGRaLLSSPR-LLLMDEP 160
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
323-472 |
3.02e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.06 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 323 EDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------------HVGTKLEVAYFDQh 390
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplHARARRGIGYLPQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 RAELDPDKTVMDNLA---EGKQEVMVNGKPRHVLGYLQDF-LFHPKRAMTpvRALSGGERNRLLLARLFLKPSNLLILDE 466
Cdd:PRK10895 86 EASIFRRLSVYDNLMavlQIRDDLSAEQREDRANELMEEFhIEHLRDSMG--QSLSGGERRRVEIARALAANPKFILLDE 163
|
....*.
gi 15830287 467 PTNDLD 472
Cdd:PRK10895 164 PFAGVD 169
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
155-234 |
3.20e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.20 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 155 SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
....
gi 15830287 231 LVTY 234
Cdd:PRK11144 207 VKAF 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
317-468 |
3.59e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 62.73 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 317 KIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFDQHRA---- 392
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGE-PVRFRSPRDAqaag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 393 ------ELD--PDKTVMDNLAEGKQevmvngkPRHvlgylqdFLFHPKRAM------------------TPVRALSGGER 446
Cdd:COG1129 81 iaiihqELNlvPNLSVAENIFLGRE-------PRR-------GGLIDWRAMrrrarellarlgldidpdTPVGDLSVAQQ 146
|
170 180
....*....|....*....|..
gi 15830287 447 NRLLLARLFLKPSNLLILDEPT 468
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPT 168
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
319-499 |
4.10e-10 |
|
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: 60.06 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVC--YQvDGK---QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAE 393
Cdd:TIGR02211 1 LLKCENLGkrYQ-EGKldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 394 LD--------------PDKTVMDNLAE----GKQEVMvNGKPRHVLGYLQDFLFHpkRAMTPVRALSGGERNRLLLARLF 455
Cdd:TIGR02211 80 LRnkklgfiyqfhhllPDFTALENVAMplliGKKSVK-EAKERAYEMLEKVGLEH--RINHRPSELSGGERQRVAIARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15830287 456 LKPSNLLILDEPTNDLDVETLELLEELI---DSYQGT-VLLVSHDRQF 499
Cdd:TIGR02211 157 VNQPSLVLADEPTGNLDNNNAKIIFDLMlelNRELNTsFLVVTHDLEL 204
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
319-472 |
4.49e-10 |
|
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: 60.14 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQVDG--KQLV--KDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKL------EVAYF 387
Cdd:COG4181 8 IIELRGLTKTVGTgaGELTilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLaGQDLfaldedARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 388 dqhRAE----------LDPDKTVMDNlaegkqeVMV----NGKP------RHVLGY--LQDFLFH-PKRamtpvraLSGG 444
Cdd:COG4181 88 ---RARhvgfvfqsfqLLPTLTALEN-------VMLplelAGRRdararaRALLERvgLGHRLDHyPAQ-------LSGG 150
|
170 180
....*....|....*....|....*...
gi 15830287 445 ERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLD 178
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-233 |
7.33e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.41 E-value: 7.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQ-----DPPRNVeGSVYDFvaegiee 93
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikevkRLRKEI-GLVFQF------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 94 qAEYLKRYHDISRLVMNDPSekNLNElakvqeqldhhNLWQLENRINEVLAQLGLDPNVALSS---LSGGWLRKAALGRA 170
Cdd:PRK13645 99 -PEYQLFQETIEKDIAFGPV--NLGE-----------NKQEAYKKVPELLKLVQLPEDYVKRSpfeLSGGQKRRVALAGI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 171 LVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVT 233
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPkgeeDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
333-472 |
8.59e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 60.87 E-value: 8.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTK---------LEVAYFDQHRAeLDPDKTVMDN 403
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardRKVGFVFQHYA-LFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 404 LAEG---------------KQEV-----MVNgkprhvLGYLQDflFHPKRamtpvraLSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK10851 95 IAFGltvlprrerpnaaaiKAKVtqlleMVQ------LAHLAD--RYPAQ-------LSGGQKQRVALARALAVEPQILL 159
|
....*....
gi 15830287 464 LDEPTNDLD 472
Cdd:PRK10851 160 LDEPFGALD 168
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
318-472 |
1.19e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 318 IVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQL--QADSGRIHVGTKlevayfdqhraELD 395
Cdd:COG2401 29 IVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDN-----------QFG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 396 PDKTVMDNLAEgkqevmvNGKPRHVLGYLQD------FLFhpkraMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTN 469
Cdd:COG2401 98 REASLIDAIGR-------KGDFKDAVELLNAvglsdaVLW-----LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
...
gi 15830287 470 DLD 472
Cdd:COG2401 166 HLD 168
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-231 |
1.35e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 58.67 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLD---DGRIIYE-QDL-IVARLQQDPPRNVE-GSVYDFvaegi 91
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLG---GLDtptSGDVIFNgQPMsKLSSAAKAELRNQKlGFIYQF----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 92 eeqaeylkrYHDISrlvmndpsekNLNELAKVQEQL--DHHNLWQLENRINEVLAQLGLD--PNVALSSLSGGWLRKAAL 167
Cdd:PRK11629 96 ---------HHLLP----------DFTALENVAMPLliGKKKPAEINSRALEMLAAVGLEhrANHRPSELSGGERQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287 168 GRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFN---GT-IIFISHDRSFIRNMaTRIVDLDRGKL 231
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNrlqGTaFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
329-473 |
1.44e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 59.75 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 329 VDGkqlVkDFSaqVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQHR-----------AE 393
Cdd:COG4608 34 VDG---V-SFD--IRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqdiTGLSGRELRPLRrrmqmvfqdpyAS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 394 LDPDKTVMDNLAEGkqeVMVNGkprhvlgylqdfLFHPKRAMTPVRAL------------------SGGERNRLLLAR-L 454
Cdd:COG4608 108 LNPRMTVGDIIAEP---LRIHG------------LASKAERRERVAELlelvglrpehadryphefSGGQRQRIGIARaL 172
|
170
....*....|....*....
gi 15830287 455 FLKPSnLLILDEPTNDLDV 473
Cdd:COG4608 173 ALNPK-LIVCDEPVSALDV 190
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-232 |
1.48e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 59.65 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 26 IEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYEQDLIVARLQQD---PPRNVEGSVYDFV-AEGIEEQAEyl 98
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLN---GLlqpTSGTVTIGERVITAGKKNKklkPLRKKVGIVFQFPeHQLFEETVE-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 99 kryHDISRLVMN-DPSEKNLNELAKvqeqldhhnlwqlenrinEVLAQLGLDPNVALSS---LSGGWLRKAALGRALVSN 174
Cdd:PRK13634 105 ---KDICFGPMNfGVSEEDAKQKAR------------------EMIELVGLPEELLARSpfeLSGGQMRRVAIAGVLAME 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 175 PRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13634 164 PEVLVLDEPTAGLDpkgrKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
321-472 |
1.69e-09 |
|
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: 60.59 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLG--QLQADSGRI--HVG----------------- 379
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyHVAlcekcgyverpskvgep 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 380 --------TKLEVAYFD-----------------QHRAELDPDKTVMDNLAEGKQEVMVNGKP---RHVLGYLQDFLFHp 431
Cdd:TIGR03269 82 cpvcggtlEPEEVDFWNlsdklrrrirkriaimlQRTFALYGDDTVLDNVLEALEEIGYEGKEavgRAVDLIEMVQLSH- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15830287 432 kRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR03269 161 -RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD 200
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
333-501 |
1.73e-09 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 58.25 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYfdQHR--------AELDP---DKTVM 401
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY--EHKylhskvslVGQEPvlfARSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 402 DNLAEGKQ-----EVMVNGKPRHVLGYLQDFlfhPKRAMTPV----RALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03248 106 DNIAYGLQscsfeCVKEAAQKAHAHSFISEL---ASGYDTEVgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190
....*....|....*....|....*....|...
gi 15830287 473 VETLELLEELIdsYQG----TVLLVSHDRQFVD 501
Cdd:cd03248 183 AESEQQVQQAL--YDWperrTVLVIAHRLSTVE 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
341-631 |
1.75e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.11 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 341 QVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVgtKLEVAYFDQhRAELDPDkTVMDNLAEGKQevMVNGKPRHV 420
Cdd:TIGR00957 660 SIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM--KGSVAYVPQ-QAWIQND-SLRENILFGKA--LNEKYYQQV 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 421 L---GYLQDFLFHPKRAMTPVRA----LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQG----- 488
Cdd:TIGR00957 734 LeacALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGvlknk 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 489 TVLLVSHDRQFVDNtvTECWIFEGGGKIGRyVGGYHD---------------ARGQQEQYVALKQPAVKKNEEPAAPKAE 553
Cdd:TIGR00957 814 TRILVTHGISYLPQ--VDVIIVMSGGKISE-MGSYQEllqrdgafaeflrtyAPDEQQGHLEDSWTALVSGEGKEAKLIE 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 554 TVKRSSSKLSYKLQRELEQLPQLLEDLEAKLEAL-QTQVADASffsqphEQTQKVL-ADMAAAEQELEQAFerWEYLEAL 631
Cdd:TIGR00957 891 NGMLVTDVVGKQLQRQLSASSSDSGDQSRHHGSSaELQKAEAK------EETWKLMeADKAQTGQVELSVY--WDYMKAI 962
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-240 |
1.81e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 60.63 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreqgLddGRIIYEQDLIV-----------------ARLQQ 73
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL-----L--GFLPYQGSLKIngielreldpeswrkhlSWVGQ 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 74 DPpRNVEGSVYDFVAEGieeqaeylkrYHDISrlvmndpseknlnelakvQEQLDHhnlwQLEN-RINEVLAQL--GLDP 150
Cdd:PRK11174 431 NP-QLPHGTLRDNVLLG----------NPDAS------------------DEQLQQ----ALENaWVSEFLPLLpqGLDT 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 151 NVALSS--LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI---ETIdwLEGFLKTFNG-TIIFISHDRSFIRNMATrIV 224
Cdd:PRK11174 478 PIGDQAagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAhseQLV--MQALNAASRRqTTLMVTHQLEDLAQWDQ-IW 554
|
250
....*....|....*.
gi 15830287 225 DLDRGKLVTyPGNYDQ 240
Cdd:PRK11174 555 VMQDGQIVQ-QGDYAE 569
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-227 |
1.88e-09 |
|
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: 58.57 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 26 IEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNvEGSVYDFVaegieeqaeylkryHDIS 105
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADY-EGTVRDLL--------------SSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 106 RLVMNDPSEKNlnELAK-VQ-EQLdhhnlwqLENRINEvlaqlgldpnvalssLSGGWLRKAALGRALVSNPRVLLLDEP 183
Cdd:cd03237 87 KDFYTHPYFKT--EIAKpLQiEQI-------LDREVPE---------------LSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15830287 184 TNHLDIETIDWLEGFLKTF----NGTIIFISHDRSFIRNMATRIVDLD 227
Cdd:cd03237 143 SAYLDVEQRLMASKVIRRFaennEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-227 |
2.04e-09 |
|
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: 56.78 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYeqdlivarlqqdPPRNvegSVYdFVAeg 90
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALA---GLwpwGSGRIGM------------PEGE---DLL-FLP-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 91 ieeQAEYLKRyhdisrlvmndpseKNLnelakvQEQLDHhnLWQLEnrinevlaqlgldpnvalssLSGGWLRKAALGRA 170
Cdd:cd03223 71 ---QRPYLPL--------------GTL------REQLIY--PWDDV--------------------LSGGEQQRLAFARL 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 171 LVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHdRSFIRNMATRIVDLD 227
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-232 |
2.11e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 58.70 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDD-----------GRIIYEQDL--IVARLQ-----QD 74
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearvegevrlfGRNIYSPDVdpIEVRREvgmvfQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 75 PPRNVEGSVYDFVAEGIEeqaeylkryhdisrlvmndpseknLNELAKVQEQLDHHNLWQLENRI--NEVLAQLGLDPnv 152
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVK------------------------LNGLVKSKKELDERVEWALKKAAlwDEVKDRLNDYP-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 153 alSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD---IETIDWLEGFLKTfNGTIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:PRK14267 148 --SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-EYTIVLVTHSPAQAARVSDYVAFLYLG 224
|
...
gi 15830287 230 KLV 232
Cdd:PRK14267 225 KLI 227
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
330-472 |
3.03e-09 |
|
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: 57.27 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQAD---SGRIHVGTKLEVAYFDQHRAELdpdktvmdnlae 406
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEI------------ 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 407 gkqeVMVNGKPRHV--LGYLQDFLFHPK-RAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03233 86 ----IYVSEEDVHFptLTVRETLDFALRcKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
324-472 |
3.50e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.89 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 324 DVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKL---------EVAYFDQHRAeL 394
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRmndvppaerGVGMVFQSYA-L 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 DPDKTVMDNLAEG-------KQEvmVNGKPRHVLGYLQdfLFH-----PKramtpvrALSGGERNRLLLARLFLKPSNLL 462
Cdd:PRK11000 87 YPHLSVAENMSFGlklagakKEE--INQRVNQVAEVLQ--LAHlldrkPK-------ALSGGQRQRVAIGRTLVAEPSVF 155
|
170
....*....|
gi 15830287 463 ILDEPTNDLD 472
Cdd:PRK11000 156 LLDEPLSNLD 165
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-232 |
3.50e-09 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 58.04 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDliVARLQQDPPRNVEG----------------SV 83
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDgQD--IAAMSRKELRELRRkkismvfqsfallphrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 84 YDFVAEGIEeqaeylkryhdisrlvmndpseknlneLAKVQEQldhhnlwQLENRINEVLAQLGLDP--NVALSSLSGGW 161
Cdd:cd03294 120 LENVAFGLE---------------------------VQGVPRA-------EREERAAEALELVGLEGweHKYPDELSGGM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287 162 LRKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03294 166 QQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
335-500 |
3.90e-09 |
|
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: 57.34 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLE---------------VAYFDQHRAELDpdKT 399
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNEsepsfeatrsrnrysVAYAAQKPWLLN--AT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 400 VMDNLAEGKQEVMVNGKPRHVLGYLQ---DFLFHPKRAMTPVRA--LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
Cdd:cd03290 95 VEENITFGSPFNKQRYKAVTDACSLQpdiDLLPFGDQTEIGERGinLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190
....*....|....*....|....*....|.
gi 15830287 475 TLELLEEL-----IDSYQGTVLLVSHDRQFV 500
Cdd:cd03290 175 LSDHLMQEgilkfLQDDKRTLVLVTHKLQYL 205
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-234 |
4.22e-09 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 57.04 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLIVARLQ----------QDPPRnVEGSVyd 85
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIeIDGIDISTIPLEdlrssltiipQDPTL-FSGTI-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 86 fvaegieeqAEYLKRYhdisrlvmNDPSEKNLNELAKVQEQldhhnlwqlenrinevlaqlGLDpnvalssLSGGWLRKA 165
Cdd:cd03369 99 ---------RSNLDPF--------DEYSDEEIYGALRVSEG--------------------GLN-------LSQGQRQLL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 166 ALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFL-KTFNG-TIIFISHDRSFIRNMAtRIVDLDRGKLVTY 234
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIrEEFTNsTILTIAHRLRTIIDYD-KILVMDAGEVKEY 204
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
330-496 |
5.02e-09 |
|
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: 57.31 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFDQHR-----------AELDPDK 398
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE-DIREQDPVElrrkigyviqqIGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 399 TVMDNLAEGKQevmVNGKPRH-----VLGYLQDFLFHPK--RAMTPvRALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
Cdd:cd03295 91 TVEENIALVPK---LLKWPKEkirerADELLALVGLDPAefADRYP-HELSGGQQQRVGVARALAADPPLLLMDEPFGAL 166
|
170 180
....*....|....*....|....*....
gi 15830287 472 DVETLELLEELIDSYQ----GTVLLVSHD 496
Cdd:cd03295 167 DPITRDQLQEEFKRLQqelgKTIVFVTHD 195
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-232 |
5.66e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 57.69 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 3 LISMHGAWLSFSDA-PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN---REQ-------GLDDGRIIYEQDL--IVA 69
Cdd:PRK13644 1 MIRLENVSYSYPDGtPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNgllRPQkgkvlvsGIDTGDFSKLQGIrkLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 70 RLQQDPPRNvegsvydFVAEGIEEQAEYlkryhdisrlvmnDPSEKNLNELakvqeqldhhnlwQLENRINEVLAQLGLD 149
Cdd:PRK13644 81 IVFQNPETQ-------FVGRTVEEDLAF-------------GPENLCLPPI-------------EIRKRVDRALAEIGLE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 150 PNVALS--SLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET-IDWLEGFLKTFN--GTIIFISHDRSFIRNmATRIV 224
Cdd:PRK13644 128 KYRHRSpkTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEkgKTIVYITHNLEELHD-ADRII 206
|
....*...
gi 15830287 225 DLDRGKLV 232
Cdd:PRK13644 207 VMDRGKIV 214
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
333-472 |
5.76e-09 |
|
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: 57.16 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQHRA--ELDP---DKTVMDN 403
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDgvdiRDLNLRWLRSQIGlvSQEPvlfDGTIAEN 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 404 LAEGK-----QEVMVNGKprhvLGYLQDFLFH-PKRAMTPVRA----LSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03249 97 IRYGKpdatdEEVEEAAK----KANIHDFIMSlPDGYDTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-184 |
5.95e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.81 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVarlqQDPPRNVE 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT----DWQTAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 81 GSVYDFVAEGieeqaeylKRYhdISRLVMndpsEKNLNE----LAKVQEQLDHHNLWQLENRINEVLAQLGldpnvalSS 156
Cdd:PRK11614 79 REAVAIVPEG--------RRV--FSRMTV----EENLAMggffAERDQFQERIKWVYELFPRLHERRIQRA-------GT 137
|
170 180
....*....|....*....|....*...
gi 15830287 157 LSGGWLRKAALGRALVSNPRVLLLDEPT 184
Cdd:PRK11614 138 MSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
30-211 |
6.00e-09 |
|
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: 56.35 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 30 ERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQdlivARLQQDPPRNVEGSVYDFVAEGIE---EQAEYLKRYHDIsr 106
Cdd:cd03231 27 EALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG----GPLDFQRDSIARGLLYLGHAPGIKttlSVLENLRFWHAD-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 107 lvmndpseknlNELAKVQEQLDHHNLWQLENRinevlaqlgldpnvALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNH 186
Cdd:cd03231 101 -----------HSDEQVEEALARVGLNGFEDR--------------PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180
....*....|....*....|....*...
gi 15830287 187 LDIETIDWLEGFLKTF---NGTIIFISH 211
Cdd:cd03231 156 LDKAGVARFAEAMAGHcarGGMVVLTTH 183
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-232 |
6.16e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.81 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQdlivarlqqdpprnvegsvydfvaegieeqaeyl 98
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSG---------------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 99 kryHDISRLvmndpseKNlNELAKVQEQL-----DHHNLWQ--------------------LENRINEVLAQLGL---DP 150
Cdd:PRK10908 64 ---HDITRL-------KN-REVPFLRRQIgmifqDHHLLMDrtvydnvaipliiagasgddIRRRVSAALDKVGLldkAK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 151 NVALSsLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLD 227
Cdd:PRK10908 133 NFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLS 211
|
....*
gi 15830287 228 RGKLV 232
Cdd:PRK10908 212 DGHLH 216
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
319-472 |
6.21e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 57.55 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQV-DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFDQHRAEL--- 394
Cdd:PRK13636 5 ILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-PIDYSRKGLMKLres 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 ------DPDKTVMD------------NLAEGKQEV---MVNGKPRHVLGYLQDflfhpkramTPVRALSGGERNRLLLAR 453
Cdd:PRK13636 84 vgmvfqDPDNQLFSasvyqdvsfgavNLKLPEDEVrkrVDNALKRTGIEHLKD---------KPTHCLSFGQKKRVAIAG 154
|
170
....*....|....*....
gi 15830287 454 LFLKPSNLLILDEPTNDLD 472
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLD 173
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-473 |
7.32e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 7.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 17 PLLDNAELHIEDNERVCLVGRNGAGKS----TLMKILnrEQGldDGRIIYEQDLIVARLQQdpprnvegsvydfVAEGIE 92
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLL--EQA--GGLVQCDKMLLRRRSRQ-------------VIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 93 EQAEYLKRYH--DISrLVMNDPSeKNLNELAKVQEQLD-----HHNLWQLEN-----------RINEVLAQLGLDPNval 154
Cdd:PRK10261 93 QSAAQMRHVRgaDMA-MIFQEPM-TSLNPVFTVGEQIAesirlHQGASREEAmveakrmldqvRIPEAQTILSRYPH--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 155 sSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:PRK10261 168 -QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiqaQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 231 LV------------TYPgnYDQYLLEKeeALRVEELQNAEFDRKLAqeevWIRQGIKARRTrnegrvralkamrRERGER 298
Cdd:PRK10261 247 AVetgsveqifhapQHP--YTRALLAA--VPQLGAMKGLDYPRRFP----LISLEHPAKQE-------------PPIEQD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 299 REVMGTAKMQVEE-----ASRSGKIVFEMEDVcyqvdgkQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADS 373
Cdd:PRK10261 306 TVVDGEPILQVRNlvtrfPLRSGLLNRVTREV-------HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 374 GRIHV---------GTKLEVA------YFDQHRAELDPDKTVMDNLAEG-KQEVMVNGKP--RHVLGYLQDFLFHPKRAM 435
Cdd:PRK10261 379 GEIIFngqridtlsPGKLQALrrdiqfIFQDPYASLDPRQTVGDSIMEPlRVHGLLPGKAaaARVAWLLERVGLLPEHAW 458
|
490 500 510
....*....|....*....|....*....|....*....
gi 15830287 436 TPVRALSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDV 473
Cdd:PRK10261 459 RYPHEFSGGQRQRICIARaLALNP-KVIIADEAVSALDV 496
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
17-183 |
7.53e-09 |
|
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: 56.40 E-value: 7.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIIYEQDLIV-------ARLqqdpprnvegsvydf 86
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMI---VGLvkpDSGKILLDGQDITklpmhkrARL--------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 87 vaeGIEeqaeYLKRYHDI-SRLVMndpsEKNLNELAKVQEQLDhhnlWQLENRINEVLAQLGLDP---NVAlSSLSGGWL 162
Cdd:cd03218 76 ---GIG----YLPQEASIfRKLTV----EENILAVLEIRGLSK----KEREEKLEELLEEFHITHlrkSKA-SSLSGGER 139
|
170 180
....*....|....*....|.
gi 15830287 163 RKAALGRALVSNPRVLLLDEP 183
Cdd:cd03218 140 RRVEIARALATNPKFLLLDEP 160
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-244 |
7.83e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.86 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 26 IEDNERVCLVGRNGAGKSTLmkiLNREQGLDD--GRII-----------YEQDLIVARL--QQDPPRNVEgsVYdfvaeg 90
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTL---LARMAGLLPgsGSIQfagqpleawsaAELARHRAYLsqQQTPPFAMP--VF------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 91 ieeqaEYLKRYhdisrlvmndpseknlnelakvqeQLDHHNLWQLENRINEVLAQLGLDPNVA--LSSLSGG-W--LRKA 165
Cdd:PRK03695 88 -----QYLTLH------------------------QPDKTRTEAVASALNEVAEALGLDDKLGrsVNQLSGGeWqrVRLA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 166 A--LGRALVSNP--RVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISHDRSFIRNMATRIVDLDRGKLVTYpGNY 238
Cdd:PRK03695 139 AvvLQVWPDINPagQLLLLDEPMNSLDVAQQAALDRLLSELcqqGIAVVMSSHDLNHTLRHADRVWLLKQGKLLAS-GRR 217
|
....*.
gi 15830287 239 DQYLLE 244
Cdd:PRK03695 218 DEVLTP 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-225 |
9.30e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 56.71 E-value: 9.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLD-----DGRIIYEQDLIVAR--------------L 71
Cdd:PRK14239 13 VYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPrtdtvdlrkeigmvF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 72 QQdpPRNVEGSVYDFVAEGIEeqaeyLKRYHDISRLvmnDpseknlnelAKVQEQLDHHNLWqlenriNEVLAQLGldpN 151
Cdd:PRK14239 93 QQ--PNPFPMSIYENVVYGLR-----LKGIKDKQVL---D---------EAVEKSLKGASIW------DEVKDRLH---D 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 152 VALsSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD------IEtiDWLEGFLKTFngTIIFISHdrsfirNM--ATRI 223
Cdd:PRK14239 145 SAL-GLSGGQQQRVCIARVLATSPKIILLDEPTSALDpisagkIE--ETLLGLKDDY--TMLLVTR------SMqqASRI 213
|
..
gi 15830287 224 VD 225
Cdd:PRK14239 214 SD 215
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
12-214 |
9.81e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.42 E-value: 9.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGLD---DGRI-IYEQDLIVARLQQDPPRNVEGSVYDFV 87
Cdd:PRK11432 15 RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLV---AGLEkptEGQIfIDGEDVTHRSIQQRDICMVFQSYALFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 88 AEGIEEQAEYLKRYHDISRlvmndpSEKNlnelAKVQEQLDHHNLWQLENRInevlaqlgldpnvaLSSLSGGWLRKAAL 167
Cdd:PRK11432 92 HMSLGENVGYGLKMLGVPK------EERK----QRVKEALELVDLAGFEDRY--------------VDQISGGQQQRVAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15830287 168 GRALVSNPRVLLLDEPTNHLDI-------ETIDWLEgflKTFNGTIIFISHDRS 214
Cdd:PRK11432 148 ARALILKPKVLLFDEPLSNLDAnlrrsmrEKIRELQ---QQFNITSLYVTHDQS 198
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
321-496 |
9.96e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.58 E-value: 9.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKlMLGQLQADSGRIHVGTKLEvaYFDQH----RAELD- 395
Cdd:PRK14258 9 KVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLK-CLNRMNELESEVRVEGRVE--FFNQNiyerRVNLNr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 396 -----------PD---KTVMDNLAEGKQevMVNGKPRHVL----------GYLQDFLFHP--KRAMTpvraLSGGERNRL 449
Cdd:PRK14258 86 lrrqvsmvhpkPNlfpMSVYDNVAYGVK--IVGWRPKLEIddivesalkdADLWDEIKHKihKSALD----LSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15830287 450 LLAR-LFLKPsNLLILDEPTNDLDVETLELLEELIDSY----QGTVLLVSHD 496
Cdd:PRK14258 160 CIARaLAVKP-KVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHN 210
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
12-473 |
1.02e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.09 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE------------QDLIVARLQQDppRNV 79
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLgkevtfngpkssQEAGIGIIHQE--LNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 80 EGSVYdfVAEGIEEQAEYLKRYHDISRLVMNDPSEKnlnelakvqeqldhhnlwqlenrineVLAQLGL--DPNVALSSL 157
Cdd:PRK10762 91 IPQLT--IAENIFLGREFVNRFGRIDWKKMYAEADK--------------------------LLARLNLrfSSDKLVGEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 158 SGGWLRKAALGRALVSNPRVLLLDEPTNHL-DIETIDWLE--GFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGklvty 234
Cdd:PRK10762 143 SIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFRviRELKSQGRGIVYISHRLKEIFEICDDVTVFRDG----- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 235 pgnydQYLLEKE-EALRVEELQNAEFDRKLaqEEVWirqgikARRTRNEGRVRalkamrrergerrevmgtakMQVEEAS 313
Cdd:PRK10762 218 -----QFIAEREvADLTEDSLIEMMVGRKL--EDQY------PRLDKAPGEVR--------------------LKVDNLS 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 314 RSGkivfemedvcyqvdgkqlVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV------------GTK 381
Cdd:PRK10762 265 GPG------------------VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdghevvtrspqdGLA 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 382 LEVAYF--DQHRAELDPDKTVMDNLA--------------EGKQEVMVNGkprhvlgylqDF--LFHPKramTPVRA--- 440
Cdd:PRK10762 327 NGIVYIseDRKRDGLVLGMSVKENMSltalryfsraggslKHADEQQAVS----------DFirLFNIK---TPSMEqai 393
|
490 500 510
....*....|....*....|....*....|....*.
gi 15830287 441 --LSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDV 473
Cdd:PRK10762 394 glLSGGNQQKVAIARgLMTRP-KVLILDEPTRGVDV 428
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-237 |
1.03e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.41 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIY-EQDLI-------------VARLQQDP-----PRNVE 80
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlGKDLLgmkddewravrsdIQMIFQDPlaslnPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 81 GSVYdfvaegieeqAEYLKRYHdisrlvmndPseknlnELAKvQEqldhhnlwqLENRINEVLAQLGLDPNVA---LSSL 157
Cdd:PRK15079 118 GEII----------AEPLRTYH---------P------KLSR-QE---------VKDRVKAMMLKVGLLPNLInryPHEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 158 SGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIvdldrgkLVT 233
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVsiqaQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRV-------LVM 235
|
....
gi 15830287 234 YPGN 237
Cdd:PRK15079 236 YLGH 239
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
332-514 |
1.08e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 56.62 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-VGTKLEVAYFDQHRA--------------ELDP 396
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwRGEPLAKLNRAQRKAfrrdiqmvfqdsisAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 397 DKTVMDNLAEgkqevmvngkP-RHVLGYLQDFLFHPKRAMtpVRA--------------LSGGERNRLLLARLFLKPSNL 461
Cdd:PRK10419 105 RKTVREIIRE----------PlRHLLSLDKAERLARASEM--LRAvdlddsvldkrppqLSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 462 LILDEPTNDLDVETLELLEELIDSYQ---GTV-LLVSHDRQFVDNTVTECWIFEGGG 514
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKLQqqfGTAcLFITHDLRLVERFCQRVMVMDNGQ 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-246 |
1.08e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 56.78 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLIVARLQQDPPRNVEGSVYdfvaEGIEEQAEY 97
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgKPIDYSRKGLMKLRESVGMVF----QDPDNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 98 LKRYHDISRLVMNDPSEKNlnelaKVQEQLDHhnlwqlenrineVLAQLGLDP--NVALSSLSGGWLRKAALGRALVSNP 175
Cdd:PRK13636 98 ASVYQDVSFGAVNLKLPED-----EVRKRVDN------------ALKRTGIEHlkDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287 176 RVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVtYPGNYDQYLLEKE 246
Cdd:PRK13636 161 KVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGNPKEVFAEKE 234
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-234 |
1.17e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 56.24 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIyeqdlivarlqqdpprnVEGSV-----------Y 84
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIA---GIlepTSGRVE-----------------VNGRVsallelgagfhP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 85 DF-VAEGIeeqaeYLK-RYHDISRlvmndpseknlnelakvqeqldhhnlWQLENRINEVL--AQLG--LD-PnvaLSSL 157
Cdd:COG1134 102 ELtGRENI-----YLNgRLLGLSR--------------------------KEIDEKFDEIVefAELGdfIDqP---VKTY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 158 SGGwlRKAALGRALVS--NPRVLLLDEPTNHLDIE----TIDWLEGFLKTfNGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:COG1134 148 SSG--MRARLAFAVATavDPDILLVDEVLAVGDAAfqkkCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
...
gi 15830287 232 VTY 234
Cdd:COG1134 225 VMD 227
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
328-504 |
1.22e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 328 QVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH--VGTKLEVAYFDQHRAEldpDKTVMD--- 402
Cdd:PRK15064 10 QFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSldPNERLGKLRQDQFAFE---EFTVLDtvi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 403 ----NLAEGKQEV--------MVNGKPRHV-------------------------LGYLQDFLFHPKRAMTPvralsgGE 445
Cdd:PRK15064 87 mghtELWEVKQERdriyalpeMSEEDGMKVadlevkfaemdgytaearagelllgVGIPEEQHYGLMSEVAP------GW 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 446 RNRLLLAR-LFLKPsNLLILDEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVdNTV 504
Cdd:PRK15064 161 KLRVLLAQaLFSNP-DILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFL-NSV 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
19-239 |
1.23e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 56.33 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGL-----DDGRIIYEQDLIVARlQQDP-------------PRNVE 80
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAP-DVDPvevrrrigmvfqkPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 81 GSVYDFVAEGIEeqaeyLKRYhdisrlvmndpsEKNLNELakVQEQLDHHNLWqleNRINEVLAQLGLdpnvalsSLSGG 160
Cdd:PRK14243 105 KSIYDNIAYGAR-----INGY------------KGDMDEL--VERSLRQAALW---DEVKDKLKQSGL-------SLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 161 WLRKAALGRALVSNPRVLLLDEPTNHLD-IETIDwLEGFLKTFNG--TIIFISHdrsfirNM--ATRIVDL--------- 226
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDpISTLR-IEELMHELKEqyTIIIVTH------NMqqAARVSDMtaffnvelt 228
|
250
....*....|...
gi 15830287 227 DRGKLVTYPGNYD 239
Cdd:PRK14243 229 EGGGRYGYLVEFD 241
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
316-495 |
1.39e-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: 55.50 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 316 GKIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVgtklevayfDQHRAELD 395
Cdd:cd03369 5 GEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI---------DGIDISTI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 396 PDKTVMDNLAEGKQE-VMVNGKPRHVLG----YLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTND 470
Cdd:cd03369 76 PLEDLRSSLTIIPQDpTLFSGTIRSNLDpfdeYSDEEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180
....*....|....*....|....*..
gi 15830287 471 LDVETLELLEELI-DSYQG-TVLLVSH 495
Cdd:cd03369 156 IDYATDALIQKTIrEEFTNsTILTIAH 182
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
310-472 |
1.49e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 56.20 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 310 EEASRSGKIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMlgqlqadsGRIH---VGTKLE--V 384
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL--------NRMNdliPGARVEgeI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 385 AYFDQ--HRAELDPD-----------------KTVMDNLAEGkqeVMVNG-KPRHVLGYL-QDFLfhpKRAM-------- 435
Cdd:COG1117 74 LLDGEdiYDPDVDVVelrrrvgmvfqkpnpfpKSIYDNVAYG---LRLHGiKSKSELDEIvEESL---RKAAlwdevkdr 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15830287 436 --TPVRALSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLD 472
Cdd:COG1117 148 lkKSALGLSGGQQQRLCIARaLAVEPEVLL-MDEPTSALD 186
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-231 |
1.52e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.13 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIvaRLQQDppRNVEGSVYDfvaegiEEQAEY 97
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTI--NLVRD--KDGQLKVAD------KNQLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 98 LKryhdiSRLVMndpseknlnelakvqeQLDHHNLWQ----LENRINEVLAQLGLDPNVAL------------------- 154
Cdd:PRK10619 90 LR-----TRLTM----------------VFQHFNLWShmtvLENVMEAPIQVLGLSKQEAReravkylakvgideraqgk 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 155 --SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:PRK10619 149 ypVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
..
gi 15830287 230 KL 231
Cdd:PRK10619 229 KI 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-255 |
1.55e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 56.63 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYeqdLIVARLQQDPPRNVEGSVYDFV----------- 87
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEW---IFKDEKNKKKTKEKEKVLEKLViqktrfkkikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 88 AEGIEEQ-------AEYLKRYHDISRLVMNDP-----SEKNLNELAKvqeqldhhnlwqlenrinEVLAQLGLDPNVALS 155
Cdd:PRK13651 100 IKEIRRRvgvvfqfAEYQLFEQTIEKDIIFGPvsmgvSKEEAKKRAA------------------KYIELVGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 156 S---LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIE-TIDWLEGF--LKTFNGTIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:PRK13651 162 SpfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFdnLNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
250 260
....*....|....*....|....*.
gi 15830287 230 KLVTYPGNYDqyLLEKEEALRVEELQ 255
Cdd:PRK13651 242 KIIKDGDTYD--ILSDNKFLIENNME 265
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-229 |
1.63e-08 |
|
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: 55.55 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLmkiLNREQGLD---DGRIIYEQDLIVArlqQDPPRNVEGSVYDFVAegieeqa 95
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTL---LNLISGLAqptSGGVILEGKQITE---PGPDRMVVFQNYSLLP------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 96 eYLKRYHDISrlvmndpseknlneLAkVQEQLDHHNLWQLENRINEVLAQLGLD--PNVALSSLSGGWLRKAALGRALVS 173
Cdd:TIGR01184 68 -WLTVRENIA--------------LA-VDRVLPDLSKSERRAIVEEHIALVGLTeaADKRPGQLSGGMKQRVAIARALSI 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 174 NPRVLLLDEPTNHLDIETIDWL-EGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:TIGR01184 132 RPKVLLLDEPFGALDALTRGNLqEELMQIWEEhrvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
319-496 |
1.66e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.28 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQVDGKQ---LVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAEL 394
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 -----DPDK-----TVMDNLAEGKQ------EVMVNgKPRHVLGY--LQDFlfhpkRAMTPVRaLSGGERNRLLLARLFL 456
Cdd:PRK13650 84 gmvfqNPDNqfvgaTVEDDVAFGLEnkgiphEEMKE-RVNEALELvgMQDF-----KEREPAR-LSGGQKQRVAIAGAVA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15830287 457 KPSNLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIkgirDDYQMTVISITHD 200
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-232 |
2.12e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 55.62 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 26 IEDNERVCLVGRNGAGKSTLmkiLNREQGLDD--GRIIYEQDLI-------VARL------QQDPPRNVegSVYdfvaeg 90
Cdd:COG4138 19 VNAGELIHLIGPNGAGKSTL---LARMAGLLPgqGEILLNGRPLsdwsaaeLARHraylsqQQSPPFAM--PVF------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 91 ieeqaEYLKRYhdisrlvmndpseknlnelakvqeQLDHHNLWQLENRINEVLAQLGLDPNVA--LSSLSGG-W--LRKA 165
Cdd:COG4138 88 -----QYLALH------------------------QPAGASSEAVEQLLAQLAEALGLEDKLSrpLTQLSGGeWqrVRLA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 166 A----LGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG4138 139 AvllqVWPTINPEGQLLLLDEPMNSLDVAQQAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-232 |
2.34e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.99 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVE---GSVYDFVAEGIEEQA 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRkkvSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 96 eylkryhdisrlVMNDPSEKNLNELAKVQEQLDHHNLWqlenrinevLAQLGLDPNVALSS---LSGGWLRKAALGRALV 172
Cdd:PRK13641 103 ------------VLKDVEFGPKNFGFSEDEAKEKALKW---------LKKVGLSEDLISKSpfeLSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830287 173 SNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
137-228 |
2.36e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 54.80 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 137 NRINEVLAQLGL------DPNvalsSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGF----LKTFNGTI 206
Cdd:COG4136 112 ARVEQALEEAGLagfadrDPA----TLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPA 187
|
90 100
....*....|....*....|..
gi 15830287 207 IFISHDRSFIRNmATRIVDLDR 228
Cdd:COG4136 188 LLVTHDEEDAPA-AGRVLDLGN 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
335-496 |
2.50e-08 |
|
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: 55.16 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQ----HRAELDPDKTVMDNLAEGKQ 409
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQITEPGPDRmvvfQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 410 EVMVN---GKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLELLEELI-- 483
Cdd:TIGR01184 81 RVLPDlskSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARaLSIRPK-VLLLDEPFGALDALTRGNLQEELmq 159
|
170
....*....|....*
gi 15830287 484 --DSYQGTVLLVSHD 496
Cdd:TIGR01184 160 iwEEHRVTVLMVTHD 174
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
304-495 |
2.70e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.95 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 304 TAKMQVEEASrsGKIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKL 382
Cdd:PRK11176 330 EGKRVIERAK--GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdGHDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 383 E----------VAYFDQHrAELDPDkTVMDNLAEGKQEVMVNGKPRHV--LGYLQDFLFHPKRAMTPV-----RALSGGE 445
Cdd:PRK11176 408 RdytlaslrnqVALVSQN-VHLFND-TIANNIAYARTEQYSREQIEEAarMAYAMDFINKMDNGLDTVigengVLLSGGQ 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15830287 446 RNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQG--TVLLVSH 495
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH 537
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
330-472 |
2.75e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 55.89 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAyfDQHR-----AE--LDPDKTVM 401
Cdd:COG4152 12 GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdGEPLDPE--DRRRigylpEErgLYPKMKVG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 402 DNL-----------AEGKQEVMVngkprhvlgYLQDF-LfhPKRAMTPVRALSGGERNRL-LLARLFLKPSnLLILDEPT 468
Cdd:COG4152 90 EQLvylarlkglskAEAKRRADE---------WLERLgL--GDRANKKVEELSKGNQQKVqLIAALLHDPE-LLILDEPF 157
|
....
gi 15830287 469 NDLD 472
Cdd:COG4152 158 SGLD 161
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
316-495 |
3.03e-08 |
|
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: 54.42 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 316 GKIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTkLEVAYFDQH----- 390
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDG-VDISKIGLHdlrsr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 ---------------RAELDP-----DKTVMDNLAEGKQEVMVNGKPrhvlGYLQdflfhpkramTPVRA----LSGGER 446
Cdd:cd03244 80 isiipqdpvlfsgtiRSNLDPfgeysDEELWQALERVGLKEFVESLP----GGLD----------TVVEEggenLSVGQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15830287 447 NRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY--QGTVLLVSH 495
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAH 196
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
344-497 |
3.38e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.88 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 344 RGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFD-----QHRAeLDPDKTVMDNLAEG------- 407
Cdd:PRK11432 31 QGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgedvTHRSIQQRDicmvfQSYA-LFPHMSLGENVGYGlkmlgvp 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 408 KQEVMVNGKPRHVLGYLQDFlfhPKRAmtpVRALSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLDVETLELLEELIDSY 486
Cdd:PRK11432 110 KEERKQRVKEALELVDLAGF---EDRY---VDQISGGQQQRVALARaLILKPKVLL-FDEPLSNLDANLRRSMREKIREL 182
|
170
....*....|....*
gi 15830287 487 QG----TVLLVSHDR 497
Cdd:PRK11432 183 QQqfniTSLYVTHDQ 197
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-232 |
3.43e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.10 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQG-----------LDDGRIIYE-QDLIVAR----LQQD 74
Cdd:PRK14271 29 LGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyrysgdvLLGGRSIFNyRDVLEFRrrvgMLFQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 75 PPRNVEGSVYDFVAEGIeeqaeylkRYHdisRLVmndpSEKNLNELAkvQEQLDHHNLWQ-LENRINEvlaqlgldpnvA 153
Cdd:PRK14271 109 RPNPFPMSIMDNVLAGV--------RAH---KLV----PRKEFRGVA--QARLTEVGLWDaVKDRLSD-----------S 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 154 LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG--TIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK14271 161 PFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDRAALFFDGRL 240
|
.
gi 15830287 232 V 232
Cdd:PRK14271 241 V 241
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
318-513 |
3.58e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.12 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 318 IVFEMEDVCYQVD---GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHraEL 394
Cdd:PRK13643 2 IKFEKVNYTYQPNspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQK--EI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 DP-----------------DKTVMDNLAEGKQEVMVN--------GKPRHVLGYLQDFLfhpkrAMTPVRaLSGGERNRL 449
Cdd:PRK13643 80 KPvrkkvgvvfqfpesqlfEETVLKDVAFGPQNFGIPkekaekiaAEKLEMVGLADEFW-----EKSPFE-LSGGQMRRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 450 LLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQ---GTVLLVSHDRQFVDNTVTECWIFEGG 513
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHqsgQTVVLVTHLMDDVADYADYVYLLEKG 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
332-495 |
3.78e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 55.05 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGtklevayfdqhraELDP-DKTVmdNLAEGKQE 410
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID-------------GVDItDKKV--KLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 411 V-MVNGKPRHVL---GYLQDFLFHP--------------KRAMTPVR------------ALSGGERNRLLLARLF-LKPS 459
Cdd:PRK13637 85 VgLVFQYPEYQLfeeTIEKDIAFGPinlglseeeienrvKRAMNIVGldyedykdkspfELSGGQKRRVAIAGVVaMEPK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15830287 460 nLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSH 495
Cdd:PRK13637 165 -ILILDEPTAGLDPKGRDEILNKIkelhKEYNMTIILVSH 203
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-212 |
4.06e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.12 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLI-----------VARLQQDPPRN-VEG 81
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteenvwdirhkIGMVFQNPDNQfVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 82 SVYDFVAEGIEEQAeylkryhdisrlvmndpseknlnelakvqeqLDHHnlwQLENRINEVLAQLGL------DPnvalS 155
Cdd:PRK13650 98 TVEDDVAFGLENKG-------------------------------IPHE---EMKERVNEALELVGMqdfkerEP----A 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 156 SLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHD 212
Cdd:PRK13650 140 RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-224 |
4.58e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 54.48 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSF----SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlivaRLQQDPp 76
Cdd:COG4525 1 MSMLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI---------TLDGVP- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 77 rnVEG------------------SVYDFVAEGieeqaeyLKryhdisrlvmndpseknlneLAKVQEQldhhnlwQLENR 138
Cdd:COG4525 71 --VTGpgadrgvvfqkdallpwlNVLDNVAFG-------LR--------------------LRGVPKA-------ERRAR 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 139 INEVLAQLGLD--PNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFL----KTFNGTIIFISHD 212
Cdd:COG4525 115 AEELLALVGLAdfARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLldvwQRTGKGVFLITHS 194
|
250
....*....|..
gi 15830287 213 RSFIRNMATRIV 224
Cdd:COG4525 195 VEEALFLATRLV 206
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-188 |
4.75e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.21 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-NReqglddgriiyeqdlIVARLQQDPPRNVEGSVYDfvaegieeqae 96
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFR---------------SPKGVKGSGSVLLNGMPID----------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 97 yLKRYHDISRLVMNDpsEKNLNELAkVQEQL---------DHHNLWQLENRINEVLAQLGL---------DPNvALSSLS 158
Cdd:TIGR00955 94 -AKEMRAISAYVQQD--DLFIPTLT-VREHLmfqahlrmpRRVTKKEKRERVDEVLQALGLrkcantrigVPG-RVKGLS 168
|
170 180 190
....*....|....*....|....*....|
gi 15830287 159 GGWLRKAALGRALVSNPRVLLLDEPTNHLD 188
Cdd:TIGR00955 169 GGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
331-473 |
5.89e-08 |
|
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: 54.48 E-value: 5.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 331 GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HVGtklEVAYFDQHrAELDPDkTVMDNLAEGKQ 409
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIkHSG---RISFSSQF-SWIMPG-TIKENIIFGVS 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 410 evMVNGKPRHVLGYLQ---DFLFHPKRAMTPVR----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03291 124 --YDEYRYKSVVKACQleeDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
10-242 |
6.67e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.19 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 10 WLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRII-----YEQDLIVARLQQDPPRNVEG--S 82
Cdd:PTZ00265 1175 YISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfkneHTNDMTNEQDYQGDEEQNVGmkN 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 83 VYDFVAEGIEEQAEYLKRYHDISRLVMN--DPSEKNLNEL----AKVQEQLDHHNLWQLEN------------------- 137
Cdd:PTZ00265 1255 VNEFSLTKEGGSGEDSTVFKNSGKILLDgvDICDYNLKDLrnlfSIVSQEPMLFNMSIYENikfgkedatredvkrackf 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 138 -RINEVLAQL--GLDPNVAL--SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEgflKTF-------NGT 205
Cdd:PTZ00265 1335 aAIDEFIESLpnKYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE---KTIvdikdkaDKT 1411
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15830287 206 IIFISHDRSFIRNMATRIV--DLDR-GKLVTYPGNYDQYL 242
Cdd:PTZ00265 1412 IITIAHRIASIKRSDKIVVfnNPDRtGSFVQAHGTHEELL 1451
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
327-498 |
6.92e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 53.67 E-value: 6.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 327 YQvDGK---QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGR-IHVGTKL--------------EVAYFD 388
Cdd:PRK11629 15 YQ-EGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDvIFNGQPMsklssaakaelrnqKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 389 QHRaELDPDKTVMDNLAE-----GKQEVMVNGKPRHVLGYLQdflfHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK11629 94 QFH-HLLPDFTALENVAMplligKKKPAEINSRALEMLAAVG----LEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 15830287 464 LDEPTNDLDVETLE---LLEELIDSYQGTV-LLVSHDRQ 498
Cdd:PRK11629 169 ADEPTGNLDARNADsifQLLGELNRLQGTAfLVVTHDLQ 207
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
312-472 |
6.95e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 55.60 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 312 ASRSGKIVFEmeDVCYQVDGK-QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKL-EVAyfd 388
Cdd:COG5265 352 VVGGGEVRFE--NVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIdGQDIrDVT--- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 389 QH--RAELD--PDKTVM------DNLAEGK-----QEVmvngkpRHV--LGYLQDFLFH-PKRAMTPV--RA--LSGGER 446
Cdd:COG5265 427 QAslRAAIGivPQDTVLfndtiaYNIAYGRpdaseEEV------EAAarAAQIHDFIESlPDGYDTRVgeRGlkLSGGEK 500
|
170 180
....*....|....*....|....*.
gi 15830287 447 NRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALD 526
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-232 |
7.21e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 54.42 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLddgriiyeqdlivaRLQQDPPRNVegsvydFVAEGIEE 93
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLIN---GL--------------LLPDDNPNSK------ITVDGITL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 94 QAEYLKRYHDISRLVMNDPSEKNLNelAKVQEQLdhhnLWQLENR----------INEVLAQLG-LD-PNVALSSLSGGW 161
Cdd:PRK13640 75 TAKTVWDIREKVGIVFQNPDNQFVG--ATVGDDV----AFGLENRavprpemikiVRDVLADVGmLDyIDSEPANLSGGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287 162 LRKAALGRALVSNPRVLLLDEPTNHLDIE----TIDWLEGFLKTFNGTIIFISHDRSFIrNMATRIVDLDRGKLV 232
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAgkeqILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLL 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
318-500 |
7.57e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.34 E-value: 7.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 318 IVFEMEDVCYqVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HVGTKL---EVAY---- 386
Cdd:PRK10908 2 IRFEHVSKAY-LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsgHDITRLknrEVPFlrrq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 387 ----FDQHraELDPDKTVMDNLAegkQEVMVNGKP-----RHVLGYLQDFLFHPKRAMTPVRaLSGGERNRLLLARLFLK 457
Cdd:PRK10908 81 igmiFQDH--HLLMDRTVYDNVA---IPLIIAGASgddirRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15830287 458 PSNLLILDEPTNDLDVETLELLEELIDSYQG---TVLLVSHDRQFV 500
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLI 200
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-183 |
7.82e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 53.49 E-value: 7.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTL--MKIlnreqGL---DDGRI-IYEQDL------IV 68
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTfyMIV-----GLvkpDSGRIfLDGEDIthlpmhKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 69 AR-----LQQDPprnvegSVydF----VAEGIeeqaeylkryhdisRLVMndpseknlnELAKVQEQldhhnlwQLENRI 139
Cdd:COG1137 76 ARlgigyLPQEA------SI--FrkltVEDNI--------------LAVL---------ELRKLSKK-------EREERL 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15830287 140 NEVLAQLGLDP--NVALSSLSGGWLRKAALGRALVSNPRVLLLDEP 183
Cdd:COG1137 118 EELLEEFGITHlrKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
331-520 |
8.23e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.30 E-value: 8.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 331 GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAyFDQHRAELD-------------PD 397
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-EMR-FASTTAALAagvaiiyqelhlvPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 398 KTVMDNLAEGK---QEVMVNGKP--RHVLGYLQ--DFLFHPKramTPVRALSGGERNRLLLARLFLKPSNLLILDEPTND 470
Cdd:PRK11288 94 MTVAENLYLGQlphKGGIVNRRLlnYEAREQLEhlGVDIDPD---TPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15830287 471 LDVETLELLEELIDSY--QGTVLL-VSHDRQFVDNTVTECWIFegggKIGRYV 520
Cdd:PRK11288 171 LSAREIEQLFRVIRELraEGRVILyVSHRMEEIFALCDAITVF----KDGRYV 219
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
332-513 |
8.37e-08 |
|
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: 54.04 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQHRAEL-----------DP 396
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgqdlYQLDRKQRRAFRRDVqlvfqdspsavNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 397 DKTVMDNLAEGKQEVM---VNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLAR-LFLKPsNLLILDEPTNDLD 472
Cdd:TIGR02769 104 RMTVRQIIGEPLRHLTsldESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARaLAVKP-KLIVLDEAVSNLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15830287 473 VETLELLEELIDSYQ---GTV-LLVSHDRQFVDNTVTECWIFEGG 513
Cdd:TIGR02769 183 MVLQAVILELLRKLQqafGTAyLFITHDLRLVQSFCQRVAVMDKG 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
318-472 |
8.67e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 53.99 E-value: 8.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 318 IVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklevaYFDQHRAELD-- 395
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI---------FYNNQAITDDnf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 396 -------------PDK-----TVMDNLAEGKQEVMVNGKPRH--VLGYLQDFLFHPKRAMTPvRALSGGERNRLLLAR-L 454
Cdd:PRK13648 79 eklrkhigivfqnPDNqfvgsIVKYDVAFGLENHAVPYDEMHrrVSEALKQVDMLERADYEP-NALSGGQKQRVAIAGvL 157
|
170
....*....|....*...
gi 15830287 455 FLKPSnLLILDEPTNDLD 472
Cdd:PRK13648 158 ALNPS-VIILDEATSMLD 174
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
331-473 |
8.94e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 8.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 331 GKQLV-KDFSAQVLRGDKIALIGPNGCGKTTLLK----LML---GQLQADSGRIHVGTKLEVAY---FDQHRAELDPDKT 399
Cdd:PRK10253 18 GKYTVaENLTVEIPDGHFTAIIGPNGCGKSTLLRtlsrLMTpahGHVWLDGEHIQHYASKEVARrigLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 400 VMDNLAEGK-------------QEVMVNGKPRHV-LGYLqdflfhpkrAMTPVRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:PRK10253 98 VQELVARGRyphqplftrwrkeDEEAVTKAMQATgITHL---------ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
....*...
gi 15830287 466 EPTNDLDV 473
Cdd:PRK10253 169 EPTTWLDI 176
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
321-376 |
1.02e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 53.62 E-value: 1.02e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
Cdd:PRK11831 9 DMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
337-473 |
1.04e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.39 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 337 DFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV----GTKLEVA----------------YFDQHRAE-LD 395
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdGQLRDLYalseaerrrllrtewgFVHQHPRDgLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 396 PDKTVMDNLAEgkqEVMVNGKpRH-------VLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPT 468
Cdd:PRK11701 104 MQVSAGGNIGE---RLMAVGA-RHygdiratAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPT 179
|
....*
gi 15830287 469 NDLDV 473
Cdd:PRK11701 180 GGLDV 184
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
30-232 |
1.26e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 30 ERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQ---DLIVARLQQDPPRNVEGSVYDFVAEgieeqaeyLKRYHDISR 106
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqriDTLSPGKLQALRRDIQFIFQDPYAS--------LDPRQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 107 LVMndpseknlnelakvqEQLDHHNLWQLE---NRINEVLAQLGLDPNVALS---SLSGGWLRKAALGRALVSNPRVLLL 180
Cdd:PRK10261 423 SIM---------------EPLRVHGLLPGKaaaARVAWLLERVGLLPEHAWRyphEFSGGQRQRICIARALALNPKVIIA 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287 181 DEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK10261 488 DEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
15-232 |
1.26e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.59 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVE---GSVYDFVAEGI 91
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRkkvGLVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 92 EEQAeylkryhdisrlVMNDPSEKNLNELAKVQEQldhhnlwqlENRINEVLAQLGLDPNVALSS---LSGGWLRKAALG 168
Cdd:PRK13649 99 FEET------------VLKDVAFGPQNFGVSQEEA---------EALAREKLALVGISESLFEKNpfeLSGGQMRRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 169 RALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsgmTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
34-473 |
1.31e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.53 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 34 LVGRNGAGKSTLMKILNREQGLDDGRIiyeqdLIVARLQQdpprnvEGSVYDFVAEGIE--EQaeylkryhdisrlvmnd 111
Cdd:PRK11288 35 LMGENGAGKSTLLKILSGNYQPDAGSI-----LIDGQEMR------FASTTAALAAGVAiiYQ----------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 112 pseknlnELAKVQEQLDHHNLW--QLENR---------INEVLAQLG-----LDPNVALSSLSGGWLRKAALGRALVSNP 175
Cdd:PRK11288 87 -------ELHLVPEMTVAENLYlgQLPHKggivnrrllNYEAREQLEhlgvdIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 176 RVLLLDEPTNHLDIETIDWLegF-----LKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV-TYPgnydqylleKEEAL 249
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQL--FrvireLRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVaTFD---------DMAQV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 250 RVEELQNAEFDRKLaqeevwirQGIKARRTRNEGRVRalkamrrergerrevmgtakMQVEEasrsgkivfemedvcyqV 329
Cdd:PRK11288 229 DRDQLVQAMVGREI--------GDIYGYRPRPLGEVR--------------------LRLDG-----------------L 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklevaYFDQHRAELdpdKTVMDNLAEG-- 407
Cdd:PRK11288 264 KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQV---------YLDGKPIDI---RSPRDAIRAGim 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 408 ------KQEVMVNGKP----------RHVLGYlqDFLFHPKR------------------AMTPVRALSGGERNRLLLAR 453
Cdd:PRK11288 332 lcpedrKAEGIIPVHSvadninisarRHHLRA--GCLINNRWeaenadrfirslniktpsREQLIMNLSGGNQQKAILGR 409
|
490 500
....*....|....*....|
gi 15830287 454 LFLKPSNLLILDEPTNDLDV 473
Cdd:PRK11288 410 WLSEDMKVILLDEPTRGIDV 429
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-234 |
1.49e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.95 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 18 LLDNAELHIEDNERVCLVGRNGAGKST----LMKILNREQG--LDDGRIIYEQDLIVARLQ-----QDPPRnVEGSvydf 86
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINESAEGeiIIDGLNIAKIGLHDLRFKitiipQDPVL-FSGS---- 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 87 vaegieeqaeylkryhdisrLVMN-DPSEKNLNELAKVQEQLDHhnlwqLENRINEVLAQLGLDPNVALSSLSGGWLRKA 165
Cdd:TIGR00957 1376 --------------------LRMNlDPFSQYSDEEVWWALELAH-----LKTFVSALPDKLDHECAEGGENLSVGQRQLV 1430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 166 ALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKT-FNG-TIIFISHDRSFIRNMaTRIVDLDRGKLVTY 234
Cdd:TIGR00957 1431 CLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTqFEDcTVLTIAHRLNTIMDY-TRVIVLDKGEVAEF 1500
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
333-472 |
1.50e-07 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 52.71 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKlMLGQLQ-ADSGRIHVGTklevAYFD--QHRAE---------------- 393
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLEtPDSGQLNIAG----HQFDfsQKPSEkairllrqkvgmvfqq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 394 --LDPDKTVMDNLAEG--------KQEVMvnGKPRHVLGYLQdflFHPKRAMTPVRaLSGGERNRLLLAR-LFLKPSNLL 462
Cdd:COG4161 91 ynLWPHLTVMENLIEApckvlglsKEQAR--EKAMKLLARLR---LTDKADRFPLH-LSGGQQQRVAIARaLMMEPQVLL 164
|
170
....*....|
gi 15830287 463 iLDEPTNDLD 472
Cdd:COG4161 165 -FDEPTAALD 173
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
19-224 |
1.64e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIE-----DNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyEQDLIVARLQQDPPRNVEGSVYDFvaegiee 93
Cdd:PRK13409 350 LGDFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISYKPQYIKPDYDGTVEDL------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 94 qaeylkryhdisrlvmndpseknlneLAKVQEQLDHHNLWqlenriNEVLAQLGLDP--NVALSSLSGGWLRKAALGRAL 171
Cdd:PRK13409 421 --------------------------LRSITDDLGSSYYK------SEIIKPLQLERllDKNVKDLSGGELQRVAIAACL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 172 VSNPRVLLLDEPTNHLDIE-------TIdwlEGFLKTFNGTIIFISHDRSFIRNMATRIV 224
Cdd:PRK13409 469 SRDADLYLLDEPSAHLDVEqrlavakAI---RRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
342-498 |
1.79e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.47 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 342 VLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAELD--------------PDKTVMDN---- 403
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRakhvgfvfqsfmliPTLNALENvelp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 404 -LAEGKQEVMVNGKPRHVLGY--LQDFLFHpkramTPVRaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:PRK10584 113 aLLRGESSRQSRNGAKALLEQlgLGKRLDH-----LPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIA 186
|
170 180
....*....|....*....|..
gi 15830287 481 ELIDS----YQGTVLLVSHDRQ 498
Cdd:PRK10584 187 DLLFSlnreHGTTLILVTHDLQ 208
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
330-473 |
1.82e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.96 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLE-------VAYFDQHRaELDPDKTVM 401
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlGQPTRqalqknlVAYVPQSE-EVDWSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 402 dnlaegKQEVMVNGKPRHvLGYLQDFLFHPKRAMTPVRA--------------LSGGERNRLLLARLFLKPSNLLILDEP 467
Cdd:PRK15056 97 ------VEDVVMMGRYGH-MGWLRRAKKRDRQIVTAALArvdmvefrhrqigeLSGGQKKRVFLARAIAQQGQVILLDEP 169
|
....*.
gi 15830287 468 TNDLDV 473
Cdd:PRK15056 170 FTGVDV 175
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-232 |
1.94e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 53.88 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLIVARLQQDPPRNVEGsvydfvaegiEEQAEYLKR 100
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLID-GVDIAKISDAELREVRR----------KKIAMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 101 YHDISRLVMNDPSEKNLnELAKVQEQldhhnlwQLENRINEVLAQLGLDpNVAL---SSLSGGWLRKAALGRALVSNPRV 177
Cdd:PRK10070 115 FALMPHMTVLDNTAFGM-ELAGINAE-------ERREKALDALRQVGLE-NYAHsypDELSGGMRQRVGLARALAINPDI 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 178 LLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK10070 186 LLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
321-468 |
1.99e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 52.43 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFDQHR-AELD---- 395
Cdd:COG4674 12 YVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGT-DLTGLDEHEiARLGigrk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 396 -------PDKTVMDNLaegkqEVMVNGK--PRHVLGY------------------LQDflfhpkRAMTPVRALSGGERNR 448
Cdd:COG4674 91 fqkptvfEELTVFENL-----ELALKGDrgVFASLFArltaeerdrieevletigLTD------KADRLAGLLSHGQKQW 159
|
170 180
....*....|....*....|
gi 15830287 449 LLLARLFLKPSNLLILDEPT 468
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPV 179
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-188 |
2.01e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 53.30 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI--IYEQDLIVARLQqdppRNVEG 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItvLGVPVPARARLA----RARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 82 SVYDFvaegieeqaeylkryhdisrlvmndpseKNLNELAKVQEQLDHHNLW------QLENRINEVL--AQLGLDPNVA 153
Cdd:PRK13536 118 VVPQF----------------------------DNLDLEFTVRENLLVFGRYfgmstrEIEAVIPSLLefARLESKADAR 169
|
170 180 190
....*....|....*....|....*....|....*
gi 15830287 154 LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD 188
Cdd:PRK13536 170 VSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-233 |
2.08e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 52.81 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 13 FSDAPLLDnAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQD---PPRNVEGSVYDFVAE 89
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikPVRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 90 GIEEQAeylkryhdisrlVMNDPSEKNLNELAKVQEQldhhnlwqlENRINEVLAQLGLDPNVALSS---LSGGWLRKAA 166
Cdd:PRK13643 96 QLFEET------------VLKDVAFGPQNFGIPKEKA---------EKIAAEKLEMVGLADEFWEKSpfeLSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 167 LGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTfNGTIIFISHDRSFIRNMATRIVDLDRGKLVT 233
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
309-472 |
2.31e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 309 VEEASRSGKIVFEMEDVCYQV----DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLqaDSGRIHVGTKL-- 382
Cdd:TIGR00956 749 KDMEKESGEDIFHWRNLTYEVkikkEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITGGDRLvn 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 383 ----------EVAYFDQHRAELdPDKTVMDNL---AEGKQ--EVMVNGKPRHVlGYLQDFLFHPKRA----MTPVRALSG 443
Cdd:TIGR00956 827 grpldssfqrSIGYVQQQDLHL-PTSTVRESLrfsAYLRQpkSVSKSEKMEYV-EEVIKLLEMESYAdavvGVPGEGLNV 904
|
170 180 190
....*....|....*....|....*....|
gi 15830287 444 GERNRLLLA-RLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR00956 905 EQRKRLTIGvELVAKPKLLLFLDEPTSGLD 934
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
344-512 |
2.43e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.03 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 344 RGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklevayfdqhraELDpdktvmdnlaegkqEVMVNGKPRHVlgy 423
Cdd:cd03222 24 EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND----------------EWD--------------GITPVYKPQYI--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 424 lqdflfhpkramtpvrALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY----QGTVLLVSHDRQF 499
Cdd:cd03222 71 ----------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAV 134
|
170
....*....|...
gi 15830287 500 VDNTVTECWIFEG 512
Cdd:cd03222 135 LDYLSDRIHVFEG 147
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
18-193 |
2.65e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.20 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLIVARLQQDPPRNVEgsvydfvaegieeqae 96
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiIDDEDISLLPLHARARRGIG---------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 97 YLKRYHDI-SRLVMNDpsekNLNELAKVQEQLDHHnlwQLENRINEVLAQLGLD--PNVALSSLSGGWLRKAALGRALVS 173
Cdd:PRK10895 82 YLPQEASIfRRLSVYD----NLMAVLQIRDDLSAE---QREDRANELMEEFHIEhlRDSMGQSLSGGERRRVEIARALAA 154
|
170 180
....*....|....*....|.
gi 15830287 174 NPRVLLLDEPTNHLD-IETID 193
Cdd:PRK10895 155 NPKFILLDEPFAGVDpISVID 175
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-245 |
2.69e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.93 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqglddGRIIYEQDLIVARlqqdppRNVEGSVYDFVAEGIEEQAEYL 98
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFN-------GLIKSKYGTIQVG------DIYIGDKKNNHELITNPYSKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 99 KRYHDISRLV-----------MNDPSEKNL--NELAKVQEQLDHHNLWQLEnrinevLAQLGLDPNVALSS---LSGGWL 162
Cdd:PRK13631 109 KNFKELRRRVsmvfqfpeyqlFKDTIEKDImfGPVALGVKKSEAKKLAKFY------LNKMGLDDSYLERSpfgLSGGQK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 163 RKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNY- 238
Cdd:PRK13631 183 RRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkanNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYe 262
|
250
....*....|
gi 15830287 239 ---DQYLLEK 245
Cdd:PRK13631 263 iftDQHIINS 272
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
317-472 |
2.96e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 52.30 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 317 KIVFEMEDVC--YQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAE 393
Cdd:PRK13632 5 SVMIKVENVSfsYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 394 L-----DPDK-----TVMDNLAEGKQEVMVNGK--PRHVLGYLQ-----DFL-FHPKRamtpvraLSGGERNRLLLAR-L 454
Cdd:PRK13632 85 IgiifqNPDNqfigaTVEDDIAFGLENKKVPPKkmKDIIDDLAKkvgmeDYLdKEPQN-------LSGGQKQRVAIASvL 157
|
170
....*....|....*...
gi 15830287 455 FLKPSnLLILDEPTNDLD 472
Cdd:PRK13632 158 ALNPE-IIIFDESTSMLD 174
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-232 |
2.98e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.30 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNReqglddgriiyeqdLIVArlqqdpprnVEGSVYdFVAEG 90
Cdd:PRK10253 15 LGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSR--------------LMTP---------AHGHVW-LDGEH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 91 IEEQA--EYLKRyhdISRLVMN--DPSEKNLNELAkVQEQLDHHNL---WQLENR--INEVLAQLGLD--PNVALSSLSG 159
Cdd:PRK10253 71 IQHYAskEVARR---IGLLAQNatTPGDITVQELV-ARGRYPHQPLftrWRKEDEeaVTKAMQATGIThlADQSVDTLSG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287 160 GWLRKAALGRALVSNPRVLLLDEPTNHLDI-ETIDWLEgFLKTFNG----TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK10253 147 GQRQRAWIAMVLAQETAIMLLDEPTTWLDIsHQIDLLE-LLSELNRekgyTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-236 |
3.13e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.32 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMK----ILNREQG--LDDGRII--YEQDLIVARLQ-- 72
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMnlsgLLRPQKGavLWQGKPLdySKRGLLALRQQva 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 73 ---QDPprnvegsvydfvaegiEEQAEYLKRYHDISRlvmndpSEKNLNelakVQEQldhhnlwQLENRINEVLAQLGLD 149
Cdd:PRK13638 81 tvfQDP----------------EQQIFYTDIDSDIAF------SLRNLG----VPEA-------EITRRVDEALTLVDAQ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 150 --PNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGT---IIFISHDRSFIRNMATRIV 224
Cdd:PRK13638 128 hfRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVY 207
|
250
....*....|....
gi 15830287 225 DLDRGKLVTY--PG 236
Cdd:PRK13638 208 VLRQGQILTHgaPG 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-276 |
3.73e-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: 53.76 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGlDDGRIiyeqdlivarlqqdpprNVEGSVYDFV-------AEG 90
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEI-----------------QIDGVSWNSVtlqtwrkAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 91 IEEQaeylKRYHDISRLVMN-DPSEK-NLNELAKVQEQLDHHN-LWQLENRINEVLAQLGLdpnvalsSLSGGWLRKAAL 167
Cdd:TIGR01271 1296 VIPQ----KVFIFSGTFRKNlDPYEQwSDEEIWKVAEEVGLKSvIEQFPDKLDFVLVDGGY-------VLSNGHKQLMCL 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 168 GRALVSNPRVLLLDEPTNHLDIETIDWLEGFLK-TF-NGTIIFISHdrsfirnmatRIvdldrgklvtypgnydQYLLEK 245
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKqSFsNCTVILSEH----------RV----------------EALLEC 1418
|
250 260 270
....*....|....*....|....*....|...
gi 15830287 246 EEALRVEELQNAEFD--RKLAQEEVWIRQGIKA 276
Cdd:TIGR01271 1419 QQFLVIEGSSVKQYDsiQKLLNETSLFKQAMSA 1451
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-231 |
3.80e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.13 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARlqqdpprnvegSVYDFVAEGIEeqaeYLKR 100
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAL-----------STAQRLARGLV----YLPE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 101 YHDISRLVMNDPSEKNLNELAkvqeqldHHN--LWQLENRINEVL----AQLGL---DPNVALSSLSGGWLRKAALGRAL 171
Cdd:PRK15439 346 DRQSSGLYLDAPLAWNVCALT-------HNRrgFWIKPARENAVLeryrRALNIkfnHAEQAARTLSGGNQQKVLIAKCL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830287 172 VSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK15439 419 EASPQLLIVDEPTRGVDVSARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
319-472 |
3.91e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.00 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQV-DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlevayfdqhraELDPD 397
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE-----------PIKYD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 398 KTvmdNLAEGKQEV-MVNGKPRHVL---GYLQDFLFHP-----------KRAMTPVRA-------------LSGGERNRL 449
Cdd:PRK13639 70 KK---SLLEVRKTVgIVFQNPDDQLfapTVEEDVAFGPlnlglskeeveKRVKEALKAvgmegfenkpphhLSGGQKKRV 146
|
170 180
....*....|....*....|...
gi 15830287 450 LLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLD 169
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-229 |
4.01e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 51.62 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVAR-------LQQD- 74
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaergvvFQNEg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 75 --PPRNVEgsvyDFVAEGIE----EQAEYLKRYHDIsrlvmndpseknlneLAKVQ-EQLDHHNLWQLenrinevlaqlg 147
Cdd:PRK11248 81 llPWRNVQ----DNVAFGLQlagvEKMQRLEIAHQM---------------LKKVGlEGAEKRYIWQL------------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 148 ldpnvalsslSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWL-EGFLKTFNGT---IIFISHDRSFIRNMATRI 223
Cdd:PRK11248 130 ----------SGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMqTLLLKLWQETgkqVLLITHDIEEAVFMATEL 199
|
....*.
gi 15830287 224 VDLDRG 229
Cdd:PRK11248 200 VLLSPG 205
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
321-500 |
4.60e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 51.66 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQV-DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAEL---- 394
Cdd:PRK13647 6 EVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVmGREVNAENEKWVRSKVglvf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 -DPD-----KTVMDNLAEGKQEV-----MVNGKPRHVLGYLQDFLFHPKramtPVRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK13647 86 qDPDdqvfsSTVWDDVAFGPVNMgldkdEVERRVEEALKAVRMWDFRDK----PPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15830287 464 LDEPTNDLDVETLELLEELID--SYQG-TVLLVSHDRQFV 500
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDrlHNQGkTVIVATHDVDLA 201
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
325-473 |
4.73e-07 |
|
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: 51.98 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 325 VCYQVDGKQL--VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQA---DSGRIHVG----TKLEVAYFDQHRAE-- 393
Cdd:COG0444 9 VYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDgedlLKLSEKELRKIRGRei 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 394 ----------LDPDKTVMDNLAE--------GKQEVMvngkpRHVLGYLQDF-LFHPKRAMtpvRA----LSGGERNRLL 450
Cdd:COG0444 89 qmifqdpmtsLNPVMTVGDQIAEplrihgglSKAEAR-----ERAIELLERVgLPDPERRL---DRypheLSGGMRQRVM 160
|
170 180
....*....|....*....|....
gi 15830287 451 LAR-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG0444 161 IARaLALEPK-LLIADEPTTALDV 183
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
344-496 |
5.34e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 344 RGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HVGTKLEVayFDQHR-AELdpdKTVMDNLAEGKQEV-----MVNGK 416
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeEEPSWDEV--LKRFRgTEL---QNYFKKLYNGEIKVvhkpqYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 417 PRHVLGYLQDFLfhpKRA--------------MTPV-----RALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLE 477
Cdd:PRK13409 173 PKVFKGKVRELL---KKVdergkldevverlgLENIldrdiSELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRL 249
|
170 180
....*....|....*....|.
gi 15830287 478 LLEELIDSYQG--TVLLVSHD 496
Cdd:PRK13409 250 NVARLIRELAEgkYVLVVEHD 270
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-232 |
5.84e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.37 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNRE-------QGLD-------DGRIIYEQD-LIVARLQQDPPRNVEGS 82
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgggapRGARvtgdvtlNGEPLAAIDaPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 83 vYDFVAEGIEeqaeYLKRYhdisrlvmndPSEKNLNELAkvqeqldHHNlwqlENRINEVLAQLGLDPNVA--LSSLSGG 160
Cdd:PRK13547 96 -FAFSAREIV----LLGRY----------PHARRAGALT-------HRD----GEIAWQALALAGATALVGrdVTTLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 161 WLRKAALGRAL---------VSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLD 227
Cdd:PRK13547 150 ELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLahqhRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLA 229
|
....*
gi 15830287 228 RGKLV 232
Cdd:PRK13547 230 DGAIV 234
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-224 |
6.41e-07 |
|
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: 52.48 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 26 IEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyEQDLIVARLQQDPPRNVEGSVYDFVAEGIEEQAEylkryhdis 105
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISPDYDGTVEEFLRSANTDDFG--------- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 106 rlvmndpseknlnelakvqeqldhHNLWQlenriNEVLAQLGLDP--NVALSSLSGGWLRKAALGRALVSNPRVLLLDEP 183
Cdd:COG1245 432 ------------------------SSYYK-----TEIIKPLGLEKllDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15830287 184 TNHLDIE-------TIdwlEGFLKTFNGTIIFISHDRSFIRNMATRIV 224
Cdd:COG1245 483 SAHLDVEqrlavakAI---RRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-188 |
7.03e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 51.34 E-value: 7.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQdpPRNVEGSV 83
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH--ARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 84 Y-------DFVaegIEEQAEYLKRY-----HDISRLVmndpseKNLNELAKvqeqldhhnlwqLENRINevlAQLGldpn 151
Cdd:PRK13537 86 PqfdnldpDFT---VRENLLVFGRYfglsaAAARALV------PPLLEFAK------------LENKAD---AKVG---- 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 15830287 152 valsSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD 188
Cdd:PRK13537 138 ----ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
344-496 |
8.45e-07 |
|
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: 52.09 E-value: 8.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 344 RGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVayFDQHR-AELdpdKTVMDNLAEGKQEV-----MVNGK 416
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEePSWDEV--LKRFRgTEL---QDYFKKLANGEIKVahkpqYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 417 PRHVLGYLQDFLfhpKRA--------------MTP-----VRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLE 477
Cdd:COG1245 173 PKVFKGTVRELL---EKVdergkldelaeklgLENildrdISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRL 249
|
170 180
....*....|....*....|..
gi 15830287 478 LLEELIDSYQG---TVLLVSHD 496
Cdd:COG1245 250 NVARLIRELAEegkYVLVVEHD 271
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
150-231 |
1.09e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 51.75 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 150 PNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET---IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDL 226
Cdd:TIGR02633 397 PFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVI 476
|
....*
gi 15830287 227 DRGKL 231
Cdd:TIGR02633 477 GEGKL 481
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-230 |
1.17e-06 |
|
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: 49.78 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSFSD-----APLLDNAELHIEDNERVCLVGRNGAGKSTL-MKILNrEQGLDDGRIiyeqdlivarlqqdppr 77
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLlSALLG-ELEKLSGSV----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 78 NVEGSVyDFVAegieeQAEYLkryhdisrlvMNdpseknlnelAKVQE------QLDhhnlwqlENRINEVLAQLGLDPN 151
Cdd:cd03250 63 SVPGSI-AYVS-----QEPWI----------QN----------GTIREnilfgkPFD-------EERYEKVIKACALEPD 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 152 VAL-------------SSLSGGwlRKA--ALGRALVSNPRVLLLDEPTNHLDIETIDWL-----EGFLKtFNGTIIFISH 211
Cdd:cd03250 110 LEIlpdgdlteigekgINLSGG--QKQriSLARAVYSDADIYLLDDPLSAVDAHVGRHIfenciLGLLL-NNKTRILVTH 186
|
250
....*....|....*....
gi 15830287 212 DRSFIRNmATRIVDLDRGK 230
Cdd:cd03250 187 QLQLLPH-ADQIVVLDNGR 204
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
319-472 |
1.23e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.57 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQVDG-KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAEL-- 394
Cdd:PRK13652 3 LIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIREVRKFVgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 ---DPDKTVMDNLAE----------GKQEVMVNGKPR---HVLGyLQDFlfhpkRAMTPvRALSGGERNRLLLARLFLKP 458
Cdd:PRK13652 83 vfqNPDDQIFSPTVEqdiafgpinlGLDEETVAHRVSsalHMLG-LEEL-----RDRVP-HHLSGGEKKRVAIAGVIAME 155
|
170
....*....|....
gi 15830287 459 SNLLILDEPTNDLD 472
Cdd:PRK13652 156 PQVLVLDEPTAGLD 169
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
330-472 |
1.34e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.00 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGK-QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFD-----QHRAeLDPDKT 399
Cdd:PRK11650 14 DGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGgrvvNELEPADRDiamvfQNYA-LYPHMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 400 VMDNLAEG-------KQEvmVNGKPRHVLGYL--QDFLfhpKRamTPvRALSGGERNRLLLARLFLKPSNLLILDEPTND 470
Cdd:PRK11650 93 VRENMAYGlkirgmpKAE--IEERVAEAARILelEPLL---DR--KP-RELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
|
..
gi 15830287 471 LD 472
Cdd:PRK11650 165 LD 166
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-212 |
1.36e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.11 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQdpprnve 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 81 gsvydfvaegieeqaeylKRYHD------ISRLVMNDPSEKN---LNELAKVQEQldhHNLwqlenrinevlaqlgldpN 151
Cdd:PRK09544 75 ------------------KLYLDttlpltVNRFLRLRPGTKKediLPALKRVQAG---HLI------------------D 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287 152 VALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIE----TIDWLEGFLKTFNGTIIFISHD 212
Cdd:PRK09544 116 APMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNgqvaLYDLIDQLRRELDCAVLMVSHD 180
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
12-253 |
1.43e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 50.01 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLDDGRIIYEQ--DLIVARLQQdpprnvEGSVYDFVAE 89
Cdd:PRK09984 13 TFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLS---GLITGDKSAGShiELLGRTVQR------EGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 90 GIEEQAEYLKRYHDISRLVM----------NDPSEKN-LNELAKVQEQldhhnlwqlenRINEVLAQLGLD--PNVALSS 156
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVlenvligalgSTPFWRTcFSWFTREQKQ-----------RALQALTRVGMVhfAHQRVST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 157 LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKlV 232
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESarivMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH-V 231
|
250 260
....*....|....*....|....*.
gi 15830287 233 TYPGNYDQYLLEKEEAL-----RVEE 253
Cdd:PRK09984 232 FYDGSSQQFDNERFDHLyrsinRVEE 257
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
345-472 |
1.56e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 49.63 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 345 GDKIALIGPNGCGKTTLLKLmLGQLQ-ADSGrihvgtKLEVA--YFD--------QHRA------------ELDPDKTVM 401
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRV-LNLLEmPRSG------TLNIAgnHFDfsktpsdkAIRElrrnvgmvfqqyNLWPHLTVQ 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287 402 DNLAEGKQEVMVNGKPR---HVLGYLQDFLFHPKRAMTPVRaLSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLD 472
Cdd:PRK11124 101 QNLIEAPCRVLGLSKDQalaRAEKLLERLRLKPYADRFPLH-LSGGQQQRVAIARaLMMEPQVLL-FDEPTAALD 173
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
319-496 |
1.74e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 49.70 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQVDGkQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQAD----SGRIHV-GTKLE--------VA 385
Cdd:PRK10418 4 QIELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLdGKPVApcalrgrkIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 386 YFDQH-RAELDPDKTVMDNLAEGKQEVMVNGKPRHVLGYLQDF-LFHPKRA--MTPVRaLSGGERNRLLLARLFLKPSNL 461
Cdd:PRK10418 83 TIMQNpRSAFNPLHTMHTHARETCLALGKPADDATLTAALEAVgLENAARVlkLYPFE-MSGGMLQRMMIALALLCEAPF 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 15830287 462 LILDEPTNDLDVETLELLEELIDSYQGT----VLLVSHD 496
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKralgMLLVTHD 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
149-232 |
1.80e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 50.79 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 149 DPNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKtfNGT-IIFISHDRSFIRNMATRI 223
Cdd:COG1129 387 SPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVgakaEIYRLIRELAA--EGKaVIVISSELPELLGLSDRI 464
|
....*....
gi 15830287 224 VDLDRGKLV 232
Cdd:COG1129 465 LVMREGRIV 473
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-232 |
1.99e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 49.69 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLM----KILNREQG---LDDGRIIYE-QDLIVARLQ-----QDPPRNV-EGSVY 84
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFlhfnGILKPTSGevlIKGEPIKYDkKSLLEVRKTvgivfQNPDDQLfAPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 85 DFVAEGieeqaeylkryhdisRLVMNDPSEknlnelakvqeqldhhnlwQLENRINEVLAQLGLD--PNVALSSLSGGWL 162
Cdd:PRK13639 98 EDVAFG---------------PLNLGLSKE-------------------EVEKRVKEALKAVGMEgfENKPPHHLSGGQK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830287 163 RKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13639 144 KRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKegiTIIISTHDVDLVPVYADKVYVMSDGKII 216
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
155-232 |
2.02e-06 |
|
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: 50.90 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 155 SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD-------IETIDwlegFLKTFNGTIIFISHDRSFIrNMATRIVDLD 227
Cdd:COG4618 466 ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalAAAIR----ALKARGATVVVITHRPSLL-AAVDKLLVLR 540
|
....*
gi 15830287 228 RGKLV 232
Cdd:COG4618 541 DGRVQ 545
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
19-187 |
2.05e-06 |
|
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: 50.39 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNeRVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVEgsvydfvaegieeqAEYL 98
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIE--------------LTFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 99 KRYHDISRLVMNDPSEKNLNE-LAKVQEQLDHHnLWQLENRINEVLAQLGLDPNVAL----------------------- 154
Cdd:COG3593 79 SLLSRLLRLLLKEEDKEELEEaLEELNEELKEA-LKALNELLSEYLKELLDGLDLELelsldeledllkslslriedgke 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15830287 155 ---SSLSGG--WLRKAALGRALV-----SNPRVLLLDEPTNHL 187
Cdd:COG3593 158 lplDRLGSGfqRLILLALLSALAelkraPANPILLIEEPEAHL 200
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-230 |
2.36e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-----QDL-------IVARLQQDP------- 75
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlKDInlkwwrsKIGVVSQDPllfsnsi 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 76 PRNVEGSVYDFV-AEGIEEQAE----------------YLKRYHDISrLVMNDPSEKNLNELAKVQEQLDHHNLWQLENR 138
Cdd:PTZ00265 477 KNNIKYSLYSLKdLEALSNYYNedgndsqenknkrnscRAKCAGDLN-DMSNTTDSNELIEMRKNYQTIKDSEVVDVSKK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 139 --INEVLAQLGlDPNVAL-----SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD-------IETIDWLEGflkTFNG 204
Cdd:PTZ00265 556 vlIHDFVSALP-DKYETLvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDnkseylvQKTINNLKG---NENR 631
|
250 260
....*....|....*....|....*.
gi 15830287 205 TIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:PTZ00265 632 ITIIIAHRLSTIRYANTIFVLSNRER 657
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
149-232 |
2.78e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.41 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 149 DPNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDW-----LEgfLKTFNGTIIFISHDRSFIRNMATRI 223
Cdd:COG3845 395 GPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFihqrlLE--LRDAGAAVLLISEDLDEILALSDRI 472
|
....*....
gi 15830287 224 VDLDRGKLV 232
Cdd:COG3845 473 AVMYEGRIV 481
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
349-501 |
2.88e-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: 48.37 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 349 ALIGPNGCGKTTLLKlmlgqlqadsgrihvgtKLEVAYFDQHRAELDPDKTVMDNLAEGKQEVMV-------NGKPRHVL 421
Cdd:cd03240 26 LIVGQNGAGKTTIIE-----------------ALKYALTGELPPNSKGGAHDPKLIREGEVRAQVklafenaNGKKYTIT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 422 GYL----------QDFLFHPkrAMTPVRALSGGERN------RLLLARLFLKPSNLLILDEPTNDLDVETLELLEELI-D 484
Cdd:cd03240 89 RSLailenvifchQGESNWP--LLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIiE 166
|
170 180
....*....|....*....|.
gi 15830287 485 SYQGT----VLLVSHDRQFVD 501
Cdd:cd03240 167 ERKSQknfqLIVITHDEELVD 187
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
332-472 |
3.11e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQ--ADSGRIHVGTkleVAYFDQhrAELDPDKTVMDNLAEG-K 408
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELShaETSSVVIRGS---VAYVPQ--VSWIFNATVRENILFGsD 704
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287 409 QEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRA----LSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PLN03232 705 FESERYWRAIDVTALQHDLDLLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
10-211 |
3.12e-06 |
|
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: 48.29 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 10 WLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL--NREQGLDDGRIIYE-QDLI------VARL-----QQDP 75
Cdd:cd03217 7 HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKgEDITdlppeeRARLgiflaFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 76 PRnVEG-SVYDFVaegieeqaeylkryhdisrlvmndpseKNLNElakvqeqldhhnlwqlenrinevlaqlgldpnval 154
Cdd:cd03217 87 PE-IPGvKNADFL---------------------------RYVNE----------------------------------- 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 155 sSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISH 211
Cdd:cd03217 104 -GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLreeGKSVLIITH 162
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-223 |
3.27e-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: 47.37 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 29 NERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYeqdlivarlqqdpprnvegsvydFVAEGIEEQAEYLKRYHDISRLV 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------------------IDGEDILEEVLDQLLLIIVGGKK 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 109 MNDPSEKNLnelakvqeqldhhnlwqlenrinevlaqlgldpnvalsslsggwlrKAALGRALVSNPRVLLLDEPTNHLD 188
Cdd:smart00382 59 ASGSGELRL----------------------------------------------RLALALARKLKPDVLILDEITSLLD 92
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15830287 189 IET---------IDWLEGFLKTFNGTIIFISHDRSFIRNMATRI 223
Cdd:smart00382 93 AEQeallllleeLRLLLLLKSEKNLTVILTTNDEKDLGPALLRR 136
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
335-521 |
3.66e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.70 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLgqlqADSGRIHVGTKLEVAYfdqhraeldPDKTVM-DNLaegkQEVMV 413
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLISFLPKFS---------RNKLIFiDQL----QFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 414 NGkprhvLGYLQdflfhPKRAMTpvrALSGGERNRLLLAR-LFLKPSN-LLILDEPTNDLDVETLELLEELIDSY--QG- 488
Cdd:cd03238 74 VG-----LGYLT-----LGQKLS---TLSGGELQRVKLASeLFSEPPGtLFILDEPSTGLHQQDINQLLEVIKGLidLGn 140
|
170 180 190
....*....|....*....|....*....|...
gi 15830287 489 TVLLVSHDRQFVDntvTECWIFEGGGKIGRYVG 521
Cdd:cd03238 141 TVILIEHNLDVLS---SADWIIDFGPGSGKSGG 170
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
333-516 |
3.78e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.81 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKL---------EVAYFDQHRAELDPDK----- 398
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgQLKVADKNQLRLLRTRltmvf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 399 ---------TVMDNLAEGKQEVM----VNGKPRHVLGYLQDFLFHPKRAMTPVRaLSGGERNRLLLARLFLKPSNLLILD 465
Cdd:PRK10619 99 qhfnlwshmTVLENVMEAPIQVLglskQEARERAVKYLAKVGIDERAQGKYPVH-LSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15830287 466 EPTNDLD---VETLELLEELIDSYQGTVLLVSHDRQFVDNtVTECWIFEGGGKI 516
Cdd:PRK10619 178 EPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARH-VSSHVIFLHQGKI 230
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
134-226 |
3.88e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.70 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 134 QLENRINEVLAQLGLDPNvaLSSLSGGWLRKAALGRALVSNPR--VLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIF 208
Cdd:cd03238 67 QLQFLIDVGLGYLTLGQK--LSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLidlGNTVIL 144
|
90
....*....|....*...
gi 15830287 209 ISHDRSFIRNmATRIVDL 226
Cdd:cd03238 145 IEHNLDVLSS-ADWIIDF 161
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
331-473 |
4.50e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.19 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 331 GKQLVK---DFSAQVLRGDKIALIGPNGCGKTTLLKLML-------GQLQADSGRIHVGTKLEVA--------YFDQHRA 392
Cdd:PRK11308 24 PERLVKaldGVSFTLERGKTLAVVGESGCGKSTLARLLTmietptgGELYYQGQDLLKADPEAQKllrqkiqiVFQNPYG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 393 ELDPDKTVMDNLAE--------GKQE-------VM--VNGKPRHVLGYLQDFlfhpkramtpvralSGGERNRLLLAR-L 454
Cdd:PRK11308 104 SLNPRKKVGQILEEpllintslSAAErrekalaMMakVGLRPEHYDRYPHMF--------------SGGQRQRIAIARaL 169
|
170
....*....|....*....
gi 15830287 455 FLKPsNLLILDEPTNDLDV 473
Cdd:PRK11308 170 MLDP-DVVVADEPVSALDV 187
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-189 |
4.82e-06 |
|
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: 48.52 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 34 LVGRNGAGKSTLMKILNREQGLDDGRiiyeqdlivarlQQDPPRnvegsvYDFVAE---GIEEQaEYLKRYHDISRLVMN 110
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGK------------FDDPPD------WDEILDefrGSELQ-NYFTKLLEGDVKVIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 111 DPseKNLNELAKVQEQLDHHNLWQLENR--INEVLAQLGLDP--NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNH 186
Cdd:cd03236 92 KP--QYVDLIPKAVKGKVGELLKKKDERgkLDELVDQLELRHvlDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
...
gi 15830287 187 LDI 189
Cdd:cd03236 170 LDI 172
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
39-231 |
5.83e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 39 GAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNveGSVYdfvaegIEEQaeylkRYHDisRLVMNDPSEKN-- 116
Cdd:PRK10762 288 GAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN--GIVY------ISED-----RKRD--GLVLGMSVKENms 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 117 ---LNELAKVQEQLDHhnlwQLENRINEVLAQL------GLDPNVALssLSGGWLRKAALGRALVSNPRVLLLDEPTNHL 187
Cdd:PRK10762 353 ltaLRYFSRAGGSLKH----ADEQQAVSDFIRLfniktpSMEQAIGL--LSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15830287 188 DI----ETIDWLEGFlKTFNGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK10762 427 DVgakkEIYQLINQF-KAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
319-496 |
6.13e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.17 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQVDGKQLVKDF---SAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAEL 394
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 -----DPDK-----TVMDNLAEGKQEvmvNGKPR-HVLGYLQDFLFHPK----RAMTPVRaLSGGERNRLLLARLFLKPS 459
Cdd:PRK13642 84 gmvfqNPDNqfvgaTVEDDVAFGMEN---QGIPReEMIKRVDEALLAVNmldfKTREPAR-LSGGQKQRVAVAGIIALRP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15830287 460 NLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIheikEKYQLTVLSITHD 200
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
35-220 |
6.89e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.42 E-value: 6.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 35 VGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLIVArlqqdpprnvegsvydfvaegiEEQAEYLKRyHDIsRLVMNDPS 113
Cdd:PRK11308 47 VGESGCGKSTLARLLTMIETPTGGELYYQgQDLLKA----------------------DPEAQKLLR-QKI-QIVFQNPY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 114 eKNLNELAKVQEQLD-----HHNLWQLENR--INEVLAQLGLDPNVALS---SLSGGWLRKAALGRALVSNPRVLLLDEP 183
Cdd:PRK11308 103 -GSLNPRKKVGQILEeplliNTSLSAAERRekALAMMAKVGLRPEHYDRyphMFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15830287 184 TNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMA 220
Cdd:PRK11308 182 VSALDVsvqaQVLNLMMDLQQELGLSYVFISHDLSVVEHIA 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
318-520 |
7.18e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 47.85 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 318 IVFEMED--VCYqvdGKQL-VKDFSAQVLRGDKIALIGPNGCGKTTLLKLM--LGQLqADSGRIhvgtKLEVAYFDQ--H 390
Cdd:PRK14243 9 TVLRTENlnVYY---GSFLaVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDL-IPGFRV----EGKVTFHGKnlY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 RAELDP-----------------DKTVMDNLAEGkqevmvngkPRhVLGYLQDFLFHPKRAM--------------TPVR 439
Cdd:PRK14243 81 APDVDPvevrrrigmvfqkpnpfPKSIYDNIAYG---------AR-INGYKGDMDELVERSLrqaalwdevkdklkQSGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 440 ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY--QGTVLLVSHDRQFVDNTVTECWIF-----EG 512
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELkeQYTIIIVTHNMQQAARVSDMTAFFnveltEG 230
|
....*...
gi 15830287 513 GGKIGRYV 520
Cdd:PRK14243 231 GGRYGYLV 238
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-232 |
7.61e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 48.16 E-value: 7.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiYEQDLIVARLQQD-PPRNVEGSVYD-----FVAEGIE 92
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV-YVDGLDTSDEENLwDIRNKAGMVFQnpdnqIVATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 93 EQAEYLKRYHDIsrlvmnDPSEKNlnelAKVQEQLDHHNLWQLENRinevlaqlgldpnvALSSLSGGWLRKAALGRALV 172
Cdd:PRK13633 105 EDVAFGPENLGI------PPEEIR----ERVDESLKKVGMYEYRRH--------------APHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287 173 SNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHdrsFIRNM--ATRIVDLDRGKLV 232
Cdd:PRK13633 161 MRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH---YMEEAveADRIIVMDSGKVV 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
326-472 |
8.01e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 48.89 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 326 CYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLM----LGQLQADSGRIHVGTKLEV-------AYFDQHRAEL 394
Cdd:TIGR00955 32 CRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrsPKGVKGSGSVLLNGMPIDAkemraisAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 dPDKTVMDNL---AEGK-QEVMVNGKPRHVLGYLQDFLFHPKRAMT------PVRALSGGERNRLLLARLFLKPSNLLIL 464
Cdd:TIGR00955 112 -PTLTVREHLmfqAHLRmPRRVTKKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFC 190
|
....*...
gi 15830287 465 DEPTNDLD 472
Cdd:TIGR00955 191 DEPTSGLD 198
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
335-472 |
1.06e-05 |
|
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: 47.19 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKL-------------EVAYFDQHRAELDpDKTV 400
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdGTDLtllsgkelrkarrRIGMIFQHFNLLS-SRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 MDNLA-----EGKQEVMVNGKPRHVLGY--LQDflfhpKRAMTPvRALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLD 472
Cdd:cd03258 100 FENVAlpleiAGVPKAEIEERVLELLELvgLED-----KADAYP-AQLSGGQKQRVGIARaLANNPK-VLLCDEATSALD 172
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
321-472 |
1.06e-05 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 47.39 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLK------------LMLGQLQADSGRIHV-GTKLEVAY- 386
Cdd:PRK09493 3 EFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdLIVDGLKVNDPKVDErLIRQEAGMv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 387 FDQHraELDPDKTVMDNLAEGkqevmvngkPRHVLGY-----------LQDFLFHPKRAMTPVRALSGGERNRLLLAR-L 454
Cdd:PRK09493 83 FQQF--YLFPHLTALENVMFG---------PLRVRGAskeeaekqareLLAKVGLAERAHHYPSELSGGQQQRVAIARaL 151
|
170
....*....|....*...
gi 15830287 455 FLKPsNLLILDEPTNDLD 472
Cdd:PRK09493 152 AVKP-KLMLFDEPTSALD 168
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
30-232 |
1.20e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 47.23 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 30 ERVCLVGRNGAGKSTLMKILNREQGLDDGRIIY----EQDLIVARLQQDPPRNVEGSVYDFV----AEGIEEQ------- 94
Cdd:PRK11701 33 EVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdGQLRDLYALSEAERRRLLRTEWGFVhqhpRDGLRMQvsaggni 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 95 AEYL-----KRYHDISrlvmndpsEKNLNELAKVQEQLDhhnlwqlenRINEvlaqlglDPnvalSSLSGGWLRKAALGR 169
Cdd:PRK11701 113 GERLmavgaRHYGDIR--------ATAGDWLERVEIDAA---------RIDD-------LP----TTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 170 ALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVqarlLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
333-468 |
2.08e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 46.41 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQHRAELDPD-------KTVM 401
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgkdiTDWQTAKIMREAVAIVPEgrrvfsrMTVE 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 402 DNLAEGKQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPT 468
Cdd:PRK11614 99 ENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-232 |
2.27e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.04 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSFSD--APL--LDNAELHIEDNERVCLVGRNGAGKS-TLMKILnreqGLDD--GRIIYEQ------DLI 67
Cdd:PRK11022 1 MALLNVDKLSVHFGDesAPFraVDRISYSVKQGEVVGIVGESGSGKSvSSLAIM----GLIDypGRVMAEKlefngqDLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 68 vaRLQQDPPRNVEGSvydfvaegieeqaeylkryhDISrLVMNDPSeKNLNELAKV----QEQLDHH---NLWQLENRIN 140
Cdd:PRK11022 77 --RISEKERRNLVGA--------------------EVA-MIFQDPM-TSLNPCYTVgfqiMEAIKVHqggNKKTRRQRAI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 141 EVLAQLGL-DP----NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISH 211
Cdd:PRK11022 133 DLLNQVGIpDPasrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELLLELQQKENMALVLITH 212
|
250 260
....*....|....*....|.
gi 15830287 212 DRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK11022 213 DLALVAEAAHKIIVMYAGQVV 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
315-471 |
2.44e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.35 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 315 SGKIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVA----- 385
Cdd:PRK15439 7 TAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGgnpcARLTPAkahql 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 386 --YFDQHRAELDPDKTVMDNLAEGKQEVMVNGKPRHVLgyLQDFLFHPKRAMtPVRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK15439 87 giYLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQL--LAALGCQLDLDS-SAGSLEVADRQIVEILRGLMRDSRILI 163
|
....*...
gi 15830287 464 LDEPTNDL 471
Cdd:PRK15439 164 LDEPTASL 171
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-216 |
2.58e-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: 45.78 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLM-KILNREQGLDdGRIIYEQDLIVARLQQDPPRNVEGSVydfvaeGIE 92
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLE-GKVHWSNKNESEPSFEATRSRNRYSV------AYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 93 EQAEYLkryhdisrlvMNDPSEKNLNELAKVQEQldhhnlwqlenRINEVLAQLGLDPNVAL-------------SSLSG 159
Cdd:cd03290 85 AQKPWL----------LNATVEENITFGSPFNKQ-----------RYKAVTDACSLQPDIDLlpfgdqteigergINLSG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 160 GWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWL--EGFLKTFNG---TIIFISHDRSFI 216
Cdd:cd03290 144 GQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLmqEGILKFLQDdkrTLVLVTHKLQYL 205
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
302-472 |
2.75e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.47 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 302 MGTAKMQVEEASRSGKIVfemEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRihVGTK 381
Cdd:PTZ00243 646 GHEATPTSERSAKTPKMK---TDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR--VWAE 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 382 LEVAYFDQHRAELdpDKTVMDNLaegkqevmvngkprhvlgylqdFLFHPKRA---MTPVRA------------------ 440
Cdd:PTZ00243 721 RSIAYVPQQAWIM--NATVRGNI----------------------LFFDEEDAarlADAVRVsqleadlaqlgggletei 776
|
170 180 190
....*....|....*....|....*....|....*...
gi 15830287 441 ------LSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PTZ00243 777 gekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
333-516 |
3.42e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 46.23 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklEVAYFDQHraeldpDKTVMDNLAEGKQEVM 412
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI------EWIFKDEK------NKKKTKEKEKVLEKLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 413 VnGKPRH---------------VLGY----------LQDFLFHP-----------KRAMTPVR--------------ALS 442
Cdd:PRK13651 89 I-QKTRFkkikkikeirrrvgvVFQFaeyqlfeqtiEKDIIFGPvsmgvskeeakKRAAKYIElvgldesylqrspfELS 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 443 GGERNRLLLARLFLKPSNLLILDEPTNDLD---VETLELLEELIDSYQGTVLLVSHDrqfVDNTV--TECWIFEGGGKI 516
Cdd:PRK13651 168 GGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD---LDNVLewTKRTIFFKDGKI 243
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-191 |
3.67e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 45.33 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqglddGRIIYEQDLIVARLQQDPPrNVEGSVYDFVAegieeqae 96
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA-------GALKGTPVAGCVDVPDNQF-GREASLIDAIG-------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 97 ylkryhdisrlvmndpseKNLNELAKVqeqldhhnlwqlenrinEVLAQLGLDPNVAL----SSLSGGWLRKAALGRALV 172
Cdd:COG2401 108 ------------------RKGDFKDAV-----------------ELLNAVGLSDAVLWlrrfKELSTGQKFRFRLALLLA 152
|
170
....*....|....*....
gi 15830287 173 SNPRVLLLDEPTNHLDIET 191
Cdd:COG2401 153 ERPKLLVIDEFCSHLDRQT 171
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-232 |
3.74e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 6 MHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLI------------VARLQQ 73
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksskealengISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 74 DPPRNVEGSVYDFVaegieeqaeYLKRYHDISRLVMNDpseKNLNELAKVQEQLDhhnlwqlenrinevlaqLGLDPNVA 153
Cdd:PRK10982 81 ELNLVLQRSVMDNM---------WLGRYPTKGMFVDQD---KMYRDTKAIFDELD-----------------IDIDPRAK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 154 LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGF---LKTFNGTIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:PRK10982 132 VATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIirkLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
..
gi 15830287 231 LV 232
Cdd:PRK10982 212 WI 213
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
324-472 |
3.88e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.80 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 324 DVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADS--GRIHVGTK------LEVAYFDQHRAELD 395
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRkptkqiLKRTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 396 PDKTVMDNLAEGKQEVMVNGKPRHVLGYLQDFLFhPKRAMTP----------VRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:PLN03211 153 PHLTVRETLVFCSLLRLPKSLTKQEKILVAESVI-SELGLTKcentiignsfIRGISGGERKRVSIAHEMLINPSLLILD 231
|
....*..
gi 15830287 466 EPTNDLD 472
Cdd:PLN03211 232 EPTSGLD 238
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
335-496 |
4.73e-05 |
|
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: 45.33 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFD----------------QHRAeLDPDK 398
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQ-DIAAMSrkelrelrrkkismvfQSFA-LLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 399 TVMDNLAEGKQEVMVNGKPRHvlgylqdflfhpKRAMTPVRA-------------LSGGERNRLLLAR-LFLKPSnLLIL 464
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAERE------------ERAAEALELvglegwehkypdeLSGGMQQRVGLARaLAVDPD-ILLM 184
|
170 180 190
....*....|....*....|....*....|....*.
gi 15830287 465 DEPTNDLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:cd03294 185 DEAFSALDPLIRREMQDELlrlqAELQKTIVFITHD 220
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-63 |
5.53e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 5.53e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 15830287 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILN--REQGLDDGRIIYE 63
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvYPHGSYEGEILFD 63
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-216 |
6.09e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 44.70 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARlqqdPPrnvegsvydfvaEGIEEQ 94
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTL----KP------------EIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 95 AEYLKRyhdiSRLVMNDPSEKNLN---ELAKVQEQldhhnlwqlENRINEVLAQLGLDPNV---ALSSLSGGWLRKAALG 168
Cdd:PRK10247 83 VSYCAQ----TPTLFGDTVYDNLIfpwQIRNQQPD---------PAIFLDDLERFALPDTIltkNIAELSGGEKQRISLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15830287 169 RALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFI 216
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDesnkHNVNEIIHRYVREQNIAVLWVTHDKDEI 201
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
333-472 |
7.09e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 44.83 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLK-----LMLGQLQADSGRIH-------------VGTKLEVAYFDQHRAEL 394
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRlfgrniyspdvdpIEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 dPDKTVMDNLAEGkqeVMVNG--KPRHVLGYLQDFLFHPKRAMTPVR--------ALSGGERNRLLLAR-LFLKPsNLLI 463
Cdd:PRK14267 98 -PHLTIYDNVAIG---VKLNGlvKSKKELDERVEWALKKAALWDEVKdrlndypsNLSGGQRQRLVIARaLAMKP-KILL 172
|
....*....
gi 15830287 464 LDEPTNDLD 472
Cdd:PRK14267 173 MDEPTANID 181
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
12-245 |
9.09e-05 |
|
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: 45.58 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 12 SFS---DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLivARLQQDPPRNVEGSV---- 83
Cdd:COG5265 364 SFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlIDGQDI--RDVTQASLRAAIGIVpqdt 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 84 ---YDFVAEGIeeqaeylkRYhdiSRLvmnDPSEKNLNELAKvqeqldhhnlwqlenrinevLAQL---------GLDPN 151
Cdd:COG5265 442 vlfNDTIAYNI--------AY---GRP---DASEEEVEAAAR--------------------AAQIhdfieslpdGYDTR 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 152 VA---LSsLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NGTIIFISHDRSFIRNmATRIVDL 226
Cdd:COG5265 488 VGergLK-LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVarGRTTLVIAHRLSTIVD-ADEILVL 565
|
250
....*....|....*....
gi 15830287 227 DRGKLVTYpGNYDQyLLEK 245
Cdd:COG5265 566 EAGRIVER-GTHAE-LLAQ 582
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-201 |
9.20e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.07 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlivaRLQQDPPRNVEGS 82
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI---------QIDGKTATRGDRS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 83 vyDFVA-----EGIEEQAEYLKRYHDISRLVMNDPSEKNLNELAKVqeqldhhnlwQLENRINEVLAQlgldpnvalssL 157
Cdd:PRK13543 82 --RFMAylghlPGLKADLSTLENLHFLCGLHGRRAKQMPGSALAIV----------GLAGYEDTLVRQ-----------L 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15830287 158 SGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKT 201
Cdd:PRK13543 139 SAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISA 182
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
34-189 |
9.85e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 44.40 E-value: 9.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 34 LVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlivarlqqdpprnVEGSVYDFvaegieeqAEYLKRYHDIsRLVMNDPS 113
Cdd:PRK15112 44 IIGENGSGKSTLAKMLAGMIEPTSGELL-----------------IDDHPLHF--------GDYSYRSQRI-RMIFQDPS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 114 eKNLNELAKVQEQLD-------HHNLWQLENRINEVLAQLGLDPNVAL---SSLSGGWLRKAALGRALVSNPRVLLLDEP 183
Cdd:PRK15112 98 -TSLNPRQRISQILDfplrlntDLEPEQREKQIIETLRQVGLLPDHASyypHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
....*.
gi 15830287 184 TNHLDI 189
Cdd:PRK15112 177 LASLDM 182
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
321-500 |
1.03e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 44.21 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-------------HVGTKLEVAYF 387
Cdd:PRK11300 7 SVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIllrgqhieglpghQIARMGVVRTF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 388 dQHrAELDPDKTVMDNLaegkqevMVnGKPRHV-LGYLQDFLFHP----------KRAMT-------------PVRALSG 443
Cdd:PRK11300 87 -QH-VRLFREMTVIENL-------LV-AQHQQLkTGLFSGLLKTPafrraesealDRAATwlervgllehanrQAGNLAY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 444 GERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDS----YQGTVLLVSHDRQFV 500
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAElrneHNVTVLLIEHDMKLV 217
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
321-376 |
1.20e-04 |
|
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: 45.17 E-value: 1.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 321 EMEDVCYQ---VDGKQL--VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
Cdd:COG4615 329 ELRGVTYRypgEDGDEGftLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
133-223 |
1.25e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.41 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 133 WQLEN----RINEVLAQLGL-DPNVALSS----LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFL 199
Cdd:PRK15093 126 WQRFGwrkrRAIELLHRVGIkDHKDAMRSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTqaqiFRLLTRLN 205
|
90 100
....*....|....*....|....
gi 15830287 200 KTFNGTIIFISHDRSFIRNMATRI 223
Cdd:PRK15093 206 QNNNTTILLISHDLQMLSQWADKI 229
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
317-473 |
1.32e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.86 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 317 KIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGqlqadsgriHVGTKL---EVAYFDQHRAE 393
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG---------HPAYKIlegDILFKGESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 394 LDPDK-------------------TVMDNL-----AEGKQEVMVNGKPRHVLGYLQDFLfhPKRAMTPV-------RALS 442
Cdd:CHL00131 76 LEPEErahlgiflafqypieipgvSNADFLrlaynSKRKFQGLPELDPLEFLEIINEKL--KLVGMDPSflsrnvnEGFS 153
|
170 180 190
....*....|....*....|....*....|.
gi 15830287 443 GGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDI 184
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
318-472 |
1.36e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 44.24 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 318 IVFEMEDVCYQVDG---KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQhrael 394
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKN----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 dpdktvmDNLAEGKQEV-MVNGKPRHVL---GYLQDFLFHP-----------KRAMTPVR--------------ALSGGE 445
Cdd:PRK13634 78 -------KKLKPLRKKVgIVFQFPEHQLfeeTVEKDICFGPmnfgvseedakQKAREMIElvglpeellarspfELSGGQ 150
|
170 180
....*....|....*....|....*..
gi 15830287 446 RNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
157-229 |
1.40e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.45 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 157 LSGGWLRKAALGRALVSNPRVLLLDEPTNHLD--------IEtIDWLEGFLKTfngTIIFISHDRSFIRNMATRIVDLDR 228
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDaklrvqmrLE-IQRLHRRLKT---TSLYVTHDQVEAMTLADRVVVMNG 210
|
.
gi 15830287 229 G 229
Cdd:PRK11650 211 G 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-267 |
1.54e-04 |
|
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: 44.94 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 4 ISMHGAWLSF--SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlivarlqqdpprNVEG 81
Cdd:TIGR00957 637 ITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-----------------HMKG 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 82 SV-YdfvaegIEEQAeylkryhdisrLVMNDPSEKNLnelakvqeqLDHHNLwqLENRINEVLAQLGLDPNVAL------ 154
Cdd:TIGR00957 700 SVaY------VPQQA-----------WIQNDSLRENI---------LFGKAL--NEKYYQQVLEACALLPDLEIlpsgdr 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 155 -------SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD-------IETIDWLEGFLKtfNGTIIFISHDRSFIRNMA 220
Cdd:TIGR00957 752 teigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahvgkhiFEHVIGPEGVLK--NKTRILVTHGISYLPQVD 829
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 15830287 221 TRIVdLDRGKlVTYPGNYdQYLLEKEEALrveelqnAEFDRKLAQEE 267
Cdd:TIGR00957 830 VIIV-MSGGK-ISEMGSY-QELLQRDGAF-------AEFLRTYAPDE 866
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
18-213 |
1.64e-04 |
|
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: 44.07 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNReqglddgrIIYEQDLIvarlqqdpprNVEGSVYDFVAegieeQAEY 97
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLR--------LLNTEGDI----------QIDGVSWNSVP-----LQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 98 LKRYHDISR--LVMNDPSEKNLN--------ELAKVQEQLDhhnlwqLENRINEVLAQLGLDPNVALSSLSGGWLRKAAL 167
Cdd:cd03289 76 RKAFGVIPQkvFIFSGTFRKNLDpygkwsdeEIWKVAEEVG------LKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15830287 168 GRALVSNPRVLLLDEPTNHLDIETIDWLEGFLK-TFNGTIIFISHDR 213
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKqAFADCTVILSEHR 196
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-212 |
1.97e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 43.60 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIvarlqqdpPRNVE 80
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI--------PAMSR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 81 GSVYdfvaegieeqaEYLKRyhdISRLVMNDPSEKNLNELAKVQEQLDHHNlwQLENRI--NEVLAQL---GLDPNVAL- 154
Cdd:PRK11831 77 SRLY-----------TVRKR---MSMLFQSGALFTDMNVFDNVAYPLREHT--QLPAPLlhSTVMMKLeavGLRGAAKLm 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830287 155 -SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG----TIIFISHD 212
Cdd:PRK11831 141 pSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalgvTCVVVSHD 203
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
166-219 |
2.16e-04 |
|
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: 42.98 E-value: 2.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 166 ALGRALVSNPRVLLLDEPTNHLDIETIDW-----LEGFLKTFNGTIIFISHDRSFIRNM 219
Cdd:cd03240 131 ALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVDAA 189
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
437-542 |
2.29e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 437 PVRALSGGERNRLLLARLFLKPS---NLLILDEPTNDLDVETLELLEELIDS--YQG-TVLLVSHDRQFVD--NTVTECW 508
Cdd:PRK00635 806 PLSSLSGGEIQRLKLAYELLAPSkkpTLYVLDEPTTGLHTHDIKALIYVLQSltHQGhTVVIIEHNMHVVKvaDYVLELG 885
|
90 100 110
....*....|....*....|....*....|....
gi 15830287 509 IfEGGGKigryvGGYHDARGQQEQYVALKQPAVK 542
Cdd:PRK00635 886 P-EGGNL-----GGYLLASCSPEELIHLHTPTAK 913
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
331-495 |
2.81e-04 |
|
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: 43.97 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 331 GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQH----------------RAEL 394
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRpymtlgtlrdqiiypdSSED 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 DPDKTVMDNLAEgkqEVMVNGKPRHVLgylqdflfhpKRAM--TPVR----ALSGGERNRLLLARLFLKPSNLLILDEPT 468
Cdd:TIGR00954 544 MKRRGLSDKDLE---QILDNVQLTHIL----------EREGgwSAVQdwmdVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180
....*....|....*....|....*..
gi 15830287 469 NDLDVETLELLEELIDSYQGTVLLVSH 495
Cdd:TIGR00954 611 SAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
315-472 |
2.81e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 43.94 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 315 SGKIvfEMEDVCYQV-DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTK----LEVAYFDQ 389
Cdd:PRK10790 338 SGRI--DIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplssLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 390 HRAELDPDKTVM-----DNLAEGKQevMVNGKPRHVLGYLQdfLFHPKRAM-----TPV----RALSGGERNRLLLARLF 455
Cdd:PRK10790 416 GVAMVQQDPVVLadtflANVTLGRD--ISEEQVWQALETVQ--LAELARSLpdglyTPLgeqgNNLSVGQKQLLALARVL 491
|
170
....*....|....*..
gi 15830287 456 LKPSNLLILDEPTNDLD 472
Cdd:PRK10790 492 VQTPQILILDEATANID 508
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-242 |
3.16e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 42.65 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 24 LHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLIVARLQQDPprnvegsvydfvaegieeqaeylkryh 102
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtLNGQDHTTTPPSRRP--------------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 103 dISRLVmndpSEKNLnelakvqeqLDHHNLWQlenRINevlaqLGLDPNVALSS-------------------------L 157
Cdd:PRK10771 73 -VSMLF----QENNL---------FSHLTVAQ---NIG-----LGLNPGLKLNAaqreklhaiarqmgiedllarlpgqL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 158 SGGWLRKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVt 233
Cdd:PRK10771 131 SGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA- 209
|
....*....
gi 15830287 234 YPGNYDQYL 242
Cdd:PRK10771 210 WDGPTDELL 218
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
348-495 |
3.84e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.17 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 348 IALI-GPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAY--FDQHRAELDPDKTVMDNL---AEGKQEVMVNGKP 417
Cdd:PRK13541 28 ITYIkGANGCGKSSLLRMIAGIMQPSSGNIYYKncniNNIAKPYctYIGHNLGLKLEMTVFENLkfwSEIYNSAETLYAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 418 RHVLGyLQDFLfhpkraMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELI---DSYQGTVLLVS 494
Cdd:PRK13541 108 IHYFK-LHDLL------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIvmkANSGGIVLLSS 180
|
.
gi 15830287 495 H 495
Cdd:PRK13541 181 H 181
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
339-472 |
3.88e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 42.59 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 339 SAQVLRGDKI--------ALIGPNGCGKTTLLKLM--LGQLQAD---SGRIHVGT----KLEVAYFdQHRAELD------ 395
Cdd:PRK14247 15 QVEVLDGVNLeipdntitALMGPSGSGKSTLLRVFnrLIELYPEarvSGEVYLDGqdifKMDVIEL-RRRVQMVfqipnp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 396 -PDKTVMDNLAEG-KQEVMVNGKP------RHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEP 467
Cdd:PRK14247 94 iPNLSIFENVALGlKLNRLVKSKKelqervRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
....*
gi 15830287 468 TNDLD 472
Cdd:PRK14247 174 TANLD 178
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
330-473 |
3.98e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.51 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAELDPD-----KTVMDNL 404
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTLNGEPLAAIDAPrlarlRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 405 AE-----GKQEVMVNGKPRHVL---------GYLQDFLFHPKRAMTPVR----ALSGGERNRLLLARLFLK--------- 457
Cdd:PRK13547 92 AQpafafSAREIVLLGRYPHARragalthrdGEIAWQALALAGATALVGrdvtTLSGGELARVQFARVLAQlwpphdaaq 171
|
170
....*....|....*.
gi 15830287 458 PSNLLILDEPTNDLDV 473
Cdd:PRK13547 172 PPRYLLLDEPTAALDL 187
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
345-472 |
4.19e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.57 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 345 GDKIALIGPNGCGKTTLLKLMLGQLQADSGRiHVGTKLEVAYFDQhrAELDPDKTVMDNLAEGKQ-EVMVNGKPRHVLGY 423
Cdd:PLN03130 643 GSLVAIVGSTGEGKTSLISAMLGELPPRSDA-SVVIRGTVAYVPQ--VSWIFNATVRDNILFGSPfDPERYERAIDVTAL 719
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15830287 424 LQDFLFHPKRAMTPV--RA--LSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PLN03130 720 QHDLDLLPGGDLTEIgeRGvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
350-472 |
4.64e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 42.69 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 350 LIGPNGCGKTTLLKLMLGQLQADSGRIHVGT----------------KLEVAY-FDQHRAELDPDKTVMD------NLAE 406
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkkikevkrlRKEIGLvFQFPEYQLFQETIEKDiafgpvNLGE 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287 407 GKQEVMvnGKPRHVLGYLQDFLFHPKRamTPVRaLSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13645 122 NKQEAY--KKVPELLKLVQLPEDYVKR--SPFE-LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
158-212 |
4.75e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 42.79 E-value: 4.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 158 SGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHD 212
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvqaQIMTLLNELKREFNTAIIMITHD 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
143-230 |
6.25e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 41.90 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 143 LAQLGLDP--NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD-IETID---WLEGFLKTFNGTIIFISHDRSFI 216
Cdd:PRK11300 138 LERVGLLEhaNRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNpKETKEldeLIAELRNEHNVTVLLIEHDMKLV 217
|
90
....*....|....
gi 15830287 217 RNMATRIVDLDRGK 230
Cdd:PRK11300 218 MGISDRIYVVNQGT 231
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
136-232 |
6.43e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.99 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 136 ENRINEVLAQLGL-DPNVALSS----LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTI 206
Cdd:PRK10418 115 DATLTAALEAVGLeNAARVLKLypfeMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVvaqaRILDLLESIVQKRALGM 194
|
90 100
....*....|....*....|....*.
gi 15830287 207 IFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK10418 195 LLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
138-261 |
6.90e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.41 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 138 RINEVLAQLGLDPNV--ALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETID--WLEGFLKTFNG-TIIFISHD 212
Cdd:NF000106 124 RADELLERFSLTEAAgrAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNevWDEVRSMVRDGaTVLLTTQY 203
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15830287 213 RSFIRNMATRIVDLDRGKLVTyPGNYDQYLLE-KEEALRVEELQNAEFDR 261
Cdd:NF000106 204 MEEAEQLAHELTVIDRGRVIA-DGKVDELKTKvGGRTLQIRPAHAAELDR 252
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
349-473 |
7.04e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 42.17 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 349 ALIGPNGCGKTTLLKLMLGQLQADSGRIHVGT---------------KLEVAY-FDQHRaeLDPDKTVMDNLAEGKQEVM 412
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaekgiclppeKRRIGYvFQDAR--LFPHYKVRGNLRYGMAKSM 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830287 413 VNGKPRHV--LGyLQDFLfhpKRamTPvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK11144 106 VAQFDKIValLG-IEPLL---DR--YP-GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
93-217 |
8.17e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.99 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 93 EQAEYLKRYHDISRLVMNDPS--EKNLNELAKVQEQLDHHNLWQLENrinevlaqlGLDPNVALSSLSGGWLRKAALGRA 170
Cdd:pfam13304 180 DLKELLQRLVRGLKLADLNLSdlGEGIEKSLLVDDRLRERGLILLEN---------GGGGELPAFELSDGTKRLLALLAA 250
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15830287 171 LVS---NPRVLLLDEPTNHLDIETIDWLEGFLK---TFNGTIIFISHDRSFIR 217
Cdd:pfam13304 251 LLSalpKGGLLLIDEPESGLHPKLLRRLLELLKelsRNGAQLILTTHSPLLLD 303
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
305-495 |
8.80e-04 |
|
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: 42.63 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 305 AKMQVEEAS------RSGKIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV 378
Cdd:TIGR00957 1266 APWQIQETAppsgwpPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 379 gTKLEVAYFDQH--------------------RAELDPDKTVMDnlaegkQEVMVNGKPRHVLGY---LQDFLFHpkRAM 435
Cdd:TIGR00957 1346 -DGLNIAKIGLHdlrfkitiipqdpvlfsgslRMNLDPFSQYSD------EEVWWALELAHLKTFvsaLPDKLDH--ECA 1416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 436 TPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY--QGTVLLVSH 495
Cdd:TIGR00957 1417 EGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQfeDCTVLTIAH 1478
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-268 |
1.12e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.01 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYeQDLIVARLQQDPPRNVEGSV-------YDF 86
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF-HDIPLTKLQLDSWRSRLAVVsqtpflfSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 87 VAEGI--------EEQAEYLKRyhdisrlvmndpseknlneLAKVQEqlDHHNLWQlenrinevlaqlGLDPNVALSS-- 156
Cdd:PRK10789 405 VANNIalgrpdatQQEIEHVAR-------------------LASVHD--DILRLPQ------------GYDTEVGERGvm 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 157 LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NGTIIFISHDRSFIRNmATRIVDLDRG----- 229
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWgeGRTVIISAHRLSALTE-ASEILVMQHGhiaqr 530
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15830287 230 ----KLVTYPGNY-DQYllekeealRVEELQNAEFDRKLAQEEV 268
Cdd:PRK10789 531 gnhdQLAQQSGWYrDMY--------RYQQLEAALDDAPEIREEA 566
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
335-496 |
1.21e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 41.56 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQHRAE----------LDPDKTV 400
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiAKISDAELREVRRKkiamvfqsfaLMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 MDNLAEGKQEVMVNGKPRH--VLGYLQDFLFHPKRAMTPvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLEL 478
Cdd:PRK10070 124 LDNTAFGMELAGINAEERRekALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180
....*....|....*....|..
gi 15830287 479 LEELI----DSYQGTVLLVSHD 496
Cdd:PRK10070 203 MQDELvklqAKHQRTIVFISHD 224
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
19-219 |
1.50e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.75 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 19 LDNAELHIEDNERV-CLVGRNGAGKSTLMKILN-----REQGLDDGRIiyeQDLIVARLQQDPPRNV------EGSVYDF 86
Cdd:COG3950 14 FEDLEIDFDNPPRLtVLVGENGSGKTTLLEAIAlalsgLLSRLDDVKF---RKLLIRNGEFGDSAKLilyygtSRLLLDG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 87 VAEGIEEQ-AEYLKRYHDISRLVMNDPSEKNLNE-LAKVQEQLDHHNLWQLENRINEV----------LAQLGLDPN--- 151
Cdd:COG3950 91 PLKKLERLkEEYFSRLDGYDSLLDEDSNLREFLEwLREYLEDLENKLSDELDEKLEAVrealnkllpdFKDIRIDRDpgr 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 152 ----------VALSSLSGG--------------WLRKAALGRALVSNPRVLLLDEPTNHLDIEtidW----LEGFLKTF- 202
Cdd:COG3950 171 lvildkngeeLPLNQLSDGersllalvgdlarrLAELNPALENPLEGEGIVLIDEIDLHLHPK---WqrriLPDLRKIFp 247
|
250
....*....|....*..
gi 15830287 203 NGTIIFISHDRSFIRNM 219
Cdd:COG3950 248 NIQFIVTTHSPLILSSL 264
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
153-189 |
1.52e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 1.52e-03
10 20 30
....*....|....*....|....*....|....*..
gi 15830287 153 ALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI 189
Cdd:PRK10982 388 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV 424
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
437-532 |
1.54e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 437 PVRALSGGERNRLLLARLFLKPSN---LLILDEPTNDL---DVETLELLEELIDSYQGTVLLVSHDrqfVDNTVTECWIF 510
Cdd:TIGR00630 826 PATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLhfdDIKKLLEVLQRLVDKGNTVVVIEHN---LDVIKTADYII 902
|
90 100
....*....|....*....|....*.
gi 15830287 511 ----EGGGKigryvGGYHDARGQQEQ 532
Cdd:TIGR00630 903 dlgpEGGDG-----GGTVVASGTPEE 923
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
332-585 |
2.10e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 40.58 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAyfdqhraeldpdKTVMDNLAEGKQEV 411
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITP------------ETGNKNLKKLRKKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 412 -MVNGKPRHVL---GYLQDFLFHPK-----------RAMTPVRA--------------LSGGERNRLLLARLFLKPSNLL 462
Cdd:PRK13641 88 sLVFQFPEAQLfenTVLKDVEFGPKnfgfsedeakeKALKWLKKvglsedliskspfeLSGGQMRRVAIAGVMAYEPEIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 463 ILDEPTNDLDVETLELLEELIDSYQG---TVLLVSHDRQFVDNTVTECWIFEGGGKIGryvggyHDArgqqEQYVALKQP 539
Cdd:PRK13641 168 CLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKLIK------HAS----PKEIFSDKE 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15830287 540 AVKKN--EEPAAPKaetVKRSSSKLSYKLQRELEQLPQLLEDLEAKLE 585
Cdd:PRK13641 238 WLKKHylDEPATSR---FASKLEKGGFKFSEMPLTIDELVDGIKNNLK 282
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-496 |
2.70e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 40.08 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 349 ALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKL----------EVAYFDQHRAEL--DPDK---TVMDNLAEG------ 407
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLlggrsifnyrDVLEFRRRVGMLfqRPNPfpmSIMDNVLAGvrahkl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 408 --KQEVMVNGKPRHVLGYLQDFLfHPKRAMTPVRaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDS 485
Cdd:PRK14271 131 vpRKEFRGVAQARLTEVGLWDAV-KDRLSDSPFR-LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS 208
|
170
....*....|...
gi 15830287 486 YQG--TVLLVSHD 496
Cdd:PRK14271 209 LADrlTVIIVTHN 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
345-472 |
2.77e-03 |
|
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: 41.15 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 345 GDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAE-LDPDKTVMDNLAEGKQEVMVNGKPRHV-- 420
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSILTNISDVHQNMgYCPQFDAIDDLLTGREHLYLYARLRGVpa 2044
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 421 ----------LGYLQDFLFHPKRAMTpvraLSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR01257 2045 eeiekvanwsIQSLGLSLYADRLAGT----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
322-471 |
2.88e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 322 MEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFDQHRA--------- 392
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK-EIDFKSSKEAlengismvh 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 393 -ELD--PDKTVMDNLAEGKQevmvngkPRHVLGYLQDFLFHPKRAM-----------TPVRALSGGERNRLLLARLFLKP 458
Cdd:PRK10982 80 qELNlvLQRSVMDNMWLGRY-------PTKGMFVDQDKMYRDTKAIfdeldididprAKVATLSVSQMQMIEIAKAFSYN 152
|
170
....*....|...
gi 15830287 459 SNLLILDEPTNDL 471
Cdd:PRK10982 153 AKIVIMDEPTSSL 165
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
319-498 |
3.35e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 39.76 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLM--LGQLQAD---SGRI-HVGTKLEVAYFD--QH 390
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIvYNGHNIYSPRTDtvDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 RAEL-----DPDK---TVMDNLAEGkqeVMVNG-KPRHVLGYLQDFLFHPKRAMTPVR--------ALSGGERNRLLLAR 453
Cdd:PRK14239 85 RKEIgmvfqQPNPfpmSIYENVVYG---LRLKGiKDKQVLDEAVEKSLKGASIWDEVKdrlhdsalGLSGGQQQRVCIAR 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15830287 454 LFLKPSNLLILDEPTNDLDVETLELLEELI----DSYqgTVLLVSHDRQ 498
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLlglkDDY--TMLLVTRSMQ 208
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
347-368 |
3.92e-03 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 38.24 E-value: 3.92e-03
10 20
....*....|....*....|..
gi 15830287 347 KIALIGPNGCGKTTLLKLMLGQ 368
Cdd:COG4917 3 RIMLIGRSGAGKTTLTQALNGE 24
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
439-543 |
4.46e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.40 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 439 RALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHDRQFVDNTvTECWIFEGGG 514
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKADKTIITIAHRIASIKRS-DKIVVFNNPD 1435
|
90 100
....*....|....*....|....*....
gi 15830287 515 KIGRYVggyhDARGQQEQYVALKQPAVKK 543
Cdd:PTZ00265 1436 RTGSFV----QAHGTHEELLSVQDGVYKK 1460
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
337-513 |
5.08e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 39.34 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 337 DFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAyfDQHRAELDP-----------------DKT 399
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITS--TSKNKDIKQirkkvglvfqfpesqlfEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 400 VMDNLAEGKQEVMVNGKPRHVLGY-------LQDFLFHpkraMTPVRaLSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13649 103 VLKDVAFGPQNFGVSQEEAEALAReklalvgISESLFE----KNPFE-LSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15830287 473 VETLELLEELIDS-YQG--TVLLVSHDRQFVDNTVTECWIFEGG 513
Cdd:PRK13649 178 PKGRKELMTLFKKlHQSgmTIVLVTHLMDDVANYADFVYVLEKG 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
14-212 |
6.54e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 38.92 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN----REQGL---DDGRIIYEQDLIVAR----LQQDPPRNVEG- 81
Cdd:PRK13642 18 SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDglfeEFEGKvkiDGELLTAENVWNLRRkigmVFQNPDNQFVGa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 82 SVYDFVAEGIEEQAeylkryhdISRLVMndpseknlneLAKVQEQLDHHNLWQLENRinevlaqlglDPnvalSSLSGGW 161
Cdd:PRK13642 98 TVEDDVAFGMENQG--------IPREEM----------IKRVDEALLAVNMLDFKTR----------EP----ARLSGGQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15830287 162 LRKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHD 212
Cdd:PRK13642 146 KQRVAVAGIIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
350-406 |
7.76e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.83 E-value: 7.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 350 LIGPNGCGKTTLLKLMLGQLQADSGR----------IHVGTKLE----VAYFDQHRAELDPDKTVMDNLAE 406
Cdd:COG3950 30 LVGENGSGKTTLLEAIALALSGLLSRlddvkfrkllIRNGEFGDsaklILYYGTSRLLLDGPLKKLERLKE 100
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| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
156-190 |
8.70e-03 |
|
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: 37.55 E-value: 8.70e-03
10 20 30
....*....|....*....|....*....|....*
gi 15830287 156 SLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIE 190
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE 105
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| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-66 |
9.07e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 38.01 E-value: 9.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMK----ILNREQG--------LDDGRIIYEQDL 66
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKliagLLNPEKGeilferqsIKKDLCTYQKQL 76
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