|
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: 1313.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 1 MSLISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQDPPRNVT 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 81 GTVYDFVAEGIAEQAAYLKGYHDVSQLVMTDPSDKNLNELARLQEQLDNLGLWQLDSRINEVLEQLNLDPNAELSSLSGG 160
Cdd:PRK11147 81 GTVYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAALSSLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 161 WLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQ 240
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 241 YLLDKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKAMRRERGERREVMGSAKMQVEEAARSGKIVF 320
Cdd:PRK11147 241 YLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVMGTAKMQVEEASRSGKIVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQHRAELDPDKTV 400
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 401 MDNLAEGKQEVMVNGKPRHVLGYLQDFMFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:PRK11147 401 MDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 481 ELVDGYQGTVMLVSHDRQFVDNTVTECWIFEGEGRIGQYVGGYHDARGQQAQYLAQKQQISKKAVEAAQPKAESVKRASG 560
Cdd:PRK11147 481 ELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGYHDARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSK 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695765469 561 KLSYNLQRELEQLPQRLEELETQLQTLQEQVADPSFFGQSHDHTQQVLAQLAEAEQALETAFERWEYLEGLKNGA 635
Cdd:PRK11147 561 KLSYKLQRELEQLPQLLEDLEAEIEALQAQVADADFFSQPHEQTQKVLADLADAEQELEVAFERWEELEALKNGG 635
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-536 |
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: 664.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 6 MHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQDPPRNVTGTVYD 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 86 FVAEGIAEQAAYLKGYHDVSQLvmTDPSDKNLNELARLQEQLDNLGLWQLDSRINEVLEQLNL---DPNAELSSLSGGWL 162
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAK--LAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFpeeDLDRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 163 RKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYL 242
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 243 LDKEEALRVEELQNAEFDRKLAQEEVWIRQ-GIKARR-TRNEGRVRALKAMRRERGERREvmGSAKMQVEEAARSGKIVF 320
Cdd:COG0488 239 EQRAERLEQEAAAYAKQQKKIAKEEEFIRRfRAKARKaKQAQSRIKALEKLEREEPPRRD--KTVEIRFPPPERLGKKVL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQHRAELDPDKTV 400
Cdd:COG0488 317 ELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKTV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 401 MDNLAEGKQevmvNGKPRHVLGYLQDFMFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:COG0488 397 LDELRDGAP----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 481 ELVDGYQGTVMLVSHDRQFVDNTVTECWIFEgEGRIGQYVGGYHDargqqaqYLAQ 536
Cdd:COG0488 473 EALDDFPGTVLLVSHDRYFLDRVATRILEFE-DGGVREYPGGYDD-------YLEK 520
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
34-551 |
9.66e-132 |
|
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: 397.77 E-value: 9.66e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 34 LVGRNGAGKSTLMKILnreQGLD---DGRIIYEQDLVVARLQQDPPRNVTGTVYDFVAEGIAEQAAYLKGYHDVSQLvMT 110
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIM---AGVDkdfNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFNEISAK-YA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 111 DPS---DKNLNELARLQEQLDNLGLWQLDSRINEVLEQLNLDPN-AELSSLSGGWLRKAALGRALVSGPRVLLLDEPTNH 186
Cdd:TIGR03719 112 EPDadfDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWdADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNH 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 187 LDIETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYLLDKEEALRVEELQNAEFDRKLAQE 266
Cdd:TIGR03719 192 LDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQKRLEQEEKEESARQKTLKRE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 267 EVWIRQGIKARRTRNEGRVRALKAMRRERGERREvmGSAKMQVEEAARSGKIVFEMENVNYQVDGKVLIKDFSAQIQRGD 346
Cdd:TIGR03719 272 LEWVRQSPKGRQAKSKARLARYEELLSQEFQKRN--ETAEIYIPPGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 347 KIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQHRAELDPDKTVMDNLAEGKQEVMVNGKPRHVLGYLQD 426
Cdd:TIGR03719 350 IVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGR 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 427 FMFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDGYQGTVMLVSHDRQFVDNTVTE 506
Cdd:TIGR03719 430 FNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATH 509
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 695765469 507 CWIFEGEGRIGQYVGGYHDargqqaqYLAQKQqiSKKAVEAAQPK 551
Cdd:TIGR03719 510 ILAFEGDSHVEWFEGNFSE-------YEEDKK--RRLGEDADQPH 545
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-551 |
2.77e-128 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 389.09 E-value: 2.77e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 34 LVGRNGAGKSTLMKILnreQGLD---DGRIIYEQDLVVARLQQDPPRNVTGTVYDFVAEGIAEQAAYLKGYHDVSQLvMT 110
Cdd:PRK11819 38 VLGLNGAGKSTLLRIM---AGVDkefEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAEVKAALDRFNEIYAA-YA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 111 DP---SDKNLNELARLQEQLDNLGLWQLDSRINEVLEQLNL-DPNAELSSLSGGWLRKAALGRALVSGPRVLLLDEPTNH 186
Cdd:PRK11819 114 EPdadFDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCpPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNH 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 187 LDIETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYLLDKEEALRVEELQNAEFDRKLAQE 266
Cdd:PRK11819 194 LDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKAKRLAQEEKQEAARQKALKRE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 267 EVWIRQGIKARRTRNEGRVRALKAMRRERGERREvmGSAKMQVEEAARSGKIVFEMENVNYQVDGKVLIKDFSAQIQRGD 346
Cdd:PRK11819 274 LEWVRQSPKARQAKSKARLARYEELLSEEYQKRN--ETNEIFIPPGPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 347 KIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQHRAELDPDKTVMDNLAEGKQEVMVNGKPRHVLGYLQD 426
Cdd:PRK11819 352 IVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKVGNREIPSRAYVGR 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 427 FMFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDGYQGTVMLVSHDRQFVDNTVTE 506
Cdd:PRK11819 432 FNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATH 511
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 695765469 507 CWIFEGEGRIGQYVGGYHDargqqaqYLAQKqqISKKAVEAAQPK 551
Cdd:PRK11819 512 ILAFEGDSQVEWFEGNFQE-------YEEDK--KRRLGADAARPH 547
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-537 |
9.64e-81 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 264.83 E-value: 9.64e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 13 FSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQDPPRNVTGTVYDFVAEGIA 92
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTVIMGHT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 93 EQAAylkgyhdvsqlVMT---------DPSDKNLNELARLQEQLDNLGLWQLDSRINEVLEQLNLDP---NAELSSLSGG 160
Cdd:PRK15064 91 ELWE-----------VKQerdriyalpEMSEEDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEeqhYGLMSEVAPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 161 WLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQ 240
Cdd:PRK15064 160 WKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 241 YLldkEEALRVEELQNAEFDRKLAQ-EEVwirQGIKARRTRNEGRVRA----LKAMRrergerrevmgsaKMQVEEAARS 315
Cdd:PRK15064 240 YM---TAATQARERLLADNAKKKAQiAEL---QSFVSRFSANASKAKQatsrAKQID-------------KIKLEEVKPS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 316 GK----IVFEM-----------ENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGT 380
Cdd:PRK15064 301 SRqnpfIRFEQdkklhrnalevENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 381 KLEVAYFDQ-HRAELDPDKTVMDNLAEGKQ----EVMVngkpRHVLGYLqdfMFHPKRAMTPVRALSGGERNRLLLARLF 455
Cdd:PRK15064 381 NANIGYYAQdHAYDFENDLTLFDWMSQWRQegddEQAV----RGTLGRL---LFSQDDIKKSVKVLSGGEKGRMLFGKLM 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 456 LKPSNLLILDEPTNDLDVETLELLEELVDGYQGTVMLVSHDRQFVDNTVTEcwIFE-GEGRIGQYVGGYHDargqqaqYL 534
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATR--IIEiTPDGVVDFSGTYEE-------YL 524
|
...
gi 695765469 535 AQK 537
Cdd:PRK15064 525 RSQ 527
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-631 |
2.42e-67 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 231.98 E-value: 2.42e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQDPPRnVTGTVYDFVAEGIAEqaay 97
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPA-LPQPALEYVIDGDRE---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 98 lkgYHDVSQLVMTDPSDKNLNELARLQEQLDNLGLWQLDSRINEVLEQLNLDpNAEL----SSLSGGWLRKAALGRALVS 173
Cdd:PRK10636 91 ---YRQLEAQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFS-NEQLerpvSDFSGGWRMRLNLAQALIC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 174 GPRVLLLDEPTNHLDIETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYllDKEEALRVEE 253
Cdd:PRK10636 167 RSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSF--EVQRATRLAQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 254 lQNAEFD---RKLAQEEVWI-RQGIKARRTRN-EGRVRALKAMRRERGERREVMGSAKMQVEEAARSGkiVFEMENVNYQ 328
Cdd:PRK10636 245 -QQAMYEsqqERVAHLQSYIdRFRAKATKAKQaQSRIKMLERMELIAPAHVDNPFHFSFRAPESLPNP--LLKMEKVSAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 329 VDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQHRAE-LDPDKTVMDNLAEG 407
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEfLRADESPLQHLARL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 408 KQEVMvngkPRHVLGYLQDFMFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDGYQ 487
Cdd:PRK10636 402 APQEL----EQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 488 GTVMLVSHDRQFVDNTVTECWIFEgEGRIGQYVGGYHDAR----GQQAQYLAQKQQISKKAVEAAQPKAESVKRASG--K 561
Cdd:PRK10636 478 GALVVVSHDRHLLRSTTDDLYLVH-DGKVEPFDGDLEDYQqwlsDVQKQENQTDEAPKENNANSAQARKDQKRREAElrT 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695765469 562 LSYNLQRELEQLPQRLEELETQLQTLQEQVADPSFFGQSHDHT-QQVLAQLAEAEQALETAFERW----EYLEGL 631
Cdd:PRK10636 557 QTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAElTACLQQQASAKSGLEECEMAWleaqEQLEQM 631
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-525 |
5.80e-54 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 196.62 E-value: 5.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 4 ISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMK---------------ILNREQGL--DDG---RIIYE 63
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhaidgipkncqILHVEQEVvgDDTtalQCVLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 64 QDLVVARLQQDPPRNVTGTvydfvaEGIAEQAAYLKGYHDVSQLVMTDPSDKNLNELARLQEQLDnlgLWQLDSRINEVL 143
Cdd:PLN03073 258 TDIERTQLLEEEAQLVAQQ------RELEFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELID---AYTAEARAASIL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 144 EQLNLDPNAEL---SSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKGTIIFISHDRSFIRNMA 220
Cdd:PLN03073 329 AGLSFTPEMQVkatKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVV 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 221 TRIVDLDRGKLVTYPGNYDQYLLDKEEALRVEELQNAEFDRKLAQEEVWI---RQGIKaRRTRNEGRVRALKAMRRERGE 297
Cdd:PLN03073 409 TDILHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIdkfRYNAK-RASLVQSRIKALDRLGHVDAV 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 298 RREVMGSAKMQVEEAARSGKIV-FEMENVNYQvDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRI 376
Cdd:PLN03073 488 VNDPDYKFEFPTPDDRPGPPIIsFSDASFGYP-GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 377 HVGTKLEVAYFDQHRAE-LDPDKTVMDNLAEgkqevMVNGKPRHVL-GYLQDFMFHPKRAMTPVRALSGGERNRLLLARL 454
Cdd:PLN03073 567 FRSAKVRMAVFSQHHVDgLDLSSNPLLYMMR-----CFPGVPEQKLrAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKI 641
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765469 455 FLKPSNLLILDEPTNDLDVETLELLEELVDGYQGTVMLVSHDRQFVDNTVTECWIFEgEGRIGQYVGGYHD 525
Cdd:PLN03073 642 TFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVS-EGKVTPFHGTFHD 711
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
321-514 |
3.04e-52 |
|
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: 176.10 E-value: 3.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQhraeldpdktv 400
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 401 mdnlaegkqevmvngkprhvlgylqdfmfhpkramtpvraLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:cd03221 71 ----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALE 110
|
170 180 190
....*....|....*....|....*....|....
gi 695765469 481 ELVDGYQGTVMLVSHDRQFVDNTVTECWIFEGEG 514
Cdd:cd03221 111 EALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-242 |
1.02e-46 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 172.56 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 3 LISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQDpprnvtgt 82
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQH-------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 83 vydfvaegiaeqaaylkgyHDvsQLvmtDPSDKNLNELARLQEQLDnlglwqlDSRINEVLEQLNLDP---NAELSSLSG 159
Cdd:COG0488 387 -------------------QE--EL---DPDKTVLDELRDGAPGGT-------EQEVRGYLGRFLFSGddaFKPVGVLSG 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 160 GWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYD 239
Cdd:COG0488 436 GEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYD 515
|
...
gi 695765469 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 |
9.68e-45 |
|
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: 9.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 4 ISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQdpprnvtgtv 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 84 ydfvaegiaeqaaylkgyhdvsqlvmtdpsdknlnelarlqeqldnlglwqldsrinevleqlnldpnaelssLSGGWLR 163
Cdd:cd03221 71 -------------------------------------------------------------------------LSGGEKM 77
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765469 164 KAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd03221 78 RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-473 |
2.58e-42 |
|
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: 160.07 E-value: 2.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFS----DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNR---EQGLDDGRIIYE-QDLV----------VARLQ 72
Cdd:COG1123 10 LSVRypggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDgRDLLelsealrgrrIGMVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 73 QDPPRNVTG-TVYDFVAEGIAEQaaylkgyhDVSQLVMTdpsdknlnelARLQEQLDNLGLWQ-LDSRINEvleqlnldp 150
Cdd:COG1123 90 QDPMTQLNPvTVGDQIAEALENL--------GLSRAEAR----------ARVLELLEAVGLERrLDRYPHQ--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 151 naelssLSGGWLRKAALGRALVSGPRVLLLDEPTNHLD----IETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDL 226
Cdd:COG1123 143 ------LSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 227 DRGKLVtypgnydqylldkeEALRVEELQnaefdrklaqeevwirqgikarrtrneGRVRALKAMRRergerrevMGSAK 306
Cdd:COG1123 217 DDGRIV--------------EDGPPEEIL---------------------------AAPQALAAVPR--------LGAAR 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 307 MQVEEAARSGKIVFEMENVN--YQVDGK---VLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG-- 379
Cdd:COG1123 248 GRAAPAAAAAEPLLEVRNLSkrYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgk 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 380 --TKLEVAYFDQHRAE-----------LDPDKTVMDNLAEG--------KQEVMvngkpRHVLGYLQDFMFHPKRAMTPV 438
Cdd:COG1123 328 dlTKLSRRSLRELRRRvqmvfqdpyssLNPRMTVGDIIAEPlrlhgllsRAERR-----ERVAELLERVGLPPDLADRYP 402
|
490 500 510
....*....|....*....|....*....|....*.
gi 695765469 439 RALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG1123 403 HELSGGQRQRVAIARaLALEPK-LLILDEPTSALDV 437
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-230 |
4.57e-34 |
|
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: 128.74 E-value: 4.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFS----DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYeQDLVVARLQQDPPRNVTGTVYDF 86
Cdd:cd03225 5 LSFSypdgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV-DGKDLTKLSLKELRRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 87 VAegiaeqaaylkgyhdvSQLVMTDPSDknlnELARLQEqldNLGLWQ--LDSRINEVLEQLNLDP--NAELSSLSGGWL 162
Cdd:cd03225 84 PD----------------DQFFGPTVEE----EVAFGLE---NLGLPEeeIEERVEEALELVGLEGlrDRSPFTLSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765469 163 RKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
12-258 |
2.86e-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: 127.67 E-value: 2.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYeqDLVVARLQQDPPRNVTGTVYDFVaegi 91
Cdd:COG4555 10 KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI--DGEDVRKEPREARRQIGVLPDER---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 92 aEQAAYLKGYhdvsqlvmtdpsdKNLNELARLQEQLDNlglwQLDSRINEVLEQLNLDPNAE--LSSLSGGWLRKAALGR 169
Cdd:COG4555 84 -GLYDRLTVR-------------ENIRYFAELYGLFDE----ELKKRIEELIELLGLEEFLDrrVGELSTGMKKKVALAR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 170 ALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIVDLDRGKLV---TYPGNYDQYLL 243
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCDRVVILHKGKVVaqgSLDELREEIGE 225
|
250
....*....|....*
gi 695765469 244 DKEEALRVEELQNAE 258
Cdd:COG4555 226 ENLEDAFVALIGSEE 240
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-231 |
3.81e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.43 E-value: 3.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 1 MSLISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLVVARL------QQ 73
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrLFGKPPRRARRrigyvpQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 74 DP-PRNVTGTVYDFVAEGIAEQAAYLKGYHdvsqlvmtdPSDKnlnelARLQEQLDNLGLWQL-DSRINEvleqlnldpn 151
Cdd:COG1121 84 AEvDWDFPITVRDVVLMGRYGRRGLFRRPS---------RADR-----EAVDEALERVGLEDLaDRPIGE---------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 152 aelssLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIVDLDR 228
Cdd:COG1121 140 -----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNR 214
|
...
gi 695765469 229 GKL 231
Cdd:COG1121 215 GLV 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
320-498 |
3.91e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.39 E-value: 3.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 320 FEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKL-----------EVAYFD 388
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 389 QhRAELdPDKTVMDNLAEGKQEVMVNGKPRHVLGYLQDFMFHPKRAMTPVRALSGGERNRLLLAR-LFLKPSNLLiLDEP 467
Cdd:COG4619 81 Q-EPAL-WGGTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRaLLLQPDVLL-LDEP 157
|
170 180 190
....*....|....*....|....*....|....*
gi 695765469 468 TNDLDVETLELLEELVDGY----QGTVMLVSHDRQ 498
Cdd:COG4619 158 TSALDPENTRRVEELLREYlaeeGRAVLWVSHDPE 192
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
317-571 |
3.05e-31 |
|
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: 128.51 E-value: 3.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 317 KIVFEMENVNYQVD-GKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQhRAELD 395
Cdd:TIGR03719 2 QYIYTMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQ-EPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 396 PDKTVMDNLAEGKQEVmvngkpRHVL------------------------GYLQDFMFHPK---------RAM------- 435
Cdd:TIGR03719 81 PTKTVRENVEEGVAEI------KDALdrfneisakyaepdadfdklaaeqAELQEIIDAADawdldsqleIAMdalrcpp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 436 --TPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDGYQGTVMLVSHDRQFVDNtVTEcWIFE-- 511
Cdd:TIGR03719 155 wdADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDN-VAG-WILEld 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765469 512 -GEGRigQYVGGYhdargqqAQYLAQKQQisKKAVEAaqpKAESVKRASgklsynLQRELE 571
Cdd:TIGR03719 233 rGRGI--PWEGNY-------SSWLEQKQK--RLEQEE---KEESARQKT------LKRELE 273
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-232 |
3.24e-31 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 122.07 E-value: 3.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 3 LISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDL----------VVARL 71
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgRDLaslsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 72 QQDPPRNVTGTVYDFVAEGiaeQAAYLKGYHDVSqlvmtdPSDknlnelarlqeqldnlglwqlDSRINEVLEQLNLDPN 151
Cdd:COG1120 81 PQEPPAPFGLTVRELVALG---RYPHLGLFGRPS------AED---------------------REAVEEALERTGLEHL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 152 AE--LSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVD 225
Cdd:COG1120 131 ADrpVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVL 210
|
....*..
gi 695765469 226 LDRGKLV 232
Cdd:COG1120 211 LKDGRIV 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-232 |
5.43e-31 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 120.90 E-value: 5.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFS---DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIY------EQDLVVARLQ-----Q 73
Cdd:COG1122 6 LSFSypgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN---GLlkpTSGEVLVdgkditKKNLRELRRKvglvfQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 74 DPpRN--VTGTVYDFVAEGiaeqaaylkgyhdvsqlvmtdpsdknlnelarlqeqLDNLGL--WQLDSRINEVLEQLNLD 149
Cdd:COG1122 83 NP-DDqlFAPTVEEDVAFG------------------------------------PENLGLprEEIRERVEEALELVGLE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 150 PNAELS--SLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIV 224
Cdd:COG1122 126 HLADRPphELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVI 205
|
....*...
gi 695765469 225 DLDRGKLV 232
Cdd:COG1122 206 VLDDGRIV 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
12-232 |
3.02e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 119.01 E-value: 3.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYeqdlvvarLQQDPPRNvtgtvydfva 88
Cdd:COG1131 9 RYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLL---GLlrpTSGEVRV--------LGEDVARD---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 89 egiaeQAAYLK--GYhdVSQLVMTDPsdkNLN--ELARLQEQLDNLGLWQLDSRINEVLEQLNLDPNAE--LSSLSGGWL 162
Cdd:COG1131 68 -----PAEVRRriGY--VPQEPALYP---DLTvrENLRFFARLYGLPRKEARERIDELLELFGLTDAADrkVGTLSGGMK 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695765469 163 RKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG1131 138 QRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAegkTVLLSTHYLEEAERLCDRVAIIDKGRIV 210
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
317-571 |
1.06e-29 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 123.69 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 317 KIVFEMENVNYQVDG-KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQhRAELD 395
Cdd:PRK11819 4 QYIYTMNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQ-EPQLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 396 PDKTVMDNLAEGKQEVM--------VN---GKPRHVL-------GYLQDFMFHP---------KRAM---------TPVR 439
Cdd:PRK11819 83 PEKTVRENVEEGVAEVKaaldrfneIYaayAEPDADFdalaaeqGELQEIIDAAdawdldsqlEIAMdalrcppwdAKVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 440 ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDGYQGTVMLVSHDRQFVDNtVTEcWIFE---GEGrI 516
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDN-VAG-WILEldrGRG-I 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 695765469 517 GqYVGGYhdargqqAQYLAQKQQisKKAVEAaqpKAESvkrasgKLSYNLQRELE 571
Cdd:PRK11819 240 P-WEGNY-------SSWLEQKAK--RLAQEE---KQEA------ARQKALKRELE 275
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
335-469 |
1.10e-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: 114.67 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 335 IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG-----------TKLEVAYFDQHrAELDPDKTVMDN 403
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQD-PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765469 404 LAEGKQEVMVNGKPR-----HVLGYLQDFMFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTN 469
Cdd:pfam00005 80 LRLGLLLKGLSKREKdaraeEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-504 |
1.25e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.50 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 319 VFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLE-----VAYFDQhRA 392
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfGKPPRrarrrIGYVPQ-RA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 393 ELDPDK--TVMDnlaegkqeVMVNGKPRHvLGylqdFMFHPKRA-------------MT-----PVRALSGGERNRLLLA 452
Cdd:COG1121 85 EVDWDFpiTVRD--------VVLMGRYGR-RG----LFRRPSRAdreavdealervgLEdladrPIGELSGGQQQRVLLA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 453 RLFLKPSNLLILDEPTNDLDVETLELLEELVDGYQG---TVMLVSHD----RQFVDNTV 504
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDlgavREYFDRVL 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-231 |
1.36e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 116.07 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 4 ISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLV-----------VARLQ 72
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLsampppewrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 73 QDPPRnVTGTVYDfvaegiaeqaaylkgyhdvsqlvmtdpsdkNLNELARLQEQLDNlglwqlDSRINEVLEQLNLDP-- 150
Cdd:COG4619 81 QEPAL-WGGTVRD------------------------------NLPFPFQLRERKFD------RERALELLERLGLPPdi 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 151 -NAELSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIET----IDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVD 225
Cdd:COG4619 124 lDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLT 203
|
....*.
gi 695765469 226 LDRGKL 231
Cdd:COG4619 204 LEAGRL 209
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-245 |
2.69e-29 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 122.31 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQDpprnvtgTVYDFvaegi 91
Cdd:PRK15064 328 GFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQD-------HAYDF----- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 92 aeqaaylkgyhdvsqlvmtdPSDKNLnelarlqeqLDNLGLWQ----LDSRINEVLEQL---NLDPNAELSSLSGGWLRK 164
Cdd:PRK15064 396 --------------------ENDLTL---------FDWMSQWRqegdDEQAVRGTLGRLlfsQDDIKKSVKVLSGGEKGR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 165 AALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYLLD 244
Cdd:PRK15064 447 MLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRS 526
|
.
gi 695765469 245 K 245
Cdd:PRK15064 527 Q 527
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
321-500 |
8.90e-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: 114.17 E-value: 8.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLE-----VAYFDQHRaEL 394
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLEkerkrIGYVPQRR-SI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 DPDK--TVMDnlaegkqeVMVNGKPRHVlgylqDFMFHPKRA-------------MT-----PVRALSGGERNRLLLARL 454
Cdd:cd03235 80 DRDFpiSVRD--------VVLMGLYGHK-----GLFRRLSKAdkakvdealervgLSeladrQIGELSGGQQQRVLLARA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695765469 455 FLKPSNLLILDEPTNDLDVETLELLEELVDGYQG---TVMLVSHDRQFV 500
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLV 195
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
323-503 |
2.53e-28 |
|
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: 112.57 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 323 ENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLEVAYFDQ-----HRAE 393
Cdd:COG4133 6 ENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgepiRDAREDYRRRlaylgHADG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 LDPDKTVMDNL---AEGKQEVMVNGKPRHVLGY--LQDFmfhpkrAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPT 468
Cdd:COG4133 86 LKPELTVRENLrfwAALYGLRADREAIDEALEAvgLAGL------ADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 695765469 469 NDLDVETLELLEELVDGY---QGTVMLVSHDRQFVDNT 503
Cdd:COG4133 160 TALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAA 197
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-230 |
4.31e-28 |
|
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: 111.80 E-value: 4.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 3 LISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIiyeqdlvvaRLQQDPPRNv 79
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRIL---AGLlppSAGEV---------LWNGEPIRD- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 80 tgtvydfVAEGIAEQAAYLkGYHDVSQLVMTdPSDkNLNELARLqeqldnLGLWQLDSRINEVLEQLNLDPNAEL--SSL 157
Cdd:COG4133 69 -------AREDYRRRLAYL-GHADGLKPELT-VRE-NLRFWAAL------YGLRADREAIDEALEAVGLAGLADLpvRQL 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 158 SGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFK---GTIIFISHDRSFIRnmATRIVDLDRGK 230
Cdd:COG4133 133 SAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
17-232 |
6.40e-28 |
|
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: 112.59 E-value: 6.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQDPPRNVtgtvydfvaegiaeqaa 96
Cdd:COG1124 19 PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV----------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 97 ylkgyhdvsQLVMTDPSD-----KNLNELarLQEQLDNLGLWQLDSRINEVLEQLNLDPnAELS----SLSGGWLRKAAL 167
Cdd:COG1124 82 ---------QMVFQDPYAslhprHTVDRI--LAEPLRIHGLPDREERIAELLEQVGLPP-SFLDryphQLSGGQRQRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 168 GRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
12-231 |
1.63e-27 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 109.02 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYEqDLVVARLQQDPPRNVtgtvydfva 88
Cdd:cd03230 9 RYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIL---GLlkpDSGEIKVL-GKDIKKEPEEVKRRI--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 89 eGIAEQAAYLkgYHDvsqlvMTdpsdknlnelarlqeqldnlglwqldsrineVLEQLNLdpnaelsslSGGWLRKAALG 168
Cdd:cd03230 76 -GYLPEEPSL--YEN-----LT-------------------------------VRENLKL---------SGGMKQRLALA 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 169 RALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFK---GTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:cd03230 108 QALLHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-473 |
2.61e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.89 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 3 LISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVarlqqdpPRNVT-- 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-------FRSPRda 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 81 -----GTVY-DF-------VAEGIaeqaaYLkGYHDVSQLVMtdpSDKNLNELARlqEQLDNLGLwqldsrinevleqlN 147
Cdd:COG1129 77 qaagiAIIHqELnlvpnlsVAENI-----FL-GREPRRGGLI---DWRAMRRRAR--ELLARLGL--------------D 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 148 LDPNAELSSLSGGwlRKA--ALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATR 222
Cdd:COG1129 132 IDPDTPVGDLSVA--QQQlvEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAqgvAIIYISHRLDEVFEIADR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 223 IVDLDRGKLVtypgnydqylldkeealrvEELQNAEFDRklaqEEVwIRQ--GikarrtrnegrvRALKAMRRergerre 300
Cdd:COG1129 210 VTVLRDGRLV-------------------GTGPVAELTE----DEL-VRLmvG------------RELEDLFP------- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 301 vmgsakmqvEEAARSGKIVFEMENVNyqVDGKVliKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-G 379
Cdd:COG1129 247 ---------KRAAAPGEVVLEVEGLS--VGGVV--RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLdG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 380 TKLE-----------VAYF--DQHRAELDPDKTVMDNLAEGKQEVMVNGKP-------RHVLGYLQDFMFHPKRAMTPVR 439
Cdd:COG1129 314 KPVRirsprdairagIAYVpeDRKGEGLVLDLSIRENITLASLDRLSRGGLldrrrerALAEEYIKRLRIKTPSPEQPVG 393
|
490 500 510
....*....|....*....|....*....|....*
gi 695765469 440 ALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG1129 394 NLSGGNQQKVVLAKwLATDPK-VLILDEPTRGIDV 427
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-232 |
3.05e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 109.76 E-value: 3.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 4 ISMHGAWLSFSDS-PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIY-EQDLvvARLQQD--PP--R 77
Cdd:COG2884 2 IRFENVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVnGQDL--SRLKRReiPYlrR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 78 NVtGTVY-DF-------VAEGIAeqaaylkgyhdvsqLVMtdpsdknlnELARLQEQldnlglwQLDSRINEVLEQLNLD 149
Cdd:COG2884 80 RI-GVVFqDFrllpdrtVYENVA--------------LPL---------RVTGKSRK-------EIRRRVREVLDLVGLS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 150 ------PNAelssLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIdwlEGFLKTFKG------TIIFISHDRSFIR 217
Cdd:COG2884 129 dkakalPHE----LSGGEQQRVAIARALVNRPELLLADEPTGNLDPETS---WEIMELLEEinrrgtTVLIATHDLELVD 201
|
250
....*....|....*
gi 695765469 218 NMATRIVDLDRGKLV 232
Cdd:COG2884 202 RMPKRVLELEDGRLV 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
321-496 |
1.09e-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: 107.14 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLE----------VAYFDQ 389
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLdGKDLAslspkelarkIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 390 HRAELDpdktvMDNLAEgkqevmvngkpRhvlgylqdfmfhpkramtPVRALSGGERNRLLLARLFLKPSNLLILDEPTN 469
Cdd:cd03214 81 ALELLG-----LAHLAD-----------R------------------PFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190
....*....|....*....|....*....|.
gi 695765469 470 DLDVETLELLEELV----DGYQGTVMLVSHD 496
Cdd:cd03214 127 HLDIAHQIELLELLrrlaRERGKTVVMVLHD 157
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
321-495 |
3.39e-26 |
|
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: 105.16 E-value: 3.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVN--YQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIhvgtklevaYFDQHraeldpdk 398
Cdd:cd03228 2 EFKNVSfsYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI---------LIDGV-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 399 tvmdNLAEGKQEVMvngkpRHVLGYL-QD-FMFHpkraMTpVRA--LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
Cdd:cd03228 65 ----DLRDLDLESL-----RKNIAYVpQDpFLFS----GT-IREniLSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180
....*....|....*....|...
gi 695765469 475 TLELLEELVDGYQG--TVMLVSH 495
Cdd:cd03228 131 TEALILEALRALAKgkTVIVIAH 153
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
310-502 |
9.50e-26 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 111.77 E-value: 9.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 310 EEAARSGKIVFEMENVNYQ-VDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLE---- 383
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILInGVDLSdldp 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 384 ------VAYFDQHrAELdPDKTVMDNLAEGK-----QEVmvngkpRHVLG--YLQDFMfhpkRAM-----TPV----RAL 441
Cdd:COG4988 407 aswrrqIAWVPQN-PYL-FAGTIRENLRLGRpdasdEEL------EAALEaaGLDEFV----AALpdgldTPLgeggRGL 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695765469 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDGY-QG-TVMLVSHDRQFVDN 502
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLaKGrTVILITHRLALLAQ 537
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
11-234 |
9.98e-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: 104.44 E-value: 9.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLvvarlQQDPPRNvtgtvydfvae 89
Cdd:cd03214 7 VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlLDGKDL-----ASLSPKE----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 90 gIAEQAAYlkgyhdVSQLvmtdpsdknlnelarlqeqLDNLGLWQLDSRinevleqlnldpnaELSSLSGGWLRKAALGR 169
Cdd:cd03214 71 -LARKIAY------VPQA-------------------LELLGLAHLADR--------------PFNELSGGERQRVLLAR 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 170 ALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVTY 234
Cdd:cd03214 111 ALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
320-516 |
1.29e-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: 105.49 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 320 FEMENVNYQV-DGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLEVAYFDQHRAEL--- 394
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdGKDITKKNLRELRRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 --DPD-----KTVMD-------NLAEGKQEVMvngkpRHVLGYLQDF-MFHPKRAmtPVRALSGGERNRLLLAR-LFLKP 458
Cdd:COG1122 81 fqNPDdqlfaPTVEEdvafgpeNLGLPREEIR-----ERVEEALELVgLEHLADR--PPHELSGGQKQRVAIAGvLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765469 459 SnLLILDEPTNDLDVETLELLEELVDGYQG---TVMLVSHDRQFVDNTVTECWIFEgEGRI 516
Cdd:COG1122 154 E-VLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLD-DGRI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-232 |
1.60e-25 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 110.76 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDlvVARLQQDPPRNVTGTVydfvaegiaeqaay 97
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgKD--LTKLSRRSLRELRRRV-------------- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 98 lkgyhdvsQLVMTDPSDkNLNELAR----LQEQLDNLGLW---QLDSRINEVLEQLNLDPNAEL---SSLSGGWLRKAAL 167
Cdd:COG1123 345 --------QMVFQDPYS-SLNPRMTvgdiIAEPLRLHGLLsraERRERVAELLERVGLPPDLADrypHELSGGQRQRVAI 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 168 GRALVSGPRVLLLDEPTNHLDIET----IDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVqaqiLNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-242 |
2.32e-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: 111.46 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFS----DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIIYEQdlvvarlqqdpprnvtgtv 83
Cdd:COG2274 479 VSFRypgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL---LGLyepTSGRILIDG------------------- 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 84 ydfvaegiaeqaaylkgyHDVSQLvmtdpsdkNLNELAR-----LQEQ-------LDNLGLWQL---DSRINEVLEQLNL 148
Cdd:COG2274 537 ------------------IDLRQI--------DPASLRRqigvvLQDVflfsgtiRENITLGDPdatDEEIIEAARLAGL 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 149 DP---------NAEL----SSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG--TIIFISHDR 213
Cdd:COG2274 591 HDfiealpmgyDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRL 670
|
250 260
....*....|....*....|....*....
gi 695765469 214 SFIRNmATRIVDLDRGKLVTYpGNYDQYL 242
Cdd:COG2274 671 STIRL-ADRIIVLDKGRIVED-GTHEELL 697
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
321-496 |
2.54e-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: 102.86 E-value: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVgtklevayFDQhraeldpdktv 400
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV--------LGK----------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 401 mdNLAEGKQEVmvngkpRHVLGYL-QDFMFHPKraMTpVR---ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETL 476
Cdd:cd03230 63 --DIKKEPEEV------KRRIGYLpEEPSLYEN--LT-VRenlKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESR 131
|
170 180
....*....|....*....|...
gi 695765469 477 ELLEELVDGY---QGTVMLVSHD 496
Cdd:cd03230 132 REFWELLRELkkeGKTILLSSHI 154
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
315-472 |
3.28e-25 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 110.69 E-value: 3.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 315 SGKIvfEMENVN--YQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGtklevayfDQHRA 392
Cdd:COG2274 471 KGDI--ELENVSfrYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID--------GIDLR 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 393 ELDPDK-----------------TVMDNLAEGKQEV----------MVNgkprhvlgyLQDF-MFHPKRAMTPV----RA 440
Cdd:COG2274 541 QIDPASlrrqigvvlqdvflfsgTIRENITLGDPDAtdeeiieaarLAG---------LHDFiEALPMGYDTVVgeggSN 611
|
170 180 190
....*....|....*....|....*....|..
gi 695765469 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:COG2274 612 LSGGQRQRLAIARALLRNPRILILDEATSALD 643
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-230 |
3.36e-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: 101.94 E-value: 3.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 5 SMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqdlvvarlqqdpprnvtgtvy 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 85 dfvaegiaeqaaylkgyhdvsqlvmtdpsDKNLNELaRLQEQLDNLGLwqldsrinevleqlnldpnaeLSSLSGGWLRK 164
Cdd:cd00267 60 -----------------------------GKDIAKL-PLEELRRRIGY---------------------VPQLSGGQRQR 88
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 165 AALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd00267 89 VALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-473 |
5.62e-25 |
|
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: 104.36 E-value: 5.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 319 VFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLE----------VAYF 387
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLAslsrrelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 388 DQHRaELDPDKTVMDNLAEGK------------------QEVMvngkprHVLGyLQDFmfhpkrAMTPVRALSGGERNRL 449
Cdd:COG1120 81 PQEP-PAPFGLTVRELVALGRyphlglfgrpsaedreavEEAL------ERTG-LEHL------ADRPVDELSGGERQRV 146
|
170 180
....*....|....*....|....
gi 695765469 450 LLARLFLKPSNLLILDEPTNDLDV 473
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDL 170
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
310-533 |
6.62e-25 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 109.09 E-value: 6.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 310 EEAARSGKIVFEMENVN--YQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLE--- 383
Cdd:COG4987 324 EPAPAPGGPSLELEDVSfrYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLgGVDLRdld 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 384 -------VAYFDQhraelDP---DKTVMDNLAEGKQEV----MvngkpRHVLG--YLQDF-MFHPKRAMTPV----RALS 442
Cdd:COG4987 404 eddlrrrIAVVPQ-----RPhlfDTTLRENLRLARPDAtdeeL-----WAALErvGLGDWlAALPDGLDTWLgeggRRLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 443 GGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDGYQG--TVMLVSHDRQFVDNTVTECWIfeGEGRIGQyV 520
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAgrTVLLITHRLAGLERMDRILVL--EDGRIVE-Q 550
|
250
....*....|...
gi 695765469 521 GGYHDARGQQAQY 533
Cdd:COG4987 551 GTHEELLAQNGRY 563
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-232 |
7.60e-25 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 102.60 E-value: 7.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 4 ISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYeQDLVVARLqqdPP--RNVtG 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI-DGRDVTGV---PPerRNI-G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 82 TVYDF--------VAEGIaeqaAY-LKgyhdvsqlVMTDPSDknlnelarlqeqldnlglwQLDSRINEVLEQLNLDPNA 152
Cdd:cd03259 76 MVFQDyalfphltVAENI----AFgLK--------LRGVPKA-------------------EIRARVRELLELVGLEGLL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 153 EL--SSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKT----FKGTIIFISHDRSFIRNMATRIVDL 226
Cdd:cd03259 125 NRypHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKElqreLGITTIYVTHDQEEALALADRIAVM 204
|
....*.
gi 695765469 227 DRGKLV 232
Cdd:cd03259 205 NEGRIV 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
321-496 |
1.15e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 102.83 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----------TKLEVAYFDQH 390
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLgedvardpaeVRRRIGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 391 rAELDPDKTVMDNLaegkqEVM--VNGKPRHVLG-----YLQDFMFHPKRAmTPVRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:COG1131 82 -PALYPDLTVRENL-----RFFarLYGLPRKEARerideLLELFGLTDAAD-RKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 695765469 464 LDEPTNDLDVETLELLEELVDGY--QG-TVMLVSHD 496
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELaaEGkTVLLSTHY 190
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
321-511 |
2.73e-24 |
|
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: 99.24 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKlEVAYFDQHRAeldpdktv 400
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-DIAKLPLEEL-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 401 mdnlaegkqevmvngkpRHVLGYL-QdfmfhpkramtpvraLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELL 479
Cdd:cd00267 72 -----------------RRRIGYVpQ---------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
170 180 190
....*....|....*....|....*....|....*
gi 695765469 480 EELVDGYQG---TVMLVSHDRQFVDNTVTECWIFE 511
Cdd:cd00267 120 LELLRELAEegrTVIIVTHDPELAELAADRVIVLK 154
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
332-538 |
3.16e-24 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 107.56 E-value: 3.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 332 KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQHRAELDpdKTVMDNLAEGKQE- 410
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALP--QPALEYVIDGDREy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 411 -------------------VMVNGK----------PR-----HVLGYLQDfmfhpkRAMTPVRALSGGERNRLLLARLFL 456
Cdd:PRK10636 92 rqleaqlhdanerndghaiATIHGKldaidawtirSRaasllHGLGFSNE------QLERPVSDFSGGWRMRLNLAQALI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 457 KPSNLLILDEPTNDLDVETLELLEELVDGYQGTVMLVSHDRQFVDNTVTECWIFEGEgRIGQYVGGYHDARGQQAQYLAQ 536
Cdd:PRK10636 166 CRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQ-SLFEYTGNYSSFEVQRATRLAQ 244
|
..
gi 695765469 537 KQ 538
Cdd:PRK10636 245 QQ 246
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
11-232 |
5.16e-24 |
|
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: 106.38 E-value: 5.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFS---DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLvvARLQQDPPRN-------- 78
Cdd:COG4988 342 VSFSypgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlINGVDL--SDLDPASWRRqiawvpqn 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 79 ---VTGTVYDFVAegiaeqaaylkgyhdvsqLVMTDPSDknlnelARLQEQLDNLGLWqldsrinEVLEQLNLDPNAEL- 154
Cdd:COG4988 420 pylFAGTIRENLR------------------LGRPDASD------EELEAALEAAGLD-------EFVAALPDGLDTPLg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 155 ---SSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIET---IdwLEGFLKTFKG-TIIFISHDRSFIRNmATRIVDLD 227
Cdd:COG4988 469 eggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETeaeI--LQALRRLAKGrTVILITHRLALLAQ-ADRILVLD 545
|
....*
gi 695765469 228 RGKLV 232
Cdd:COG4988 546 DGRIV 550
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
17-232 |
1.33e-23 |
|
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: 99.50 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqdlvvarlqqdpPRNVTGTvydfvaegiaeQAA 96
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFD------------GKDLLKL-----------SRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 97 YLKGYHDVSQLVMTDPsDKNLNELARLQEQL--------DNLGLWQLDSRINEVLEQLNLDP---NAELSSLSGGWLRKA 165
Cdd:cd03257 76 LRKIRRKEIQMVFQDP-MSSLNPRMTIGEQIaeplrihgKLSKKEARKEAVLLLLVGVGLPEevlNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765469 166 ALGRALVSGPRVLLLDEPTNHLD----IETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDvsvqAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
321-515 |
1.85e-23 |
|
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: 98.69 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDG--KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQHRAEL---- 394
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 --DPD-----KTVMDNLAEGkqevMVN-GKPRH-----VLGYLQDFMFHPKRAmTPVRALSGGERNRLLLAR-LFLKPsN 460
Cdd:cd03225 81 fqNPDdqffgPTVEEEVAFG----LENlGLPEEeieerVEEALELVGLEGLRD-RSPFTLSGGQKQRVAIAGvLAMDP-D 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695765469 461 LLILDEPTNDLDVETLELLEELVDGYQG---TVMLVSHDRQFVDNTVTECWIFEgEGR 515
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLE-DGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-230 |
3.62e-23 |
|
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: 96.87 E-value: 3.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 4 ISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLVVARLQQDPPRNVTGT 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 83 VYdfvaegiaeqaaylkgyhdvsqlvmtdpsdknlnelarlQEqldnlglWQLDSRINeVLEQLNLdpnaelsSLSGGWL 162
Cdd:cd03229 81 VF---------------------------------------QD-------FALFPHLT-VLENIAL-------GLSGGQQ 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695765469 163 RKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKT----FKGTIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd03229 107 QRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-231 |
4.72e-23 |
|
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: 97.60 E-value: 4.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 5 SMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRI------IYEQDLVVARLQQ-- 73
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAI---LGLlkpTSGSIrvfgkpLEKERKRIGYVPQrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 74 DPPRNVTGTVYDFVAEGIAEQAAYLKGYhdvsqlvmtDPSDKnlnelARLQEQLDNLGLWQLDSRinevleqlnldpnaE 153
Cdd:cd03235 78 SIDRDFPISVRDVVLMGLYGHKGLFRRL---------SKADK-----AKVDEALERVGLSELADR--------------Q 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 154 LSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd03235 130 IGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLLNRTV 209
|
.
gi 695765469 231 L 231
Cdd:cd03235 210 V 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-473 |
6.24e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.80 E-value: 6.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYEQDLVVARLQQDPPRNVTGTVY-DF-------V 87
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILY---GLyqpDSGEILIDGKPVRIRSPRDAIALGIGMVHqHFmlvpnltV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 88 AEGIAeqaayLkGYHDVSQLVMtdpsdkNLNELARlqeqldnlglwqldsRINEVLEQ--LNLDPNAELSSLSGGWLRKA 165
Cdd:COG3845 98 AENIV-----L-GLEPTKGGRL------DRKAARA---------------RIRELSERygLDVDPDAKVEDLSVGEQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 166 ALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIVDLDRGKLVtypgnydqyl 242
Cdd:COG3845 151 EILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAegkSIIFITHKLREVMAIADRVTVLRRGKVV---------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 243 ldkeEALRVEELQNAEfdrkLAQEEVwirqgikarrtrneGRVRALKAmrrergerrevmgsakmqVEEAARSGKIVFEM 322
Cdd:COG3845 221 ----GTVDTAETSEEE----LAELMV--------------GREVLLRV------------------EKAPAEPGEVVLEV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 323 ENVNYQVD-GKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG------------TKLEVAYF-- 387
Cdd:COG3845 261 ENLSVRDDrGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDgeditglsprerRRLGVAYIpe 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 388 DQHRAELDPDKTVMDNLAEGKQE-------VMVNGKP--RHVLGYLQDFMFHPKRAMTPVRALSGGERNRLLLARLFLKP 458
Cdd:COG3845 341 DRLGRGLVPDMSVAENLILGRYRrppfsrgGFLDRKAirAFAEELIEEFDVRTPGPDTPARSLSGGNQQKVILARELSRD 420
|
490
....*....|....*
gi 695765469 459 SNLLILDEPTNDLDV 473
Cdd:COG3845 421 PKLLIAAQPTRGLDV 435
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
19-232 |
7.18e-23 |
|
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: 97.89 E-value: 7.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDL------VVARL------QQdpPRNVTG-TVY 84
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgEDItglpphEIARLgigrtfQI--PRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 85 DFVAegIAEQAAYLKGYHdvsqlvmtdpSDKNLNELARLQEqldnlglwqldsRINEVLEQLNLDPNAEL--SSLSGGWL 162
Cdd:cd03219 94 ENVM--VAAQARTGSGLL----------LARARREEREARE------------RAEELLERVGLADLADRpaGELSYGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695765469 163 RKAALGRALVSGPRVLLLDEPT---NHLDIE-TIDWLEGfLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAaglNPEETEeLAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
321-472 |
1.06e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 97.05 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNY-QVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKL---EVAY------ 386
Cdd:COG2884 3 RFENVSKrYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNgqdlSRLkrrEIPYlrrrig 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 387 --FDQHRaeLDPDKTVMDNLA-----EGKQEVMVNGKPRHVLGY--LQDFMFHpkramtPVRALSGGERNRLLLARLFL- 456
Cdd:COG2884 83 vvFQDFR--LLPDRTVYENVAlplrvTGKSRKEIRRRVREVLDLvgLSDKAKA------LPHELSGGEQQRVAIARALVn 154
|
170
....*....|....*.
gi 695765469 457 KPSnLLILDEPTNDLD 472
Cdd:COG2884 155 RPE-LLLADEPTGNLD 169
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
19-232 |
1.08e-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: 97.80 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDlvVARLqqdPPRNVTG---------------- 81
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDgRD--ITGL---PPHRIARlgiartfqnprlfpel 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 82 TVYDFVAegIAEQAAYlkGYHDVSQLVMTDPSDKNLNELARlqeqldnlglwqldsRINEVLEQLNLDP--NAELSSLSG 159
Cdd:COG0411 95 TVLENVL--VAAHARL--GRGLLAALLRLPRARREEREARE---------------RAEELLERVGLADraDEPAGNLSY 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765469 160 GWLRKAALGRALVSGPRVLLLDEPT---NHLDI-ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAaglNPEETeELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
12-232 |
1.71e-22 |
|
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: 95.75 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIIYEQDLVVarlQQDPPRNVTGTVydfva 88
Cdd:cd03268 9 TYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKII---LGLikpDSGEITFDGKSYQ---KNIEALRRIGAL----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 89 egIAEQAAYlkGYhdvsqlvMTdpSDKNLNELARLqeqldnLGLwqLDSRINEVLEQLNLDPNAEL--SSLSGGWLRKAA 166
Cdd:cd03268 78 --IEAPGFY--PN-------LT--ARENLRLLARL------LGI--RKKRIDEVLDVVGLKDSAKKkvKGFSLGMKQRLG 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 167 LGRALVSGPRVLLLDEPTNHLDIETIDWLEGF---LKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELilsLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-232 |
2.23e-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: 96.69 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 1 MSLISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNRE--QGLDDGRIIYEQDL------------ 66
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlpPTYGNDVRLFGERRggedvwelrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 67 --VVARLQQDPPRNVTgtVYDFVaegiaeqaayLKGYHDVSQLVMtDPSDKnlnELARLQEQLDNLGLWQLDSRinevle 144
Cdd:COG1119 81 glVSPALQLRFPRDET--VLDVV----------LSGFFDSIGLYR-EPTDE---QRERARELLELLGLAHLADR------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 145 qlnldpnaELSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIET----IDWLEGFLKTFKGTIIFISHDRSFIRNMA 220
Cdd:COG1119 139 --------PFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTHHVEEIPPGI 210
|
250
....*....|..
gi 695765469 221 TRIVDLDRGKLV 232
Cdd:COG1119 211 THVLLLKDGRVV 222
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
11-250 |
2.24e-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: 101.38 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFS----DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLvvARLQQDPPRNVTGTVyd 85
Cdd:COG4987 339 VSFRypgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItLGGVDL--RDLDEDDLRRRIAVV-- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 86 fvaegiaEQAAYLkgyhdvsqLVMT--DpsdkNLnELARlqEQLDnlglwqlDSRINEVLEQLNLDP---------NAEL 154
Cdd:COG4987 415 -------PQRPHL--------FDTTlrE----NL-RLAR--PDAT-------DEELWAALERVGLGDwlaalpdglDTWL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 155 ----SSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETID-WLEGFLKTFKG-TIIFISHDRSFIRNMaTRIVDLDR 228
Cdd:COG4987 466 geggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQaLLADLLEALAGrTVLLITHRLAGLERM-DRILVLED 544
|
250 260
....*....|....*....|..
gi 695765469 229 GKLVTyPGNYDQyLLDKEEALR 250
Cdd:COG4987 545 GRIVE-QGTHEE-LLAQNGRYR 564
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
312-497 |
4.97e-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: 100.05 E-value: 4.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 312 AARSGKIVFEMENVNYQvDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGtklevayfDQHR 391
Cdd:TIGR02857 316 AAPASSLEFSGVSVAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN--------GVPL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 392 AELDPD-----------------KTVMDNLAEGKQEV---MVNGKPRHVlgYLQDFMFH-PKRAMTPV----RALSGGER 446
Cdd:TIGR02857 387 ADADADswrdqiawvpqhpflfaGTIAENIRLARPDAsdaEIREALERA--GLDEFVAAlPQGLDTPIgeggAGLSGGQA 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695765469 447 NRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDGY-QG-TVMLVSHDR 497
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaQGrTVLLVTHRL 517
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-232 |
7.27e-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: 7.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 3 LISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYE-QDLVVA-RLQQDPPR 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLII---GLlrpDSGEILVDgQDITGLsEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 78 NVTG------------TVYDFVAEGiaeqaaylkgyhdvsqlvmtdpsdknLNELARLQEQLdnlglwqLDSRINEVLEQ 145
Cdd:COG1127 82 RRIGmlfqggalfdslTVFENVAFP--------------------------LREHTDLSEAE-------IRELVLEKLEL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 146 LNLDPNAEL--SSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIET---IDWLEGFL-KTFKGTIIFISHDRSFIRNM 219
Cdd:COG1127 129 VGLPGAADKmpSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITsavIDELIRELrDELGLTSVVVTHDLDSAFAI 208
|
250
....*....|...
gi 695765469 220 ATRIVDLDRGKLV 232
Cdd:COG1127 209 ADRVAVLADGKII 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
17-231 |
1.39e-21 |
|
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: 93.71 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLDD---GRIIY---------EQDLVVARLQQdpprnvTGTVY 84
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILG---GLDRptsGEVRVdgtdisklsEKELAAFRRRH------IGFVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 85 dfvaegiaeQAAYLKGYHDVSQLVMtdpsdknlnelarLQEQLDNLGLWQLDSRINEVLEQLNLDPNAEL--SSLSGGWL 162
Cdd:cd03255 89 ---------QSFNLLPDLTALENVE-------------LPLLLAGVPKKERRERAEELLERVGLGDRLNHypSELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695765469 163 RKAALGRALVSGPRVLLLDEPTNHLDIET----IDWLEGFLKTFKGTIIFISHDRSFIRnMATRIVDLDRGKL 231
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
321-472 |
1.93e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 95.26 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSG----------------RIHVGTkleV 384
Cdd:PRK13537 9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGsislcgepvpsrarhaRQRVGV---V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 385 AYFDQhraeLDPDKTVMDNL-AEGKQEVMVNGKPRHVLGYLQDFMFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK13537 86 PQFDN----LDPDFTVRENLlVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
....*....
gi 695765469 464 LDEPTNDLD 472
Cdd:PRK13537 162 LDEPTTGLD 170
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-249 |
3.55e-21 |
|
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: 97.70 E-value: 3.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQ-----DPPRnvtgTVYDF 86
Cdd:TIGR03719 331 AFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQsrdalDPNK----TVWEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 87 VAEGiaeqaaylkgyhdvsqlvmtdpsdknlnelarlQEQLDnLGLWQLDSRinEVLEQLNL---DPNAELSSLSGGWLR 163
Cdd:TIGR03719 407 ISGG---------------------------------LDIIK-LGKREIPSR--AYVGRFNFkgsDQQKKVGQLSGGERN 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 164 KAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLD-RGKLVTYPGNYDQYL 242
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEYE 530
|
....*..
gi 695765469 243 LDKEEAL 249
Cdd:TIGR03719 531 EDKKRRL 537
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-185 |
3.63e-21 |
|
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: 90.40 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLV----------VARLQQDPPRNVTGTVYDFV 87
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgQDLTdderkslrkeIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 88 AEGIAEQAaylkgyhdvsqlVMTDPSDknlnelARLQEQLDNLGLWQLDSRInevleqlnldPNAELSSLSGGWLRKAAL 167
Cdd:pfam00005 81 RLGLLLKG------------LSKREKD------ARAEEALEKLGLGDLADRP----------VGERPGTLSGGQRQRVAI 132
|
170
....*....|....*...
gi 695765469 168 GRALVSGPRVLLLDEPTN 185
Cdd:pfam00005 133 ARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-230 |
3.73e-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: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFS----DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLvvarlQQDPPRNVTGTVyd 85
Cdd:cd03228 6 VSFSypgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlIDGVDL-----RDLDLESLRKNI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 86 fvaeGIAEQAAYLkgyhdVSQLVMtdpsdknlnelarlqeqlDNLglwqldsrinevleqlnldpnaelssLSGGWLRKA 165
Cdd:cd03228 79 ----AYVPQDPFL-----FSGTIR------------------ENI--------------------------LSGGQRQRI 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765469 166 ALGRALVSGPRVLLLDEPTNHLDIET-IDWLEGFLKTFKG-TIIFISHDRSFIRnMATRIVDLDRGK 230
Cdd:cd03228 106 AIARALLRDPPILILDEATSALDPETeALILEALRALAKGkTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
321-473 |
4.09e-21 |
|
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: 93.00 E-value: 4.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV----------GTKLEVAYFDQH 390
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdgedvrkeprEARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 391 RaELDPDKTVMDNL---AEGKQEVMVNGKPR-----HVLGyLQDFMfhpKRamtPVRALSGGERNRLLLARLFLKPSNLL 462
Cdd:COG4555 83 R-GLYDRLTVRENIryfAELYGLFDEELKKRieeliELLG-LEEFL---DR---RVGELSTGMKKKVALARALVHDPKVL 154
|
170
....*....|.
gi 695765469 463 ILDEPTNDLDV 473
Cdd:COG4555 155 LLDEPTNGLDV 165
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
561-629 |
4.13e-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: 87.14 E-value: 4.13e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 561 KLSYNLQRELEQLPQRLEELETQLQTLQEQVADPSFFgQSHDHTQQVLAQLAEAEQALETAFERWEYLE 629
Cdd:pfam16326 1 KLSYKEQRELEELEAEIEKLEEEIAELEAQLADPELY-SDYEKLQELSAELEELEAELEELYERWEELE 68
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
319-517 |
4.24e-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: 92.84 E-value: 4.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 319 VFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQL-KADSGRIHV-GTKLE------------- 383
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLfGERRGgedvwelrkrigl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 384 VAYFDQHRaeLDPDKTVMDNLAEGK----------QEVMVNgKPRHVLGYLQdfMFHpkRAMTPVRALSGGERNRLLLAR 453
Cdd:COG1119 83 VSPALQLR--FPRDETVLDVVLSGFfdsiglyrepTDEQRE-RARELLELLG--LAH--LADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695765469 454 LFLKPSNLLILDEPTNDLDVETLELLEELVDGY--QG--TVMLVSHDRQFVDNTVTECWIFEgEGRIG 517
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGapTLVLVTHHVEEIPPGITHVLLLK-DGRVV 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-232 |
7.41e-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: 7.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 1 MSLISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYEqDLVVARLqqdPP- 76
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIA---GFetpDSGRILLD-GRDVTGL---PPe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 77 -RNVtGTVY-DF-------VAEGIAeqaaY-LKGyhdvsqlvmtdpsdKNLNELARlqeqldnlglwqlDSRINEVLEQL 146
Cdd:COG3842 76 kRNV-GMVFqDYalfphltVAENVA----FgLRM--------------RGVPKAEI-------------RARVAELLELV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 147 NLDPNAEL--SSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLD----IETIDWLEGFLKTFKGTIIFISHDRS--FIrn 218
Cdd:COG3842 124 GLEGLADRypHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHDQEeaLA-- 201
|
250
....*....|....
gi 695765469 219 MATRIVDLDRGKLV 232
Cdd:COG3842 202 LADRIAVMNDGRIE 215
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
320-472 |
7.73e-21 |
|
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: 90.06 E-value: 7.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 320 FEMENVNYQVDG--KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQHRAELdpd 397
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLI--- 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 398 kTVMDnlaegkQEVMV-NGKPRHVLGylqdfmfhpkramtpvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03247 78 -SVLN------QRPYLfDTTLRNNLG----------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-516 |
1.09e-20 |
|
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: 96.02 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 13 FSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGLDD-----GRIIYEQDLVVARLQQDPPRNV-------- 79
Cdd:TIGR03269 10 FDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVL---RGMDQyeptsGRIIYHVALCEKCGYVERPSKVgepcpvcg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 80 ---TGTVYDFVAEGIAEQAAYLKGYHDVSQLVMTDPSDKNLneLARLQEQLDNLGLWQLDS--RINEVLEQLNLDPNAE- 153
Cdd:TIGR03269 87 gtlEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTV--LDNVLEALEEIGYEGKEAvgRAVDLIEMVQLSHRITh 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 154 -LSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDW----LEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDR 228
Cdd:TIGR03269 165 iARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIEDLSDKAIWLEN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 229 GKLVTyPGNYDQYLldkeeALRVEELQNAEFDRKLAQEEVWIRqgikarrtrnegrvralkamrrergerrevmgsakmq 308
Cdd:TIGR03269 245 GEIKE-EGTPDEVV-----AVFMEGVSEVEKECEVEVGEPIIK------------------------------------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 309 veeaarsgkivfeMENVN---YQVDGKVL--IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG---- 379
Cdd:TIGR03269 282 -------------VRNVSkryISVDRGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgde 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 380 ----TKLEVayFDQHRAE-----------LDPDKTVMDNLAEG-KQEVMVNGKPRHVLGYLQDFMFHPKRAMTPVR---- 439
Cdd:TIGR03269 349 wvdmTKPGP--DGRGRAKryigilhqeydLYPHRTVLDNLTEAiGLELPDELARMKAVITLKMVGFDEEKAEEILDkypd 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 440 ALSGGERNRLLLARLFLKPSNLLILDEPTNDLD----VETLELLEELVDGYQGTVMLVSHDRQFVDNTVTECWIFEGeGR 515
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRD-GK 505
|
.
gi 695765469 516 I 516
Cdd:TIGR03269 506 I 506
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-515 |
1.13e-20 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 89.55 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 320 FEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQHRAE------ 393
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrrrigm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 ------LDPDKTVMDNLAEGkqevmvngkprhvlgylqdfmfhpkramtpvraLSGGERNRLLLAR-LFLKPsNLLILDE 466
Cdd:cd03229 81 vfqdfaLFPHLTVLENIALG---------------------------------LSGGQQQRVALARaLAMDP-DVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695765469 467 PTNDLDVETLELLEELV----DGYQGTVMLVSHDRQFVDnTVTECWIFEGEGR 515
Cdd:cd03229 127 PTSALDPITRREVRALLkslqAQLGITVVLVTHDLDEAA-RLADRVVVLRDGK 178
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-232 |
1.29e-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: 91.02 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 4 ISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE----QDLVVARLQQDPpRNV 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgediSGLSEAELYRLR-RRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 80 tgtvydfvaeGIAEQAAYLKGYHDVSQLVMTdpsdkNLNELARLQEqldnlglWQLDSRINEVLEQLNLDPNAEL--SSL 157
Cdd:cd03261 80 ----------GMLFQSGALFDSLTVFENVAF-----PLREHTRLSE-------EEIREIVLEKLEAVGLRGAEDLypAEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 158 SGGWLRKAALGRALVSGPRVLLLDEPTNHLD-------IETIDWLEgflKTFKGTIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd03261 138 SGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLK---KELGLTSIMVTHDLDTAFAIADRIAVLYDGK 214
|
..
gi 695765469 231 LV 232
Cdd:cd03261 215 IV 216
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-232 |
1.41e-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: 89.02 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 4 ISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlvvarlqqdpprnVTGTV 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL-----------------VDGKE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 84 YDFvaegiaeqaaylkgyhdvsqlvmTDPSDknlnelARlqeqldNLGLwqldsrinEVLEQLnldpnaelsslSGGWLR 163
Cdd:cd03216 64 VSF-----------------------ASPRD------AR------RAGI--------AMVYQL-----------SVGERQ 89
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695765469 164 KAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03216 90 MVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
320-516 |
1.76e-20 |
|
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: 90.34 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 320 FEMENVNYQVDG--KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLEVAYFDQHRAE 393
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDgtdiRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 LDPDK-----TVMDNLAEGK-----QEVMVNGKprhvLGYLQDFM-FHPKRAMTPV----RALSGGERNRLLLARLFLKP 458
Cdd:cd03245 83 VPQDVtlfygTLRDNITLGApladdERILRAAE----LAGVTDFVnKHPNGLDLQIgergRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 459 SNLLILDEPTNDLDVETLELLEELVDGYQG--TVMLVSHdRQFVDNTVTECWIFEGeGRI 516
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDS-GRI 216
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
321-496 |
2.05e-20 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 90.26 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVN--YQVDGKV--LIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRI----HVGTKLEVAYFDQHRA 392
Cdd:cd03257 3 EVKNLSvsFPTGGGSvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgKDLLKLSRRLRKIRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 393 E-----------LDPDKTVMDNLAEG--KQEVMVNGKPRHVLGYLQDFMFH-PKRAMT--PvRALSGGERNRLLLAR-LF 455
Cdd:cd03257 83 EiqmvfqdpmssLNPRMTIGEQIAEPlrIHGKLSKKEARKEAVLLLLVGVGlPEEVLNryP-HELSGGQRQRVAIARaLA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695765469 456 LKPSnLLILDEPTNDLDVETLELL----EELVDGYQGTVMLVSHD 496
Cdd:cd03257 162 LNPK-LLIADEPTSALDVSVQAQIldllKKLQEELGLTLLFITHD 205
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-232 |
2.63e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 90.10 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 2 SLISMHGAWLSFSDS----PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLDdgriiyeqdlvvarlqqdPPR 77
Cdd:COG1136 3 PLLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILG---GLD------------------RPT 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 78 nvTGTVYdfvaegiaeqaayLKGyHDVSQLvmtdpSDKNLNELaRLQE-----Q----------LDNLGL---------W 133
Cdd:COG1136 62 --SGEVL-------------IDG-QDISSL-----SERELARL-RRRHigfvfQffnllpeltaLENVALplllagvsrK 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 134 QLDSRINEVLEQLNLDPNAEL--SSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIET----IDWLEGFLKTFKGTII 207
Cdd:COG1136 120 ERRERARELLERVGLGDRLDHrpSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIV 199
|
250 260
....*....|....*....|....*
gi 695765469 208 FISHDRsFIRNMATRIVDLDRGKLV 232
Cdd:COG1136 200 MVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
327-496 |
4.63e-20 |
|
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: 89.10 E-value: 4.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 327 YQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----------TKLEVAYFDQHRAeLDP 396
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINgysirtdrkaARQSLGYCPQFDA-LFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 397 DKTVMDNL---AegkqevMVNGKPRH-----VLGYLQDFMFHPKRAmTPVRALSGGERNRLLLARLFLKPSNLLILDEPT 468
Cdd:cd03263 89 ELTVREHLrfyA------RLKGLPKSeikeeVELLLRVLGLTDKAN-KRARTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190
....*....|....*....|....*....|
gi 695765469 469 NDLDVETLELLEELVDGYQG--TVMLVSHD 496
Cdd:cd03263 162 SGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-231 |
5.16e-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: 89.00 E-value: 5.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 15 DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLVVARLQQDPP-RNVTGTVY-DF----- 86
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrVNGQDVSDLRGRAIPYlRRKIGVVFqDFrllpd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 87 --VAEGIAeqaaylkgyhdvSQLVMTDPSDKNLNElaRLQEQLDNLGLwqlDSRINEVLEQLnldpnaelsslSGGWLRK 164
Cdd:cd03292 93 rnVYENVA------------FALEVTGVPPREIRK--RVPAALELVGL---SHKHRALPAEL-----------SGGEQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695765469 165 AALGRALVSGPRVLLLDEPTNHLDIET----IDWLEGFLKtfKGTIIFIS-HDRSFIRNMATRIVDLDRGKL 231
Cdd:cd03292 145 VAIARAIVNSPTILIADEPTGNLDPDTtweiMNLLKKINK--AGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
321-517 |
6.60e-20 |
|
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: 88.47 E-value: 6.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQV-DGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKlevayfDQHRAEL----- 394
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK------PIKAKERrksig 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 ----DPD-----KTVMDNLAEGKQEvmVNGKPRHVLGYLQDFMFHPKRAMTPvRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:cd03226 75 yvmqDVDyqlftDSVREELLLGLKE--LDAGNEQAETVLKDLDLYALKERHP-LSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695765469 466 EPTNDLDVETLELLEELVD--GYQGTVMLV-SHDRQFVDNTVTECwIFEGEGRIG 517
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRelAAQGKAVIViTHDYEFLAKVCDRV-LLLANGAIV 205
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
330-496 |
7.25e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 87.67 E-value: 7.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 330 DGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQHRAelDPDK---TVMDNLAE 406
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSE--VPDSlplTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 407 GK-QEVMVNGKPRHV-----------LGyLQDFmfhpkrAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
Cdd:NF040873 81 GRwARRGLWRRLTRDdraavddalerVG-LADL------AGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180
....*....|....*....|....*
gi 695765469 475 TLELLEELVD---GYQGTVMLVSHD 496
Cdd:NF040873 154 SRERIIALLAeehARGATVVVVTHD 178
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-517 |
8.28e-20 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 93.33 E-value: 8.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 34 LVGRNGAGKSTLMKIL---------NREQGLDDGRII---------------YEQDLVVARLQQdpprnvtgtvY-DFVA 88
Cdd:PRK13409 104 ILGPNGIGKTTAVKILsgelipnlgDYEEEPSWDEVLkrfrgtelqnyfkklYNGEIKVVHKPQ----------YvDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 89 EgiaeqaaYLKGyhDVSQLVmtdpsdknlnelarlqEQLDNLGLWqldsriNEVLEQLNLDP--NAELSSLSGGWLRKAA 166
Cdd:PRK13409 174 K-------VFKG--KVRELL----------------KKVDERGKL------DEVVERLGLENilDRDISELSGGELQRVA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 167 LGRALVSGPRVLLLDEPTNHLDI-------ETIDWLegflkTFKGTIIFISHDRSFIRNMATRIVdldrgklVTY--PGN 237
Cdd:PRK13409 223 IAAALLRDADFYFFDEPTSYLDIrqrlnvaRLIREL-----AEGKYVLVVEHDLAVLDYLADNVH-------IAYgePGA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 238 Y-------------DQYLldkeealrveelqnaefDRKLAQEEVWIRQgikarrtrnegrvralkamrrergerrevmgs 304
Cdd:PRK13409 291 YgvvskpkgvrvgiNEYL-----------------KGYLPEENMRIRP-------------------------------- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 305 akmqveEAarsgkIVFEMENVNYQVDGKVLIK---------DFS-----AQIQRGDKIALIGPNGCGKTTLLKLMLGQLK 370
Cdd:PRK13409 322 ------EP-----IEFEERPPRDESERETLVEypdltkklgDFSlevegGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 371 ADSGRihVGTKLEVAYFDQhRAELDPDKTVMDNLAEGKQEVMVNgkprhvlgYLQDFMFHP---KRAMT-PVRALSGGER 446
Cdd:PRK13409 391 PDEGE--VDPELKISYKPQ-YIKPDYDGTVEDLLRSITDDLGSS--------YYKSEIIKPlqlERLLDkNVKDLSGGEL 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 447 NRLLLARLFLKPSNLLILDEPTNDLDVETLELLEE----LVDGYQGTVMLVSHDRQFVDNTVTECWIFEGE-GRIG 517
Cdd:PRK13409 460 QRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKairrIAEEREATALVVDHDIYMIDYISDRLMVFEGEpGKHG 535
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
321-497 |
8.77e-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: 88.35 E-value: 8.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKL---------EVAYFDQHR 391
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgvpperrNIGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 392 AeLDPDKTVMDNLAEG--KQEVMVNGKPRHVLGYLQDFMFHPKRAMTPvRALSGGERNRLLLAR-LFLKPSnLLILDEPT 468
Cdd:cd03259 82 A-LFPHLTVAENIAFGlkLRGVPKAEIRARVRELLELVGLEGLLNRYP-HELSGGQQQRVALARaLAREPS-LLLLDEPL 158
|
170 180 190
....*....|....*....|....*....|...
gi 695765469 469 NDLDVETLELLEELVDGYQG----TVMLVSHDR 497
Cdd:cd03259 159 SALDAKLREELREELKELQRelgiTTIYVTHDQ 191
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-232 |
9.50e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 91.29 E-value: 9.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 1 MSLISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGLDD---GRIIYEqDLVVARLqqdPP- 76
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMI---AGLEDptsGEILIG-GRDVTDL---PPk 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 77 -RNV-----------TGTVYDFVAEGiaeqaayLKgyhdvsqlvmtdpsdknlneLARLQEQldnlglwQLDSRINEVLE 144
Cdd:COG3839 74 dRNIamvfqsyalypHMTVYENIAFP-------LK--------------------LRKVPKA-------EIDRRVREAAE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 145 QLNLDPNAEL--SSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLD----IETIDWLEGFLKTFKGTIIFISHDRSFIRN 218
Cdd:COG3839 120 LLGLEDLLDRkpKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHDQVEAMT 199
|
250
....*....|....
gi 695765469 219 MATRIVDLDRGKLV 232
Cdd:COG3839 200 LADRIAVMNDGRIQ 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
320-495 |
1.10e-19 |
|
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: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 320 FEMENVNYQVDG--KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLEVAYFDQHRaeldp 396
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADISQWDPNELG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 397 dktvmdnlaegkqevmvngkpRHVlGYL-QDFMFHPKRAMTPVraLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03246 76 ---------------------DHV-GYLpQDDELFSGSIAENI--LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180
....*....|....*....|...
gi 695765469 476 LELLEELV---DGYQGTVMLVSH 495
Cdd:cd03246 132 ERALNQAIaalKAAGATRIVIAH 154
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-517 |
1.32e-19 |
|
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: 92.93 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 34 LVGRNGAGKSTLMKIL-----------NREQGLDD------G-------RIIYEQDLVVARLQQ--DP-PRNVTGTVYDf 86
Cdd:COG1245 104 ILGPNGIGKSTALKILsgelkpnlgdyDEEPSWDEvlkrfrGtelqdyfKKLANGEIKVAHKPQyvDLiPKVFKGTVRE- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 87 vaegiaeqaaylkgyhdvsqlvmtdpsdknlnelarLQEQLDNLGLWqldsriNEVLEQLNLDP--NAELSSLSGGWLRK 164
Cdd:COG1245 183 ------------------------------------LLEKVDERGKL------DELAEKLGLENilDRDISELSGGELQR 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 165 AALGRALVSGPRVLLLDEPTNHLDI-------ETIdwlEGFLKTFKgTIIFISHDRSFIRNMATRIVdldrgklVTY--P 235
Cdd:COG1245 221 VAIAAALLRDADFYFFDEPSSYLDIyqrlnvaRLI---RELAEEGK-YVLVVEHDLAILDYLADYVH-------ILYgeP 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 236 GNYdqylldkeealrveelqnaefdrklaqeevwirqGI--KARRTRN------EGRVRAlkamrrergerrevmgsAKM 307
Cdd:COG1245 290 GVY----------------------------------GVvsKPKSVRVginqylDGYLPE-----------------ENV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 308 QVeeaaRSGKIVFEMENVNYQVDGKVLIK---------DFS-----AQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADS 373
Cdd:COG1245 319 RI----RDEPIEFEVHAPRREKEEETLVEypdltksygGFSlevegGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 374 GRIHvgTKLEVAYFDQhRAELDPDKTVMDNLAEgkqevmVNGKPrhvLG--YLQDFMFHP---KRAMT-PVRALSGGERN 447
Cdd:COG1245 395 GEVD--EDLKISYKPQ-YISPDYDGTVEEFLRS------ANTDD---FGssYYKTEIIKPlglEKLLDkNVKDLSGGELQ 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695765469 448 RLLLARLFLKPSNLLILDEPTNDLDVETLELLEEL----VDGYQGTVMLVSHDRQFVDNTVTECWIFEGE-GRIG 517
Cdd:COG1245 463 RVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAirrfAENRGKTAMVVDHDIYLIDYISDRLMVFEGEpGVHG 537
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-224 |
1.48e-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: 87.53 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 4 ISMHGAWLSFSDS----PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVAR-------LQ 72
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPgpdrgyvFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 73 QD---PPRnvtgTVYDFVAEGIaeqaaylkgyhdvsqlvmtdpsdknlnELARLQEQldnlglwQLDSRINEVLEQLNLD 149
Cdd:cd03293 81 QDallPWL----TVLDNVALGL---------------------------ELQGVPKA-------EARERAEELLELVGLS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 150 PNAEL--SSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIET----IDWLEGFLKTFKGTIIFISHDrsfIRN---MA 220
Cdd:cd03293 123 GFENAypHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTreqlQEELLDIWRETGKTVLLVTHD---IDEavfLA 199
|
....
gi 695765469 221 TRIV 224
Cdd:cd03293 200 DRVV 203
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-232 |
1.89e-19 |
|
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: 87.31 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 4 ISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLVVARLqqdPP--RNVT- 80
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIG-GRDVTDL---PPkdRDIAm 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 81 ----------GTVYDFVAEGiaeqaayLKgyhdvSQLVMTDPSDKNLNELARLQeQLDNLglwqldsrinevleqLNLDP 150
Cdd:cd03301 77 vfqnyalyphMTVYDNIAFG-------LK-----LRKVPKDEIDERVREVAELL-QIEHL---------------LDRKP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 151 NAelssLSGGWLRKAALGRALVSGPRVLLLDEPTNHLD----IETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDL 226
Cdd:cd03301 129 KQ----LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM 204
|
....*.
gi 695765469 227 DRGKLV 232
Cdd:cd03301 205 NDGQIQ 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
321-496 |
1.92e-19 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 87.94 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTK--------------LEVAY 386
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 387 FDQHRAELDpDKTVMDNLA------EGKQEVMVNGKprhVLGYLQDFMFHPKRAMTPvRALSGGERNRLLLAR-LFLKPS 459
Cdd:cd03261 82 LFQSGALFD-SLTVFENVAfplrehTRLSEEEIREI---VLEKLEAVGLRGAEDLYP-AELSGGMKKRVALARaLALDPE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695765469 460 nLLILDEPTNDLDVETLELLEELV----DGYQGTVMLVSHD 496
Cdd:cd03261 157 -LLLYDEPTAGLDPIASGVIDDLIrslkKELGLTSIMVTHD 196
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-234 |
2.16e-19 |
|
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: 87.24 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 4 ISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLD-----------DGRIIYEQDLVVARL- 71
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdegevllDGKDIYDLDVDVLELr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 72 -------QQDPPrnVTGTVYDFVAEGIAeqaayLKGYHDvsqlvmtdpsDKNLNELARlqEQLDNLGLWqldsriNEVLE 144
Cdd:cd03260 81 rrvgmvfQKPNP--FPGSIYDNVAYGLR-----LHGIKL----------KEELDERVE--EALRKAALW------DEVKD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 145 QLNldpnaeLSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG--TIIFISHDRSFIRNMATR 222
Cdd:cd03260 136 RLH------ALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHNMQQAARVADR 209
|
250
....*....|..
gi 695765469 223 IVDLDRGKLVTY 234
Cdd:cd03260 210 TAFLLNGRLVEF 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
17-232 |
2.51e-19 |
|
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: 87.25 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLV-VARLQQDPPRNVTGTVYD----FVAEG 90
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgTDLTlLSGKELRKARRRIGMIFQhfnlLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 91 IAEQAAY-LkgyhdvsqlvmtdpsdknlnELARLQEQldnlglwQLDSRINEVLEQLNLDPNAEL--SSLSGGWLRKAAL 167
Cdd:cd03258 99 VFENVALpL--------------------EIAGVPKA-------EIEERVLELLELVGLEDKADAypAQLSGGQKQRVGI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 168 GRALVSGPRVLLLDEPTNHLDIET----IDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETtqsiLALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
12-234 |
4.37e-19 |
|
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: 86.40 E-value: 4.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDlvVARLQQDPPRNVtgtvydfvaeG 90
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyINGYS--IRTDRKAARQSL----------G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 91 IAEQaaylkgyHDVsqLvmtdpsDKNLN--ELARLQEQLDNLGLWQLDSRINEVLEQLNLDP--NAELSSLSGGWLRKAA 166
Cdd:cd03263 79 YCPQ-------FDA--L------FDELTvrEHLRFYARLKGLPKSEIKEEVELLLRVLGLTDkaNKRARTLSGGMKRKLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 167 LGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG--TIIFISHDRSFIRNMATRIVDLDRGKLVTY 234
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRIAIMSDGKLRCI 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-224 |
1.26e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 85.91 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 1 MSLISMHGAWLSFSDS----PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLDD---GRIIYEQDLVVAR--- 70
Cdd:COG1116 5 APALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA---GLEKptsGEVLVDGKPVTGPgpd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 71 ----LQQD---PPRnvtgTVYDFVAEGIaeqaaylkgyhdvsqlvmtdpsdknlnELARLQEQldnlglwQLDSRINEVL 143
Cdd:COG1116 82 rgvvFQEPallPWL----TVLDNVALGL---------------------------ELRGVPKA-------ERRERARELL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 144 EQLNLDPNAEL--SSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETI----DWLEGFLKTFKGTIIFISHDrsfIR 217
Cdd:COG1116 124 ELVGLAGFEDAypHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRerlqDELLRLWQETGKTVLFVTHD---VD 200
|
250
....*....|
gi 695765469 218 N---MATRIV 224
Cdd:COG1116 201 EavfLADRVV 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
34-232 |
1.55e-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: 84.55 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 34 LVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLVVAR---------LQQDPPRNVTGTVYDFVAegiaeQAAYLKGYHD 103
Cdd:cd03264 30 LLGPNGAGKTTLMRILATLTPPSSGTIrIDGQDVLKQPqklrrrigyLPQEFGVYPNFTVREFLD-----YIAWLKGIPS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 104 VsqlvmtdpsdknlnelarlqeqldnlglwQLDSRINEVLEQLNLDPNAE--LSSLSGGWLRKAALGRALVSGPRVLLLD 181
Cdd:cd03264 105 K-----------------------------EVKARVDEVLELVNLGDRAKkkIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695765469 182 EPTNHLDIETIDWLEGFLKTF-KGTIIFIS-HDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELgEDRIVILStHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
16-242 |
1.61e-18 |
|
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: 85.43 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 16 SPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI------IYEQDLVVARlqqdppRNVtgtvydfvae 89
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedIREQDPVELR------RKI---------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 90 GIAEQAAYLKGYHDVSQLVMTDPSdknlneLARLQEQldnlglwQLDSRINEVLEQLNLDPnAEL-----SSLSGGWLRK 164
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPK------LLKWPKE-------KIRERADELLALVGLDP-AEFadrypHELSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 165 AALGRALVSGPRVLLLDEPTNHLDIETIDWL-EGFLK---TFKGTIIFISHDRSFIRNMATRIVDLDRGKLVTYpGNYDQ 240
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALDPITRDQLqEEFKRlqqELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQV-GTPDE 222
|
..
gi 695765469 241 YL 242
Cdd:cd03295 223 IL 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
321-467 |
1.78e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 85.53 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVN--YQVDGK--VLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV------GTKLEVAY-FDQ 389
Cdd:COG1116 9 ELRGVSkrFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDRGVvFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 390 HRaeLDPDKTVMDNLAEGkqeVMVNGKPR-----HVLGY-----LQDFM-FHPkramtpvRALSGGERNRLLLAR-LFLK 457
Cdd:COG1116 89 PA--LLPWLTVLDNVALG---LELRGVPKaerreRARELlelvgLAGFEdAYP-------HQLSGGMRQRVAIARaLAND 156
|
170
....*....|
gi 695765469 458 PSnLLILDEP 467
Cdd:COG1116 157 PE-VLLMDEP 165
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-473 |
1.78e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.07 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 3 LISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlvvarlqqdpprNVTGT 82
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI-----------------TINNI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 83 VYDFVAEGIAEQAAYLKGYHDVSQlvmtdpsdknLNELArLQEQL------------DNLGLW-QLDSRINEVLEQLNL- 148
Cdd:PRK09700 68 NYNKLDHKLAAQLGIGIIYQELSV----------IDELT-VLENLyigrhltkkvcgVNIIDWrEMRVRAAMMLLRVGLk 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 149 -DPNAELSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIV 224
Cdd:PRK09700 137 vDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKegtAIVYISHKLAEIRRICDRYT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 225 DLDRGklvTYPGNYDqylldkeealrVEELQNAEFDRKLAQEEvwirqgIKARRTRNEGRVRALkamrrergerrevmgs 304
Cdd:PRK09700 217 VMKDG---SSVCSGM-----------VSDVSNDDIVRLMVGRE------LQNRFNAMKENVSNL---------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 305 akmqveeaarSGKIVFEMENVNYQVDGKVliKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLE 383
Cdd:PRK09700 261 ----------AHETVFEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLnGKDIS 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 384 -----------VAYFDQHRAE--LDPDKTVMDNLAEGKQevMVNGKPRHVLGylqdfMFHPK---------RAMTPVRA- 440
Cdd:PRK09700 329 prspldavkkgMAYITESRRDngFFPNFSIAQNMAISRS--LKDGGYKGAMG-----LFHEVdeqrtaenqRELLALKCh 401
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 695765469 441 --------LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK09700 402 svnqniteLSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
318-472 |
2.25e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.81 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 318 IVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVgtkLEVAYFDQHRA----- 392
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV---LGVPVPARARLarari 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 393 -------ELDPDKTVMDNL-AEGKQEVMVNGKPRHVLGYLQDFMFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLIL 464
Cdd:PRK13536 117 gvvpqfdNLDLEFTVRENLlVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
....*...
gi 695765469 465 DEPTNDLD 472
Cdd:PRK13536 197 DEPTTGLD 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
321-496 |
2.66e-18 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 84.65 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVgtklevayFDQHRAELDPDK-- 398
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV--------DGQDITGLSEKEly 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 399 -------------------TVMDNLA----E----GKQEV--MVNGKPRHV-LGYLQDFMfhPkramtpvRALSGGERNR 448
Cdd:COG1127 79 elrrrigmlfqggalfdslTVFENVAfplrEhtdlSEAEIreLVLEKLELVgLPGAADKM--P-------SELSGGMRKR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695765469 449 LLLAR-LFLKPSnLLILDEPTNDLDVETLELLEELV----DGYQGTVMLVSHD 496
Cdd:COG1127 150 VALARaLALDPE-ILLYDEPTAGLDPITSAVIDELIrelrDELGLTSVVVTHD 201
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-232 |
3.11e-18 |
|
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: 83.79 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQ------DLVVAR-----LQQDPpRNVTGTVYD 85
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqlDPADLRrnigyVPQDV-TLFYGTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 86 FVAEGIAE-------QAAYLKGyhdVSQLVMTDPSDKNLnelaRLQEQLDNLglwqldsrinevleqlnldpnaelsslS 158
Cdd:cd03245 97 NITLGAPLadderilRAAELAG---VTDFVNKHPNGLDL----QIGERGRGL---------------------------S 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 159 GGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG--TIIFISHDRSFIrNMATRIVDLDRGKLV 232
Cdd:cd03245 143 GGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
315-472 |
3.16e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 88.30 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 315 SGKIVFEmeNVN--YQVDGKVLiKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKlEVAYFDQH-- 390
Cdd:COG1132 337 RGEIEFE--NVSfsYPGDRPVL-KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV-DIRDLTLEsl 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 391 RAEL-----DP---DKTVMDNLAEGK-----QEVM-----------VNGKPRhvlGYlqDfmfhpkramTPV----RALS 442
Cdd:COG1132 413 RRQIgvvpqDTflfSGTIRENIRYGRpdatdEEVEeaakaaqahefIEALPD---GY--D---------TVVgergVNLS 478
|
170 180 190
....*....|....*....|....*....|
gi 695765469 443 GGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALD 508
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
310-496 |
5.21e-18 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 87.42 E-value: 5.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 310 EEAARSGKIVFEMENVNYQVDG-KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLEVAYF 387
Cdd:TIGR02868 325 AGAVGLGKPTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLdGVPVSSLDQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 388 DQHRAEL-----DP---DKTVMDNLAEGKQEV----MVNGKPRHVLG-YLQDFmfhPKRAMTPV----RALSGGERNRLL 450
Cdd:TIGR02868 405 DEVRRRVsvcaqDAhlfDTTVRENLRLARPDAtdeeLWAALERVGLAdWLRAL---PDGLDTVLgeggARLSGGERQRLA 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695765469 451 LARLFLKPSNLLILDEPTNDLDVETLELLEELV-DGYQG-TVMLVSHD 496
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADELLEDLlAALSGrTVVLITHH 529
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
321-501 |
8.38e-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: 82.54 E-value: 8.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDG----KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKL------------- 382
Cdd:cd03255 2 ELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdGTDIsklsekelaafrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 383 -EVAY-FDQHRaeLDPDKTVMDNLA-----EGKQEVMVNGKPRHVLGY--LQDFMFHpkramtPVRALSGGERNRLLLAR 453
Cdd:cd03255 82 rHIGFvFQSFN--LLPDLTALENVElplllAGVPKKERRERAEELLERvgLGDRLNH------YPSELSGGQQQRVAIAR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695765469 454 LFLKPSNLLILDEPTNDLDVETLELL----EELVDGYQGTVMLVSHDRQFVD 501
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVmellRELNKEAGTTIVVVTHDPELAE 205
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-232 |
8.80e-18 |
|
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: 82.30 E-value: 8.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFSDSP---LLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIIYEQDLVVAR--------LQQDPP 76
Cdd:cd03226 5 ISFSYKKgteILDDLSLDLYAGEIIALTGKNGAGKTTLAKIL---AGLikeSSGSILLNGKPIKAKerrksigyVMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 77 RNVTG-TVYDFVAEGiaeqaayLKGYHDvsqlvmtdpsdknlnELARLQEQLDNLGLWQLDSRinevleqlnlDPnaelS 155
Cdd:cd03226 82 YQLFTdSVREELLLG-------LKELDA---------------GNEQAETVLKDLDLYALKER----------HP----L 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 156 SLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03226 126 SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
12-232 |
9.09e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 85.20 E-value: 9.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIIY-EQDLVVARLQQDppRNVtG------ 81
Cdd:COG1118 11 RFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRII---AGLetpDSGRIVLnGRDLFTNLPPRE--RRV-Gfvfqhy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 82 ------TVYDFVAEGiaeqaaylkgyhdvsqLVMTDPSDKNLNelARLQEQLDNLGLWQLDSRInevleqlnldPnaelS 155
Cdd:COG1118 85 alfphmTVAENIAFG----------------LRVRPPSKAEIR--ARVEELLELVQLEGLADRY----------P----S 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 156 SLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:COG1118 133 QLSGGQRQRVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
.
gi 695765469 232 V 232
Cdd:COG1118 213 E 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
332-496 |
1.22e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 82.38 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 332 KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQH----------RAELDPDKTVM 401
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFlrrigvvfgqKTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 402 DNLAEGKQevMVNGKPRHV---LGYLQDFMFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLEL 478
Cdd:cd03267 114 DSFYLLAA--IYDLPPARFkkrLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180
....*....|....*....|..
gi 695765469 479 LEELVDGY----QGTVMLVSHD 496
Cdd:cd03267 192 IRNFLKEYnrerGTTVLLTSHY 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
321-503 |
1.28e-17 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 82.07 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVL-IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKL------EVAYFDQHRA 392
Cdd:cd03292 2 EFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVsdlrgrAIPYLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 393 ------ELDPDKTVMDNLAEGKQEVMVNGK--PRHVLGYLQDF-MFHPKRAMTpvRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:cd03292 82 vvfqdfRLLPDRNVYENVAFALEVTGVPPReiRKRVPAALELVgLSHKHRALP--AELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695765469 464 LDEPTNDLDVETLELLEELVDGYQ---GTVMLVSHDRQFVDNT 503
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDTT 202
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-232 |
1.31e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 82.65 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 1 MSLISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNR-----------EQGLDDGRIIYEQDLVVA 69
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielypearvsGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 70 RLQ-----QDPPRNVTGTVYDFVAEGIaeqaaylkgyhDVSQLVmtdpsdKNLNEL-ARLQEQLDNLGLWQldsrinEVL 143
Cdd:PRK14247 81 RRRvqmvfQIPNPIPNLSIFENVALGL-----------KLNRLV------KSKKELqERVRWALEKAQLWD------EVK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 144 EQLnldpNAELSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG--TIIFISHdrsfIRNMAT 221
Cdd:PRK14247 138 DRL----DAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH----FPQQAA 209
|
250
....*....|....*
gi 695765469 222 RIVD----LDRGKLV 232
Cdd:PRK14247 210 RISDyvafLYKGQIV 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
321-472 |
1.61e-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: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLE-----VAYFDQHR 391
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvTDLPpkdrdIAMVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 392 AeLDPDKTVMDNLAEG-----KQEVMVNGKPRHVLGYLQ-DFMFHPKramtpVRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:cd03301 82 A-LYPHMTVYDNIAFGlklrkVPKDEIDERVREVAELLQiEHLLDRK-----PKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
....*..
gi 695765469 466 EPTNDLD 472
Cdd:cd03301 156 EPLSNLD 162
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
337-496 |
1.77e-17 |
|
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: 81.75 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 337 DFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKL-----EVAY-FDQHRaeLDPDKTVMDNLAEGkq 409
Cdd:cd03293 22 DISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdGEPVtgpgpDRGYvFQQDA--LLPWLTVLDNVALG-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 410 eVMVNGKPR-----HVLGY-----LQDFMFH-PKramtpvrALSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDVETLE 477
Cdd:cd03293 98 -LELQGVPKaeareRAEELlelvgLSGFENAyPH-------QLSGGMRQRVALARaLAVDP-DVLLLDEPFSALDALTRE 168
|
170 180
....*....|....*....|...
gi 695765469 478 LLEELV----DGYQGTVMLVSHD 496
Cdd:cd03293 169 QLQEELldiwRETGKTVLLVTHD 191
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
335-496 |
2.07e-17 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 82.00 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 335 IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GT--------KLEVAYFDQHRAeLDPDKTVMDNLA 405
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKditnlppeKRDISYVPQNYA-LFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 406 EG--KQEVMVNGKPRHVL---GYLQ-DFMFHPKramtpVRALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLEL 478
Cdd:cd03299 94 YGlkKRKVDKKEIERKVLeiaEMLGiDHLLNRK-----PETLSGGEQQRVAIARaLVVNPK-ILLLDEPFSALDVRTKEK 167
|
170 180
....*....|....*....|..
gi 695765469 479 LEELV----DGYQGTVMLVSHD 496
Cdd:cd03299 168 LREELkkirKEFGVTVLHVTHD 189
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-246 |
3.22e-17 |
|
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: 81.12 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 15 DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE----QDLVVARLqqdppRNVTGTV------- 83
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghdvRDYTLASL-----RRQIGLVsqdvflf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 84 YDFVAEGIAeqaaYlkGYHDVSQLVMTDPSdknlnELARLQEQLDNLGLwQLDSRINEvleqlnldpnaELSSLSGGWLR 163
Cdd:cd03251 89 NDTVAENIA----Y--GRPGATREEVEEAA-----RAANAHEFIMELPE-GYDTVIGE-----------RGVKLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 164 KAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFL-KTFKG-TIIFISHDRSFIRNmATRIVDLDRGKLVTYpGNYDQy 241
Cdd:cd03251 146 RIAIARALLKDPPILILDEATSALDTESERLVQAALeRLMKNrTTFVIAHRLSTIEN-ADRIVVLEDGKIVER-GTHEE- 222
|
....*
gi 695765469 242 LLDKE 246
Cdd:cd03251 223 LLAQG 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
19-232 |
3.69e-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: 81.08 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLVVARLQQDPPRNV---TGTVYdfvaegiaeqa 95
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLID-GTDINKLKGKALRQLrrqIGMIF----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 96 aylKGYHDVSQL-VMTDPSDKNLNELARLQeqldnlGLWQLDSRIN-----EVLEQLNLDPNAEL--SSLSGGWLRKAAL 167
Cdd:cd03256 85 ---QQFNLIERLsVLENVLSGRLGRRSTWR------SLFGLFPKEEkqralAALERVGLLDKAYQraDQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 168 GRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTF---KGTIIFIS-HDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRInreEGITVIVSlHQVDLAREYADRIVGLKDGRIV 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-229 |
3.71e-17 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 80.94 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQDPPRNVT-------GTV------ 83
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQASPREILalrrrtiGYVsqflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 84 ------YDFVAE-----GIAEQAAYLKgyhdvsqlvmtdpsdknlnelARlqeqldnlglwqldsrinEVLEQLNLDPna 152
Cdd:COG4778 105 iprvsaLDVVAEpllerGVDREEARAR---------------------AR------------------ELLARLNLPE-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 153 ELSSL-----SGGWLRKAALGRALVSGPRVLLLDEPTNHLDIET----IDWLEGfLKTFKGTIIFISHDRSFIRNMATRI 223
Cdd:COG4778 144 RLWDLppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEE-AKARGTAIIGIFHDEEVREAVADRV 222
|
....*.
gi 695765469 224 VDLDRG 229
Cdd:COG4778 223 VDVTPF 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
318-472 |
4.25e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 81.36 E-value: 4.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 318 IVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTK-------LEVAyfdQH 390
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwspAELA---RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 391 RAELdPDKTVMdNLAEGKQEVMVNGKPRHVLGYLQDfMFHPKRAMTPV----------RALSGGERNRLLLARLFL---- 456
Cdd:PRK13548 78 RAVL-PQHSSL-SFPFTVEEVVAMGRAPHGLSRAED-DALVAAALAQVdlahlagrdyPQLSGGEQQRVQLARVLAqlwe 154
|
170
....*....|....*...
gi 695765469 457 --KPSNLLILDEPTNDLD 472
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALD 172
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
321-495 |
4.46e-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: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTK---------LEVAYFDQHR 391
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdepHENILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 392 AELDPDKTVMDNLAEGkqevmvngkpRHVLGYLQDFMFHPKRAM-------TPVRALSGGERNRLLLARLFLKPSNLLIL 464
Cdd:TIGR01189 82 PGLKPELSALENLHFW----------AAIHGGAQRTIEDALAAVgltgfedLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 695765469 465 DEPTNDLDVETLELLEELVDGY---QGTVMLVSH 495
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-226 |
4.71e-17 |
|
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: 84.65 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 16 SPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlvvarlqqdpprNVTG-TVYDFVAEGIAEQ 94
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI-----------------AVNGvPLADADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 95 AAYlkgyhdVSQL-VMTDPSDKNLNELAR-------LQEQLDNLGLWQLDSRINEVLEQLnLDPNAelSSLSGGWLRKAA 166
Cdd:TIGR02857 398 IAW------VPQHpFLFAGTIAENIRLARpdasdaeIREALERAGLDEFVAALPQGLDTP-IGEGG--AGLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695765469 167 LGRALVSGPRVLLLDEPTNHLDIET-IDWLEGFLKTFKG-TIIFISHDRSFIRNmATRIVDL 226
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETeAEVLEALRALAQGrTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
320-472 |
5.34e-17 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 80.30 E-value: 5.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 320 FEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGtklEVAYFDQHRAELDPD-- 397
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEG---EVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 398 -----------------KTVMDNLAEGKQevmVNG-KPRHVLGYLqdfmfhPKRAMTPV------------RALSGGERN 447
Cdd:cd03260 78 elrrrvgmvfqkpnpfpGSIYDNVAYGLR---LHGiKLKEELDER------VEEALRKAalwdevkdrlhaLGLSGGQQQ 148
|
170 180
....*....|....*....|....*.
gi 695765469 448 RLLLAR-LFLKPSNLLiLDEPTNDLD 472
Cdd:cd03260 149 RLCLARaLANEPEVLL-LDEPTSALD 173
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
321-500 |
6.37e-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: 80.56 E-value: 6.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKlEVAYFDQHR--------- 391
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGE-DITGLPPHEiarlgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 392 ---AELDPDKTVMDNlaegkqeVMVNGKPRHVLGYLQDFMFHPKRAM------------------TPVRALSGGERNRLL 450
Cdd:cd03219 81 fqiPRLFPELTVLEN-------VMVAAQARTGSGLLLARARREEREAreraeellervgladladRPAGELSYGQQRRLE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 451 LAR-LFLKPSnLLILDEPT---NDLDVETLELLEELV--DGYqgTVMLVSHDRQFV 500
Cdd:cd03219 154 IARaLATDPK-LLLLDEPAaglNPEETEELAELIRELreRGI--TVLLVEHDMDVV 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-234 |
6.51e-17 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 80.46 E-value: 6.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQdlvvARLQQDPP--RNVtGTVYD----FVAEGIA 92
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG----KDITNLPPekRDI-SYVPQnyalFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 93 EQAAY-LKgyhdvSQLVMTDPSDKNLNELARLqeqldnLGLWQLdsrinevleqLNLDPnaelSSLSGGWLRKAALGRAL 171
Cdd:cd03299 90 KNIAYgLK-----KRKVDKKEIERKVLEIAEM------LGIDHL----------LNRKP----ETLSGGEQQRVAIARAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765469 172 VSGPRVLLLDEPTNHLDIET----IDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVTY 234
Cdd:cd03299 145 VVNPKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
331-472 |
9.11e-17 |
|
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: 79.18 E-value: 9.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 331 GKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIhvgTKLEVAYFDQHRA-----------ELDPDKT 399
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI---TFDGKSYQKNIEAlrrigalieapGFYPNLT 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 400 VMDNLAEGKQEVMVNGKPRH-VLGY--LQDfmfHPKRamtPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03268 89 ARENLRLLARLLGIRKKRIDeVLDVvgLKD---SAKK---KVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
12-232 |
1.04e-16 |
|
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: 79.59 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLVVARLqqdPP--RNVtGTVYD---- 85
Cdd:cd03300 9 FYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD-GKDITNL---PPhkRPV-NTVFQnyal 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 86 FVAEGIAEQAAY-LKgyhdvsqlvmtdpsdknlneLARLQEQldnlglwQLDSRINEVLEQLNLD--PNAELSSLSGGWL 162
Cdd:cd03300 84 FPHLTVFENIAFgLR--------------------LKKLPKA-------EIKERVAEALDLVQLEgyANRKPSQLSGGQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695765469 163 RKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG----TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03300 137 QRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-231 |
1.07e-16 |
|
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: 79.69 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 13 FSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQDppRNVtG----------- 81
Cdd:cd03296 12 FGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNV-Gfvfqhyalfrh 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 82 -TVYDFVAEGIAEQaaylkgyhdvsqlvmtdPSDKNLNELarlqeqldnlglwQLDSRINEVLEQLNLDPNAEL--SSLS 158
Cdd:cd03296 89 mTVFDNVAFGLRVK-----------------PRSERPPEA-------------EIRAKVHELLKLVQLDWLADRypAQLS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765469 159 GGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG----TIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:cd03296 139 GGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelhvTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-231 |
1.12e-16 |
|
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: 82.08 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 22 AELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVV---ARLQQDPPRNVTGTVYD----FVAEGIAEQ 94
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdsrKGIFLPPEKRRIGYVFQearlFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 95 AAYlkGYHDvsqlvmTDPSDKNLNElarlqeqldnlglwqldsriNEVLEQLNLDPNAE--LSSLSGGWLRKAALGRALV 172
Cdd:TIGR02142 96 LRY--GMKR------ARPSERRISF--------------------ERVIELLGIGHLLGrlPGRLSGGEKQRVAIGRALL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695765469 173 SGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:TIGR02142 148 SSPRLLLMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
317-472 |
1.22e-16 |
|
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: 78.36 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 317 KIVFEMENVNYQVDGKV------LIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLK--ADSGrihvgtklevayfd 388
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPsksgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 389 qhraeldpdktvmdnlaegkqEVMVNGKPRH------VLGY-LQDFMFHPKraMTPV---------RALSGGERNRLLLA 452
Cdd:cd03213 67 ---------------------EVLINGRPLDkrsfrkIIGYvPQDDILHPT--LTVRetlmfaaklRGLSGGERKRVSIA 123
|
170 180
....*....|....*....|.
gi 695765469 453 R-LFLKPSnLLILDEPTNDLD 472
Cdd:cd03213 124 LeLVSNPS-LLFLDEPTSGLD 143
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
341-472 |
1.24e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 79.12 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 341 QIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTK--------LEVAYFDqHRAELDPDKTVMDNLaegkqevm 412
Cdd:PRK13543 33 HVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsRFMAYLG-HLPGLKADLSTLENL-------- 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695765469 413 vngkprHVLGYLQDFmfHPKR--------------AMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13543 104 ------HFLCGLHGR--RAKQmpgsalaivglagyEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
322-500 |
1.45e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.77 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 322 MENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQhRAELDPD---- 397
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ-KLYLDTTlplt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 398 -KTVMDNLAEGKQEVMVNGKPRHVLGYLQDFmfhpkramtPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETL 476
Cdd:PRK09544 86 vNRFLRLRPGTKKEDILPALKRVQAGHLIDA---------PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180
....*....|....*....|....*...
gi 695765469 477 ELLEELVDGYQGT----VMLVSHDRQFV 500
Cdd:PRK09544 157 VALYDLIDQLRREldcaVLMVSHDLHLV 184
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-234 |
1.49e-16 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 78.88 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 30 ERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLVVARLQQD-PP--RNVtGTVYD----FVAEGIAEQAAYlkGY 101
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgTVLFDSRKKINlPPqqRKI-GLVFQqyalFPHLNVRENLAF--GL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 102 HDVSQLVMTDpsdknlnelarlqeqldnlglwqldsRINEVLEQLNLDP--NAELSSLSGGWLRKAALGRALVSGPRVLL 179
Cdd:cd03297 101 KRKRNREDRI--------------------------SVDELLDLLGLDHllNRYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 180 LDEPTNHLDIETIDWLEGFL----KTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVTY 234
Cdd:cd03297 155 LDEPFSALDRALRLQLLPELkqikKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-232 |
1.98e-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: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 3 LISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLV------VARLQQDpp 76
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdskkdINKLRRK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 77 rnvTGTVY-DF-------VAEGIAEQAAYLKGYhdvsqlvmtdpSDKNLNELARlqEQLDNLGLwqldsrinevLEQLNL 148
Cdd:COG1126 79 ---VGMVFqQFnlfphltVLENVTLAPIKVKKM-----------SKAEAEERAM--ELLERVGL----------ADKADA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 149 DPnaelSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDwleGFLKTFKG------TIIFISHDRSFIRNMATR 222
Cdd:COG1126 133 YP----AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVG---EVLDVMRDlakegmTMVVVTHEMGFAREVADR 205
|
250
....*....|
gi 695765469 223 IVDLDRGKLV 232
Cdd:COG1126 206 VVFMDGGRIV 215
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
321-473 |
2.21e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 79.39 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG-------TKLEVAyfdQHRAE 393
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgrplaawSPWELA---RRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 LdPDKTVMdNLAEGKQEVMVNGKPRHVLGYLQDFMfHPKRAMTPV----------RALSGGERNRLLLARLFL------- 456
Cdd:COG4559 80 L-PQHSSL-AFPFTVEEVVALGRAPHGSSAAQDRQ-IVREALALVglahlagrsyQTLSGGEQQRVQLARVLAqlwepvd 156
|
170
....*....|....*..
gi 695765469 457 KPSNLLILDEPTNDLDV 473
Cdd:COG4559 157 GGPRWLFLDEPTSALDL 173
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-237 |
2.48e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 81.23 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 1 MSLISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGLDDgriIYEQDLVVA--RLQQDPP-- 76
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMI---AGLED---ITSGDLFIGekRMNDVPPae 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 77 RNVtGTVYDFVA----EGIAEQAAY-LKgyhdvsqlvmtdpsdknlneLARLQEQldnlglwQLDSRINEVLEQLNLD-- 149
Cdd:PRK11000 75 RGV-GMVFQSYAlyphLSVAENMSFgLK--------------------LAGAKKE-------EINQRVNQVAEVLQLAhl 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 150 ----PNAelssLSGGWLRKAALGRALVSGPRVLLLDEPTNHLD--------IEtIDWLEgflKTFKGTIIFISHDRSFIR 217
Cdd:PRK11000 127 ldrkPKA----LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqmrIE-ISRLH---KRLGRTMIYVTHDQVEAM 198
|
250 260
....*....|....*....|....*....
gi 695765469 218 NMATRIVDLDRGK---------LVTYPGN 237
Cdd:PRK11000 199 TLADKIVVLDAGRvaqvgkpleLYHYPAN 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
320-495 |
2.73e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 76.81 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 320 FEMENVNYQV-DGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQHraeldPdk 398
Cdd:cd03223 1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQR-----P-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 399 tvmdnlaegkqeVMVNGKPRHVLGYLQDfmfhpkramtpvRALSGGERNRLLLARLFL-KPSnLLILDEPTNDLDVETLE 477
Cdd:cd03223 74 ------------YLPLGTLREQLIYPWD------------DVLSGGEQQRLAFARLLLhKPK-FVFLDEATSALDEESED 128
|
170
....*....|....*...
gi 695765469 478 LLEELVDGYQGTVMLVSH 495
Cdd:cd03223 129 RLYQLLKELGITVISVGH 146
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
331-473 |
2.90e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.99 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 331 GKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRI-------HVGTKLEVAYFDQHRAELDPDKTVMDN 403
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIkldggdiDDPDVAEACHYLGHRNAMKPALTVAEN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 404 LaEGKQEVMvNGKPRHVLGYLQDFMFHPKrAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK13539 94 L-EFWAAFL-GGEELDIAAALEAVGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
335-500 |
4.51e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 78.54 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 335 IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKlEVAYFDQHR------------AELDPDKTVMD 402
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGR-DITGLPPHRiarlgiartfqnPRLFPELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 403 NlaegkqeVMVNGKPRHVLGYLQDFMFHPK----------RAM-------------TPVRALSGGERNRLLLAR-LFLKP 458
Cdd:COG0411 99 N-------VLVAAHARLGRGLLAALLRLPRarreereareRAEellervgladradEPAGNLSYGQQRRLEIARaLATEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695765469 459 SnLLILDEPT---NDLDVETLELLEELVDGYQG-TVMLVSHDRQFV 500
Cdd:COG0411 172 K-LLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLV 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-473 |
5.43e-16 |
|
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: 81.27 E-value: 5.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 1 MSLISMHGAWLSF----SDSPLLDNAELHIEDNERVCLVGRNGAGKS----TLMKILNREQGLDDGRIIYE-QDLvvarL 71
Cdd:COG4172 4 MPLLSVEDLSVAFgqggGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDgQDL----L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 72 QQDPP--RNVTGtvydfvaegiaeqaaylkgyHDVS---QLVMTdpsdkNLNELARLQEQL-------DNLGLWQLDSRI 139
Cdd:COG4172 80 GLSERelRRIRG--------------------NRIAmifQEPMT-----SLNPLHTIGKQIaevlrlhRGLSGAAARARA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 140 NEVLEQLNLdPNAE--LSS----LSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIeTI-----DWLEGFLKTFKGTIIF 208
Cdd:COG4172 135 LELLERVGI-PDPErrLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVqaqilDLLKDLQRELGMALLL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 209 ISHDRSFIRNMATRIVDLDRGKLV---------TYPGN-YDQYLLDKE-------------EALRVEELQnaefdrklaq 265
Cdd:COG4172 213 ITHDLGVVRRFADRVAVMRQGEIVeqgptaelfAAPQHpYTRKLLAAEprgdprpvppdapPLLEARDLK---------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 266 eeVW--IRQGIKARRTrneGRVRALKamrrergerrevmgsakmqveeaarsgkivfemenvnyqvdgkvlikDFSAQIQ 343
Cdd:COG4172 283 --VWfpIKRGLFRRTV---GHVKAVD-----------------------------------------------GVSLTLR 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 344 RGDKIALIGPNGCGKTTLLKLMLGqLKADSGRIHV-GTKLEVAYFDQHR--------------AELDPDKTVMDNLAEG- 407
Cdd:COG4172 311 RGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFdGQDLDGLSRRALRplrrrmqvvfqdpfGSLSPRMTVGQIIAEGl 389
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 408 -KQEVMVNGKPRH--VLGYLQ------DFMF---HpkramtpvrALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG4172 390 rVHGPGLSAAERRarVAEALEevgldpAARHrypH---------EFSGGQRQRIAIARaLILEPK-LLVLDEPTSALDV 458
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-232 |
5.78e-16 |
|
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: 79.33 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKI---LNREQGLDDGRIIYE-QDLV-----------VARLQ---QDP----- 75
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAilgLLPPPGITSGEILFDgEDLLklsekelrkirGREIQmifQDPmtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 76 PRNvtgTVYDFVAEGIAeqaaylkgYHdvsqlvmtdpsdKNLNELARLQeqldnlglwqldsRINEVLEQLNL-DPNAEL 154
Cdd:COG0444 101 PVM---TVGDQIAEPLR--------IH------------GGLSKAEARE-------------RAIELLERVGLpDPERRL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 155 SS----LSGGWLRKAALGRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDL 226
Cdd:COG0444 145 DRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVtiqaQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVM 224
|
....*.
gi 695765469 227 DRGKLV 232
Cdd:COG0444 225 YAGRIV 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
316-473 |
5.78e-16 |
|
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: 77.65 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 316 GKIVFEmeNVNYQVDGKVL-IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGtklEVAYFDQHRAEL 394
Cdd:cd03254 1 GEIEFE--NVNFSYDEKKPvLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILID---GIDIRDISRKSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 ---------DP---DKTVMDNLAEGKQ-----EVMVNGKPRHvlgyLQDF-MFHPKRAMTPVR----ALSGGERNRLLLA 452
Cdd:cd03254 76 rsmigvvlqDTflfSGTIMENIRLGRPnatdeEVIEAAKEAG----AHDFiMKLPNGYDTVLGenggNLSQGERQLLAIA 151
|
170 180
....*....|....*....|.
gi 695765469 453 RLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDT 172
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
318-472 |
6.08e-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: 77.66 E-value: 6.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 318 IVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLEVAYFDQHRAEL-- 394
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDVRDYTLASLRRQIgl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 ---DP---DKTVMDNLAEGK-----QEVMVNGKprhvLGYLQDF-MFHPKRAMTPV--RA--LSGGERNRLLLARLFLKP 458
Cdd:cd03251 81 vsqDVflfNDTVAENIAYGRpgatrEEVEEAAR----AANAHEFiMELPEGYDTVIgeRGvkLSGGQRQRIAIARALLKD 156
|
170
....*....|....
gi 695765469 459 SNLLILDEPTNDLD 472
Cdd:cd03251 157 PPILILDEATSALD 170
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-247 |
7.91e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.78 E-value: 7.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 10 WLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLV-----VARLQQDPPRNVTGTVY 84
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdIFQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 85 D----FVAEGIAEQAAYLKGYHDVsqlvmtdpsdKNLNELARLQEQ-LDNLGLWQldsrinEVLEQLNldpnAELSSLSG 159
Cdd:PRK14246 97 QqpnpFPHLSIYDNIAYPLKSHGI----------KEKREIKKIVEEcLRKVGLWK------EVYDRLN----SPASQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 160 GWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG--TIIFISHDRSFIRNMATRIVDLDRGKLVTYPGN 237
Cdd:PRK14246 157 GQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
250
....*....|
gi 695765469 238 YDQYLLDKEE 247
Cdd:PRK14246 237 NEIFTSPKNE 246
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
321-472 |
9.53e-16 |
|
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: 76.46 E-value: 9.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGdKIALIGPNGCGKTTLLKLMLGQLKADSGRIhvgtklevaYFDQHRAELDPDKTv 400
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTI---------RIDGQDVLKQPQKL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 401 mdnlaegkqevmvngkpRHVLGYL-QDFMFHPK------------------------------------RAMTPVRALSG 443
Cdd:cd03264 71 -----------------RRRIGYLpQEFGVYPNftvrefldyiawlkgipskevkarvdevlelvnlgdRAKKKIGSLSG 133
|
170 180
....*....|....*....|....*....
gi 695765469 444 GERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03264 134 GMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-258 |
9.66e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 77.06 E-value: 9.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGriiyeqDLVVARLQ-QDPPRNV------TGTVY 84
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSG------DLIVDGLKvNDPKVDErlirqeAGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 85 dfvaegiaeQAAYLKGYHDVSQLVMTDP------SDKNLNELARlqEQLDNLGLwqldsrinevLEQLNLDPnaelSSLS 158
Cdd:PRK09493 84 ---------QQFYLFPHLTALENVMFGPlrvrgaSKEEAEKQAR--ELLAKVGL----------AERAHHYP----SELS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 159 GGWLRKAALGRALVSGPRVLLLDEPTNHLDIETidwLEGFLKTFKG------TIIFISHDRSFIRNMATRIVDLDRGKlV 232
Cdd:PRK09493 139 GGQQQRVAIARALAVKPKLMLFDEPTSALDPEL---RHEVLKVMQDlaeegmTMVIVTHEIGFAEKVASRLIFIDKGR-I 214
|
250 260
....*....|....*....|....*..
gi 695765469 233 TYPGNYDQyLLDKEEALRVEE-LQNAE 258
Cdd:PRK09493 215 AEDGDPQV-LIKNPPSQRLQEfLQHVS 240
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-231 |
9.87e-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: 76.41 E-value: 9.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 4 ISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQ-DPPRNVTGT 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 83 VYdfvaegiaeQAAYLKGYHDVSQLVMTDP------SDKNLNELARlqEQLDNLGLwqldsrinevLEQLNLDPnaelSS 156
Cdd:cd03262 81 VF---------QQFNLFPHLTVLENITLAPikvkgmSKAEAEERAL--ELLEKVGL----------ADKADAYP----AQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695765469 157 LSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTF---KGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:cd03262 136 LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
338-473 |
1.02e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 77.28 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 338 FSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKAdSGRIHV-GTKLE---VAYFDQHRAEL---DPDKTVMD---NLAEG 407
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFaGQPLEawsAAELARHRAYLsqqQTPPFAMPvfqYLTLH 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695765469 408 KQEVMVNGKPRHVLGYL-QDFMFHPKRAmTPVRALSGGERNRLLLARLFLK------P-SNLLILDEPTNDLDV 473
Cdd:PRK03695 94 QPDKTRTEAVASALNEVaEALGLDDKLG-RSVNQLSGGEWQRVRLAAVVLQvwpdinPaGQLLLLDEPMNSLDV 166
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
322-473 |
1.25e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.80 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 322 MENVNYQVDGKVLikDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGqLKADSGRIHV-GTKLE---VAYFDQHRAELD-- 395
Cdd:COG4138 1 LQLNDVAVAGRLG--PISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLnGRPLSdwsAAELARHRAYLSqq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 396 ----PDKTVMDNLAEGKQEVMVNGKPRHVLGYL-QDFMFHPKrAMTPVRALSGGERNRLLLARLFLK-------PSNLLI 463
Cdd:COG4138 78 qsppFAMPVFQYLALHQPAGASSEAVEQLLAQLaEALGLEDK-LSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLL 156
|
170
....*....|
gi 695765469 464 LDEPTNDLDV 473
Cdd:COG4138 157 LDEPMNSLDV 166
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-246 |
1.28e-15 |
|
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: 76.76 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 15 DSPL-LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLVVArlqqDPP--RNVTGTVydfvaeg 90
Cdd:cd03252 13 DGPViLDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDgHDLALA----DPAwlRRQVGVV------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 91 IAEQAAYLKGYHDVSQLVMTDPSDKNLNELARLQEQLDnlglwqldsRINEVLEQLNLDPNAELSSLSGGWLRKAALGRA 170
Cdd:cd03252 82 LQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHD---------FISELPEGYDTIVGEQGAGLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695765469 171 LVSGPRVLLLDEPTNHLDIETIDWLEGFLKTF-KG-TIIFISHDRSFIRNmATRIVDLDRGKLVTyPGNYDQyLLDKE 246
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNMHDIcAGrTVIIIAHRLSTVKN-ADRIIVMEKGRIVE-QGSHDE-LLAEN 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-232 |
1.45e-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: 80.15 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 15 DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE----QDLVVARLqqdppRN----VTGTVY-- 84
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDghdlADYTLASL-----RRqvalVSQDVVlf 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 85 -DFVAEGIAeqaaylkgYHDVSQLVMTDPSDknLNELARLQEQLDNLGLwQLDSRINEvleqlnldpNAelSSLSGGWLR 163
Cdd:TIGR02203 419 nDTIANNIA--------YGRTEQADRAEIER--ALAAAYAQDFVDKLPL-GLDTPIGE---------NG--VLLSGGQRQ 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695765469 164 KAALGRALVSGPRVLLLDEPTNHLDIET----IDWLEGFLKtfKGTIIFISHDRSFIRNmATRIVDLDRGKLV 232
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESerlvQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIV 546
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
10-245 |
1.62e-15 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 76.11 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 10 WLSF-SDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE----QDLVVARLqqdppRNVTGTVY 84
Cdd:cd03254 9 NFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDgidiRDISRKSL-----RSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 85 --DFVAEG-IAEQAAYLKgyhdvsqlvmTDPSDKNLNELARlQEQLDNLglwqLDSRINEVLEQLNldPNAELssLSGGW 161
Cdd:cd03254 84 qdTFLFSGtIMENIRLGR----------PNATDEEVIEAAK-EAGAHDF----IMKLPNGYDTVLG--ENGGN--LSQGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 162 LRKAALGRALVSGPRVLLLDEPTNHLDIETIDWL-EGFLKTFKG-TIIFISHDRSFIRNmATRIVDLDRGKLVTyPGNYD 239
Cdd:cd03254 145 RQLLAIARAMLRDPKILILDEATSNIDTETEKLIqEALEKLMKGrTSIIIAHRLSTIKN-ADKILVLDDGKIIE-EGTHD 222
|
....*.
gi 695765469 240 QYLLDK 245
Cdd:cd03254 223 ELLAKK 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-232 |
2.16e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 76.65 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 1 MSLISMHGAWLSFSDSPL---------LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYeQDLVVARL 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGLsgkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW-RGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 72 QQdpprnvtgtvydfvaegiAEQAAYLKgyhDVsQLVMTD-PSDKNLNELAR--LQEQLDNLglWQLD-----SRINEVL 143
Cdd:PRK10419 80 NR------------------AQRKAFRR---DI-QMVFQDsISAVNPRKTVReiIREPLRHL--LSLDkaerlARASEML 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 144 EQLNLDPnaELSS-----LSGGWLRKAALGRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRS 214
Cdd:PRK10419 136 RAVDLDD--SVLDkrppqLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLR 213
|
250
....*....|....*...
gi 695765469 215 FIRNMATRIVDLDRGKLV 232
Cdd:PRK10419 214 LVERFCQRVMVMDNGQIV 231
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
311-472 |
2.40e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 78.07 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 311 EAARSGKIVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRI-------------- 376
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgqdithvpaen 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 377 -HVGTKLevayfdQHRAeLDPDKTVMDNLAEG-------KQEVmvngKPRhVLGYLQdfMFH-PKRAMTPVRALSGGERN 447
Cdd:PRK09452 86 rHVNTVF------QSYA-LFPHMTVFENVAFGlrmqktpAAEI----TPR-VMEALR--MVQlEEFAQRKPHQLSGGQQQ 151
|
170 180
....*....|....*....|....*
gi 695765469 448 RLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALD 176
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
342-513 |
2.49e-15 |
|
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: 75.91 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 342 IQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIhvGTKLE-VAYFDQHrAELDPDKTVMDNLAEG----------KQE 410
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--EIELDtVSYKPQY-IKADYEGTVRDLLSSItkdfythpyfKTE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 411 VMvngKPRHVLGYLQdfmfhpkramTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDGY---- 486
Cdd:cd03237 99 IA---KPLQIEQILD----------REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaenn 165
|
170 180
....*....|....*....|....*..
gi 695765469 487 QGTVMLVSHDRQFVDNTVTECWIFEGE 513
Cdd:cd03237 166 EKTAFVVEHDIIMIDYLADRLIVFEGE 192
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-232 |
2.58e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 79.05 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFS---DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDL-------------VVarlQQ 73
Cdd:COG1132 345 VSFSypgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlIDGVDIrdltleslrrqigVV---PQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 74 DPPRnVTGTVYD---FVAEGIA----EQAAylkgyhdvsqlvmtdpsdknlnELARLQEQLDNL--GLwqlDSRINEvle 144
Cdd:COG1132 422 DTFL-FSGTIREnirYGRPDATdeevEEAA----------------------KAAQAHEFIEALpdGY---DTVVGE--- 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 145 qlnldpnaELSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIET---IdwLEGFLKTFKG-TIIFISHDRSFIRNmA 220
Cdd:COG1132 473 --------RGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETealI--QEALERLMKGrTTIVIAHRLSTIRN-A 541
|
250
....*....|..
gi 695765469 221 TRIVDLDRGKLV 232
Cdd:COG1132 542 DRILVLDDGRIV 553
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
321-496 |
2.60e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.89 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGtKLEVAYFdqhraeldPDKTV 400
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVD-GLDVATT--------PSREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 401 MDNLAEGKQEVMVN------------------GKP-----RHV---LGYLQdfmfhpkraMTPVRA-----LSGGERNRL 449
Cdd:COG4604 74 AKRLAILRQENHINsrltvrelvafgrfpyskGRLtaedrEIIdeaIAYLD---------LEDLADryldeLSGGQRQRA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695765469 450 LLARLFLKPSNLLILDEPTNDLD----VETLELLEELVDGYQGTVMLVSHD 496
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADELGKTVVIVLHD 195
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
321-473 |
2.89e-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: 75.73 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVD-GKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLEVAYFDQHRAELD 395
Cdd:cd03253 2 EFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdiREVTLDSLRRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 396 PD-----KTVMDNLAEGK-----QEVMVNGKPRHVLGYLQDFmfhPKRAMTPV--RA--LSGGERNRLLLARLFLKPSNL 461
Cdd:cd03253 82 QDtvlfnDTIGYNIRYGRpdatdEEVIEAAKAAQIHDKIMRF---PDGYDTIVgeRGlkLSGGEKQRVAIARAILKNPPI 158
|
170
....*....|..
gi 695765469 462 LILDEPTNDLDV 473
Cdd:cd03253 159 LLLDEATSALDT 170
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
277-596 |
2.93e-15 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 79.52 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 277 RRTRNEGRVRALKAMRRERGERREVMGSAKMQVEEAARSGKIV---FEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGP 353
Cdd:PLN03073 132 RRKRKEERQREVQYQAHVAEMEAAKAGMPGVYVNHDGNGGGPAikdIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGR 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 354 NGCGKTTLLKLM----LGQLKADSGRIHVG---------------------TKL--EVAYFDQHRAELD----------P 396
Cdd:PLN03073 212 NGTGKTTFLRYMamhaIDGIPKNCQILHVEqevvgddttalqcvlntdierTQLleEEAQLVAQQRELEfetetgkgkgA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 397 DKTVMDNLAEGKQEVMVNGKPRHVLGY---------LQDFMFHPKRAMTPVRALSGGERNRLLLAR-LFLKPsNLLILDE 466
Cdd:PLN03073 292 NKDGVDKDAVSQRLEEIYKRLELIDAYtaearaasiLAGLSFTPEMQVKATKTFSGGWRMRIALARaLFIEP-DLLLLDE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 467 PTNDLDVETLELLEELVDGYQGTVMLVSHDRQFVDNTVTECWIFEGEgRIGQYVGGYHDARGQQAQYLAQKQqiskKAVE 546
Cdd:PLN03073 371 PTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQ-KLVTYKGDYDTFERTREEQLKNQQ----KAFE 445
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 695765469 547 AAQPKAESVKRASGKLSYNLQR-ELEQlpQRLEELEtQLQTLQEQVADPSF 596
Cdd:PLN03073 446 SNERSRSHMQAFIDKFRYNAKRaSLVQ--SRIKALD-RLGHVDAVVNDPDY 493
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
321-472 |
3.55e-15 |
|
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: 75.45 E-value: 3.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTK---------LEVAYFDQHR 391
Cdd:cd03296 4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqeRNVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 392 AeLDPDKTVMDNLAEGKQEVMVNGKP-----RHVLGYLQDFMFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDE 466
Cdd:cd03296 84 A-LFRHMTVFDNVAFGLRVKPRSERPpeaeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
....*.
gi 695765469 467 PTNDLD 472
Cdd:cd03296 163 PFGALD 168
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
321-472 |
3.61e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 77.42 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLE-----VAY-FdQH 390
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGgrdvTDLPpkdrnIAMvF-QS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 391 RAeLDPDKTVMDNLAEG-------KQEvmVNGKPRHVLGYLQdfmfhpkraMTP-----VRALSGGERNRLLLARLFLKP 458
Cdd:COG3839 84 YA-LYPHMTVYENIAFPlklrkvpKAE--IDRRVREAAELLG---------LEDlldrkPKQLSGGQRQRVALGRALVRE 151
|
170
....*....|....
gi 695765469 459 SNLLILDEPTNDLD 472
Cdd:COG3839 152 PKVFLLDEPLSNLD 165
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
321-473 |
3.73e-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: 75.10 E-value: 3.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV----------GTKLEVAYFDQH 390
Cdd:cd03265 2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghdvvreprEVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 391 RAeLDPDKTVMDNLA-EGKQEVMVNGKPRHVLGYLQDFMFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTN 469
Cdd:cd03265 82 LS-VDDELTGWENLYiHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
....
gi 695765469 470 DLDV 473
Cdd:cd03265 161 GLDP 164
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-232 |
3.96e-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: 74.12 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 10 WLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqglddGRIIYEQdlvvarlqqdpprnVTGTVYdfvae 89
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALA-------GRRTGLG--------------VSGEVL----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 90 gIAEQAAYLKGYHDVSQLVMTDpsdknlnelarlqeqldnlglwqldsriNEVLEQL----NLDPNAELSSLSGGWLRKA 165
Cdd:cd03213 70 -INGRPLDKRSFRKIIGYVPQD----------------------------DILHPTLtvreTLMFAAKLRGLSGGERKRV 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695765469 166 ALGRALVSGPRVLLLDEPTNHLDIETIDWLegfLKTFKG------TIIFISHD-RSFIRNMATRIVDLDRGKLV 232
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGLDSSSALQV---MSLLRRladtgrTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
316-472 |
4.78e-15 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 78.22 E-value: 4.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 316 GKIVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLEVAYFDQHRAEL 394
Cdd:TIGR02203 329 GDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLdGHDLADYTLASLRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 DP--------DKTVMDNLAEGKQEVMVNGKPRHVL--GYLQDFMFH-PKRAMTPVRA----LSGGERNRLLLARLFLKPS 459
Cdd:TIGR02203 409 ALvsqdvvlfNDTIANNIAYGRTEQADRAEIERALaaAYAQDFVDKlPLGLDTPIGEngvlLSGGQRQRLAIARALLKDA 488
|
170
....*....|...
gi 695765469 460 NLLILDEPTNDLD 472
Cdd:TIGR02203 489 PILILDEATSALD 501
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-212 |
5.23e-15 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 78.17 E-value: 5.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFS---DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLVVARLQQDPPRNVTGTVydfv 87
Cdd:TIGR02868 340 LSAGypgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD-GVPVSSLDQDEVRRRVSVC---- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 88 aegiaEQAAYLKGyHDVSQLVMTDPSDKNLNELARLQEQLdNLGLWqldsrINEVLEQLNLDPNAELSSLSGGWLRKAAL 167
Cdd:TIGR02868 415 -----AQDAHLFD-TTVRENLRLARPDATDEELWAALERV-GLADW-----LRALPDGLDTVLGEGGARLSGGERQRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695765469 168 GRALVSGPRVLLLDEPTNHLDIETID-WLEGFLKTFKG-TIIFISHD 212
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADeLLEDLLAALSGrTVVLITHH 529
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
323-497 |
5.71e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 76.72 E-value: 5.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 323 ENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTklEVAYFD------------QH 390
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG--RDLFTNlpprerrvgfvfQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 391 RAeLDPDKTVMDNLAEGKQevmVNGKPRH-----VLGYLQdfMFH--------PKRamtpvraLSGGERNRLLLAR-LFL 456
Cdd:COG1118 84 YA-LFPHMTVAENIAFGLR---VRPPSKAeirarVEELLE--LVQlegladryPSQ-------LSGGQRQRVALARaLAV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695765469 457 KPSnLLILDEPTNDLDVetlelleeLV------------DGYQGTVMLVSHDR 497
Cdd:COG1118 151 EPE-VLLLDEPFGALDA--------KVrkelrrwlrrlhDELGGTTVFVTHDQ 194
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
321-473 |
7.42e-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: 76.29 E-value: 7.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLE-----VAYFDQHR 391
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvTGLPpekrnVGMVFQDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 392 AeLDPDKTVMDNLAEG-------KQEV---------MVNgkprhvlgyLQDFMfhpKRAmtpVRALSGGERNRLLLAR-L 454
Cdd:COG3842 87 A-LFPHLTVAENVAFGlrmrgvpKAEIrarvaelleLVG---------LEGLA---DRY---PHQLSGGQQQRVALARaL 150
|
170
....*....|....*....
gi 695765469 455 FLKPSnLLILDEPTNDLDV 473
Cdd:COG3842 151 APEPR-VLLLDEPLSALDA 168
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
321-498 |
7.44e-15 |
|
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: 74.20 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKlEVAYFD----------QH 390
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK-DITNLPphkrpvntvfQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 391 RAeLDPDKTVMDNLAEG-----------KQEVMVNGKPRHVLGYLQDFmfhpkramtpVRALSGGERNRLLLAR-LFLKP 458
Cdd:cd03300 81 YA-LFPHLTVFENIAFGlrlkklpkaeiKERVAEALDLVQLEGYANRK----------PSQLSGGQQQRVAIARaLVNEP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695765469 459 SnLLILDEPTNDLDVETLELLEELVDGYQG----TVMLVSHDRQ 498
Cdd:cd03300 150 K-VLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQE 192
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
15-232 |
7.85e-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: 74.01 E-value: 7.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 15 DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIIYEqdlvvarlqqdpPRNVTGT-VYDFVAEG 90
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTI---MGLlppRSGSIRFD------------GRDITGLpPHERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 91 IA------------------EQAAYLKGYHDVSQLVmtdpsDKNLNELARLQEQLDNLGlwqldsrinevleqlnldpna 152
Cdd:cd03224 77 IGyvpegrrifpeltveenlLLGAYARRRAKRKARL-----ERVYELFPRLKERRKQLA--------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 153 elSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:cd03224 131 --GTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDegvTILLVEQNARFALEIADRAYVLERG 208
|
...
gi 695765469 230 KLV 232
Cdd:cd03224 209 RVV 211
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-234 |
8.69e-15 |
|
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: 73.68 E-value: 8.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 4 ISMHGAWLSFSD--SPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIY-EQDLVVARLQ-------- 72
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdGVDISKIGLHdlrsrisi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 73 --QDPpRNVTGTVYDFVaegiaeqaaylkgyhdvsqlvmtDPsdknLNEL--ARLQEQLDNLGLWqldSRINEVLEQLNL 148
Cdd:cd03244 83 ipQDP-VLFSGTIRSNL-----------------------DP----FGEYsdEELWQALERVGLK---EFVESLPGGLDT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 149 DPNAELSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKT-FKG-TIIFISHdRsfIRNMAT--RIV 224
Cdd:cd03244 132 VVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREaFKDcTVLTIAH-R--LDTIIDsdRIL 208
|
250
....*....|
gi 695765469 225 DLDRGKLVTY 234
Cdd:cd03244 209 VLDKGRVVEF 218
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
316-473 |
9.46e-15 |
|
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: 77.86 E-value: 9.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 316 GKIVFEMENVNYQVDGKVLiKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLeVAYFDQH--RAE 393
Cdd:TIGR01193 472 GDIVINDVSYSYGYGSNIL-SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS-LKDIDRHtlRQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 L-----DP---DKTVMDNLAEGKQEVMVNGKPRHV--------------LGYLQDFMFHPKramtpvrALSGGERNRLLL 451
Cdd:TIGR01193 550 InylpqEPyifSGSILENLLLGAKENVSQDEIWAAceiaeikddienmpLGYQTELSEEGS-------SISGGQKQRIAL 622
|
170 180
....*....|....*....|..
gi 695765469 452 ARLFLKPSNLLILDEPTNDLDV 473
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDT 644
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
127-500 |
1.13e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.05 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 127 LDNLGLWQLDSRINEVLEQLnldpnaelsslSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG-- 204
Cdd:PRK15134 138 LDRVGIRQAAKRLTDYPHQL-----------SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQel 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 205 --TIIFISHDRSFIRNMATRIVDLDRGKLV------------TYPgnYDQYLLDKEEA-------------LRVEELQNA 257
Cdd:PRK15134 207 nmGLLFITHNLSIVRKLADRVAVMQNGRCVeqnraatlfsapTHP--YTQKLLNSEPSgdpvplpepasplLDVEQLQVA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 258 eFDrklaqeevwIRQGIKARRtrnegrvralkamrrergerrevmgsakmqveeaarsgkivfemenvnyqVDGKVLIKD 337
Cdd:PRK15134 285 -FP---------IRKGILKRT--------------------------------------------------VDHNVVVKN 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 338 FSAQIQRGDKIALIGPNGCGKTT----LLKLML--GQLKADSGRIH---------VGTKLEVAYFDQHRAeLDPDKTVMD 402
Cdd:PRK15134 305 ISFTLRPGETLGLVGESGSGKSTtglaLLRLINsqGEIWFDGQPLHnlnrrqllpVRHRIQVVFQDPNSS-LNPRLNVLQ 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 403 NLAEGKQ--EVMVNGKPR--HVLGYLQDFMFHPK-RAMTPVrALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETL 476
Cdd:PRK15134 384 IIEEGLRvhQPTLSAAQReqQVIAVMEEVGLDPEtRHRYPA-EFSGGQRQRIAIARaLILKPS-LIILDEPTSSLDKTVQ 461
|
410 420
....*....|....*....|....*...
gi 695765469 477 ELLEELVDGYQGTVML----VSHDRQFV 500
Cdd:PRK15134 462 AQILALLKSLQQKHQLaylfISHDLHVV 489
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
317-472 |
1.37e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 73.54 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 317 KIVFEMENVN--YQVDG---KVLiKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLEVAYF 387
Cdd:COG1136 2 SPLLELRNLTksYGTGEgevTAL-RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDgqdiSSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 388 DQHRAE----------LDPDKTVMDNLA-----EGKQEVMVNGKPRHVLGY--LQDFMFHpkramtPVRALSGGERNRLL 450
Cdd:COG1136 81 ARLRRRhigfvfqffnLLPELTALENVAlplllAGVSRKERRERARELLERvgLGDRLDH------RPSQLSGGQQQRVA 154
|
170 180
....*....|....*....|...
gi 695765469 451 LAR-LFLKPSnLLILDEPTNDLD 472
Cdd:COG1136 155 IARaLVNRPK-LILADEPTGNLD 176
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-245 |
1.54e-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: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 16 SPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL----NREQG--LDDGRIIYEQDLVVAR-----LQQDPpRNVTGTVY 84
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLvgffQARSGeiLLNGFSLKDIDRHTLRqfinyLPQEP-YIFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 85 DFVAEGIAEQAAYlkgyHDVSQLVmtdpsdknlnELARLQEQLDNLGLwQLDSRINEvleqlnldpnaELSSLSGGWLRK 164
Cdd:TIGR01193 566 ENLLLGAKENVSQ----DEIWAAC----------EIAEIKDDIENMPL-GYQTELSE-----------EGSSISGGQKQR 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 165 AALGRALVSGPRVLLLDEPTNHLDIET---IdwLEGFLKTFKGTIIFISHdRSFIRNMATRIVDLDRGKLVTyPGNYDQY 241
Cdd:TIGR01193 620 IALARALLTDSKVLILDESTSNLDTITekkI--VNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIE-QGSHDEL 695
|
....
gi 695765469 242 LLDK 245
Cdd:TIGR01193 696 LDRN 699
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
321-495 |
1.57e-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: 72.70 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-------GTKLEVAYFDQHRAe 393
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgkpldiAARNRIGYLPEERG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 LDPDKTVMDNL---AE----GKQEVMvngkpRHVLGYLQDFMFHPKRAmTPVRALSGGERNRLLLARLFLKPSNLLILDE 466
Cdd:cd03269 81 LYPKMKVIDQLvylAQlkglKKEEAR-----RRIDEWLERLELSEYAN-KRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190
....*....|....*....|....*....|..
gi 695765469 467 PTNDLDVETLELLEELVDGYQG---TVMLVSH 495
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARagkTVILSTH 186
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
324-496 |
1.58e-14 |
|
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: 76.48 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 324 NVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKAD---SGRIHVGTKLEVAYFDQHRAEL------ 394
Cdd:COG1123 11 SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRigmvfq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 DPDK-----TVMDNLAEGKQEVMVNGKPRH--VLGYLQDFMFhPKRAMTPVRALSGGERNRLLLAR-LFLKPSnLLILDE 466
Cdd:COG1123 91 DPMTqlnpvTVGDQIAEALENLGLSRAEARarVLELLEAVGL-ERRLDRYPHQLSGGQRQRVAIAMaLALDPD-LLIADE 168
|
170 180 190
....*....|....*....|....*....|....
gi 695765469 467 PTNDLDVETLELLEELVDGYQG----TVMLVSHD 496
Cdd:COG1123 169 PTTALDVTTQAEILDLLRELQRergtTVLLITHD 202
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
321-473 |
1.79e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.65 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLEVAYFDQHRAELDP 396
Cdd:PRK09536 5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvEALSARAASRRVASVPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 397 DKTVMDNLaEGKQEVMVNGKPrhvlgYLQDFMFHP-------KRAMT----------PVRALSGGERNRLLLARLFLKPS 459
Cdd:PRK09536 85 DTSLSFEF-DVRQVVEMGRTP-----HRSRFDTWTetdraavERAMErtgvaqfadrPVTSLSGGERQRVLLARALAQAT 158
|
170
....*....|....
gi 695765469 460 NLLILDEPTNDLDV 473
Cdd:PRK09536 159 PVLLLDEPTASLDI 172
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
323-496 |
1.84e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 73.25 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 323 ENVNYQVDGkvLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLEVA------YFDQHra 392
Cdd:COG3840 5 DDLTYRYGD--FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgqdlTALPPAerpvsmLFQEN-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 393 ELDPDKTVMDNLAEG-----------KQEVM-----VNgkprhvLGYLQDFMfhpkramtPvRALSGGERNRLLLARLFL 456
Cdd:COG3840 81 NLFPHLTVAQNIGLGlrpglkltaeqRAQVEqalerVG------LAGLLDRL--------P-GQLSGGQRQRVALARCLV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695765469 457 KPSNLLILDEPTNDLDVETLELLEELVDG----YQGTVMLVSHD 496
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDElcreRGLTVLMVTHD 189
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
320-472 |
2.53e-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: 72.18 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 320 FEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKL------------EVAY 386
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdGLKLtddkkninelrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 387 FDQHrAELDPDKTVMDNLAEGkqEVMVNGKPR-----HVLGYLQDFMFHPKRAMTPvRALSGGERNRLLLAR-LFLKPSn 460
Cdd:cd03262 81 VFQQ-FNLFPHLTVLENITLA--PIKVKGMSKaeaeeRALELLEKVGLADKADAYP-AQLSGGQQQRVAIARaLAMNPK- 155
|
170
....*....|..
gi 695765469 461 LLILDEPTNDLD 472
Cdd:cd03262 156 VMLFDEPTSALD 167
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
336-496 |
3.00e-14 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 71.94 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 336 KDFSAQIQ---RGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG---------------TKLEVAYFDQHRAeLDPD 397
Cdd:cd03297 11 PDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsrkkinlppQQRKIGLVFQQYA-LFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 398 KTVMDNLAEGKQEVMVNGK---PRHVLGYLQdfMFHPKRAmtPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
Cdd:cd03297 90 LNVRENLAFGLKRKRNREDrisVDELLDLLG--LDHLLNR--YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180
....*....|....*....|....*.
gi 695765469 475 TLELLEELVD----GYQGTVMLVSHD 496
Cdd:cd03297 166 LRLQLLPELKqikkNLNIPVIFVTHD 191
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
34-232 |
3.33e-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: 72.92 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 34 LVGRNGAGKSTLMKILNREQGLDDGRIIY-----------EQDLVVARLQQDPPRNVTGTVYDFVAEGiaeQAAYLkgyh 102
Cdd:TIGR03873 32 LLGPNGSGKSTLLRLLAGALRPDAGTVDLagvdlhglsrrARARRVALVEQDSDTAVPLTVRDVVALG---RIPHR---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 103 dvSQLVMTDPSDknlNELARlqEQLDNLGLWQLDSRinevleqlnldpnaELSSLSGGWLRKAALGRALVSGPRVLLLDE 182
Cdd:TIGR03873 105 --SLWAGDSPHD---AAVVD--RALARTELSHLADR--------------DMSTLSGGERQRVHVARALAQEPKLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695765469 183 PTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:TIGR03873 164 PTNHLDVRAQLETLALVRELAAtgvTVVAALHDLNLAASYCDHVVVLDGGRVV 216
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
17-232 |
3.59e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 72.92 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreqglddgriiyeqdLVVARLQQdpprnvtGTVYdFVAEGIAE-QA 95
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLL----------------LGLEKPAQ-------GTVS-FRGQDLYQlDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 96 AYLKGYHDVSQLVMTD-PSDKNLNELAR--LQEQLDNLGlwQLD-----SRINEVLEQLNLDPNAEL---SSLSGGWLRK 164
Cdd:TIGR02769 81 KQRRAFRRDVQLVFQDsPSAVNPRMTVRqiIGEPLRHLT--SLDeseqkARIAELLDMVGLRSEDADklpRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695765469 165 AALGRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-232 |
3.85e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 72.42 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 4 ISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDL------VVAR----LQ 72
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVlVDGLDVattpsrELAKrlaiLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 73 QDPPRNVTGTVYDFVAEGiaeQAAYLKGyhdvsqlvmtdpsdknlnelaRLQEQldnlglwqlDSR-INEVLEQLNLDPN 151
Cdd:COG4604 82 QENHINSRLTVRELVAFG---RFPYSKG---------------------RLTAE---------DREiIDEAIAYLDLEDL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 152 AE--LSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVD 225
Cdd:COG4604 129 ADryLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVA 208
|
....*..
gi 695765469 226 LDRGKLV 232
Cdd:COG4604 209 MKDGRVV 215
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-232 |
4.02e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 72.35 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 1 MSlISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlvvarlqqdpprNVT 80
Cdd:PRK11124 1 MS-IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL-----------------NIA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 81 GTVYDFVAEGIAEQAAYLK--------GYHDVSQLVMTDpsdkNLNE----LARLQEQldnlglwQLDSRINEVLEQLNL 148
Cdd:PRK11124 63 GNHFDFSKTPSDKAIRELRrnvgmvfqQYNLWPHLTVQQ----NLIEapcrVLGLSKD-------QALARAEKLLERLRL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 149 DPNAEL--SSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKGTII---FISHDRSFIRNMATRI 223
Cdd:PRK11124 132 KPYADRfpLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHEVEVARKTASRV 211
|
....*....
gi 695765469 224 VDLDRGKLV 232
Cdd:PRK11124 212 VYMENGHIV 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
335-468 |
4.16e-14 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 71.70 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 335 IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG------------TKLEVAYFDQHRaELDPDKTVMD 402
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditglppherARAGIGYVPEGR-RIFPELTVEE 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 403 NLAEGKQeVMVNGKPRHVLGYLQDfMFhPK---RAMTPVRALSGGERNRLLLAR-LFLKPSnLLILDEPT 468
Cdd:cd03224 95 NLLLGAY-ARRRAKRKARLERVYE-LF-PRlkeRRKQLAGTLSGGEQQMLAIARaLMSRPK-LLLLDEPS 160
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
330-472 |
4.36e-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: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 330 DGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLEVAYFDQHRAE---------LDP 396
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdiNKLKGKALRQLRRQigmifqqfnLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 397 DKTVMDNLAEGKqevmvngkprhvLGYLQDF-----MFHP----------------KRAMTPVRALSGGERNRLLLARLF 455
Cdd:cd03256 92 RLSVLENVLSGR------------LGRRSTWrslfgLFPKeekqralaalervgllDKAYQRADQLSGGQQQRVAIARAL 159
|
170
....*....|....*..
gi 695765469 456 LKPSNLLILDEPTNDLD 472
Cdd:cd03256 160 MQQPKLILADEPVASLD 176
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
317-505 |
4.42e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 72.05 E-value: 4.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 317 KIVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKL----------EVA 385
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDIstlkpeiyrqQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 386 YFDQHRAeLDPDkTVMDNLAEGKQEVMVNGKPRHVLGYLQDFMFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:PRK10247 85 YCAQTPT-LFGD-TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695765469 466 EPTNDLDVETLELLEELVDGY----QGTVMLVSHDR---QFVDNTVT 505
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYvreqNIAVLWVTHDKdeiNHADKVIT 209
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-192 |
5.27e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.06 E-value: 5.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDlvvarlQQDPPRnvtgtvydfvaegIAEQAA 96
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG------DIDDPD-------------VAEACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 97 YLkGYHDVSQLVMTdpsdknlnelarlqeQLDNLGLW-----QLDSRINEVLEQLNLDPNAEL--SSLSGGWLRKAALGR 169
Cdd:PRK13539 77 YL-GHRNAMKPALT---------------VAENLEFWaaflgGEELDIAAALEAVGLAPLAHLpfGYLSAGQKRRVALAR 140
|
170 180
....*....|....*....|...
gi 695765469 170 ALVSGPRVLLLDEPTNHLDIETI 192
Cdd:PRK13539 141 LLVSNRPIWILDEPTAALDAAAV 163
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-473 |
5.75e-14 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 69.76 E-value: 5.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 320 FEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHvgtklevayfdqhraeldpdkt 399
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL---------------------- 58
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695765469 400 vmdnlaegkqevmVNGKPRHVLGylqdfmfhPKRAM----TPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03216 59 -------------VDGKEVSFAS--------PRDARragiAMVYQLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
335-473 |
5.96e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.20 E-value: 5.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 335 IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLEVAY-------FDQhRAELDPDKTVMDN 403
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLgyvpFKRRKEFarrigvvFGQ-RSQLWWDLPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 404 L-----------AEGKQ--EVMVNgkprhVLGyLQDFMfhpkraMTPVRALSGGERNRL-LLARLFLKPSnLLILDEPTN 469
Cdd:COG4586 117 FrllkaiyripdAEYKKrlDELVE-----LLD-LGELL------DTPVRQLSLGQRMRCeLAAALLHRPK-ILFLDEPTI 183
|
....
gi 695765469 470 DLDV 473
Cdd:COG4586 184 GLDV 187
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-234 |
6.53e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 71.41 E-value: 6.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlvvarlqqdpprnVTGTVYDFVAEGIAEQAAyL 98
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT-----------------VRGRVSSLLGLGGGFNPE-L 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 99 KGYhdvsqlvmtdpsdKNLNELARLqeqldnLGLW--QLDSRINEVLE--QLNLDPNAELSSLSGGWLRKAALGRALVSG 174
Cdd:cd03220 100 TGR-------------ENIYLNGRL------LGLSrkEIDEKIDEIIEfsELGDFIDLPVKTYSSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695765469 175 PRVLLLDEPTNHLDIET----IDWLEGFLKTFKgTIIFISHDRSFIRNMATRIVDLDRGKLVTY 234
Cdd:cd03220 161 PDILLIDEVLAVGDAAFqekcQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-229 |
6.87e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.84 E-value: 6.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 14 SDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYEQDLVVARLQQDP--PrnvTGTvydfva 88
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIA---GLwpyGSGRIARPAGARVLFLPQRPylP---LGT------ 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 89 egIAEQAAYlkgyhdvsqlvmtdPSDKNLNELARLQEQLDNLGLWQLDSRINEVL--EQLnldpnaelssLSGGWLRKAA 166
Cdd:COG4178 442 --LREALLY--------------PATAEAFSDAELREALEAVGLGHLAERLDEEAdwDQV----------LSLGEQQRLA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695765469 167 LGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKT--FKGTIIFISHdRSFIRNMATRIVDLDRG 229
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
336-466 |
7.39e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 71.65 E-value: 7.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 336 KDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTK----LEVAyfdqhrAELDPDKTVMDNlaegkqeV 411
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsalLELG------AGFHPELTGREN-------I 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695765469 412 MVNGkprHVLGY-----------------LQDFMfhpkraMTPVRALSGGERNRLLLA-RLFLKPsNLLILDE 466
Cdd:COG1134 110 YLNG---RLLGLsrkeidekfdeivefaeLGDFI------DQPVKTYSSGMRARLAFAvATAVDP-DILLVDE 172
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-232 |
9.40e-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: 70.86 E-value: 9.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLVVARLQQDPPRNVtGTVYDfvAEGI------A 92
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVD-GFDVVKEPAEARRRL-GFVSD--STGLydrltaR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 93 EQAAYLKGYHDVsqlvmtdpsdKNLNELARLQEQLDNLGlwqldsrINEVLEQlnldpnaELSSLSGGWLRKAALGRALV 172
Cdd:cd03266 97 ENLEYFAGLYGL----------KGDELTARLEELADRLG-------MEELLDR-------RVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695765469 173 SGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
321-473 |
1.01e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.22 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLEVAYFDQ-----HR 391
Cdd:PRK13538 3 EARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQgepiRRQRDEYHQDllylgHQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 392 AELDPDKTVMDNLA-------EGKQEVMvngkpRHVLGY--LQDFMfhpkraMTPVRALSGGERNRLLLARLFLKPSNLL 462
Cdd:PRK13538 83 PGIKTELTALENLRfyqrlhgPGDDEAL-----WEALAQvgLAGFE------DVPVRQLSAGQQRRVALARLWLTRAPLW 151
|
170
....*....|.
gi 695765469 463 ILDEPTNDLDV 473
Cdd:PRK13538 152 ILDEPFTAIDK 162
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
312-472 |
1.10e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 72.95 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 312 AARSGKIV---FEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRI--------HVGT 380
Cdd:PRK11607 9 QAKTRKALtplLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvdlsHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 381 KLEVAYFDQHRAELDPDKTVMDNLAEG-KQEVM----VNGKPRHVLG--YLQDFmfhpkrAMTPVRALSGGERNRLLLAR 453
Cdd:PRK11607 89 YQRPINMMFQSYALFPHMTVEQNIAFGlKQDKLpkaeIASRVNEMLGlvHMQEF------AKRKPHQLSGGQRQRVALAR 162
|
170
....*....|....*....
gi 695765469 454 LFLKPSNLLILDEPTNDLD 472
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALD 181
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-246 |
1.21e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.09 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFS----DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLvvARLQQDPPRN----VTG 81
Cdd:PRK11160 344 VSFTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIlLNGQPI--ADYSEAALRQaisvVSQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 82 TVYDFvaegiaeqAAYLKgyhDVSQLVMTDPSDKNLNE------LARLQEQLDNLGLWqldsrINEVLEQLnldpnaels 155
Cdd:PRK11160 422 RVHLF--------SATLR---DNLLLAAPNASDEALIEvlqqvgLEKLLEDDKGLNAW-----LGEGGRQL--------- 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 156 slSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIET---IdwLEGFLKTFKG-TIIFISHDRSFIRNMaTRIVDLDRGKL 231
Cdd:PRK11160 477 --SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqI--LELLAEHAQNkTVLMITHRLTGLEQF-DRICVMDNGQI 551
|
250
....*....|....*
gi 695765469 232 VTYpGNYDQyLLDKE 246
Cdd:PRK11160 552 IEQ-GTHQE-LLAQQ 564
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
330-472 |
1.28e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 73.73 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 330 DGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKAdSGRIHVG----TKLEVAYFDQHRAELD-----PDKTV 400
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINgielRELDPESWRKHLSWVGqnpqlPHGTL 439
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 401 MDNLAEGKQEvMVNGKPRHVL--GYLQDFMF-HPKRAMTPVR----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK11174 440 RDNVLLGNPD-ASDEQLQQALenAWVSEFLPlLPQGLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-232 |
1.29e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 71.62 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYEQ-DLVVARLQQDPPRNVTGTV-----YDFVAE 89
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLN---GLlkpTSGKIIIDGvDITDKKVKLSDIRKKVGLVfqypeYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 90 GIAEQAAYlkgyhdvsqlvmtDPSDKNLNElarlqEQLDNlglwqldsRINEVLEQLNLDPN--AELS--SLSGGWLRKA 165
Cdd:PRK13637 100 TIEKDIAF-------------GPINLGLSE-----EEIEN--------RVKRAMNIVGLDYEdyKDKSpfELSGGQKRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765469 166 ALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKT----FKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKElhkeYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-234 |
1.41e-13 |
|
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: 70.00 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 4 ISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqdlvvARLQQDPPRNVTGtv 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD-----GKPLDIAARNRIG-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 84 ydFVAEgiaEQAAYLKgyhdvsQLVMtdpsdKNLNELARLQeqldNLGLWQLDSRINEVLEQLNLDPNAE--LSSLSGGW 161
Cdd:cd03269 74 --YLPE---ERGLYPK------MKVI-----DQLVYLAQLK----GLKKEEARRRIDEWLERLELSEYANkrVEELSKGN 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 162 LRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIVDLDRGKLVTY 234
Cdd:cd03269 134 QQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-234 |
1.76e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 70.43 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 1 MSlISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlvvarlqqdpprNVT 80
Cdd:COG4161 1 MS-IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL-----------------NIA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 81 GTVYDFVAEGIAEQAAYLKG--------YHDVSQL-VMtdpsdKNLNE----LARLQEQldnlglwQLDSRINEVLEQLN 147
Cdd:COG4161 63 GHQFDFSQKPSEKAIRLLRQkvgmvfqqYNLWPHLtVM-----ENLIEapckVLGLSKE-------QAREKAMKLLARLR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 148 LDPNAEL--SSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKGTII---FISHDRSFIRNMATR 222
Cdd:COG4161 131 LTDKADRfpLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGItqvIVTHEVEFARKVASQ 210
|
250
....*....|..
gi 695765469 223 IVDLDRGKLVTY 234
Cdd:COG4161 211 VVYMEKGRIIEQ 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
12-231 |
2.06e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.48 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGLDdgriiyeqdlvvarlqqdpprnvTGTVYDFVAegi 91
Cdd:PRK11247 21 RYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLL---AGLE-----------------------TPSAGELLA--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 92 aeQAAYLKGYHDVSQLVMTDpsdknlnelARL---QEQLDNLGL-----WQLDSRinEVLEQLNLDPNAE--LSSLSGGW 161
Cdd:PRK11247 72 --GTAPLAEAREDTRLMFQD---------ARLlpwKKVIDNVGLglkgqWRDAAL--QALAAVGLADRANewPAALSGGQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695765469 162 LRKAALGRALVSGPRVLLLDEPTNHLD----IETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK11247 139 KQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
321-468 |
2.16e-13 |
|
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: 70.01 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVN--YqvdGKVLI-KDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLE--------VA 385
Cdd:COG0410 5 EVENLHagY---GGIHVlHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgediTGLPphriarlgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 386 YFDQHRaELDPDKTVMDNLAEGKQEVMVNGKPRHVLgylqDFMFH--PK---RAMTPVRALSGGERNRLLLAR-LFLKPS 459
Cdd:COG0410 82 YVPEGR-RIFPSLTVEENLLLGAYARRDRAEVRADL----ERVYElfPRlkeRRRQRAGTLSGGEQQMLAIGRaLMSRPK 156
|
....*....
gi 695765469 460 nLLILDEPT 468
Cdd:COG0410 157 -LLLLDEPS 164
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
334-472 |
2.20e-13 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 69.99 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 334 LIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKAD---SGRIHVG--------TKLEVAYFDQHRAELdPDKTVMD 402
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNgqprkpdqFQKCVAYVRQDDILL-PGLTVRE 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695765469 403 NLAEGKQEVMVNGKPRHVLGYLQDFMFHPKRAMTPVR-----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03234 101 TLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGgnlvkGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
19-232 |
2.31e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 71.65 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIY---------EQDLVVARlqqdppRNVtGTVydF--- 86
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVdgvdltalsERELRAAR------RKI-GMI--Fqhf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 87 -------VAEGIA---EQAAYLKGyhdvsqlvmtdpsdknlnelarlqeqldnlglwQLDSRINEVLEQLNLDP--NAEL 154
Cdd:COG1135 92 nllssrtVAENVAlplEIAGVPKA---------------------------------EIRKRVAELLELVGLSDkaDAYP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 155 SSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIET---IdwLEgFLK----TFKGTIIFISHDRSFIRNMATRIVDLD 227
Cdd:COG1135 139 SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtrsI--LD-LLKdinrELGLTIVLITHEMDVVRRICDRVAVLE 215
|
....*
gi 695765469 228 RGKLV 232
Cdd:COG1135 216 NGRIV 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-226 |
2.38e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 68.80 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQ--DPPRNVTGTVYDFVAE 89
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsEVPDSLPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 90 GIAEQAAYLKGYhdvsqlvmtDPSDKnlnelARLQEQLDNLGLWQLDSRinevleqlnldpnaELSSLSGGWLRKAALGR 169
Cdd:NF040873 81 GRWARRGLWRRL---------TRDDR-----AAVDDALERVGLADLAGR--------------QLGELSGGQRQRALLAQ 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 170 ALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNmATRIVDL 226
Cdd:NF040873 133 GLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLELVRR-ADPCVLL 191
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-231 |
2.53e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 71.65 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDlvVARLQ-QDppRNVtG-------- 81
Cdd:PRK10851 11 SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgTD--VSRLHaRD--RKV-Gfvfqhyal 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 82 ----TVYDFVAEGIAeqaaylkgyhdvsqlVMtdPSDKNLNELArlqeqldnlglwqLDSRINEVLEQLNLDPNAEL--S 155
Cdd:PRK10851 86 frhmTVFDNIAFGLT---------------VL--PRRERPNAAA-------------IKAKVTQLLEMVQLAHLADRypA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 156 SLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK10851 136 QLSGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-244 |
2.57e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 72.90 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 3 LISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlvvarlqqdpprnvtgt 82
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---------------------- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 83 vydFVAEGIAeqaaylKGYHDVSQLVMTDPSDKNLNELARL-----QEQL-DNLGLWQLD-SRINEVLEQLnldpnaels 155
Cdd:PRK10636 370 ---GLAKGIK------LGYFAQHQLEFLRADESPLQHLARLapqelEQKLrDYLGGFGFQgDKVTEETRRF--------- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 156 slSGGwlRKAALGRALV--SGPRVLLLDEPTNHLDIETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVT 233
Cdd:PRK10636 432 --SGG--EKARLVLALIvwQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEP 507
|
250
....*....|....
gi 695765469 234 YPG---NYDQYLLD 244
Cdd:PRK10636 508 FDGdleDYQQWLSD 521
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
324-472 |
3.27e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 69.89 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 324 NVNYQVDG--KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV------GTKLEVAYFDQHRAeLD 395
Cdd:COG4525 10 SVRYPGGGqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdgvpvtGPGADRGVVFQKDA-LL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 396 PDKTVMDNLAEGKQevmVNGKPRH-----------VLGyLQDFmfhpkrAMTPVRALSGGERNRLLLARLFLKPSNLLIL 464
Cdd:COG4525 89 PWLNVLDNVAFGLR---LRGVPKAerraraeellaLVG-LADF------ARRRIWQLSGGMRQRVGIARALAADPRFLLM 158
|
....*...
gi 695765469 465 DEPTNDLD 472
Cdd:COG4525 159 DEPFGALD 166
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
310-472 |
3.64e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 72.55 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 310 EEAARSGKIVFEMENVN--YQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYF 387
Cdd:PRK11160 329 TSTAAADQVSLTLNNVSftYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 388 DQ----------HRAELDPDkTVMDNLAEGK----QEVMVNGKPRHVLGYLQDfmfHPKRAMTPV----RALSGGERNRL 449
Cdd:PRK11160 409 EAalrqaisvvsQRVHLFSA-TLRDNLLLAApnasDEALIEVLQQVGLEKLLE---DDKGLNAWLgeggRQLSGGEQRRL 484
|
170 180
....*....|....*....|...
gi 695765469 450 LLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLD 507
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
12-232 |
3.84e-13 |
|
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: 68.94 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGR-IIYEQDLVvarlqqDPPRNVTGTVydfvaeg 90
Cdd:cd03265 9 KYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGHDVV------REPREVRRRI------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 91 iaeqaaylkGYhdVSQLVMTDP---SDKNLNELARLQeqldNLGLWQLDSRINEVLEQLNLDPNAE--LSSLSGGWLRKA 165
Cdd:cd03265 76 ---------GI--VFQDLSVDDeltGWENLYIHARLY----GVPGAERRERIDELLDFVGLLEAADrlVKTYSGGMRRRL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765469 166 ALGRALVSGPRVLLLDEPTNHLDIETID--W--LEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03265 141 EIARSLVHRPEVLFLDEPTIGLDPQTRAhvWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-250 |
3.88e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 72.45 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFS-----DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNR------EQGLDDGRIIYEQDLV-----VARLQQDP 75
Cdd:TIGR00958 485 SFSypnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNlyqptgGQVLLDGVPLVQYDHHylhrqVALVGQEP 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 76 PRnVTGTVYDFVAEGIAE-------QAAYLKGYHDvsqLVMTDPSDknlnelarlqeqldnlglwqLDSRINEVLEQLnl 148
Cdd:TIGR00958 565 VL-FSGSVRENIAYGLTDtpdeeimAAAKAANAHD---FIMEFPNG--------------------YDTEVGEKGSQL-- 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 149 dpnaelsslSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIEtIDWLEGFLKTFKG-TIIFISHDRSFIRNmATRIVDLD 227
Cdd:TIGR00958 619 ---------SGGQKQRIAIARALVRKPRVLILDEATSALDAE-CEQLLQESRSRASrTVLLIAHRLSTVER-ADQILVLK 687
|
250 260
....*....|....*....|...
gi 695765469 228 RGKLVTYpGNYDQyLLDKEEALR 250
Cdd:TIGR00958 688 KGSVVEM-GTHKQ-LMEDQGCYK 708
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-225 |
4.37e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.41 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 1 MSLISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQDPPRNVT 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 81 GTvydfvaegiaEQAAYLKGYHDVSQLVmtdpsdknlnELARlQEQLDNLGLWQLDSR--INEVLEQLNLDPNAE--LSS 156
Cdd:PRK09536 81 SV----------PQDTSLSFEFDVRQVV----------EMGR-TPHRSRFDTWTETDRaaVERAMERTGVAQFADrpVTS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695765469 157 LSGGWLRKAALGRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFIsHDrsfiRNMATRIVD 225
Cdd:PRK09536 140 LSGGERQRVLLARALAQATPVLLLDEPTASLDInhqvRTLELVRRLVDDGKTAVAAI-HD----LDLAARYCD 207
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
335-466 |
4.84e-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: 68.71 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 335 IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTK----LEVAYFdqhraeLDPDKTVMDNlaegkqe 410
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsslLGLGGG------FNPELTGREN------- 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695765469 411 VMVNGKprhVLGYLQDFMfhpkRAM---------------TPVRALSGGERNRLLLA-RLFLKPsNLLILDE 466
Cdd:cd03220 105 IYLNGR---LLGLSRKEI----DEKideiiefselgdfidLPVKTYSSGMKARLAFAiATALEP-DILLIDE 168
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
320-467 |
6.31e-13 |
|
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: 67.88 E-value: 6.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 320 FEMENVNY-----QVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKleVAY-------- 386
Cdd:cd03250 1 ISVEDASFtwdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYvsqepwiq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 387 -------------FDQHRAE-------LDPDktvMDNLAEGKQ-EVMVNGkprhvlgylqdfmfhpkramtpvRALSGGE 445
Cdd:cd03250 79 ngtirenilfgkpFDEERYEkvikacaLEPD---LEILPDGDLtEIGEKG-----------------------INLSGGQ 132
|
170 180
....*....|....*....|..
gi 695765469 446 RNRLLLARLFLKPSNLLILDEP 467
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDP 154
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
315-473 |
6.40e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 71.53 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 315 SGKIVFEmeNVNYQVDGKVL-IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLEvayfDQHRA 392
Cdd:PRK13657 332 KGAVEFD--DVSFSYDNSRQgVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTDIR----TVTRA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 393 EL---------DP---DKTVMDNLAEGK-----QEVMVNGKPRHVLgylqDFMF-HPKRAMTPV----RALSGGERNRLL 450
Cdd:PRK13657 406 SLrrniavvfqDAglfNRSIEDNIRVGRpdatdEEMRAAAERAQAH----DFIErKPDGYDTVVgergRQLSGGERQRLA 481
|
170 180
....*....|....*....|...
gi 695765469 451 LARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK13657 482 IARALLKDPPILILDEATSALDV 504
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-189 |
7.02e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 68.99 E-value: 7.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE---------QDLvvAR----LQQDPPR 77
Cdd:COG4559 9 VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgrplaawspWEL--ARrravLPQHSSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 78 NVTGTVYDFVAEGIaeqAAYLKGYHDVSQLVmtdpsdknlnelarlQEQLDNLGLWQLDSRInevleqlnldpnaeLSSL 157
Cdd:COG4559 87 AFPFTVEEVVALGR---APHGSSAAQDRQIV---------------REALALVGLAHLAGRS--------------YQTL 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 695765469 158 SGGWLRKAALGRALV-------SGPRVLLLDEPTNHLDI 189
Cdd:COG4559 135 SGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDL 173
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
320-467 |
7.57e-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: 68.34 E-value: 7.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 320 FEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLEV--------AYF 387
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqdiTKLPMhkrarlgiGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 388 DQhRAELDPDKTVMDNLAEGKQEVMVNGKPRH--VLGYLQDFMFHPKRAmTPVRALSGGERNRLLLAR-LFLKPSNLLiL 464
Cdd:cd03218 81 PQ-EASIFRKLTVEENILAVLEIRGLSKKEREekLEELLEEFHITHLRK-SKASSLSGGERRRVEIARaLATNPKFLL-L 157
|
...
gi 695765469 465 DEP 467
Cdd:cd03218 158 DEP 160
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
12-232 |
7.69e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 70.63 E-value: 7.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLV-VARLQQdpPRNVTGTVYDFVAE 89
Cdd:PRK11607 28 SFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgVDLShVPPYQR--PINMMFQSYALFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 90 GIAEQ--AAYLKGyhdvsqlvmtdpsdknlnelarlqeqlDNLGLWQLDSRINEVLEQLNLDPNAELS--SLSGGWLRKA 165
Cdd:PRK11607 106 MTVEQniAFGLKQ---------------------------DKLPKAEIASRVNEMLGLVHMQEFAKRKphQLSGGQRQRV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695765469 166 ALGRALVSGPRVLLLDEPTNHLD--------IETIDWLEgflkTFKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDkklrdrmqLEVVDILE----RVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
327-496 |
9.32e-13 |
|
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: 67.06 E-value: 9.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 327 YQVDGKVLiKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKlevayfdqhraELDPDKTvmdNLAE 406
Cdd:TIGR01166 1 YPGGPEVL-KGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGE-----------PLDYSRK---GLLE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 407 GKQEV-MVNGKPRHVLGYL---QDFMFHP--------------KRAMT----------PVRALSGGERNRLLLA-RLFLK 457
Cdd:TIGR01166 66 RRQRVgLVFQDPDDQLFAAdvdQDVAFGPlnlglseaeverrvREALTavgasglrerPTHCLSGGEKKRVAIAgAVAMR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695765469 458 PsNLLILDEPTNDLDVETLELLEELVDGY--QG-TVMLVSHD 496
Cdd:TIGR01166 146 P-DVLLLDEPTAGLDPAGREQMLAILRRLraEGmTVVISTHD 186
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-248 |
1.03e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.82 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 15 DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE----QDLVVARLqqdppRN----VTGTVYDF 86
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDghdlRDYTLASL-----RNqvalVSQNVHLF 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 87 vAEGIAEQAAYLKGYHdvsqlvmtdPSDKNLNELARLQ------EQLDNlglwQLDSRINEvleqlnldpNAelSSLSGG 160
Cdd:PRK11176 430 -NDTIANNIAYARTEQ---------YSREQIEEAARMAyamdfiNKMDN----GLDTVIGE---------NG--VLLSGG 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 161 WLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG--TIIFISHDRSFIRNmATRIVDLDRGKLVTYpGNY 238
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAHRLSTIEK-ADEILVVEDGEIVER-GTH 562
|
250
....*....|
gi 695765469 239 DQyLLDKEEA 248
Cdd:PRK11176 563 AE-LLAQNGV 571
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-232 |
1.20e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 68.24 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 1 MSLISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI------------IYEQDLVV 68
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtarsLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 69 ARLQQDpprnvTGTVY-DF-------VAEGIAEQAAYLKGyhdvsqlvmtDPSDKnlnELARLQEQLDNLGLwqldsrin 140
Cdd:PRK11264 81 RQLRQH-----VGFVFqNFnlfphrtVLENIIEGPVIVKG----------EPKEE---ATARARELLAKVGL-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 141 evleqlNLDPNAELSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTF---KGTIIFISHDRSFIR 217
Cdd:PRK11264 135 ------AGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVIVTHEMSFAR 208
|
250
....*....|....*
gi 695765469 218 NMATRIVDLDRGKLV 232
Cdd:PRK11264 209 DVADRAIFMDQGRIV 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-232 |
1.25e-12 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 66.57 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFS----DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlvvarLQQDPPRNVTGTVYDF 86
Cdd:cd03247 6 VSFSypeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT---------LDGVPVSDLEKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 87 VaeGIAEQAAYLkgyhdvsqlvmtdpSDKNLnelarlqeqLDNLGLwqldsrinevleqlnldpnaelsSLSGGWLRKAA 166
Cdd:cd03247 77 I--SVLNQRPYL--------------FDTTL---------RNNLGR-----------------------RFSGGERQRLA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695765469 167 LGRALVSGPRVLLLDEPTNHLDIET-IDWLEGFLKTFKG-TIIFISHDRSFIRNMaTRIVDLDRGKLV 232
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITeRQLLSLIFEVLKDkTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-223 |
1.25e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 69.38 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLVVA----------RLQ---QDP-----PRNv 79
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgQDITGLsgrelrplrrRMQmvfQDPyaslnPRM- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 80 tgTVYDFVAEGIAeqaaylkgyhdvsqlvmtdpsdknLNELARLQEQLDnlglwqldsRINEVLEQLNLDPNA------E 153
Cdd:COG4608 113 --TVGDIIAEPLR------------------------IHGLASKAERRE---------RVAELLELVGLRPEHadryphE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695765469 154 LSslsGGWLRKAALGRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRI 223
Cdd:COG4608 158 FS---GGQRQRIGIARALALNPKLIVCDEPVSALDVsiqaQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRV 228
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
320-473 |
1.42e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.28 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 320 FEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKL-----------EVAYFD 388
Cdd:PRK10575 12 FALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 389 QhraELDPdktvmdnlAEG---KQEVMVNGKPRHvlGYLQDFMFHPKR---------AMTP-----VRALSGGERNRLLL 451
Cdd:PRK10575 92 Q---QLPA--------AEGmtvRELVAIGRYPWH--GALGRFGAADREkveeaislvGLKPlahrlVDSLSGGERQRAWI 158
|
170 180
....*....|....*....|..
gi 695765469 452 ARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDI 180
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-232 |
1.53e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 69.06 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIY---------EQDLVVARlqqdppRNV---------- 79
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVdgqdltalsEKELRKAR------RQIgmifqhfnll 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 80 -TGTVYDFVAegiaeqaaylkgyhdvsqLVMtdpsdknlnELARLQEQldnlglwQLDSRINEVLEQLNLDPNAEL--SS 156
Cdd:PRK11153 95 sSRTVFDNVA------------------LPL---------ELAGTPKA-------EIKARVTELLELVGLSDKADRypAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 157 LSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIET----IDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATtrsiLELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
322-496 |
1.90e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.78 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 322 MENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQHR-----AELDP 396
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRlmfqdARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 397 DKTVMDNLAEGkqevmVNGKPR-------HVLGyLQDfmfhpkRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTN 469
Cdd:PRK11247 95 WKKVIDNVGLG-----LKGQWRdaalqalAAVG-LAD------RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190
....*....|....*....|....*....|.
gi 695765469 470 DLDVETLELLEELVDG----YQGTVMLVSHD 496
Cdd:PRK11247 163 ALDALTRIEMQDLIESlwqqHGFTVLLVTHD 193
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
321-516 |
2.25e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.47 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG------------TKLEVAYFD 388
Cdd:PRK11264 5 EVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtarslsqQKGLIRQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 389 QHRA------ELDPDKTVMDNLAEGKqeVMVNGKPRH---VLG--YLQDFMFHPKRAMTPvRALSGGERNRLLLARLFLK 457
Cdd:PRK11264 85 QHVGfvfqnfNLFPHRTVLENIIEGP--VIVKGEPKEeatARAreLLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695765469 458 PSNLLILDEPTNDLD---VETLELLEELVDGYQGTVMLVSHDRQFVDNtVTECWIFEGEGRI 516
Cdd:PRK11264 162 RPEVILFDEPTSALDpelVGEVLNTIRQLAQEKRTMVIVTHEMSFARD-VADRAIFMDQGRI 222
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
15-232 |
2.26e-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: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 15 DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQdlvvarlqqdppRNVTG-TVYDFVAEGIAe 93
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG------------EDITGlPPHRIARLGIG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 94 qaaylkgyhdvsqLVmtdPSDKNLneLARL--QEQLDnLGLWQLDSR--INEVLEQ-LNLDPN-AEL-----SSLSGGWL 162
Cdd:COG0410 82 -------------YV---PEGRRI--FPSLtvEENLL-LGAYARRDRaeVRADLERvYELFPRlKERrrqraGTLSGGEQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 163 RKAALGRALVSGPRVLLLDEPTNHL------DI-ETIDWL--EGFlktfkgTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG0410 143 QMLAIGRALMSRPKLLLLDEPSLGLapliveEIfEIIRRLnrEGV------TILLVEQNARFALEIADRAYVLERGRIV 215
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-266 |
2.27e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 67.42 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLV----------VARLQQDPprnVTGTVYDF 86
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlIDGKDVTklpeykrakyIGRVFQDP---MMGTAPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 87 -VAEGIAeqAAYLKGyhdvsqlvmtdpSDKNL------NELARLQEQLDNLGLwQLDSRInevleqlnldpNAELSSLSG 159
Cdd:COG1101 98 tIEENLA--LAYRRG------------KRRGLrrgltkKRRELFRELLATLGL-GLENRL-----------DTKVGLLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 160 GWlRKA-ALGRALVSGPRVLLLDEPTNHLDIET----IDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVty 234
Cdd:COG1101 152 GQ-RQAlSLLMATLTKPKLLLLDEHTAALDPKTaalvLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII-- 228
|
250 260 270
....*....|....*....|....*....|....
gi 695765469 235 pgnYDqylLDKEE--ALRVEELQnAEFDRKLAQE 266
Cdd:COG1101 229 ---LD---VSGEEkkKLTVEDLL-ELFEEIRGEE 255
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-232 |
2.43e-12 |
|
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: 66.97 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIiyeqdlvvarlqqdpprnvtgTVYDFV----AE 89
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILS---GLlqpTSGEV---------------------RVAGLVpwkrRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 90 GIAEQAAYLKGYHdvSQLVMTDPSDKNLNELARLQeqldNLGLWQLDSRINEVLEQLNLDP--NAELSSLSGGWLRKAAL 167
Cdd:cd03267 91 KFLRRIGVVFGQK--TQLWWDLPVIDSFYLLAAIY----DLPPARFKKRLDELSELLDLEEllDTPVRQLSLGQRMRAEI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 168 GRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTF----KGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
329-472 |
3.24e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 67.03 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 329 VDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKlEVAYFDQH-RAEL------DP----- 396
Cdd:COG1101 16 VNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK-DVTKLPEYkRAKYigrvfqDPmmgta 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 397 -DKTVMDNL--AEGKqevmvnGKPRH----VLGYLQDFmFH----------PKRAMTPVRALSGGERNRLLLARLFLKPS 459
Cdd:COG1101 95 pSMTIEENLalAYRR------GKRRGlrrgLTKKRREL-FRellatlglglENRLDTKVGLLSGGQRQALSLLMATLTKP 167
|
170
....*....|...
gi 695765469 460 NLLILDEPTNDLD 472
Cdd:COG1101 168 KLLLLDEHTAALD 180
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
14-234 |
3.65e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.14 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 14 SDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqglddGRIIYEQDLVVARLQQDPPRNVTgTVYDFVaeGIAE 93
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFN-------GILKPTSGSVLIRGEPITKENIR-EVRKFV--GLVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 94 QAAYLKGYH-DVSQLVMTDPSDKNLNELA---RLQEQLDNLGLWQLDSRInevleqlnldPNaelsSLSGGWLRKAALGR 169
Cdd:PRK13652 85 QNPDDQIFSpTVEQDIAFGPINLGLDEETvahRVSSALHMLGLEELRDRV----------PH----HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 170 ALVSGPRVLLLDEPTNHLD----IETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVTY 234
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDpqgvKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-473 |
3.79e-12 |
|
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: 69.08 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 3 LISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN--REQGLDDGRIIYEQDLVVARLQQDPPRnvt 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSgvYPHGTWDGEIYWSGSPLKASNIRDTER--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 81 gtvydfvaegiaeqaaylKGYHDVSQLVMTDPSDKNLNELARLQEQLDNLGLWQLDS---RINEVLEQLNLD--PNA-EL 154
Cdd:TIGR02633 78 ------------------AGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAmylRAKNLLRELQLDadNVTrPV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 155 SSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:TIGR02633 140 GDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRDGQH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 232 VTypgnydqylldkeealrVEELQNAEFDRKLAQeevwirqgIKARRTRNegrvralkamrrergerrevmgsakMQVEE 311
Cdd:TIGR02633 220 VA-----------------TKDMSTMSEDDIITM--------MVGREITS-------------------------LYPHE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 312 AARSGKIVFEMENVN-YQVDGKVL--IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLG---------------QLKADS 373
Cdd:TIGR02633 250 PHEIGDVILEARNLTcWDVINPHRkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaypgkfegnvfingkPVDIRN 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 374 GRIHVGTKLEVAYFDQHRAELDPDKTVMDNL---------------AEGKQEVMVNGKPRhvlgyLQDFMFHPkraMTPV 438
Cdd:TIGR02633 330 PAQAIRAGIAMVPEDRKRHGIVPILGVGKNItlsvlksfcfkmridAAAELQIIGSAIQR-----LKVKTASP---FLPI 401
|
490 500 510
....*....|....*....|....*....|....*
gi 695765469 439 RALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
332-473 |
4.15e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.58 E-value: 4.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 332 KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQHRAE---LDPDKTVMdnlAEG- 407
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARrlaLLPQHHLT---PEGi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 408 -KQEVMVNGKPRHV--LGYL-QDFMFHPKRAMT----------PVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK11231 92 tVRELVAYGRSPWLslWGRLsAEDNARVNQAMEqtrinhladrRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
315-472 |
4.27e-12 |
|
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: 69.01 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 315 SGKIVFEmeNVNYQVDG--KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRI---------------- 376
Cdd:COG4618 328 KGRLSVE--NLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdreelg 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 377 -HVGtklevaYFDQH-------------R-AELDPDKTVMDNLAEGKQEvMVNGKPrhvLGYlqDfmfhpkramTPV--- 438
Cdd:COG4618 406 rHIG------YLPQDvelfdgtiaeniaRfGDADPEKVVAAAKLAGVHE-MILRLP---DGY--D---------TRIgeg 464
|
170 180 190
....*....|....*....|....*....|....*.
gi 695765469 439 -RALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLD 472
Cdd:COG4618 465 gARLSGGQRQRIGLARaLYGDPR-LVVLDEPNSNLD 499
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
17-231 |
4.38e-12 |
|
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: 64.93 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreqglddgriiyeqdlvvARLQQDpprnVTGTVYdfvAEGIAEQAA 96
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLI-------------------LGLLRP----TSGRVR---LDGADISQW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 97 YLKGYHDVSQLVMTDpsdknlnelarlqeqlDNLglwqLDSRINEvleqlNLdpnaelssLSGGWLRKAALGRALVSGPR 176
Cdd:cd03246 70 DPNELGDHVGYLPQD----------------DEL----FSGSIAE-----NI--------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695765469 177 VLLLDEPTNHLDIETIDWLE---GFLKTFKGTIIFISHDRSFIRnMATRIVDLDRGKL 231
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNqaiAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-232 |
5.07e-12 |
|
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: 68.56 E-value: 5.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMK-ILnreqGLDD--GRIIYE-QDLVV----------ARLQ---QDP-----P 76
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLaLL----RLIPseGEIRFDgQDLDGlsrralrplrRRMQvvfQDPfgslsP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 77 RNvtgTVYDFVAEGIAeqaaylkgYHDVSqlvmtdpsdknLNELARLQeqldnlglwqldsRINEVLEQLNLDPNA---- 152
Cdd:COG4172 378 RM---TVGQIIAEGLR--------VHGPG-----------LSAAERRA-------------RVAEALEEVGLDPAArhry 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 153 --ELSslsGGWLRKAALGRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDL 226
Cdd:COG4172 423 phEFS---GGQRQRIAIARALILEPKLLVLDEPTSALDVsvqaQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVM 499
|
....*.
gi 695765469 227 DRGKLV 232
Cdd:COG4172 500 KDGKVV 505
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
330-472 |
6.04e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 68.68 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 330 DGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQ----------------HRAE 393
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQrpylplgtlreallypATAE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 LDPDKTVMDNLAEgkqevmVNgkprhvLGYLQDfMFHPKRAMTpvRALSGGERNRLLLARLFL-KPSnLLILDEPTNDLD 472
Cdd:COG4178 454 AFSDAELREALEA------VG------LGHLAE-RLDEEADWD--QVLSLGEQQRLAFARLLLhKPD-WLFLDEATSALD 517
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-277 |
6.48e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 66.67 E-value: 6.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYEQdlvvARLQQDPPRNVtgtvydfva 88
Cdd:COG4152 10 RFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIIL---GIlapDSGEVLWDG----EPLDPEDRRRI--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 89 eG-------------IAEQAAYlkgyhdvsqlvmtdpsdknlneLARLQeqldNLGLWQLDSRINEVLEQLNLDP--NAE 153
Cdd:COG4152 74 -GylpeerglypkmkVGEQLVY----------------------LARLK----GLSKAEAKRRADEWLERLGLGDraNKK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 154 LSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFK--G-TIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:COG4152 127 VEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAakGtTVIFSSHQMELVEELCDRIVIINKGR 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 695765469 231 LVTYpGN----YDQYlldKEEALRVEELQNAEFDRKLAQEEVWIRQGIKAR 277
Cdd:COG4152 207 KVLS-GSvdeiRRQF---GRNTLRLEADGDAGWLRALPGVTVVEEDGDGAE 253
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
21-250 |
7.66e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 65.55 E-value: 7.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLV--------VARLQQDppRNVTG--TVYDFVAE 89
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgQDLTalppaerpVSMLFQE--NNLFPhlTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 90 GIaeqaaylkgyhdvsqlvmtDPSDKnLNELARlqeqldnlglwqldSRINEVLEQLNLdpnAEL-----SSLSGGWLRK 164
Cdd:COG3840 95 GL-------------------RPGLK-LTAEQR--------------AQVEQALERVGL---AGLldrlpGQLSGGQRQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 165 AALGRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKlVTYPGNYDQ 240
Cdd:COG3840 138 VALARCLVRKRPILLLDEPFSALDPalrqEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGR-IAADGPTAA 216
|
250
....*....|..
gi 695765469 241 yLLDKE--EALR 250
Cdd:COG3840 217 -LLDGEppPALA 227
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-245 |
7.88e-12 |
|
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: 65.33 E-value: 7.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDlvVARLQQDPPRNVTGTV-YDFVA--EGIA 92
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIlIDGQD--IREVTLDSLRRAIGVVpQDTVLfnDTIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 93 EQAAYLKgyhdvsqlvmTDPSDKNLNELARLqeqldnlglwqldSRINEVLEQLNLDPNAELSS----LSGGWLRKAALG 168
Cdd:cd03253 93 YNIRYGR----------PDATDEEVIEAAKA-------------AQIHDKIMRFPDGYDTIVGErglkLSGGEKQRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 169 RALVSGPRVLLLDEPTNHLDIET---IdwLEGFLKTFKG-TIIFISHDRSFIRNmATRIVDLDRGKLVTyPGNYDQYLLD 244
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTereI--QAALRDVSKGrTTIVIAHRLSTIVN-ADKIIVLKDGRIVE-RGTHEELLAK 225
|
.
gi 695765469 245 K 245
Cdd:cd03253 226 G 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
311-498 |
7.94e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 65.84 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 311 EAARSGKIVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKleVAYFDQH 390
Cdd:PRK14246 2 EAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGK--VLYFGKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 391 RAELD------------------PDKTVMDNLA--------EGKQEV--MVNGKPRHVlGYLQDFMfhpKRAMTPVRALS 442
Cdd:PRK14246 80 IFQIDaiklrkevgmvfqqpnpfPHLSIYDNIAyplkshgiKEKREIkkIVEECLRKV-GLWKEVY---DRLNSPASQLS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 443 GGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLELLEELVDGYQG--TVMLVSHDRQ 498
Cdd:PRK14246 156 GGQQQRLTIARaLALKPK-VLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQ 213
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
321-472 |
8.02e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 65.88 E-value: 8.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV------GTKLEVAYFDQHRAEL 394
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpveGPGAERGVVFQNEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 dPDKTVMDNLAEGKQEVMVNGKPRHVLGY----LQDFMFHPKRamtPVRALSGGERNRLLLARLFLKPSNLLILDEPTND 470
Cdd:PRK11248 83 -PWRNVQDNVAFGLQLAGVEKMQRLEIAHqmlkKVGLEGAEKR---YIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
..
gi 695765469 471 LD 472
Cdd:PRK11248 159 LD 160
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
316-473 |
8.27e-12 |
|
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: 64.38 E-value: 8.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 316 GKIVFEMENVnyQVDGKVliKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG------------TKLE 383
Cdd:cd03215 1 GEPVLEVRGL--SVKGAV--RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgkpvtrrsprdaIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 384 VAYF--DQHRAELDPDKTVMDNLAegkqevmvngkprhvLGYLqdfmfhpkramtpvraLSGGERNRLLLARLFLKPSNL 461
Cdd:cd03215 77 IAYVpeDRKREGLVLDLSVAENIA---------------LSSL----------------LSGGNQQKVVLARWLARDPRV 125
|
170
....*....|..
gi 695765469 462 LILDEPTNDLDV 473
Cdd:cd03215 126 LILDEPTRGVDV 137
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
324-497 |
9.95e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.59 E-value: 9.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 324 NVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV---GTKLEVAYFDQ------HRAEL 394
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFerqSIKKDLCTYQKqlcfvgHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 DPDKTVMDNL---------AEGKQEVMVNGKprhvLGYLQDFmfhpkramtPVRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:PRK13540 86 NPYLTLRENClydihfspgAVGITELCRLFS----LEHLIDY---------PCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|....*
gi 695765469 466 EPTNDLDVETLELLEELVDGYQ---GTVMLVSHDR 497
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEHRakgGAVLLTSHQD 187
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
333-473 |
1.30e-11 |
|
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: 64.70 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 333 VLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIhvgtklEVAYFDQHRAELD--------PDK------ 398
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA------TVDGFDVVKEPAEarrrlgfvSDStglydr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 399 -TVMDNLA-----EGKQEVMVNGKPRHVLGYLQDFMFHPKRamtpVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03266 93 lTARENLEyfaglYGLKGDELTARLEELADRLGMEELLDRR----VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
.
gi 695765469 473 V 473
Cdd:cd03266 169 V 169
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
338-495 |
1.39e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.60 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 338 FSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRI------HVGT---KLEVAYFDQHRaELDPDKTVMDNLAEGK 408
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdHTTTppsRRPVSMLFQEN-NLFSHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 409 QE-VMVNGKPRHVLGY------LQDFMfhpkrAMTPvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEE 481
Cdd:PRK10771 97 NPgLKLNAAQREKLHAiarqmgIEDLL-----ARLP-GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170
....*....|....*...
gi 695765469 482 LVDGY----QGTVMLVSH 495
Cdd:PRK10771 171 LVSQVcqerQLTLLMVSH 188
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-233 |
1.66e-11 |
|
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: 64.38 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 2 SLISMHGAWLSFSDS--PL--LDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGLD---DGRI-IYEQDLvvARLQQ 73
Cdd:COG4181 7 PIIELRGLTKTVGTGagELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLL---AGLDrptSGTVrLAGQDL--FALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 74 DP-----PRNVtgtvydfvaeGIAEQAaylkgyhdvSQL---------VMTdP----SDKNLNELARlqEQLDNLGLwql 135
Cdd:COG4181 82 DArarlrARHV----------GFVFQS---------FQLlptltalenVML-PlelaGRRDARARAR--ALLERVGL--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 136 DSRINEVLEQLnldpnaelsslSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIET----IDWLEGFLKTFKGTIIFISH 211
Cdd:COG4181 137 GHRLDHYPAQL-----------SGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRERGTTLVLVTH 205
|
250 260
....*....|....*....|..
gi 695765469 212 DRSFIRnMATRIVDLDRGKLVT 233
Cdd:COG4181 206 DPALAA-RCDRVLRLRAGRLVE 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
318-472 |
2.02e-11 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 64.43 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 318 IVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLEVAYFDQHRAELDP 396
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 397 --------DKTVMDNLAEGKQevmvnGKPRHVLGYL------QDFMFH-PKRAMTPV----RALSGGERNRLLLARLFLK 457
Cdd:cd03252 81 vlqenvlfNRSIRDNIALADP-----GMSMERVIEAaklagaHDFISElPEGYDTIVgeqgAGLSGGQRQRIAIARALIH 155
|
170
....*....|....*
gi 695765469 458 PSNLLILDEPTNDLD 472
Cdd:cd03252 156 NPRILIFDEATSALD 170
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-231 |
2.03e-11 |
|
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: 64.03 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 14 SDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRII--------YEQDL---VVARLQQDPPRnVTGT 82
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgkpisqYEHKYlhsKVSLVGQEPVL-FARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 83 VYDFVAEGIAEqaaylKGYHDVSQLVMTDPSDKNLNELArlqeqldnLGLWQldsrinEVLEQLNLdpnaelssLSGGWL 162
Cdd:cd03248 104 LQDNIAYGLQS-----CSFECVKEAAQKAHAHSFISELA--------SGYDT------EVGEKGSQ--------LSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765469 163 RKAALGRALVSGPRVLLLDEPTNHLDIET--------IDWLEgflktfKGTIIFISHDRSFIRNmATRIVDLDRGKL 231
Cdd:cd03248 157 QRVAIARALIRNPQVLILDEATSALDAESeqqvqqalYDWPE------RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-227 |
2.85e-11 |
|
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: 62.17 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 14 SDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYeqdlvvarlqqdPPRNvtgTVYdFVAeg 90
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALA---GLwpwGSGRIGM------------PEGE---DLL-FLP-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 91 iaeQAAYLKgyhdvsqlvmtdpsdknlneLARLQEQLdnLGLWQldsrinevleqlnldpnaelSSLSGGWLRKAALGRA 170
Cdd:cd03223 71 ---QRPYLP--------------------LGTLREQL--IYPWD--------------------DVLSGGEQQRLAFARL 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695765469 171 LVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKGTIIFISHdRSFIRNMATRIVDLD 227
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
321-513 |
2.90e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 66.36 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLG--QLKADSGRI--HVG----------------- 379
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyHVAlcekcgyverpskvgep 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 380 --------TKLEVAYFD-----------------QHRAELDPDKTVMDNLAEGKQEVMVNGKprHVLGYLQDF--MFHPK 432
Cdd:TIGR03269 82 cpvcggtlEPEEVDFWNlsdklrrrirkriaimlQRTFALYGDDTVLDNVLEALEEIGYEGK--EAVGRAVDLieMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 433 RAMTPV-RALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETL----ELLEELVDGYQGTVMLVSHDRQFVDNTVTEC 507
Cdd:TIGR03269 160 HRITHIaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
....*..
gi 695765469 508 -WIFEGE 513
Cdd:TIGR03269 240 iWLENGE 246
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-211 |
3.09e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.11 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 3 LISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN--REQGLDDGRIIYEQDLVVARlqqdpprnvt 80
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSgvYPHGTYEGEIIFEGEELQAS---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 81 gTVYDFVAEGIA--EQAAYLkgyhdVSQLVMTDpsdkNL---NELARLQEQLDNlglwQLDSRINEVLEQLNLD--PNAE 153
Cdd:PRK13549 75 -NIRDTERAGIAiiHQELAL-----VKELSVLE----NIflgNEITPGGIMDYD----AMYLRAQKLLAQLKLDinPATP 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765469 154 LSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISH 211
Cdd:PRK13549 141 VGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAhgiACIYISH 201
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-473 |
3.18e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.23 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 3 LISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlvvarlqqdpprNVTGT 82
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL-----------------EIGGN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 83 VYDFVAEGIAEQ-AAYLkgyhdVSQLVMTDPsdkNL----NELARLQEQLDNLglwqldSRINEVLEQLN--LDPNAELS 155
Cdd:PRK15439 74 PCARLTPAKAHQlGIYL-----VPQEPLLFP---NLsvkeNILFGLPKRQASM------QKMKQLLAALGcqLDLDSSAG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 156 SLSGGWLRKAALGRALVSGPRVLLLDEPTNHLD-IETiDWLEGFLKTF--KGT-IIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK15439 140 SLEVADRQIVEILRGLMRDSRILILDEPTASLTpAET-ERLFSRIRELlaQGVgIVFISHKLPEIRQLADRISVMRDGTI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 232 VtYPGNYDQYLLDKEEALRVEELQNAEFDRKlaqEEVWIRQGIKARRTRNEGRVralkamrrergerrevmgsakMQVEE 311
Cdd:PRK15439 219 A-LSGKTADLSTDDIIQAITPAAREKSLSAS---QKLWLELPGNRRQQAAGAPV---------------------LTVED 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 312 AARSGkivfemenvnyqvdgkvlIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIhvgtklevaYFDQHr 391
Cdd:PRK15439 274 LTGEG------------------FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI---------MLNGK- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 392 aELDPDKTVmDNLAEGkqeVMVNGKPRHVLG-YL---------------QDFMFHPKR------------------AMTP 437
Cdd:PRK15439 326 -EINALSTA-QRLARG---LVYLPEDRQSSGlYLdaplawnvcalthnrRGFWIKPARenavleryrralnikfnhAEQA 400
|
490 500 510
....*....|....*....|....*....|....*.
gi 695765469 438 VRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK15439 401 ARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
319-472 |
3.27e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 64.27 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 319 VFEMENVNYQVDG--KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLEVAYFDQHRAEL- 394
Cdd:PRK13635 5 IIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVgGMVLSEETVWDVRRQVg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 ----DPDK-----TVMDNLAEGKQEvmvNGKPR-----------HVLGyLQDFMFH-PKRamtpvraLSGGERNRLLLAR 453
Cdd:PRK13635 85 mvfqNPDNqfvgaTVQDDVAFGLEN---IGVPReemvervdqalRQVG-MEDFLNRePHR-------LSGGQKQRVAIAG 153
|
170 180
....*....|....*....|
gi 695765469 454 -LFLKPSnLLILDEPTNDLD 472
Cdd:PRK13635 154 vLALQPD-IIILDEATSMLD 172
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-232 |
3.54e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 63.71 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 13 FSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDD-----------GRIIYEQDL-------VVARLQQD 74
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearvegevrlfGRNIYSPDVdpievrrEVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 75 PPRNVTGTVYDFVAEGIaeqaaylkgyhdvsqlvmtdpsdkNLNELARLQEQLDNLGLWQLDSRI--NEVLEQLNLDPna 152
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGV------------------------KLNGLVKSKKELDERVEWALKKAAlwDEVKDRLNDYP-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 153 elSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG--TIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:PRK14267 148 --SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTHSPAQAARVSDYVAFLYLGK 225
|
..
gi 695765469 231 LV 232
Cdd:PRK14267 226 LI 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
349-472 |
3.93e-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: 65.13 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 349 ALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GT--------------KLEVAYFDQhRAELDPDKTVMDNLAEGKQEVMV 413
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLnGRtlfdsrkgiflppeKRRIGYVFQ-EARLFPHLSVRGNLRYGMKRARP 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765469 414 ---NGKPRHV-----LGYLQDfmfhpkramTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR02142 106 serRISFERViellgIGHLLG---------RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
337-495 |
4.08e-11 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 62.90 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 337 DFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLEVA------YFDQHraELDPDKTVMDNLAE 406
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvdvTAAPPAdrpvsmLFQEN--NLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 407 G---------KQEVMVNGKPRHVlgYLQDFMfhpKRAmtpVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLE 477
Cdd:cd03298 94 GlspglkltaEDRQAIEVALARV--GLAGLE---KRL---PGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180
....*....|....*....|..
gi 695765469 478 LLEELVDGY----QGTVMLVSH 495
Cdd:cd03298 166 EMLDLVLDLhaetKMTVLMVTH 187
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
321-495 |
4.36e-11 |
|
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: 62.51 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRI---------HVGTKLEVAYFDQHR 391
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVllnggpldfQRDSIARGLLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 392 AELDPDKTVMDNL----AEGKQEVMVNGKPRHVLGYLQDfmfhpkramTPVRALSGGERNRLLLARLFLKPSNLLILDEP 467
Cdd:cd03231 82 PGIKTTLSVLENLrfwhADHSDEQVEEALARVGLNGFED---------RPVAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190
....*....|....*....|....*....|.
gi 695765469 468 TNDLDVETLELLEELVDGYQ---GTVMLVSH 495
Cdd:cd03231 153 TTALDKAGVARFAEAMAGHCargGMVVLTTH 183
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
14-212 |
4.85e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 63.62 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 14 SDSPL-LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQDPPRNVtGTVY-----DFV 87
Cdd:PRK13648 19 SDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI-GIVFqnpdnQFV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 88 AEGIAEQAAYLKGYHDVsqlvmtdPSDKnlnelarlqeqldnlglwqLDSRINEVLEQLNL--DPNAELSSLSGGWLRKA 165
Cdd:PRK13648 98 GSIVKYDVAFGLENHAV-------PYDE-------------------MHRRVSEALKQVDMleRADYEPNALSGGQKQRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695765469 166 ALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG----TIIFISHD 212
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehniTIISITHD 202
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
319-472 |
5.04e-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: 62.26 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 319 VFEMENVNYQVDG----KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMlgqlkadSGRIHVGTklevayfdqhrael 394
Cdd:cd03232 3 VLTWKNLNYTVPVkggkRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVL-------AGRKTAGV-------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 dpdktvmdnlAEGkqEVMVNGKP-----RHVLGYLQDFMFHPK--------RAMTPVRALSGGERNRLLLA-RLFLKPSn 460
Cdd:cd03232 62 ----------ITG--EILINGRPldknfQRSTGYVEQQDVHSPnltvrealRFSALLRGLSVEQRKRLTIGvELAAKPS- 128
|
170
....*....|..
gi 695765469 461 LLILDEPTNDLD 472
Cdd:cd03232 129 ILFLDEPTSGLD 140
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
319-467 |
5.15e-11 |
|
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: 63.06 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 319 VFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRI------------HVGTKLEVAY 386
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKIlidgqdithlpmHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 387 FDQHrAELDPDKTVMDNLA---EGKQEVMVNGKPRHVLGYLQDF-MFHPKRAmtPVRALSGGERNRLLLARLFLKPSNLL 462
Cdd:TIGR04406 81 LPQE-ASIFRKLTVEENIMavlEIRKDLDRAEREERLEALLEEFqISHLRDN--KAMSLSGGERRRVEIARALATNPKFI 157
|
....*
gi 695765469 463 ILDEP 467
Cdd:TIGR04406 158 LLDEP 162
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-232 |
5.17e-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: 5.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 24 LHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLVVArlqqDPPRNVTGTVYdfvaegiaeQAAYLKGYH 102
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlINGVDVTAA----PPADRPVSMLF---------QENNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 103 DVSQLV--MTDPSDKnLNELAR--LQEQLDNLGLWQLDSRINEvleqlnldpnaelsSLSGGWLRKAALGRALVSGPRVL 178
Cdd:cd03298 86 TVEQNVglGLSPGLK-LTAEDRqaIEVALARVGLAGLEKRLPG--------------ELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695765469 179 LLDEPTNHLD----IETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03298 151 LLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
17-232 |
6.46e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 63.25 E-value: 6.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDL----------VVARLQQDPPRNVTGTVYD 85
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrLNGRPLadwspaelarRRAVLPQHSSLSFPFTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 86 FVAEGIaeqAAYLKGYHDVSQLVmtdpsdknlnelarlQEQLDNLGLWQLDSRinevleqlnldpnaELSSLSGGWLRKA 165
Cdd:PRK13548 96 VVAMGR---APHGLSRAEDDALV---------------AAALAQVDLAHLAGR--------------DYPQLSGGEQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 166 ALGRALV------SGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDrsfiRNMAT----RIVDLDRGKL 231
Cdd:PRK13548 144 QLARVLAqlwepdGPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD----LNLAAryadRIVLLHQGRL 219
|
.
gi 695765469 232 V 232
Cdd:PRK13548 220 V 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-257 |
6.68e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 65.12 E-value: 6.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFS---DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLV-----------VARLQQDPP 76
Cdd:PRK10790 346 VSFAyrdDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLsslshsvlrqgVAMVQQDPV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 77 RnVTGTVYDFVAEG--IAEQAAYlkgyhDVSQLVmtdpsdkNLNELARlqeqldnlglwQLDSRINEVL-EQLNldpnae 153
Cdd:PRK10790 426 V-LADTFLANVTLGrdISEEQVW-----QALETV-------QLAELAR-----------SLPDGLYTPLgEQGN------ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 154 lsSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTF--KGTIIFISHDRSFIRNmATRIVDLDRGKL 231
Cdd:PRK10790 476 --NLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHRLSTIVE-ADTILVLHRGQA 552
|
250 260
....*....|....*....|....*.
gi 695765469 232 VTYpGNYDQYLLDKEEALRVEELQNA 257
Cdd:PRK10790 553 VEQ-GTHQQLLAAQGRYWQMYQLQLA 577
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-234 |
6.70e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 63.13 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNReqgLDD--------GRIIYE--------QDLVVARLQ-- 72
Cdd:COG1117 19 VYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNR---MNDlipgarveGEILLDgediydpdVDVVELRRRvg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 73 ---QDP---PRnvtgTVYDFVAEGIAeqaayLKGYHDvsqlvmtdpsDKNLNELARlqEQLDNLGLWqldsriNEVLEQL 146
Cdd:COG1117 96 mvfQKPnpfPK----SIYDNVAYGLR-----LHGIKS----------KSELDEIVE--ESLRKAALW------DEVKDRL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 147 NLdpNAelSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLD-IET--IdwlEGFLKTFKG--TIIFISHdrsfirNM-- 219
Cdd:COG1117 149 KK--SA--LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTakI---EELILELKKdyTIVIVTH------NMqq 215
|
250
....*....|....*....
gi 695765469 220 ATRIVD----LDRGKLVTY 234
Cdd:COG1117 216 AARVSDytafFYLGELVEF 234
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-260 |
7.04e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.09 E-value: 7.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFS----DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL----NREQG--LDDGRIIYEQDLVVAR-----LQQDP 75
Cdd:PRK13632 13 VSFSypnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILtgllKPQSGeiKIDGITISKENLKEIRkkigiIFQNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 76 PRNVTG-TVYDFVAEGIAEQaaylkgyhdvsqlvMTDPSDknlnelarlqeqldnlglwqLDSRINEVLEQLNLDP--NA 152
Cdd:PRK13632 93 DNQFIGaTVEDDIAFGLENK--------------KVPPKK--------------------MKDIIDDLAKKVGMEDylDK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 153 ELSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLD-------IETIDWLEgflKTFKGTIIFISHDRSFIRNmATRIVD 225
Cdd:PRK13632 139 EPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgkreiKKIMVDLR---KTRKKTLISITHDMDEAIL-ADKVIV 214
|
250 260 270
....*....|....*....|....*....|....*
gi 695765469 226 LDRGKLVtYPGNYDQYLLDKeealrvEELQNAEFD 260
Cdd:PRK13632 215 FSEGKLI-AQGKPKEILNNK------EILEKAKID 242
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
331-467 |
7.51e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 62.74 E-value: 7.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 331 GKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIhvgtklevaYFDQH---------RAEL------- 394
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI---------FLDGEdithlpmhkRARLgigylpq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 DP----DKTVMDNLAEGKQEVMVNGKPRH--VLGYLQDFMFHPKRAmTPVRALSGGERNRLLLAR-LFLKPSNLLiLDEP 467
Cdd:COG1137 86 EAsifrKLTVEDNILAVLELRKLSKKEREerLEELLEEFGITHLRK-SKAYSLSGGERRRVEIARaLATNPKFIL-LDEP 163
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
318-472 |
7.62e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.28 E-value: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 318 IVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKAdsgrihvgtKLEVAYFDQHRAELDPD 397
Cdd:COG2401 29 IVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKG---------TPVAGCVDVPDNQFGRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 398 KTVMDNLAEgkqevmvNGKPRHVLGYLQD------FMFhpkraMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
Cdd:COG2401 100 ASLIDAIGR-------KGDFKDAVELLNAvglsdaVLW-----LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
.
gi 695765469 472 D 472
Cdd:COG2401 168 D 168
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-230 |
7.83e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.20 E-value: 7.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 1 MSLISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDlvVARLqqdPP--R 77
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgQD--ITHV---PAenR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 78 NVTG-----------TVYDFVAEGIAEQAAylkGYHDVSQLVMtdpsdknlnelarlqeqlDNLGLWQLDSRINEVLEQL 146
Cdd:PRK09452 87 HVNTvfqsyalfphmTVFENVAFGLRMQKT---PAAEITPRVM------------------EALRMVQLEEFAQRKPHQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 147 nldpnaelsslSGGWLRKAALGRALVSGPRVLLLDEPTNHLD--------IEtidwLEGFLKTFKGTIIFISHDRSFIRN 218
Cdd:PRK09452 146 -----------SGGQQQRVAIARAVVNKPKVLLLDESLSALDyklrkqmqNE----LKALQRKLGITFVFVTHDQEEALT 210
|
250
....*....|..
gi 695765469 219 MATRIVDLDRGK 230
Cdd:PRK09452 211 MSDRIVVMRDGR 222
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
11-233 |
8.07e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 62.72 E-value: 8.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLV----------VARLQQDPPrnv 79
Cdd:PRK11231 10 VGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVfLGDKPISmlssrqlarrLALLPQHHL--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 80 tgtvydfVAEGIAeqaaylkgyhdVSQLVMTDPSdKNLNELARLQEQlDNlglwqldSRINEVLEQLNLDPNAE--LSSL 157
Cdd:PRK11231 87 -------TPEGIT-----------VRELVAYGRS-PWLSLWGRLSAE-DN-------ARVNQAMEQTRINHLADrrLTDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 158 SGGWLRKAALGRALVSGPRVLLLDEPTNHLDI----ETIDwLEGFLKTFKGTIIFISHDrsfiRNMATRIVD----LDRG 229
Cdd:PRK11231 140 SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDInhqvELMR-LMRELNTQGKTVVTVLHD----LNQASRYCDhlvvLANG 214
|
....
gi 695765469 230 KLVT 233
Cdd:PRK11231 215 HVMA 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
31-225 |
9.99e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.88 E-value: 9.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 31 RVC-LVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLV-----------VARLQQDPPRNVTGTVYDFVAEGIAEQAAYL 98
Cdd:PRK10575 38 KVTgLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsskafarkVAYLPQQLPAAEGMTVRELVAIGRYPWHGAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 99 KGYhdvsqlvmtdpsdkNLNELARLQEQLDNLGLWQLDSRInevleqlnldpnaeLSSLSGGWLRKAALGRALVSGPRVL 178
Cdd:PRK10575 118 GRF--------------GAADREKVEEAISLVGLKPLAHRL--------------VDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695765469 179 LLDEPTNHLDI-ETIDWLEGF--LKTFKG-TIIFISHDrsfiRNMATRIVD 225
Cdd:PRK10575 170 LLDEPTSALDIaHQVDVLALVhrLSQERGlTVIAVLHD----INMAARYCD 216
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-241 |
1.05e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.88 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 2 SLISMHGAWLSFSDSPLL-DNAELHIEDNERVCLVGRNGAGKSTLMKilnreqglddgriiyeqdLVVARLQQdpprnVT 80
Cdd:PLN03073 507 PIISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILK------------------LISGELQP-----SS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 81 GTVYDFVAEGIAeqaayLKGYHDVSQLvmtDPSDKNLNELAR---------LQEQLDNLGlwqldsrineVLEQLNLDPn 151
Cdd:PLN03073 564 GTVFRSAKVRMA-----VFSQHHVDGL---DLSSNPLLYMMRcfpgvpeqkLRAHLGSFG----------VTGNLALQP- 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 152 aeLSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PLN03073 625 --MYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
250
....*....|
gi 695765469 232 VTYPGNYDQY 241
Cdd:PLN03073 703 TPFHGTFHDY 712
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-240 |
1.17e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 64.60 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFS---DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE----QDLVVARLqqdppRNVTGTVY 84
Cdd:PRK13657 341 SFSydnSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDgtdiRTVTRASL-----RRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 85 dfvaegiaeQAAYL--KGYHDVSQLVMTDPSDKNLNELARLQEQLDNL--GLWQLDSRINEvleqlnldpnaELSSLSGG 160
Cdd:PRK13657 416 ---------QDAGLfnRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIerKPDGYDTVVGE-----------RGRQLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 161 WLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTF-KG-TIIFISHDRSFIRNmATRIVDLDRGKLVTyPGNY 238
Cdd:PRK13657 476 ERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELmKGrTTFIIAHRLSTVRN-ADRILVFDNGRVVE-SGSF 553
|
..
gi 695765469 239 DQ 240
Cdd:PRK13657 554 DE 555
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
321-473 |
1.40e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 61.00 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLG--QLKADSGRIhvgtklevaYFD-QHRAELDPD 397
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEI---------LFKgEDITDLPPE 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 398 KTVMDNLAEGKQE-VMVNG-KPRHVLGYLQDfmfhpkramtpvrALSGGERNRL-LLARLFLKPSnLLILDEPTNDLDV 473
Cdd:cd03217 73 ERARLGIFLAFQYpPEIPGvKNADFLRYVNE-------------GFSGGEKKRNeILQLLLLEPD-LAILDEPDSGLDI 137
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-232 |
1.44e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.43 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIY---------EQDLVVARLQ-----QDPPRNVTGTVY 84
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsghditrlkNREVPFLRRQigmifQDHHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 85 DFVAegiaeqaaylkgyhdvSQLVMTDPSDKNLNElaRLQEQLDNLGLwqLDSRINEVLEqlnldpnaelssLSGGWLRK 164
Cdd:PRK10908 98 DNVA----------------IPLIIAGASGDDIRR--RVSAALDKVGL--LDKAKNFPIQ------------LSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695765469 165 AALGRALVSGPRVLLLDEPTNHLDIETIdwlEGFLKTFKG------TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK10908 146 VGIARAVVNKPAVLLADEPTGNLDDALS---EGILRLFEEfnrvgvTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
224-291 |
1.98e-10 |
|
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: 57.58 E-value: 1.98e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 224 VDLDRGKLVTYPGNYDQYLLDKEEALRVEELQNAEFDRKLAQEEVWI-RQGIKARRTR-NEGRVRALKAM 291
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIdRFRAKASKAKqAQSRIKALEKM 70
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-232 |
2.06e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 61.95 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 15 DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN----REQGLD--DGRIIYEQDLVVARLQ-----QDPPRNVTG-T 82
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNglllPEAGTItvGGMVLSEETVWDVRRQvgmvfQNPDNQFVGaT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 83 VYDFVAEGiaeqaaylkgyhdvsqlvmtdpsdknlnelarlqeqLDNLGLWQLD--SRINEVLEQLNLDPNA--ELSSLS 158
Cdd:PRK13635 99 VQDDVAFG------------------------------------LENIGVPREEmvERVDQALRQVGMEDFLnrEPHRLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 159 GGWLRKAALGRALVSGPRVLLLDEPTNHLD-------IETIDWL--EGFLktfkgTIIFISHDRSFIRNmATRIVDLDRG 229
Cdd:PRK13635 143 GGQKQRVAIAGVLALQPDIIILDEATSMLDprgrrevLETVRQLkeQKGI-----TVLSITHDLDEAAQ-ADRVIVMNKG 216
|
...
gi 695765469 230 KLV 232
Cdd:PRK13635 217 EIL 219
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
344-513 |
2.15e-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: 59.31 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 344 RGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVgtklevayfdqhraeLDPDKTVMDNLAEGKQEVMVNGKprhvlgy 423
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------IDGEDILEEVLDQLLLIIVGGKK------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 424 lqdfmfhpkramtpvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDGYQGTVMLVSHDRQFVDNT 503
Cdd:smart00382 59 ---------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTT 123
|
170
....*....|
gi 695765469 504 VTECWIFEGE 513
Cdd:smart00382 124 NDEKDLGPAL 133
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-232 |
2.39e-10 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 61.02 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 15 DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRII----YEQDLVVARL-------QQDPprnV--TG 81
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILldgvDIRDLNLRWLrsqiglvSQEP---VlfDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 82 TVYDFVAEGI-------AEQAAYLKGYHDvsqLVMTDPSdknlnelarlqeqldnlglwQLDSRINEVLeqlnldpnael 154
Cdd:cd03249 92 TIAENIRYGKpdatdeeVEEAAKKANIHD---FIMSLPD--------------------GYDTLVGERG----------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 155 SSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG--TIIFISHDRSFIRNmATRIVDLDRGKLV 232
Cdd:cd03249 138 SQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKgrTTIVIAHRLSTIRN-ADLIAVLQNGQVV 216
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
324-549 |
2.40e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 63.37 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 324 NVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIH--VGTKLEVAYFDQHRAEldpDKTVM 401
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSldPNERLGKLRQDQFAFE---EFTVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 402 D-------NLAEGKQEV--------MVNGKPRHV-------------------------LGYLQDFMFHPKRAMTPvral 441
Cdd:PRK15064 83 DtvimghtELWEVKQERdriyalpeMSEEDGMKVadlevkfaemdgytaearagelllgVGIPEEQHYGLMSEVAP---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 442 sgGERNRLLLAR-LFLKPsNLLILDEPTNDLDVETLELLEELVDGYQGTVMLVSHDRQFVDNTVTE-CWIFEGEGRIgqY 519
Cdd:PRK15064 159 --GWKLRVLLAQaLFSNP-DILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHmADLDYGELRV--Y 233
|
250 260 270
....*....|....*....|....*....|
gi 695765469 520 VGGYHDArgQQAQYLAQKQQISKKAVEAAQ 549
Cdd:PRK15064 234 PGNYDEY--MTAATQARERLLADNAKKKAQ 261
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-226 |
2.43e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.59 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLD-----DGRI------IYEQDLVVARLQQD----- 74
Cdd:PRK14258 15 FYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVeffnqnIYERRVNLNRLRRQvsmvh 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 75 -PPRNVTGTVYDFVAEGIAeqaayLKGYHDVSQLvmtdpsdKNLNELArlqeqLDNLGLWqldSRINEVLEQLNLDpnae 153
Cdd:PRK14258 95 pKPNLFPMSVYDNVAYGVK-----IVGWRPKLEI-------DDIVESA-----LKDADLW---DEIKHKIHKSALD---- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765469 154 lssLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFK----GTIIFISHDRSFIrnmaTRIVDL 226
Cdd:PRK14258 151 ---LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHNLHQV----SRLSDF 220
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
329-473 |
2.44e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 62.44 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 329 VDGkVlikDFSaqIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLEVAYFDQHR-----------AE 393
Cdd:COG4608 34 VDG-V---SFD--IRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqdiTGLSGRELRPLRrrmqmvfqdpyAS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 LDPDKTVMDNLAEGkqeVMVNGkprhvlgylqdfMFHPKRAMTPVRAL------------------SGGERNRLLLAR-L 454
Cdd:COG4608 108 LNPRMTVGDIIAEP---LRIHG------------LASKAERRERVAELlelvglrpehadryphefSGGQRQRIGIARaL 172
|
170
....*....|....*....
gi 695765469 455 FLKPSnLLILDEPTNDLDV 473
Cdd:COG4608 173 ALNPK-LIVCDEPVSALDV 190
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
327-501 |
2.68e-10 |
|
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: 60.91 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 327 YQVDGKVL--IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV---GTKLEVAyfdqhRAeldPDKTVM 401
Cdd:COG4778 17 HLQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWVDLA-----QA---SPREIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 402 DNLaegkqevmvngkpRHVLGYLQDFMfhpkRAMTPVRAL---------------------------------------- 441
Cdd:COG4778 89 ALR-------------RRTIGYVSQFL----RVIPRVSALdvvaepllergvdreearararellarlnlperlwdlppa 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695765469 442 --SGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDGY--QGTVML-VSHDRQFVD 501
Cdd:COG4778 152 tfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkaRGTAIIgIFHDEEVRE 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-212 |
2.76e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.95 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGLDDGriiyeQDLVVARLQQDpprnvtgtVYDFVAEGIAEQAAY 97
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAIL---AGLDDG-----SSGEVSLVGQP--------LHQMDEEARAKLRAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 98 LKGYhdVSQLVMTDPSdknLNELARLQEQLDNLGLWQLDSRIN--EVLEQLNLDPNAEL--SSLSGGWLRKAALGRALVS 173
Cdd:PRK10584 89 HVGF--VFQSFMLIPT---LNALENVELPALLRGESSRQSRNGakALLEQLGLGKRLDHlpAQLSGGEQQRVALARAFNG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695765469 174 GPRVLLLDEPTNHLDIETIDWLEGFL----KTFKGTIIFISHD 212
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
321-472 |
2.86e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 62.41 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLML-------GQLK---ADSGRIHVGTKlEVAYFDQH 390
Cdd:PRK10851 4 EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAglehqtsGHIRfhgTDVSRLHARDR-KVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 391 RAeLDPDKTVMDNLAEG---------------KQEV-----MVNgkprhvLGYLQDfmFHPKRamtpvraLSGGERNRLL 450
Cdd:PRK10851 83 YA-LFRHMTVFDNIAFGltvlprrerpnaaaiKAKVtqlleMVQ------LAHLAD--RYPAQ-------LSGGQKQRVA 146
|
170 180
....*....|....*....|..
gi 695765469 451 LARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALD 168
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
321-472 |
2.91e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 62.43 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLEVAYFD-----QHR 391
Cdd:PRK11432 8 VLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgedvTHRSIQQRDicmvfQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 392 AeLDPDKTVMDNLAEG-------KQEVMVNGKPRHVLGYLQDFmfhPKRAmtpVRALSGGERNRLLLAR-LFLKPSNLLi 463
Cdd:PRK11432 88 A-LFPHMSLGENVGYGlkmlgvpKEERKQRVKEALELVDLAGF---EDRY---VDQISGGQQQRVALARaLILKPKVLL- 159
|
....*....
gi 695765469 464 LDEPTNDLD 472
Cdd:PRK11432 160 FDEPLSNLD 168
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-234 |
3.35e-10 |
|
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: 60.12 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 16 SPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLVVARLQ----------QDPPRnVTGTVY 84
Cdd:cd03369 21 PPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIeIDGIDISTIPLEdlrssltiipQDPTL-FSGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 85 dfvaegiaeqaaylkgyhdvSQLvmtDP----SDKNLNELARLQEQLDNLglwqldsrinevleqlnldpnaelsslSGG 160
Cdd:cd03369 100 --------------------SNL---DPfdeySDEEIYGALRVSEGGLNL---------------------------SQG 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 161 WLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFL-KTFKG-TIIFISHDRSFIRNMAtRIVDLDRGKLVTY 234
Cdd:cd03369 130 QRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIrEEFTNsTILTIAHRLRTIIDYD-KILVMDAGEVKEY 204
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
330-472 |
3.66e-10 |
|
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: 59.97 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 330 DGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKAD---SGRIHVGTKLEVAYFDQHRAELdpdktvmdnlae 406
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEI------------ 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 407 gkqeVMVNGKPRHV--LGYLQDFMFHPK-RAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03233 86 ----IYVSEEDVHFptLTVRETLDFALRcKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
341-617 |
3.66e-10 |
|
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: 63.43 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 341 QIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVgtKLEVAYFDQhRAELDPDkTVMDNLAEGKQevMVNGKPRHV 420
Cdd:TIGR00957 660 SIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM--KGSVAYVPQ-QAWIQND-SLRENILFGKA--LNEKYYQQV 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 421 L---GYLQDFMFHPKRAMTPVRA----LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDGYQG----- 488
Cdd:TIGR00957 734 LeacALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGvlknk 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 489 TVMLVSHDRQFVDNtvTECWIFEGEGRIGQyVGGYH---DARGQQAQYLaqKQQISKKAVEAAQPKAESVKRASGKlsyn 565
Cdd:TIGR00957 814 TRILVTHGISYLPQ--VDVIIVMSGGKISE-MGSYQellQRDGAFAEFL--RTYAPDEQQGHLEDSWTALVSGEGK---- 884
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 695765469 566 lqrELEQLPQRLEELETQLQTLQEQVADPSFFG--QSHDHTQQVLAQLAEAEQA 617
Cdd:TIGR00957 885 ---EAKLIENGMLVTDVVGKQLQRQLSASSSDSgdQSRHHGSSAELQKAEAKEE 935
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
321-520 |
3.69e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.82 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKlMLGQLKADSGRIHVGTKLEvaYFDQH----RAELD- 395
Cdd:PRK14258 9 KVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLK-CLNRMNELESEVRVEGRVE--FFNQNiyerRVNLNr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 396 -----------PD---KTVMDNLAEGKQevMVNGKPRHVL----------GYLQDFMFHP--KRAMTpvraLSGGERNRL 449
Cdd:PRK14258 86 lrrqvsmvhpkPNlfpMSVYDNVAYGVK--IVGWRPKLEIddivesalkdADLWDEIKHKihKSALD----LSGGQQQRL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765469 450 LLAR-LFLKPsNLLILDEPTNDLDVETLELLEELVDGY----QGTVMLVSHDRQFVDNTVTECWIFEG-EGRIGQYV 520
Cdd:PRK14258 160 CIARaLAVKP-KVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHNLHQVSRLSDFTAFFKGnENRIGQLV 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-232 |
3.73e-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: 62.04 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 21 NAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIIY-EQDLVVARLQQD-PP--RNVtgtvydfvaegiae 93
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAI---AGLerpDSGRIRLgGEVLQDSARGIFlPPhrRRI-------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 94 qaaylkGYhdVSQLvmtdpsdknlnelARLQEQLD---NL--GLWQLD-----SRINEVLEQLNLDPnaeL-----SSLS 158
Cdd:COG4148 80 ------GY--VFQE-------------ARLFPHLSvrgNLlyGRKRAPraerrISFDEVVELLGIGH---LldrrpATLS 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695765469 159 GGWLRKAALGRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG4148 136 GGERQRVAIGRALLSSPRLLLMDEPLAALDLarkaEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
332-495 |
3.95e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.22 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 332 KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGtklevayfdqhraELDP-DKTVmdNLAEGKQE 410
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID-------------GVDItDKKV--KLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 411 V-MVNGKPRHVL---GYLQDFMFHP--------------KRAMTPVR------------ALSGGERNRLLLARLF-LKPS 459
Cdd:PRK13637 85 VgLVFQYPEYQLfeeTIEKDIAFGPinlglseeeienrvKRAMNIVGldyedykdkspfELSGGQKRRVAIAGVVaMEPK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 695765469 460 nLLILDEPTNDLDVETLELLEELV----DGYQGTVMLVSH 495
Cdd:PRK13637 165 -ILILDEPTAGLDPKGRDEILNKIkelhKEYNMTIILVSH 203
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
321-472 |
4.38e-10 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 60.25 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQV----DGKVLiKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLEVAYFDQHRA 392
Cdd:cd03249 2 EFKNVSFRYpsrpDVPIL-KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDgvdiRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 393 --ELDP---DKTVMDNLAEGK-----QEVMVNGKprhvLGYLQDF-MFHPKRAMTPVRA----LSGGERNRLLLARLFLK 457
Cdd:cd03249 81 lvSQEPvlfDGTIAENIRYGKpdatdEEVEEAAK----KANIHDFiMSLPDGYDTLVGErgsqLSGGQKQRIAIARALLR 156
|
170
....*....|....*
gi 695765469 458 PSNLLILDEPTNDLD 472
Cdd:cd03249 157 NPKILLLDEATSALD 171
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
319-499 |
4.46e-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: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 319 VFEMENVN--YQvDGKVLI---KDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQHRAE 393
Cdd:TIGR02211 1 LLKCENLGkrYQ-EGKLDTrvlKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 LD--------------PDKTVMDNLAE----GKQEVMvNGKPRhVLGYLQDFMFHPKRAMTPvRALSGGERNRLLLARLF 455
Cdd:TIGR02211 80 LRnkklgfiyqfhhllPDFTALENVAMplliGKKSVK-EAKER-AYEMLEKVGLEHRINHRP-SELSGGERQRVAIARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695765469 456 LKPSNLLILDEPTNDLDVETLEL---LEELVDGYQGTVML-VSHDRQF 499
Cdd:TIGR02211 157 VNQPSLVLADEPTGNLDNNNAKIifdLMLELNRELNTSFLvVTHDLEL 204
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
320-498 |
5.46e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 59.42 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 320 FEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKAD---SGRIhvgtklevaYFDQHR-AELD 395
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEV---------LLNGRRlTALP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 396 PDK----------------TVMDNLAEGkqevMVNGKPRH-----VLGYLQDFMFHPKRAMTPVrALSGGERNRLLLAR- 453
Cdd:COG4136 73 AEQrrigilfqddllfphlSVGENLAFA----LPPTIGRAqrrarVEQALEEAGLAGFADRDPA-TLSGGQRARVALLRa 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695765469 454 LFLKPSNLLiLDEPTNDLDVETLELLEELV----DGYQGTVMLVSHDRQ 498
Cdd:COG4136 148 LLAEPRALL-LDEPFSKLDAALRAQFREFVfeqiRQRGIPALLVTHDEE 195
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
317-468 |
5.96e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.96 E-value: 5.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 317 KIVFEMENVNYQVDG-KVLiKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKlEVAYFDQHRA--- 392
Cdd:COG1129 2 EPLLEMRGISKSFGGvKAL-DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGE-PVRFRSPRDAqaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 393 -------ELD--PDKTVMDNLAEGKQevmvngkPRHvlgylqdFMFHPKRAM------------------TPVRALSGGE 445
Cdd:COG1129 80 giaiihqELNlvPNLSVAENIFLGRE-------PRR-------GGLIDWRAMrrrarellarlgldidpdTPVGDLSVAQ 145
|
170 180
....*....|....*....|...
gi 695765469 446 RNRLLLARLFLKPSNLLILDEPT 468
Cdd:COG1129 146 QQLVEIARALSRDARVLILDEPT 168
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
323-472 |
6.66e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.91 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 323 ENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRI------------HVGTKLEVAYFDQh 390
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplHARARRGIGYLPQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 391 RAELDPDKTVMDNLA---EGKQEVMVNGKPRHVLGYLQDF-MFHPKRAMTpvRALSGGERNRLLLARLFLKPSNLLILDE 466
Cdd:PRK10895 86 EASIFRRLSVYDNLMavlQIRDDLSAEQREDRANELMEEFhIEHLRDSMG--QSLSGGERRRVEIARALAANPKFILLDE 163
|
....*.
gi 695765469 467 PTNDLD 472
Cdd:PRK10895 164 PFAGVD 169
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
319-472 |
7.50e-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: 59.37 E-value: 7.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 319 VFEMENVNYQV---DGKVLI-KDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKL------EVAYF 387
Cdd:COG4181 8 IIELRGLTKTVgtgAGELTIlKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLaGQDLfaldedARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 388 dqhRAE----------LDPDKTVMDNlaegkqeVMV----NGKP------RHVLGY--LQDFMFH-PKRamtpvraLSGG 444
Cdd:COG4181 88 ---RARhvgfvfqsfqLLPTLTALEN-------VMLplelAGRRdararaRALLERvgLGHRLDHyPAQ-------LSGG 150
|
170 180
....*....|....*....|....*...
gi 695765469 445 ERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLD 178
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
151-231 |
8.04e-10 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 58.60 E-value: 8.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 151 NAELSS-LSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFK---GTIIFISHDRSFIRNMATRIVDL 226
Cdd:cd03215 98 NIALSSlLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdagKAVLLISSELDELLGLCDRILVM 177
|
....*
gi 695765469 227 DRGKL 231
Cdd:cd03215 178 YEGRI 182
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
155-234 |
8.95e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 60.66 E-value: 8.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 155 SSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
....
gi 695765469 231 LVTY 234
Cdd:PRK11144 207 VKAF 210
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
316-525 |
9.74e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 61.66 E-value: 9.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 316 GKIVFEMENVNYQVDGKVLI-KDFSAQIQRGDKIALIGPNGCGKTTLLKLML-------GQLKADSGRIhvgTKLEVAYF 387
Cdd:TIGR00958 477 GLIEFQDVSFSYPNRPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQnlyqptgGQVLLDGVPL---VQYDHHYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 388 DQHRAELDPD-----KTVMDNLAEG-----KQEVMVNGKPRHVLGYLQDFmfhPKRAMTPV----RALSGGERNRLLLAR 453
Cdd:TIGR00958 554 HRQVALVGQEpvlfsGSVRENIAYGltdtpDEEIMAAAKAANAHDFIMEF---PNGYDTEVgekgSQLSGGQKQRIAIAR 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695765469 454 LFLKPSNLLILDEPTNDLDVETLELLEELVDGYQGTVMLVSHDRQFVDNtVTECwIFEGEGRIGQyvGGYHD 525
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVER-ADQI-LVLKKGSVVE--MGTHK 698
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-227 |
1.02e-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: 59.34 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 26 IEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQDPPRNvTGTVYDFVaegiaeqaaylkgyHDVS 105
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADY-EGTVRDLL--------------SSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 106 QLVMTDPSDKN--LNELarlqeQLDNLglwqLDSRINEvleqlnldpnaelssLSGGWLRKAALGRALVSGPRVLLLDEP 183
Cdd:cd03237 87 KDFYTHPYFKTeiAKPL-----QIEQI----LDREVPE---------------LSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695765469 184 TNHLDIETIDWLEGFLKTF----KGTIIFISHDRSFIRNMATRIVDLD 227
Cdd:cd03237 143 SAYLDVEQRLMASKVIRRFaennEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
324-472 |
1.07e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.81 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 324 NVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKL---------EVAYFDQHRAeL 394
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRmndvppaerGVGMVFQSYA-L 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 DPDKTVMDNLAEG-------KQEvmVNGKPRHVLGYLQdfMFH-----PKramtpvrALSGGERNRLLLARLFLKPSNLL 462
Cdd:PRK11000 87 YPHLSVAENMSFGlklagakKEE--INQRVNQVAEVLQ--LAHlldrkPK-------ALSGGQRQRVAIGRTLVAEPSVF 155
|
170
....*....|
gi 695765469 463 ILDEPTNDLD 472
Cdd:PRK11000 156 LLDEPLSNLD 165
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-236 |
1.19e-09 |
|
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: 58.82 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMK-ILNREQGLD--DGRIIY-----EQDLV---VARLQQDPpRNVTG-TVYD 85
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDaISGRVEGGGttSGQILFngqprKPDQFqkcVAYVRQDD-ILLPGlTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 86 FVaegiaeqaaylkgyHDVSQLVMTDPSDKnlnelARLQEQLDNLGLWQL-DSRINevleqlnldpNAELSSLSGGWLRK 164
Cdd:cd03234 101 TL--------------TYTAILRLPRKSSD-----AIRKKRVEDVLLRDLaLTRIG----------GNLVKGISGGERRR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 165 AALGRALVSGPRVLLLDEPTNHLD----IETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVtYPG 236
Cdd:cd03234 152 VSIAVQLLWDPKVLILDEPTSGLDsftaLNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV-YSG 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-237 |
1.32e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 61.28 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGriIYE---QDlvVARLQQDPPRNVTGTVYDFVAEGIaEQA 95
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSG--TYRvagQD--VATLDADALAQLRREHFGFIFQRY-HLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 96 AYLKGYHDVSQLVMTDPSDKNlNELARLQEQLDNLGLWqldsrinevlEQLNLDPnaelSSLSGGWLRKAALGRALVSGP 175
Cdd:PRK10535 99 SHLTAAQNVEVPAVYAGLERK-QRLLRAQELLQRLGLE----------DRVEYQP----SQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695765469 176 RVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSfIRNMATRIVDLDRGKLVTYPGN 237
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDrghTVIIVTHDPQ-VAAQAERVIEIRDGEIVRNPPA 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-239 |
1.38e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.10 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---------DDGRIIYEQDLVVAR-----------LQQD-PPR 77
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLT---GIlvptsgevrVLGYVPFKRRKEFARrigvvfgqrsqLWWDlPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 78 ---NVTGTVYdfvaeGIAEQAAylkgyhdvsqlvmtdpsDKNLNELArlqEQLDnlglwqldsrINEVLEQlnldPNAEL 154
Cdd:COG4586 115 dsfRLLKAIY-----RIPDAEY-----------------KKRLDELV---ELLD----------LGELLDT----PVRQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 155 SslsggwL--R-KAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLK----TFKGTIIFISHDRSFIRNMATRIVDLD 227
Cdd:COG4586 156 S------LgqRmRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKeynrERGTTILLTSHDMDDIEALCDRVIVID 229
|
250
....*....|..
gi 695765469 228 RGKLVtypgnYD 239
Cdd:COG4586 230 HGRII-----YD 236
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
10-242 |
1.39e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.58 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 10 WLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRII-----YEQDLVVARLQQDPPRNVTG--T 82
Cdd:PTZ00265 1175 YISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfkneHTNDMTNEQDYQGDEEQNVGmkN 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 83 VYDFVAEGIAEQAAYLKGYHDVSQLVM--TDPSDKNLNELARL-----QEQL-------DNLGLWQLDSR---------- 138
Cdd:PTZ00265 1255 VNEFSLTKEGGSGEDSTVFKNSGKILLdgVDICDYNLKDLRNLfsivsQEPMlfnmsiyENIKFGKEDATredvkrackf 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 139 --INEVLEQL------NLDPNAElsSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG----TI 206
Cdd:PTZ00265 1335 aaIDEFIESLpnkydtNVGPYGK--SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTI 1412
|
250 260 270
....*....|....*....|....*....|....*....
gi 695765469 207 IFISHDRSFIRNMATRIV--DLDR-GKLVTYPGNYDQYL 242
Cdd:PTZ00265 1413 ITIAHRIASIKRSDKIVVfnNPDRtGSFVQAHGTHEELL 1451
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-232 |
1.41e-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: 59.19 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDlvVARLQQDPPRNVTGTVYDFVAEGIA------- 92
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDgQD--IAAMSRKELRELRRKKISMVFQSFAllphrtv 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 93 -EQAAY---LKGyhdVSQLVmtdpsdknlnELARLQEQLDNLGLW-QLDSRINEvleqlnldpnaelssLSGGWLRKAAL 167
Cdd:cd03294 120 lENVAFgleVQG---VPRAE----------REERAAEALELVGLEgWEHKYPDE---------------LSGGMQQRVGL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 168 GRALVSGPRVLLLDEPTNHLD----IETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03294 172 ARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
349-467 |
1.45e-09 |
|
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: 60.11 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 349 ALIGPNGCGKTTLLKLMLGQLKADSGRIHVGtklEVAYFDQ--------HR---------AELDPDKTVMDNLAEG-KQE 410
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLG---GEVLQDSargiflppHRrrigyvfqeARLFPHLSVRGNLLYGrKRA 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695765469 411 VMVNGKPRH-----VLGyLQDFMfhpKRamtPVRALSGGERNRLLLAR-LFLKPSnLLILDEP 467
Cdd:COG4148 106 PRAERRISFdevveLLG-IGHLL---DR---RPATLSGGERQRVAIGRaLLSSPR-LLLMDEP 160
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
310-472 |
1.56e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 58.89 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 310 EEAARSGKIVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMlgqlkadsGRIH---VGTKLE--V 384
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL--------NRMNdliPGARVEgeI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 385 AYFDQ--HRAELDPD-----------------KTVMDNLAEGkqeVMVNG-KPRHVLG-----YLqdfmfhpKRAM---- 435
Cdd:COG1117 74 LLDGEdiYDPDVDVVelrrrvgmvfqkpnpfpKSIYDNVAYG---LRLHGiKSKSELDeiveeSL-------RKAAlwde 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695765469 436 ------TPVRALSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLD 472
Cdd:COG1117 144 vkdrlkKSALGLSGGQQQRLCIARaLAVEPEVLL-MDEPTSALD 186
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-232 |
1.60e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 59.34 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQG-----------LDDGRIIYE-QDLVVAR----LQQD 74
Cdd:PRK14271 29 LGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyrysgdvLLGGRSIFNyRDVLEFRrrvgMLFQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 75 PPRNVTGTVYDFVAEGI-AEQAAYLKGYHDVSQlvmtdpsdknlnelARLQEqldnLGLWqldsriNEVLEQLNLDPnae 153
Cdd:PRK14271 109 RPNPFPMSIMDNVLAGVrAHKLVPRKEFRGVAQ--------------ARLTE----VGLW------DAVKDRLSDSP--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 154 lSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTF--KGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK14271 162 -FRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
.
gi 695765469 232 V 232
Cdd:PRK14271 241 V 241
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-234 |
1.92e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.55 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNReqglddgriIYEQDlvvarlqqdpprnvTGTVydfvaegiaeqaaYL 98
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG---------ILEPT--------------SGRV-------------EV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 99 KGYhdVSQLVmtdpsdkNLN----------ELARLQEQLDNLGLWQLDSRINEVLEqlnldpNAELS--------SLSGG 160
Cdd:COG1134 86 NGR--VSALL-------ELGagfhpeltgrENIYLNGRLLGLSRKEIDEKFDEIVE------FAELGdfidqpvkTYSSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 161 wlRKAALGRALVSG--PRVLLLDEptnhldietidWL-----------EGFLKTFK---GTIIFISHDRSFIRNMATRIV 224
Cdd:COG1134 151 --MRARLAFAVATAvdPDILLVDE-----------VLavgdaafqkkcLARIRELResgRTVIFVSHSMGAVRRLCDRAI 217
|
250
....*....|
gi 695765469 225 DLDRGKLVTY 234
Cdd:COG1134 218 WLEKGRLVMD 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
321-472 |
2.26e-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: 58.47 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQV-DGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKlEVAYFDQHR-------- 391
Cdd:cd03295 2 EFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE-DIREQDPVElrrkigyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 392 ---AELDPDKTVMDNLAEGKQevmVNGKPRH-----VLGYLQDFMFHPK--RAMTPvRALSGGERNRLLLARLFLKPSNL 461
Cdd:cd03295 81 iqqIGLFPHMTVEENIALVPK---LLKWPKEkirerADELLALVGLDPAefADRYP-HELSGGQQQRVGVARALAADPPL 156
|
170
....*....|.
gi 695765469 462 LILDEPTNDLD 472
Cdd:cd03295 157 LLMDEPFGALD 167
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-225 |
2.46e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.25 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLD-----DGRIIYE--------QDLVVAR------L 71
Cdd:PRK14239 13 VYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNghniysprTDTVDLRkeigmvF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 72 QQdpPRNVTGTVYDFVAEGIAeqaayLKGYHDVSQLvmtdpsDknlnelARLQEQLDNLGLWqldsriNEVLEQLNldpn 151
Cdd:PRK14239 93 QQ--PNPFPMSIYENVVYGLR-----LKGIKDKQVL------D------EAVEKSLKGASIW------DEVKDRLH---- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695765469 152 AELSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG--TIIFISHdrsfirNM--ATRIVD 225
Cdd:PRK14239 144 DSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTR------SMqqASRISD 215
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
30-197 |
2.50e-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: 57.50 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 30 ERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqdlvvarlqqdpprnvtGTVYDFVAEGIAEQAAYLkGYHDVSQLVM 109
Cdd:cd03231 27 EALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLN-----------------GGPLDFQRDSIARGLLYL-GHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 110 TdpsdknlnelarlqeQLDNLGLWQL---DSRINEVLEQLNLD--PNAELSSLSGGWLRKAALGRALVSGPRVLLLDEPT 184
Cdd:cd03231 89 S---------------VLENLRFWHAdhsDEQVEEALARVGLNgfEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170
....*....|...
gi 695765469 185 NHLDIETIDWLEG 197
Cdd:cd03231 154 TALDKAGVARFAE 166
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
326-473 |
2.88e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 60.31 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 326 NYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRI-HVGtklEVAYFDQHrAELDPDkTVMDNL 404
Cdd:TIGR01271 433 NFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIkHSG---RISFSPQT-SWIMPG-TIKDNI 507
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 405 AEGKQevMVNGKPRHVLGYLQ---DFMFHPKRAMTPVR----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:TIGR01271 508 IFGLS--YDEYRYTSVIKACQleeDIALFPEKDKTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-237 |
3.49e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 58.21 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-----------IYEQDLVVARLQQDPPRNV-TGTVYDF 86
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrevnaenEKWVRSKVGLVFQDPDDQVfSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 87 VAEGiaeqaaylkgyhdvsqlvmtdPSdknlnelarlqeqldNLGLWQ--LDSRINEVLEQLNLDPNAELSS--LSGGWL 162
Cdd:PRK13647 101 VAFG---------------------PV---------------NMGLDKdeVERRVEEALKAVRMWDFRDKPPyhLSYGQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695765469 163 RKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIVDLDRGKLVTYPGN 237
Cdd:PRK13647 145 KRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNqgkTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-188 |
3.61e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 58.69 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 4 ISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQdpPRNVTGTV 83
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARL--ARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 84 YDF--------VAEGIAEQAAYLKGYHDVSQLVMtdPSdknLNELARLQEQLDnlglwqldsrinevleqlnldpnAELS 155
Cdd:PRK13536 120 PQFdnldleftVRENLLVFGRYFGMSTREIEAVI--PS---LLEFARLESKAD-----------------------ARVS 171
|
170 180 190
....*....|....*....|....*....|...
gi 695765469 156 SLSGGWLRKAALGRALVSGPRVLLLDEPTNHLD 188
Cdd:PRK13536 172 DLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
326-473 |
3.78e-09 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 58.33 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 326 NYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRI-HVGtklEVAYFDQHrAELDPDkTVMDNL 404
Cdd:cd03291 44 NLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIkHSG---RISFSSQF-SWIMPG-TIKENI 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 405 AEGKQevMVNGKPRHVLGYLQ---DFMFHPKRAMTPVR----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03291 119 IFGVS--YDEYRYKSVVKACQleeDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
319-472 |
3.90e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 58.32 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 319 VFEMENVNYQV-DGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKlEVAYFDQHRAEL--- 394
Cdd:PRK13636 5 ILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-PIDYSRKGLMKLres 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 ------DPDKTVMD------------NLAEGKQEV---MVNGKPRHVLGYLQDfmfhpkramTPVRALSGGERNRLLLAR 453
Cdd:PRK13636 84 vgmvfqDPDNQLFSasvyqdvsfgavNLKLPEDEVrkrVDNALKRTGIEHLKD---------KPTHCLSFGQKKRVAIAG 154
|
170
....*....|....*....
gi 695765469 454 LFLKPSNLLILDEPTNDLD 472
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLD 173
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-233 |
3.95e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.10 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQDPP----RNVTGTVYDFvaegiaeq 94
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEvkrlRKEIGLVFQF-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 95 aaylKGYHDVSQLVMTDPSDKNLNELARLQEQLdnlglwqldSRINEVLEQLNLDPNAELSS---LSGGWLRKAALGRAL 171
Cdd:PRK13645 99 ----PEYQLFQETIEKDIAFGPVNLGENKQEAY---------KKVPELLKLVQLPEDYVKRSpfeLSGGQKRRVALAGII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 172 VSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVT 233
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPkgeeDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
34-473 |
4.76e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.15 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 34 LVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLVVArlqqdpprnvtgTVYDFVAEGIAEqaaylkgYHDVSQLV--MT 110
Cdd:PRK11288 35 LMGENGAGKSTLLKILSGNYQPDAGSIlIDGQEMRFA------------STTAALAAGVAI-------IYQELHLVpeMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 111 dpsdknlneLArlqeqlDNLGLWQLDSR---------INEVLEQL-----NLDPNAELSSLSGGWLRKAALGRALVSGPR 176
Cdd:PRK11288 96 ---------VA------ENLYLGQLPHKggivnrrllNYEAREQLehlgvDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 177 VLLLDEPTNHLDIETIDWLEGFLKTFK--GT-IIFISHDRSFIRNMATRIVDLDRGKLVTYpgnydqylLDKEEALRVEE 253
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRaeGRvILYVSHRMEEIFALCDAITVFKDGRYVAT--------FDDMAQVDRDQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 254 LQNAEFDRKLaqeevwirQGIKARRTRNEGRVRalkamrrergerrevmgsakMQVEEaarsgkivfemenvnyqVDGKV 333
Cdd:PRK11288 233 LVQAMVGREI--------GDIYGYRPRPLGEVR--------------------LRLDG-----------------LKGPG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 334 LIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIhvgtklevaYFDQHRAELdpdKTVMDNLAEG------ 407
Cdd:PRK11288 268 LREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQV---------YLDGKPIDI---RSPRDAIRAGimlcpe 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 408 --KQEVMVNGKP----------RHVLGYlqDFMFHPKR------------------AMTPVRALSGGERNRLLLARLFLK 457
Cdd:PRK11288 336 drKAEGIIPVHSvadninisarRHHLRA--GCLINNRWeaenadrfirslniktpsREQLIMNLSGGNQQKAILGRWLSE 413
|
490
....*....|....*.
gi 695765469 458 PSNLLILDEPTNDLDV 473
Cdd:PRK11288 414 DMKVILLDEPTRGIDV 429
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-232 |
5.04e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.87 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLVVARLQQD----PPRNVTGTVYDFVAEGIAEQ 94
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-DITITHKTKDkyirPVRKRIGMVFQFPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 95 aaylkgyhDVSQLVMTDPSDKNLNelarlqeqldnlgLWQLDSRINEVLEQLNLDPNAELSS---LSGGWLRKAALGRAL 171
Cdd:PRK13646 102 --------TVEREIIFGPKNFKMN-------------LDEVKNYAHRLLMDLGFSRDVMSQSpfqMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695765469 172 VSGPRVLLLDEPTNHLDIETIDWLEGFLKTFK----GTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
19-239 |
5.16e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.48 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGL-----DDGRIIY-EQDLVVARLqqDP-------------PRNV 79
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFhGKNLYAPDV--DPvevrrrigmvfqkPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 80 TGTVYDFVAEGiaeqaAYLKGYHDvsqlvmtdpsdkNLNELarLQEQLDNLGLWqldsriNEVLEQLNLDPnaelSSLSG 159
Cdd:PRK14243 104 PKSIYDNIAYG-----ARINGYKG------------DMDEL--VERSLRQAALW------DEVKDKLKQSG----LSLSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 160 GWLRKAALGRALVSGPRVLLLDEPTNHLD-IETIDwLEGFLKTFKG--TIIFISHdrsfirNM--ATRIVDL-------- 226
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDpISTLR-IEELMHELKEqyTIIIVTH------NMqqAARVSDMtaffnvel 227
|
250
....*....|....
gi 695765469 227 -DRGKLVTYPGNYD 239
Cdd:PRK14243 228 tEGGGRYGYLVEFD 241
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
30-232 |
5.46e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.95 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 30 ERVCLVGRNGAGKST----LMKILNREQGLD-DGRIIYE----QDLVV-ARLQ---QDP-----PRNvtgTVYDFVAEGI 91
Cdd:PRK15134 313 ETLGLVGESGSGKSTtglaLLRLINSQGEIWfDGQPLHNlnrrQLLPVrHRIQvvfQDPnsslnPRL---NVLQIIEEGL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 92 AeqaaylkgyhdVSQLVMTdpsdknlnelARLQEQldnlglwqldsRINEVLEQLNLDPNAEL---SSLSGGWLRKAALG 168
Cdd:PRK15134 390 R-----------VHQPTLS----------AAQREQ-----------QVIAVMEEVGLDPETRHrypAEFSGGQRQRIAIA 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695765469 169 RALVSGPRVLLLDEPTNHLD----IETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK15134 438 RALILKPSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
327-498 |
5.60e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.13 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 327 YQvDGKVL---IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGR-IHVGTKL--------------EVAYFD 388
Cdd:PRK11629 15 YQ-EGSVQtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDvIFNGQPMsklssaakaelrnqKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 389 QHRaELDPDKTVMDNLAE-----GKQEVMVNGKPRHVLGYLQdfmfHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK11629 94 QFH-HLLPDFTALENVAMplligKKKPAEINSRALEMLAAVG----LEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 695765469 464 LDEPTNDLDVETLE---LLEELVDGYQGTVML-VSHDRQ 498
Cdd:PRK11629 169 ADEPTGNLDARNADsifQLLGELNRLQGTAFLvVTHDLQ 207
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-188 |
5.63e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 57.89 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 4 ISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlvvaRLQQDPprnvtgtv 83
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI---------SLCGEP-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 84 ydfvAEGIAEQAAYLKGYhdVSQLVMTDPsDKNLNELARLQEQLDNLGLWQLDSRINEVLEQLNLDPNAE--LSSLSGGW 161
Cdd:PRK13537 71 ----VPSRARHARQRVGV--VPQFDNLDP-DFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADakVGELSGGM 143
|
170 180
....*....|....*....|....*..
gi 695765469 162 LRKAALGRALVSGPRVLLLDEPTNHLD 188
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
318-472 |
5.64e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.45 E-value: 5.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 318 IVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIhvgtklevaYFDQHRAELD-- 395
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI---------FYNNQAITDDnf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 396 -------------PDK-----TVMDNLAEGKQEVMVNGKPRH--VLGYLQDFMFHPKRAMTPvRALSGGERNRLLLAR-L 454
Cdd:PRK13648 79 eklrkhigivfqnPDNqfvgsIVKYDVAFGLENHAVPYDEMHrrVSEALKQVDMLERADYEP-NALSGGQKQRVAIAGvL 157
|
170
....*....|....*...
gi 695765469 455 FLKPSnLLILDEPTNDLD 472
Cdd:PRK13648 158 ALNPS-VIILDEATSMLD 174
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
17-183 |
5.96e-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: 56.78 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRI-IYEQDLVV------AR-----LQQDPP--RNV 79
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMI---VGLvkpDSGKIlLDGQDITKlpmhkrARlgigyLPQEASifRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 80 TgtvydfVAEGIaeqaaylkgyhdvsqlvmtdpsdknlneLARLQEQldNLGLWQLDSRINEVLEQLNLDPNAE--LSSL 157
Cdd:cd03218 91 T------VEENI----------------------------LAVLEIR--GLSKKEREEKLEELLEEFHITHLRKskASSL 134
|
170 180
....*....|....*....|....*.
gi 695765469 158 SGGWLRKAALGRALVSGPRVLLLDEP 183
Cdd:cd03218 135 SGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
335-496 |
6.56e-09 |
|
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: 56.71 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 335 IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLEVAYFDQ----HRAELDPDKTVMDNLAEGKQ 409
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQITEPGPDRmvvfQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 410 EVMVN---GKPRHVLGYLQDFMFHPKRAMTPVRALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLELLEEL--- 482
Cdd:TIGR01184 81 RVLPDlskSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARaLSIRPK-VLLLDEPFGALDALTRGNLQEElmq 159
|
170
....*....|....*
gi 695765469 483 -VDGYQGTVMLVSHD 496
Cdd:TIGR01184 160 iWEEHRVTVLMVTHD 174
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-232 |
7.76e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 56.77 E-value: 7.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 26 IEDNERVCLVGRNGAGKSTLmkiLNREQGLDD--GRIIY-EQDLVVARLQQdpprnvtgtvydfvaegIAEQAAYLkgyh 102
Cdd:COG4138 19 VNAGELIHLIGPNGAGKSTL---LARMAGLLPgqGEILLnGRPLSDWSAAE-----------------LARHRAYL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 103 dvSQLVMTDPSDKNLNELARLQEqlDNLGLWQLDSRINEVLEQLNLDP--NAELSSLSGG-W--LRKAA----LGRALVS 173
Cdd:COG4138 75 --SQQQSPPFAMPVFQYLALHQP--AGASSEAVEQLLAQLAEALGLEDklSRPLTQLSGGeWqrVRLAAvllqVWPTINP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695765469 174 GPRVLLLDEPTNHLDIETIDWLEGFLKTFK---GTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG4138 151 EGQLLLLDEPMNSLDVAQQAALDRLLRELCqqgITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
321-472 |
9.11e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 57.04 E-value: 9.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLEVAyfDQHR-----AE- 393
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdGEPLDPE--DRRRigylpEEr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 -LDPDKTVMDNL-----------AEGKQEVMVngkprhvlgYLQDFMFhPKRAMTPVRALSGGERNRL-LLARLFLKPSn 460
Cdd:COG4152 81 gLYPKMKVGEQLvylarlkglskAEAKRRADE---------WLERLGL-GDRANKKVEELSKGNQQKVqLIAALLHDPE- 149
|
170
....*....|..
gi 695765469 461 LLILDEPTNDLD 472
Cdd:COG4152 150 LLILDEPFSGLD 161
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-232 |
1.02e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 56.92 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 3 LISMHGAWLSFSD-SPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdLVVARLQQDPPRnvtg 81
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV-----LVSGIDTGDFSK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 82 tvydfvaegiaeqaayLKGYHDVSQLVMTDPSDKNLNElaRLQEQL----DNLGL--WQLDSRINEVLEQLNLDPNAELS 155
Cdd:PRK13644 72 ----------------LQGIRKLVGIVFQNPETQFVGR--TVEEDLafgpENLCLppIEIRKRVDRALAEIGLEKYRHRS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 156 --SLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIET-IDWLEGFLKTF-KG-TIIFISHDRSFIRNmATRIVDLDRGK 230
Cdd:PRK13644 134 pkTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHeKGkTIVYITHNLEELHD-ADRIIVMDRGK 212
|
..
gi 695765469 231 LV 232
Cdd:PRK13644 213 IV 214
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-234 |
1.11e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.42 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLVVARLqqdpprnvtgtvydfvaegiaeqaay 97
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID-GLNIAKI-------------------------- 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 98 lkGYHDVSQLVMTDPSDK---------NLNELARLQEQ--LDNLGLWQLDSRINEVLEQLNLDPNAELSSLSGGWLRKAA 166
Cdd:TIGR00957 1354 --GLHDLRFKITIIPQDPvlfsgslrmNLDPFSQYSDEevWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVC 1431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 167 LGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKT-FKG-TIIFISHDRSFIRNMaTRIVDLDRGKLVTY 234
Cdd:TIGR00957 1432 LARALLRKTKILVLDEATAAVDLETDNLIQSTIRTqFEDcTVLTIAHRLNTIMDY-TRVIVLDKGEVAEF 1500
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-229 |
1.17e-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: 55.93 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLmkiLNREQGLD---DGRIIYEQDLVVArlqQDPPRNVTGTVYDFVAEGIAEQA 95
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTL---LNLISGLAqptSGGVILEGKQITE---PGPDRMVVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 96 AYLkgyhdVSQLVMTDPSDKNLNELARlqEQLDNLGLWQL-DSRINEvleqlnldpnaelssLSGGWLRKAALGRALVSG 174
Cdd:TIGR01184 75 IAL-----AVDRVLPDLSKSERRAIVE--EHIALVGLTEAaDKRPGQ---------------LSGGMKQRVAIARALSIR 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 175 PRVLLLDEPTNHLDIETIDWL-EGFLKTFKG---TIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:TIGR01184 133 PKVLLLDEPFGALDALTRGNLqEELMQIWEEhrvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
317-472 |
1.37e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 56.54 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 317 KIVFEMENV--NYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLEVAYFDQHRAE 393
Cdd:PRK13632 5 SVMIKVENVsfSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 L-----DPDK-----TVMDNLAEGKQEVMVNGKP--------RHVLGYLQDFMFHPKRamtpvraLSGGERNRLLLAR-L 454
Cdd:PRK13632 85 IgiifqNPDNqfigaTVEDDIAFGLENKKVPPKKmkdiiddlAKKVGMEDYLDKEPQN-------LSGGQKQRVAIASvL 157
|
170
....*....|....*...
gi 695765469 455 FLKPSnLLILDEPTNDLD 472
Cdd:PRK13632 158 ALNPE-IIIFDESTSMLD 174
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-520 |
1.43e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 1 MSLISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDG----------RIIYE--QDLVV 68
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfshitRLSFEqlQKLVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 69 ARLQqdppRNVTgtvyDFVAEG---IAEQAAylkgyhDVSQLVMTDPsdknlnelARLQEQLDNLGLWQLDSRinevleq 145
Cdd:PRK10938 81 DEWQ----RNNT----DMLSPGeddTGRTTA------EIIQDEVKDP--------ARCEQLAQQFGITALLDR------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 146 lnldpnaELSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATR 222
Cdd:PRK10938 132 -------RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLVLNRFDEIPDFVQF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 223 IVDLDRGKLvTYPGNYDQYLldkEEALrVEELQNAEfdrKLAQEEVWIRQGIKARRTRNEGRVRalkamrrergerrevm 302
Cdd:PRK10938 205 AGVLADCTL-AETGEREEIL---QQAL-VAQLAHSE---QLEGVQLPEPDEPSARHALPANEPR---------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 303 gsakmqveeaarsgkivFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQ-------------L 369
Cdd:PRK10938 261 -----------------IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpqgysndltlfgR 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 370 KADSG------RIHVG--------------TKLEV---AYFDQ---HRAeldpdktVMDNLAEGKQEVMvngkprHVLGy 423
Cdd:PRK10938 324 RRGSGetiwdiKKHIGyvssslhldyrvstSVRNVilsGFFDSigiYQA-------VSDRQQKLAQQWL------DILG- 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 424 lqdfmFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVD---GYQGTVML-VSHDRQF 499
Cdd:PRK10938 390 -----IDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDvliSEGETQLLfVSHHAED 464
|
570 580
....*....|....*....|.
gi 695765469 500 VDNTVTECWIFEGEGRIGQYV 520
Cdd:PRK10938 465 APACITHRLEFVPDGDIYRYV 485
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
316-473 |
1.62e-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: 55.58 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 316 GKIVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLEVAYFDQH- 390
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDgvdiSKIGLHDLRSRi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 391 --------------RAELDP-----DKTVMDNLAEGKQEVMVNGKPrhvlGYLQdfmfhpkramTPVRA----LSGGERN 447
Cdd:cd03244 81 siipqdpvlfsgtiRSNLDPfgeysDEELWQALERVGLKEFVESLP----GGLD----------TVVEEggenLSVGQRQ 146
|
170 180
....*....|....*....|....*.
gi 695765469 448 RLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVDP 172
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
321-468 |
1.86e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 55.51 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKlEVAYFDQHR-AELD---- 395
Cdd:COG4674 12 YVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGT-DLTGLDEHEiARLGigrk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 396 -------PDKTVMDNLaegkqEVMVNGK--PRHVLGY------------------LQDfmfhpkRAMTPVRALSGGERNR 448
Cdd:COG4674 91 fqkptvfEELTVFENL-----ELALKGDrgVFASLFArltaeerdrieevletigLTD------KADRLAGLLSHGQKQW 159
|
170 180
....*....|....*....|
gi 695765469 449 LLLARLFLKPSNLLILDEPT 468
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPV 179
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-233 |
1.86e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 56.28 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 13 FSDSPLLDnAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQD---PPRNVTGTVYDFVAE 89
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikPVRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 90 GIAEQAaylkgyhdVSQLVMTDPSDKNLN--ELARLQ-EQLDNLGLWQldsrinEVLEQLNLDpnaelssLSGGWLRKAA 166
Cdd:PRK13643 96 QLFEET--------VLKDVAFGPQNFGIPkeKAEKIAaEKLEMVGLAD------EFWEKSPFE-------LSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765469 167 LGRALVSGPRVLLLDEPTNHLD----IETIDWLEGFLKTFKgTIIFISHDRSFIRNMATRIVDLDRGKLVT 233
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-224 |
2.08e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.10 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 26 IEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyEQDLVVARLQQDPPRNVTGTVYDFVAEGIAEqaaylkgyhdvs 105
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISPDYDGTVEEFLRSANTD------------ 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 106 qlvmtdpsdknlnelarlqeqldnlglwQLDSRI--NEVLEQLNLDP--NAELSSLSGGWLRKAALGRALVSGPRVLLLD 181
Cdd:COG1245 429 ----------------------------DFGSSYykTEIIKPLGLEKllDKNVKDLSGGELQRVAIAACLSRDADLYLLD 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695765469 182 EPTNHLDIE-------TIdwlEGFLKTFKGTIIFISHDRSFIRNMATRIV 224
Cdd:COG1245 481 EPSAHLDVEqrlavakAI---RRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-240 |
2.11e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.16 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqglddGRIIYEQDLVV-----------------ARLQQ 73
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL-------GFLPYQGSLKIngielreldpeswrkhlSWVGQ 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 74 DPpRNVTGTVYDFVAEGiaeqaaylkgyhdvsqlvmtdpsDKNLNElARLQEQLDNlglwqldSRINEVLEQLNLDPNAE 153
Cdd:PRK11174 431 NP-QLPHGTLRDNVLLG-----------------------NPDASD-EQLQQALEN-------AWVSEFLPLLPQGLDTP 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 154 LS----SLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDI---ETIdwLEGFLKTFKG-TIIFISHDRSFIRNMATrIVD 225
Cdd:PRK11174 479 IGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAhseQLV--MQALNAASRRqTTLMVTHQLEDLAQWDQ-IWV 555
|
250
....*....|....*
gi 695765469 226 LDRGKLVTyPGNYDQ 240
Cdd:PRK11174 556 MQDGQIVQ-QGDYAE 569
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
312-472 |
2.17e-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: 57.14 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 312 AARSGKIVFEmeNVN--YQVDGKVLiKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKL-EVAyf 387
Cdd:COG5265 352 VVGGGEVRFE--NVSfgYDPERPIL-KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIdGQDIrDVT-- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 388 dQH--RAELD--PDKTVM------DNLAEGK-----QEVmvngkpRHV--LGYLQDFMFH-PKRAMTPV--RA--LSGGE 445
Cdd:COG5265 427 -QAslRAAIGivPQDTVLfndtiaYNIAYGRpdaseEEV------EAAarAAQIHDFIESlPDGYDTRVgeRGlkLSGGE 499
|
170 180
....*....|....*....|....*..
gi 695765469 446 RNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:COG5265 500 KQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
335-500 |
2.37e-08 |
|
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: 55.03 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 335 IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLE---------------VAYFDQHRAELDpdKT 399
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNEsepsfeatrsrnrysVAYAAQKPWLLN--AT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 400 VMDNLAEGKQEVMVNGKPRHVLGYLQ---DFMFHPKRAMTPVRA--LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
Cdd:cd03290 95 VEENITFGSPFNKQRYKAVTDACSLQpdiDLLPFGDQTEIGERGinLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190
....*....|....*....|....*....|.
gi 695765469 475 TLELLEEL-----VDGYQGTVMLVSHDRQFV 500
Cdd:cd03290 175 LSDHLMQEgilkfLQDDKRTLVLVTHKLQYL 205
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
316-500 |
3.06e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 316 GKIVFEMENVNYQVDGKV---LIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLK--ADSGRIHVGTkleVAYFDQh 390
Cdd:PLN03232 611 GAPAISIKNGYFSWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELShaETSSVVIRGS---VAYVPQ- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 391 rAELDPDKTVMDNLAEG-KQEVMVNGKPRHVLGYLQDFMFHPKRAMTPVRA----LSGGERNRLLLARLFLKPSNLLILD 465
Cdd:PLN03232 687 -VSWIFNATVRENILFGsDFESERYWRAIDVTALQHDLDLLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190
....*....|....*....|....*....|....*...
gi 695765469 466 EPTNDLD--VETLELLEELVDGYQG-TVMLVSHDRQFV 500
Cdd:PLN03232 766 DPLSALDahVAHQVFDSCMKDELKGkTRVLVTNQLHFL 803
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-232 |
3.21e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.94 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 26 IEDNERVCLVGRNGAGKSTLmkiLNREQGLDDGriiyeqdlvvarlqqdpprnvTGTVY-------DFVAEGIAEQAAYL 98
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTL---LARMAGLLPG---------------------SGSIQfagqpleAWSAAELARHRAYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 99 kgyhdvSQLVMTDPSDKNLNELARLQEQLDNLGlwQLDSRINEVLEQLNLDPNAE--LSSLSGG-W--LRKAA----LGR 169
Cdd:PRK03695 75 ------SQQQTPPFAMPVFQYLTLHQPDKTRTE--AVASALNEVAEALGLDDKLGrsVNQLSGGeWqrVRLAAvvlqVWP 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 170 ALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTF---KGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK03695 147 DINPAGQLLLLDEPMNSLDVAQQAALDRLLSELcqqGIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-212 |
3.35e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.12 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 14 SDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLV-----------VARLQQDPPRNVTG- 81
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteenvwdirhkIGMVFQNPDNQFVGa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 82 TVYDFVAEGIAEQAAYLKgyhdvsqlvmtdpsdknlnelarlqeqldnlglwQLDSRINEVLEQLNLD--PNAELSSLSG 159
Cdd:PRK13650 98 TVEDDVAFGLENKGIPHE----------------------------------EMKERVNEALELVGMQdfKEREPARLSG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695765469 160 GWLRKAALGRALVSGPRVLLLDEPTNHLD----IETIDWLEGFLKTFKGTIIFISHD 212
Cdd:PRK13650 144 GQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
319-496 |
3.45e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.12 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 319 VFEMENVNYQVDG---KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLEVAYFDQHRAEL 394
Cdd:PRK13650 4 IIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 -----DPDK-----TVMDNLAEGKQ------EVMVNgKPRHVLGY--LQDFmfhpkRAMTPVRaLSGGERNRLLLARLFL 456
Cdd:PRK13650 84 gmvfqNPDNqfvgaTVEDDVAFGLEnkgiphEEMKE-RVNEALELvgMQDF-----KEREPAR-LSGGQKQRVAIAGAVA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695765469 457 KPSNLLILDEPTNDLDVETLELLEELV----DGYQGTVMLVSHD 496
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIkgirDDYQMTVISITHD 200
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
330-501 |
3.78e-08 |
|
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: 54.40 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 330 DGKVLiKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYfdQHR--------AELDP---DK 398
Cdd:cd03248 26 DTLVL-QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY--EHKylhskvslVGQEPvlfAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 399 TVMDNLAEGKQ-----EVMVNGKPRHVLGYLQDFmfhPKRAMTPV----RALSGGERNRLLLARLFLKPSNLLILDEPTN 469
Cdd:cd03248 103 SLQDNIAYGLQscsfeCVKEAAQKAHAHSFISEL---ASGYDTEVgekgSQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 695765469 470 DLDVETLELLEELVdgYQG----TVMLVSHDRQFVD 501
Cdd:cd03248 180 ALDAESEQQVQQAL--YDWperrTVLVIAHRLSTVE 213
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
332-473 |
4.43e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.61 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 332 KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLK----LML---GQLKADSGRIHVGTKLEVAY---FDQHRAELDPDKTVM 401
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRtlsrLMTpahGHVWLDGEHIQHYASKEVARrigLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 402 DNLAEGK-------------QEVMVNGKPRHV-LGYLqdfmfhpkrAMTPVRALSGGERNRLLLARLFLKPSNLLILDEP 467
Cdd:PRK10253 100 ELVARGRyphqplftrwrkeDEEAVTKAMQATgITHL---------ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
....*.
gi 695765469 468 TNDLDV 473
Cdd:PRK10253 171 TTWLDI 176
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
157-473 |
4.88e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.02 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 157 LSGGWLRKAALGRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiqaQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 233 ------------TYPgnYDQYLLdkEEALRVEELQNAEFDRKLAqeevWIRQGIKARRTrnegrvralkamrRERGERRE 300
Cdd:PRK10261 249 etgsveqifhapQHP--YTRALL--AAVPQLGAMKGLDYPRRFP----LISLEHPAKQE-------------PPIEQDTV 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 301 VMGSAKMQVEEAA-----RSGKivfeMENVNYQVDGkvlIKDFSAQIQRGDKIALIGPNGCGKTT----LLKLM---LGQ 368
Cdd:PRK10261 308 VDGEPILQVRNLVtrfplRSGL----LNRVTREVHA---VEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVesqGGE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 369 LKADSGRIHV--GTKLEVA------YFDQHRAELDPDKTVMDNLAEG-KQEVMVNGKP--RHVLGYLQDFMFHPKRAMTP 437
Cdd:PRK10261 381 IIFNGQRIDTlsPGKLQALrrdiqfIFQDPYASLDPRQTVGDSIMEPlRVHGLLPGKAaaARVAWLLERVGLLPEHAWRY 460
|
330 340 350
....*....|....*....|....*....|....*..
gi 695765469 438 VRALSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDV 473
Cdd:PRK10261 461 PHEFSGGQRQRICIARaLALNP-KVIIADEAVSALDV 496
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
318-504 |
5.15e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.50 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 318 IVFEMENVNYQvDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLE-------VAYFDQ 389
Cdd:PRK15056 7 IVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlGQPTRqalqknlVAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 390 HRaELDPDKTVMdnlaegKQEVMVNGKPRHvLGYLQDFMFHPKRAMTPVRA--------------LSGGERNRLLLARLF 455
Cdd:PRK15056 86 SE-EVDWSFPVL------VEDVVMMGRYGH-MGWLRRAKKRDRQIVTAALArvdmvefrhrqigeLSGGQKKRVFLARAI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 456 LKPSNLLILDEPTNDLDVETLELLEELVDGY--QGTVMLVS-HD----RQFVDNTV 504
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELrdEGKTMLVStHNlgsvTEFCDYTV 213
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
316-473 |
5.80e-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: 53.57 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 316 GKIVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVgtklevayfDQHRAELD 395
Cdd:cd03369 5 GEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI---------DGIDISTI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 396 PDKTVMDNLAEGKQE-VMVNGKPRHVLG----YLQDFMFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTND 470
Cdd:cd03369 76 PLEDLRSSLTIIPQDpTLFSGTIRSNLDpfdeYSDEEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
...
gi 695765469 471 LDV 473
Cdd:cd03369 156 IDY 158
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
19-224 |
6.39e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIE-----DNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyEQDLVVA----RLQQDPPrnvtGTVYDFvae 89
Cdd:PRK13409 350 LGDFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISykpqYIKPDYD----GTVEDL--- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 90 giaeqaaylkgyhdvsqlvmtdpsdknlneLARLQEQLDNLGLWqldsriNEVLEQLNLDP--NAELSSLSGGWLRKAAL 167
Cdd:PRK13409 421 ------------------------------LRSITDDLGSSYYK------SEIIKPLQLERllDKNVKDLSGGELQRVAI 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695765469 168 GRALVSGPRVLLLDEPTNHLDIE-------TIdwlEGFLKTFKGTIIFISHDRSFIRNMATRIV 224
Cdd:PRK13409 465 AACLSRDADLYLLDEPSAHLDVEqrlavakAI---RRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
321-500 |
7.02e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 54.36 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQV-DGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLEVAYFDQHRAEL---- 394
Cdd:PRK13647 6 EVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVmGREVNAENEKWVRSKVglvf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 -DPD-----KTVMDNLAEGKQEV-----MVNGKPRHVLGYLQDFMFHPKramtPVRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK13647 86 qDPDdqvfsSTVWDDVAFGPVNMgldkdEVERRVEEALKAVRMWDFRDK----PPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 695765469 464 LDEPTNDLDVETLELLEELVDGY--QG-TVMLVSHDRQFV 500
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLhnQGkTVIVATHDVDLA 201
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
342-513 |
7.23e-08 |
|
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: 52.57 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 342 IQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIhvgtklevayfdqhraELDpdktvmdnlaegkqEVMVNGKPRHVl 421
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND----------------EWD--------------GITPVYKPQYI- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 422 gylqdfmfhpkramtpvrALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDGY----QGTVMLVSHDR 497
Cdd:cd03222 71 ------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDL 132
|
170
....*....|....*.
gi 695765469 498 QFVDNTVTECWIFEGE 513
Cdd:cd03222 133 AVLDYLSDRIHVFEGE 148
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-236 |
7.38e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 54.24 E-value: 7.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 3 LISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqdlvvarlqqdpprnvtGT 82
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQ-----------------GK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 83 VYDFVAEGI---AEQAAYLkgYHDVSQLVMTDPSDKNLnelarlQEQLDNLGLWQ--LDSRINEVLEQLNLD--PNAELS 155
Cdd:PRK13638 64 PLDYSKRGLlalRQQVATV--FQDPEQQIFYTDIDSDI------AFSLRNLGVPEaeITRRVDEALTLVDAQhfRHQPIQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 156 SLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKGT---IIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13638 136 CLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
....*.
gi 695765469 233 TY--PG 236
Cdd:PRK13638 216 THgaPG 221
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
30-248 |
9.19e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.78 E-value: 9.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 30 ERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYeqdlvvarlqqdppRNVTGTVYDFVAEGIAEQAAYLK---GYhdVSQ 106
Cdd:PRK11701 33 EVLGIVGESGSGKTTLLNALSARLAPDAGEVHY--------------RMRDGQLRDLYALSEAERRRLLRtewGF--VHQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 107 lvmtDPSD---KNLNELARLQEQLDNLGlWQLDSRINEV----LEQLNLDPNA---ELSSLSGGWLRKAALGRALVSGPR 176
Cdd:PRK11701 97 ----HPRDglrMQVSAGGNIGERLMAVG-ARHYGDIRATagdwLERVEIDAARiddLPTTFSGGMQQRLQIARNLVTHPR 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 177 VLLLDEPTNHLDIET----IDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVTyPGNYDQYLLDKEEA 248
Cdd:PRK11701 172 LVFMDEPTGGLDVSVqarlLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVE-SGLTDQVLDDPQHP 246
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
319-472 |
9.40e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 53.93 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 319 VFEMENVNYQV-DGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKlevayfdqhraELDPD 397
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE-----------PIKYD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 398 KTvmdNLAEGKQEV-MVNGKPRHVL---GYLQDFMFHP-----------KRAMTPVRA-------------LSGGERNRL 449
Cdd:PRK13639 70 KK---SLLEVRKTVgIVFQNPDDQLfapTVEEDVAFGPlnlglskeeveKRVKEALKAvgmegfenkpphhLSGGQKKRV 146
|
170 180
....*....|....*....|...
gi 695765469 450 LLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLD 169
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-232 |
9.87e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.55 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 4 ISMHGAWLSfSDSPLLDNAELHIEDNERVCLVGRNGAGKStlmkilnreqglddgriiyeqdLVVARLQQDPPRNVTGTV 83
Cdd:PRK10418 5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKS----------------------LTCAAALGILPAGVRQTA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 84 YDFVAEGIAEQAAYLKGYHdVSqLVMTDP-SDKN--LNELARLQEQLDNLGLWQLDSRINEVLEQLNL-DPNAELSS--- 156
Cdd:PRK10418 62 GRVLLDGKPVAPCALRGRK-IA-TIMQNPrSAFNplHTMHTHARETCLALGKPADDATLTAALEAVGLeNAARVLKLypf 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 157 -LSGGWLRKAALGRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK10418 140 eMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVvaqaRILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
.
gi 695765469 232 V 232
Cdd:PRK10418 220 V 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
306-472 |
1.03e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 55.02 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 306 KMQVEEAarSGKIVFEmeNVNYQVDGK--VLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKL 382
Cdd:PRK11176 332 KRVIERA--KGDIEFR--NVTFTYPGKevPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdGHDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 383 E----------VAYFDQHrAELDPDkTVMDNLAEGKQEVMVNGKPRHV--LGYLQDFMFHPKRAMTPV-----RALSGGE 445
Cdd:PRK11176 408 RdytlaslrnqVALVSQN-VHLFND-TIANNIAYARTEQYSREQIEEAarMAYAMDFINKMDNGLDTVigengVLLSGGQ 485
|
170 180
....*....|....*....|....*..
gi 695765469 446 RNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALD 512
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
343-473 |
1.21e-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: 54.79 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 343 QRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLEVayFDQHR-AELdpdKTVMDNLAEGKQEV--------- 411
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEePSWDEV--LKRFRgTEL---QDYFKKLANGEIKVahkpqyvdl 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 412 ---MVNGKPRHVL------GYLQDFMfhPKRAMTP-----VRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:COG1245 172 ipkVFKGTVRELLekvderGKLDELA--EKLGLENildrdISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
332-516 |
1.24e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.54 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 332 KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIH-VGTKLEVAYFDQHRA--------------ELDP 396
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwRGEPLAKLNRAQRKAfrrdiqmvfqdsisAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 397 DKTVMDNLAEgkqevmvngkP-RHVLGYLQDFMFHPKRAMtpVRA--------------LSGGERNRLLLARLFLKPSNL 461
Cdd:PRK10419 105 RKTVREIIRE----------PlRHLLSLDKAERLARASEM--LRAvdlddsvldkrppqLSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 462 LILDEPTNDLDVETLELLEELVDGYQ---GTVML-VSHDRQFVDNTVTECWIFEgEGRI 516
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKLQqqfGTACLfITHDLRLVERFCQRVMVMD-NGQI 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
12-473 |
1.27e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.62 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYeqdlvvarlqQDPPRNVTGTVydfvaegi 91
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILY----------LGKEVTFNGPK-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 92 AEQAAYLKGYHdvsqlvmtdpsdKNLNELARL---------QEQLDNLG--LWQ-LDSRINEVLEQLNL--DPNAELSSL 157
Cdd:PRK10762 75 SSQEAGIGIIH------------QELNLIPQLtiaeniflgREFVNRFGriDWKkMYAEADKLLARLNLrfSSDKLVGEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 158 SGGWLRKAALGRALVSGPRVLLLDEPTNHL-DIETIDWLE--GFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVty 234
Cdd:PRK10762 143 SIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFRviRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFI-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 235 pGNYDQYLLDkEEALrVEELqnaeFDRKLaqEEVWirqgikARRTRNEGRVRalkamrrergerrevmgsakMQVEEAAR 314
Cdd:PRK10762 221 -AEREVADLT-EDSL-IEMM----VGRKL--EDQY------PRLDKAPGEVR--------------------LKVDNLSG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 315 SGkivfemenvnyqvdgkvlIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV------------GTKL 382
Cdd:PRK10762 266 PG------------------VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdghevvtrspqdGLAN 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 383 EVAYF--DQHRAELDPDKTVMDNLA--------------EGKQEVMVNGkprhvlgylqDF--MFHPKramTPVRA---- 440
Cdd:PRK10762 328 GIVYIseDRKRDGLVLGMSVKENMSltalryfsraggslKHADEQQAVS----------DFirLFNIK---TPSMEqaig 394
|
490 500 510
....*....|....*....|....*....|....*
gi 695765469 441 -LSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDV 473
Cdd:PRK10762 395 lLSGGNQQKVAIARgLMTRP-KVLILDEPTRGVDV 428
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-232 |
1.30e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 53.65 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 14 SDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL------DDGRIIYE-----QDLV------VARLQQDPP 76
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLIN---GLllpddnPNSKITVDgitltAKTVwdirekVGIVFQNPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 77 RNVTG-TVYDFVAEGIAEQAaylkgyhdVSQLVMTDPSDKNLNELARLQEQldnlglwqldsrinevleqlnldpNAELS 155
Cdd:PRK13640 95 NQFVGaTVGDDVAFGLENRA--------VPRPEMIKIVRDVLADVGMLDYI------------------------DSEPA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 156 SLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIE----TIDWLEGFLKTFKGTIIFISHDRSFIrNMATRIVDLDRGKL 231
Cdd:PRK13640 143 NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAgkeqILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKL 221
|
.
gi 695765469 232 V 232
Cdd:PRK13640 222 L 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
318-495 |
1.32e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 53.58 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 318 IVFEMENVNYQVDGKVLIK---DFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQHraEL 394
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRalfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQK--EI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 DP-----------------DKTVMDNLAEGKQEVMVN--------GKPRHVLGYLQDFMfhpkrAMTPVRaLSGGERNRL 449
Cdd:PRK13643 80 KPvrkkvgvvfqfpesqlfEETVLKDVAFGPQNFGIPkekaekiaAEKLEMVGLADEFW-----EKSPFE-LSGGQMRRV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695765469 450 LLARLFLKPSNLLILDEPTNDLDVETLELLEELVDGYQ---GTVMLVSH 495
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHqsgQTVVLVTH 202
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
332-516 |
1.38e-07 |
|
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: 53.27 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 332 KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLEVAYFDQHRAEL-----------DP 396
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgqdlYQLDRKQRRAFRRDVqlvfqdspsavNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 397 DKTVMDNLAEGKQEVM---VNGKPRHVLGYLQDFMFHPKRAMTPVRALSGGERNRLLLAR-LFLKPsNLLILDEPTNDLD 472
Cdd:TIGR02769 104 RMTVRQIIGEPLRHLTsldESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARaLAVKP-KLIVLDEAVSNLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695765469 473 VETLELLEELVDGYQ---GTV-MLVSHDRQFVDNTVTECWIFEGeGRI 516
Cdd:TIGR02769 183 MVLQAVILELLRKLQqafGTAyLFITHDLRLVQSFCQRVAVMDK-GQI 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-232 |
1.45e-07 |
|
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: 54.42 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqglddGRIIYEQDLVVARLQQD------PPRNVTGTVYDFVaeGIA 92
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIA-------GVLEPTSGEVNVRVGDEwvdmtkPGPDGRGRAKRYI--GIL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 93 EQAAYLKGYHDVSQlVMTDPSDKNL-NELARLQE--QLDNLGLwqLDSRINEVLEQLNldpnaelSSLSGGWLRKAALGR 169
Cdd:TIGR03269 371 HQEYDLYPHRTVLD-NLTEAIGLELpDELARMKAviTLKMVGF--DEEKAEEILDKYP-------DELSEGERHRVALAQ 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765469 170 ALVSGPRVLLLDEPTNHLD-IETIDWLEGFLKT---FKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:TIGR03269 441 VLIKEPRIVILDEPTGTMDpITKVDVTHSILKAreeMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
15-232 |
1.50e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.21 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 15 DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQD---PPRNVTGTVYDF----- 86
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikQIRKKVGLVFQFpesql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 87 VAEGIAEQAAYLKGYHDVSQlvmtdpsdKNLNELARlqEQLDNLGlwqldsrINEVLEQLNldPnaelSSLSGGWLRKAA 166
Cdd:PRK13649 99 FEETVLKDVAFGPQNFGVSQ--------EEAEALAR--EKLALVG-------ISESLFEKN--P----FELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695765469 167 LGRALVSGPRVLLLDEPTNHLDIETIDWLegfLKTFKG------TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKEL---MTLFKKlhqsgmTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-188 |
1.52e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 54.67 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKIL--NREQGLddgriiyeqdlvvarlQQDPPRNVTGTVYDfvAEGIAEQA 95
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafRSPKGV----------------KGSGSVLLNGMPID--AKEMRAIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 96 AYlkgyhdVSQLVMTDPS---DKNLNELARLQEQlDNLGLWQLDSRINEVLEQLNLDPNA--------ELSSLSGGWLRK 164
Cdd:TIGR00955 102 AY------VQQDDLFIPTltvREHLMFQAHLRMP-RRVTKKEKRERVDEVLQALGLRKCAntrigvpgRVKGLSGGERKR 174
|
170 180
....*....|....*....|....
gi 695765469 165 AALGRALVSGPRVLLLDEPTNHLD 188
Cdd:TIGR00955 175 LAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
321-376 |
1.61e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 53.23 E-value: 1.61e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRI 376
Cdd:PRK11831 9 DMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
321-472 |
1.66e-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: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTklevAYFD--QHRAE----- 393
Cdd:COG4161 4 QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAG----HQFDfsQKPSEkairl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 -------------LDPDKTVMDNLAEG--------KQEVMvnGKPRHVLGYLQdfmFHPKRAMTPVRaLSGGERNRLLLA 452
Cdd:COG4161 80 lrqkvgmvfqqynLWPHLTVMENLIEApckvlglsKEQAR--EKAMKLLARLR---LTDKADRFPLH-LSGGQQQRVAIA 153
|
170 180
....*....|....*....|.
gi 695765469 453 R-LFLKPSNLLiLDEPTNDLD 472
Cdd:COG4161 154 RaLMMEPQVLL-FDEPTAALD 173
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
337-473 |
1.68e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.01 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 337 DFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV----GTKLEVA----------------YFDQHRAE-LD 395
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdGQLRDLYalseaerrrllrtewgFVHQHPRDgLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 396 PDKTVMDNLAEgkqEVMVNGKpRH-------VLGYLQDFMFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPT 468
Cdd:PRK11701 104 MQVSAGGNIGE---RLMAVGA-RHygdiratAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPT 179
|
....*
gi 695765469 469 NDLDV 473
Cdd:PRK11701 180 GGLDV 184
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-246 |
1.96e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 52.93 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqdlvvarlqqdpprnvtGTVYDFVAEGIAEqaayl 98
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFD-----------------GKPIDYSRKGLMK----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 99 kgYHDVSQLVMTDPSDKNLNelARLQEQLD----NLGLW--QLDSRINEVLEQLNLDP--NAELSSLSGGWLRKAALGRA 170
Cdd:PRK13636 80 --LRESVGMVFQDPDNQLFS--ASVYQDVSfgavNLKLPedEVRKRVDNALKRTGIEHlkDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 171 LVSGPRVLLLDEPTNHLD----IETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVtYPGNYDQYLLDKE 246
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGNPKEVFAEKE 234
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
321-472 |
2.12e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 52.40 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLK------------LMLGQLKADSGRIHV-GTKLEVAY- 386
Cdd:PRK09493 3 EFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdLIVDGLKVNDPKVDErLIRQEAGMv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 387 FDQHraELDPDKTVMDNLAEGkqevmvngkPRHVLGY-LQDFMFHPKRAMTPV----RA------LSGGERNRLLLAR-L 454
Cdd:PRK09493 83 FQQF--YLFPHLTALENVMFG---------PLRVRGAsKEEAEKQARELLAKVglaeRAhhypseLSGGQQQRVAIARaL 151
|
170
....*....|....*...
gi 695765469 455 FLKPsNLLILDEPTNDLD 472
Cdd:PRK09493 152 AVKP-KLMLFDEPTSALD 168
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
12-214 |
2.15e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 53.18 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGLD---DGRI-IYEQDLVVARLQQDPPRNVTGTVYDFV 87
Cdd:PRK11432 15 RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLV---AGLEkptEGQIfIDGEDVTHRSIQQRDICMVFQSYALFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 88 AEGIAEQAAYlkgyhdvsqlvmtdpsdkNLNELARLQEQLDnlglwqldSRINEVLEQLNLDPNAE--LSSLSGGWLRKA 165
Cdd:PRK11432 92 HMSLGENVGY------------------GLKMLGVPKEERK--------QRVKEALELVDLAGFEDryVDQISGGQQQRV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 166 ALGRALVSGPRVLLLDEPTNHLDI-------ETIDWLEgflKTFKGTIIFISHDRS 214
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDAnlrrsmrEKIRELQ---QQFNITSLYVTHDQS 198
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
15-228 |
2.23e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 51.71 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 15 DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqG-LDD-----GRIIYEQdlvvARLQQDPP--RNVtgtvydf 86
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIA---GtLSPafsasGEVLLNG----RRLTALPAeqRRI------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 87 vaeGIAEQAAYLKGYHDVSQlvmtdpsdkNL-----NELARLQEQldnlglwqldSRINEVLEQLNLDP--NAELSSLSG 159
Cdd:COG4136 79 ---GILFQDDLLFPHLSVGE---------NLafalpPTIGRAQRR----------ARVEQALEEAGLAGfaDRDPATLSG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695765469 160 GWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGF----LKTFKGTIIFISHDRSFIRNmATRIVDLDR 228
Cdd:COG4136 137 GQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDEEDAPA-AGRVLDLGN 208
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-213 |
2.82e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.15 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGlDDGRIiyeqdlvvarlqqdpprNVTGTVYDFVAegiaeQAAY 97
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEI-----------------QIDGVSWNSVT-----LQTW 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 98 LKGYHDVSQ--LVMTDPSDKNLNELARLQEQldnlGLWQLDSRI--NEVLEQLNLDPNAELSS----LSGGWLRKAALGR 169
Cdd:TIGR01271 1291 RKAFGVIPQkvFIFSGTFRKNLDPYEQWSDE----EIWKVAEEVglKSVIEQFPDKLDFVLVDggyvLSNGHKQLMCLAR 1366
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695765469 170 ALVSGPRVLLLDEPTNHLDIETIDWLEGFLK-TFKGTIIFISHDR 213
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQIIRKTLKqSFSNCTVILSEHR 1411
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-184 |
3.15e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 51.80 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLV---VARLQQDPPRNVTGTVYDFVAEGIAEQ 94
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgKDITdwqTAKIMREAVAIVPEGRRVFSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 95 AAYLKGYHDVSQlvmtdpsdknlnelarLQEQLDNlgLWQLDSRINEVLEQlnldpnaELSSLSGGWLRKAALGRALVSG 174
Cdd:PRK11614 101 LAMGGFFAERDQ----------------FQERIKW--VYELFPRLHERRIQ-------RAGTMSGGEQQMLAIGRALMSQ 155
|
170
....*....|
gi 695765469 175 PRVLLLDEPT 184
Cdd:PRK11614 156 PRLLLLDEPS 165
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-231 |
3.36e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 51.74 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLD---DGRIIYE-QDL--VVARLQQDPPRNVTGTVY------- 84
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLG---GLDtptSGDVIFNgQPMskLSSAAKAELRNQKLGFIYqfhhllp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 85 DFVA-EGIAeqaaylkgyhdvSQLVMTDPSDKNLNELARlqEQLDNLGLwqlDSRINEvleqlnldpnaELSSLSGGWLR 163
Cdd:PRK11629 101 DFTAlENVA------------MPLLIGKKKPAEINSRAL--EMLAAVGL---EHRANH-----------RPSELSGGERQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695765469 164 KAALGRALVSGPRVLLLDEPTNHLDIETID---WLEGFLKTFKGT-IIFISHDRSFIRNMaTRIVDLDRGKL 231
Cdd:PRK11629 153 RVAIARALVNNPRLVLADEPTGNLDARNADsifQLLGELNRLQGTaFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
324-473 |
3.62e-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: 52.36 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 324 NVNYQVDGKVL--IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKA---DSGRIHVG----TKLEVAYFDQHRAE- 393
Cdd:COG0444 8 KVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDgedlLKLSEKELRKIRGRe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 -----------LDPDKTVMDNLAE--------GKQEVMvngkpRHVLGYLQDF-MFHPKRAMtpvRA----LSGGERNRL 449
Cdd:COG0444 88 iqmifqdpmtsLNPVMTVGDQIAEplrihgglSKAEAR-----ERAIELLERVgLPDPERRL---DRypheLSGGMRQRV 159
|
170 180
....*....|....*....|....*
gi 695765469 450 LLAR-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG0444 160 MIARaLALEPK-LLIADEPTTALDV 183
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
18-193 |
4.28e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 51.43 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLVVARLQQDPPRNVtgtvydfvaeGIAEQAA 96
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiIDDEDISLLPLHARARRGI----------GYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 97 YLkgyhdVSQLVMTDpsdknlNELARLQEQlDNLGLWQLDSRINEVLEQLNLD--PNAELSSLSGGWLRKAALGRALVSG 174
Cdd:PRK10895 88 SI-----FRRLSVYD------NLMAVLQIR-DDLSAEQREDRANELMEEFHIEhlRDSMGQSLSGGERRRVEIARALAAN 155
|
170 180
....*....|....*....|
gi 695765469 175 PRVLLLDEPTNHLD-IETID 193
Cdd:PRK10895 156 PKFILLDEPFAGVDpISVID 175
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
12-253 |
4.34e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.55 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLDDGRIIYEQDLVV--------ARLQQDPPRNVTGTV 83
Cdd:PRK09984 13 TFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLS---GLITGDKSAGSHIELlgrtvqreGRLARDIRKSRANTG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 84 YDFVAEGIAEQAAYLKGYHdVSQLVMTDPSDKNLNELARLQEQldnlglwqldsRINEVLEQLNLDPNA--ELSSLSGGW 161
Cdd:PRK09984 90 YIFQQFNLVNRLSVLENVL-IGALGSTPFWRTCFSWFTREQKQ-----------RALQALTRVGMVHFAhqRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 162 LRKAALGRALVSGPRVLLLDEPTNHLDIET----IDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKlVTYPGN 237
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESarivMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH-VFYDGS 236
|
250 260
....*....|....*....|.
gi 695765469 238 YDQYLLDKEEAL-----RVEE 253
Cdd:PRK09984 237 SQQFDNERFDHLyrsinRVEE 257
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-232 |
4.35e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.14 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRII---YEQDLVVARLQQDPPRNVTGTVYDFVAEGIAEQA 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagYHITPETGNKNLKKLRKKVSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 96 aylkgyhdVSQLVMTDPSdknlnelarlqeqldNLGLWQLDSRINEV--LEQLNLDPNAELSS---LSGGWLRKAALGRA 170
Cdd:PRK13641 103 --------VLKDVEFGPK---------------NFGFSEDEAKEKALkwLKKVGLSEDLISKSpfeLSGGQMRRVAIAGV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695765469 171 LVSGPRVLLLDEPTNHLDIET-IDWLEGFLKTFKG--TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAghTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-230 |
4.42e-07 |
|
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: 50.93 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 4 ISMHGAWLSFSD-----SPLLDNAELHIEDNERVCLVGRNGAGKSTL-MKILNrEQGLDDGRIiyeqdlvvarlqqdppr 77
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLlSALLG-ELEKLSGSV----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 78 NVTGTVydfvaeGIAEQAAYLkgyhdvsqlvmtdpsdknLNELARlqeqlDN-LGLWQLDS-RINEVLE--QLNLD---- 149
Cdd:cd03250 63 SVPGSI------AYVSQEPWI------------------QNGTIR-----ENiLFGKPFDEeRYEKVIKacALEPDleil 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 150 PNAELS-------SLSGGwlRKA--ALGRALVSGPRVLLLDEPTNHLDIETIDWL-----EGFLKTFKgTIIFISHDRSF 215
Cdd:cd03250 114 PDGDLTeigekgiNLSGG--QKQriSLARAVYSDADIYLLDDPLSAVDAHVGRHIfenciLGLLLNNK-TRILVTHQLQL 190
|
250
....*....|....*
gi 695765469 216 IRNmATRIVDLDRGK 230
Cdd:cd03250 191 LPH-ADQIVVLDNGR 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
107-232 |
5.38e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 52.71 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 107 LVMTDPSDKNLNeLARLqEQLDNLGLwqLDSR-----INEVLEQLNL---DPNAELSSLSGGWLRKAALGRALVSGPRVL 178
Cdd:COG1129 341 LVLDLSIRENIT-LASL-DRLSRGGL--LDRRreralAEEYIKRLRIktpSPEQPVGNLSGGNQQKVVLAKWLATDPKVL 416
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 179 LLDEPTNHLDI----ETIDWLEGFLKtfKGT-IIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG1129 417 ILDEPTRGIDVgakaEIYRLIRELAA--EGKaVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
339-473 |
6.44e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.89 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 339 SAQIQRGDKIALIGPNGCGKTTLLKLML-------GQLKADSGRIHVGTKLEVA--------YFDQHRAELDPDKTVMDN 403
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTmietptgGELYYQGQDLLKADPEAQKllrqkiqiVFQNPYGSLNPRKKVGQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 404 LAE--------GKQE-------VM--VNGKPRHVLGYLQdfMFhpkramtpvralSGGERNRLLLAR-LFLKPsNLLILD 465
Cdd:PRK11308 115 LEEpllintslSAAErrekalaMMakVGLRPEHYDRYPH--MF------------SGGQRQRIAIARaLMLDP-DVVVAD 179
|
....*...
gi 695765469 466 EPTNDLDV 473
Cdd:PRK11308 180 EPVSALDV 187
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
318-500 |
6.89e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 50.64 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 318 IVFEMENVNYqVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRI----HVGTKL---EVAY---- 386
Cdd:PRK10908 2 IRFEHVSKAY-LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsgHDITRLknrEVPFlrrq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 387 ----FDQHraELDPDKTVMDNLAegkQEVMVNGKP-----RHVLGYLQDFMFHPKRAMTPVRaLSGGERNRLLLARLFLK 457
Cdd:PRK10908 81 igmiFQDH--HLLMDRTVYDNVA---IPLIIAGASgddirRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695765469 458 PSNLLILDEPTNDLDVETLELLEELVDGYQG---TVMLVSHDRQFV 500
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLI 200
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
342-473 |
7.81e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 342 IQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRI-HVGTKLEVayFDQHR-AELdpdKTVMDNLAEGK-------QEV- 411
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeEEPSWDEV--LKRFRgTEL---QNYFKKLYNGEikvvhkpQYVd 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695765469 412 ----MVNGKPRHVL------GYLQDFMfhpKR-AMTPV-----RALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK13409 171 lipkVFKGKVRELLkkvderGKLDEVV---ERlGLENIldrdiSELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
337-472 |
8.52e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 50.40 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 337 DFSAQIQRGDKIALIGPNGCGKTTLLKLmLGQLK-ADSGrihvgtKLEVA--YFD--------QHRA------------E 393
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRV-LNLLEmPRSG------TLNIAgnHFDfsktpsdkAIRElrrnvgmvfqqyN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 LDPDKTVMDNLAEGKQEVMVNGKPR---HVLGYLQDFMFHPKRAMTPVRaLSGGERNRLLLAR-LFLKPSNLLiLDEPTN 469
Cdd:PRK11124 93 LWPHLTVQQNLIEAPCRVLGLSKDQalaRAEKLLERLRLKPYADRFPLH-LSGGQQQRVAIARaLMMEPQVLL-FDEPTA 170
|
...
gi 695765469 470 DLD 472
Cdd:PRK11124 171 ALD 173
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-183 |
8.82e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 50.41 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 1 MSLISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTL--MKIlnreqGL---DDGRIiyeqdlvvarlqqdp 75
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTfyMIV-----GLvkpDSGRI--------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 76 prnvtgtvydfvaegiaeqaaYLKGyHDVSQLVMtdpsdknlNELARL------QE-----QL---DN----LGLWQLDS 137
Cdd:COG1137 61 ---------------------FLDG-EDITHLPM--------HKRARLgigylpQEasifrKLtveDNilavLELRKLSK 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695765469 138 -----RINEVLEQLNLDPNAEL--SSLSGGWLRKAALGRALVSGPRVLLLDEP 183
Cdd:COG1137 111 kereeRLEELLEEFGITHLRKSkaYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-232 |
9.03e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 50.76 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 11 LSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDlvvaRLQQDPPRNVTGTVydfvaeG 90
Cdd:PRK10253 15 LGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGE----HIQHYASKEVARRI------G 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 91 IAEQAAylkgyhdvsqlvmTDPSDKNLNEL---ARLQEQlDNLGLWQLDSR--INEVLEQLNLDPNAELS--SLSGGWLR 163
Cdd:PRK10253 85 LLAQNA-------------TTPGDITVQELvarGRYPHQ-PLFTRWRKEDEeaVTKAMQATGITHLADQSvdTLSGGQRQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695765469 164 KAALGRALVSGPRVLLLDEPTNHLDI-ETIDWLEGF--LKTFKG-TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK10253 151 RAWIAMVLAQETAIMLLDEPTTWLDIsHQIDLLELLseLNREKGyTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-212 |
9.37e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.50 E-value: 9.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 1 MSLISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDL----VVARLQQDPP 76
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLrigyVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 77 RNVTgtvydfvaegiaeqaaylkgyhdVSQLVMTDPSDKN---LNELARLQEQldnlglwqldsrinEVLEQlnldpnaE 153
Cdd:PRK09544 82 LPLT-----------------------VNRFLRLRPGTKKediLPALKRVQAG--------------HLIDA-------P 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695765469 154 LSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIE----TIDWLEGFLKTFKGTIIFISHD 212
Cdd:PRK09544 118 MQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNgqvaLYDLIDQLRRELDCAVLMVSHD 180
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-255 |
9.57e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 50.86 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-----------------IYEQDLVVARLQQDPPRNV-- 79
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekeKVLEKLVIQKTRFKKIKKIke 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 80 ----TGTVYDFVAEGIAEQAaylkgyhdVSQLVMTDP-----SDKNLNELARlqeqldnlglwqldsrinEVLEQLNLDP 150
Cdd:PRK13651 103 irrrVGVVFQFAEYQLFEQT--------IEKDIIFGPvsmgvSKEEAKKRAA------------------KYIELVGLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 151 NAELSS---LSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIE-TIDWLEGFLKTFKG--TIIFISHDRSFIRNMATRIV 224
Cdd:PRK13651 157 SYLQRSpfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFDNLNKQgkTIILVTHDLDNVLEWTKRTI 236
|
250 260 270
....*....|....*....|....*....|.
gi 695765469 225 DLDRGKLVTYPGNYDqyLLDKEEALRVEELQ 255
Cdd:PRK13651 237 FFKDGKIIKDGDTYD--ILSDNKFLIENNME 265
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
321-472 |
9.58e-07 |
|
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: 50.27 E-value: 9.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVN--YQVDGK--VLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKL------------- 382
Cdd:cd03258 3 ELKNVSkvFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdGTDLtllsgkelrkarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 383 EVAYFDQHRAELDpDKTVMDNLA-------EGKQEVmvngkPRHVLGYLQDFMFHPKRAMTPvRALSGGERNRLLLAR-L 454
Cdd:cd03258 83 RIGMIFQHFNLLS-SRTVFENVAlpleiagVPKAEI-----EERVLELLELVGLEDKADAYP-AQLSGGQKQRVGIARaL 155
|
170
....*....|....*...
gi 695765469 455 FLKPSnLLILDEPTNDLD 472
Cdd:cd03258 156 ANNPK-VLLCDEATSALD 172
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
130-231 |
1.01e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 50.74 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 130 LGLWQLDSRINEV--LEQLNLDPNAEL---SSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFK- 203
Cdd:PRK10619 121 LGLSKQEARERAVkyLAKVGIDERAQGkypVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAe 200
|
90 100 110
....*....|....*....|....*....|
gi 695765469 204 --GTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK10619 201 egKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
318-498 |
1.06e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.55 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 318 IVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLM--LGQLkADSGRIhvgtKLEVAYFDQ--HRAE 393
Cdd:PRK14243 9 TVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDL-IPGFRV----EGKVTFHGKnlYAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 LDP-----------------DKTVMDNLAEGkqevmvngkPRhVLGYLQDFMFHPKRAM--------------TPVRALS 442
Cdd:PRK14243 84 VDPvevrrrigmvfqkpnpfPKSIYDNIAYG---------AR-INGYKGDMDELVERSLrqaalwdevkdklkQSGLSLS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695765469 443 GGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVD--GYQGTVMLVSHDRQ 498
Cdd:PRK14243 154 GGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHelKEQYTIIIVTHNMQ 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-472 |
1.16e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 50.23 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 317 KIVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLK-----LMLGQLKADSGRIH-------------V 378
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRlfgrniyspdvdpI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 379 GTKLEVAYFDQHRAELdPDKTVMDNLAEGkqeVMVNG--KPRHVLGYLQDFMFHPKRAMTPVR--------ALSGGERNR 448
Cdd:PRK14267 82 EVRREVGMVFQYPNPF-PHLTIYDNVAIG---VKLNGlvKSKKELDERVEWALKKAALWDEVKdrlndypsNLSGGQRQR 157
|
170 180
....*....|....*....|....*
gi 695765469 449 LLLAR-LFLKPsNLLILDEPTNDLD 472
Cdd:PRK14267 158 LVIARaLAMKP-KILLMDEPTANID 181
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
332-472 |
1.18e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.59 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 332 KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLM----LGQLKADSGRIHVGTKLEV-------AYFDQHRAELdPDKTV 400
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrsPKGVKGSGSVLLNGMPIDAkemraisAYVQQDDLFI-PTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 401 MDNL---AEGK-QEVMVNGKPRHVLGYLQDFMFHPKRAMT------PVRALSGGERNRLLLARLFLKPSNLLILDEPTND 470
Cdd:TIGR00955 117 REHLmfqAHLRmPRRVTKKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
..
gi 695765469 471 LD 472
Cdd:TIGR00955 197 LD 198
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-232 |
1.34e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.21 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNRE---QGLDDG-RIIYEQDLVVARLQQ-DPPRNVTgtvydfvAEGIA 92
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgGGAPRGaRVTGDVTLNGEPLAAiDAPRLAR-------LRAVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 93 EQAAYLKGYHDVSQLVMTD--PSDKNLNELARLQEQLdnlgLWQldsrineVLEQLNLDPNA--ELSSLSGGWLRKAALG 168
Cdd:PRK13547 89 PQAAQPAFAFSAREIVLLGryPHARRAGALTHRDGEI----AWQ-------ALALAGATALVgrDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 169 RAL---------VSGPRVLLLDEPTNHLD-------IETI-----DWLEGFLKtfkgtiifISHDRSFIRNMATRIVDLD 227
Cdd:PRK13547 158 RVLaqlwpphdaAQPPRYLLLDEPTAALDlahqhrlLDTVrrlarDWNLGVLA--------IVHDPNLAARHADRIAMLA 229
|
....*
gi 695765469 228 RGKLV 232
Cdd:PRK13547 230 DGAIV 234
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
10-253 |
1.48e-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: 49.06 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 10 WLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqglddGRIIYEqdlvvarlqqdpprnVT-GTVydfva 88
Cdd:cd03217 7 HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIM-------GHPKYE---------------VTeGEI----- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 89 egiaeqaaYLKGyHDVSQLVMtdpsdknlNELARLqeqldNLGL-WQLDSRI-----NEVLEQLNLdpnaelsSLSGGWL 162
Cdd:cd03217 60 --------LFKG-EDITDLPP--------EERARL-----GIFLaFQYPPEIpgvknADFLRYVNE-------GFSGGEK 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 163 RKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISH-DRSFIRNMATRIVDLDRGKLVTyPGny 238
Cdd:cd03217 111 KRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITHyQRLLDYIKPDRVHVLYDGRIVK-SG-- 187
|
250
....*....|....*
gi 695765469 239 dqyllDKEEALRVEE 253
Cdd:cd03217 188 -----DKELALEIEK 197
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-237 |
1.53e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 50.48 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIY-EQDL----------VVARLQ---QDP-----PRNvt 80
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlGKDLlgmkddewraVRSDIQmifQDPlaslnPRM-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 81 gTVYDFVAEGiaeqaayLKGYHdvsqlvmtdPSDKNLNELARLQEQLDNLGLwqLDSRINEVleqlnldPNaelsSLSGG 160
Cdd:PRK15079 116 -TIGEIIAEP-------LRTYH---------PKLSRQEVKDRVKAMMLKVGL--LPNLINRY-------PH----EFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 161 WLRKAALGRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIvdldrgkLVTYPG 236
Cdd:PRK15079 166 QCQRIGIARALILEPKLIICDEPVSALDVsiqaQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRV-------LVMYLG 238
|
.
gi 695765469 237 N 237
Cdd:PRK15079 239 H 239
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
334-530 |
1.54e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 49.97 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 334 LIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKL---------EVAYFDQHRAELDPDK------ 398
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgQLKVADKNQLRLLRTRltmvfq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 399 --------TVMDNLAEGKQEVM----VNGKPRHVLGYLQDFMFHPKRAMTPVRaLSGGERNRLLLARLFLKPSNLLILDE 466
Cdd:PRK10619 100 hfnlwshmTVLENVMEAPIQVLglskQEARERAVKYLAKVGIDERAQGKYPVH-LSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695765469 467 PTNDLD---VETLELLEELVDGYQGTVMLVSHDRQFVDNtVTECWIF------EGEGRIGQYVGGYHDARGQQ 530
Cdd:PRK10619 179 PTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARH-VSSHVIFlhqgkiEEEGAPEQLFGNPQSPRLQQ 250
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
324-472 |
1.54e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 50.61 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 324 NVNYQVDGKVL-IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLEVAYFD-----QHRAe 393
Cdd:PRK11650 8 AVRKSYDGKTQvIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGgrvvNELEPADRDiamvfQNYA- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 LDPDKTVMDNLAEG-------KQEvmVNGKPRHVLGYLQ-DFMFHPKramtPvRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:PRK11650 87 LYPHMSVRENMAYGlkirgmpKAE--IEERVAEAARILElEPLLDRK----P-RELSGGQRQRVAMGRAIVREPAVFLFD 159
|
....*..
gi 695765469 466 EPTNDLD 472
Cdd:PRK11650 160 EPLSNLD 166
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
309-472 |
1.55e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 309 VEEAARSGKIVFEMENVNYQV----DGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLkaDSGRIHVGTKL-- 382
Cdd:TIGR00956 749 KDMEKESGEDIFHWRNLTYEVkikkEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITGGDRLvn 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 383 ----------EVAYFDQHRAELdPDKTVMDNL---AEGKQ--EVMVNGKPRHVlGYLQDF--MFHPKRAM--TPVRALSG 443
Cdd:TIGR00956 827 grpldssfqrSIGYVQQQDLHL-PTSTVRESLrfsAYLRQpkSVSKSEKMEYV-EEVIKLleMESYADAVvgVPGEGLNV 904
|
170 180 190
....*....|....*....|....*....|
gi 695765469 444 GERNRLLLA-RLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR00956 905 EQRKRLTIGvELVAKPKLLLFLDEPTSGLD 934
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
342-498 |
1.59e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.78 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 342 IQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQHRAELD--------------PDKTVMDN---- 403
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRakhvgfvfqsfmliPTLNALENvelp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 404 -LAEGKQEVMVNGKPRHVLGYLQdfmfHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEEL 482
Cdd:PRK10584 113 aLLRGESSRQSRNGAKALLEQLG----LGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170 180
....*....|....*....|
gi 695765469 483 V----DGYQGTVMLVSHDRQ 498
Cdd:PRK10584 189 LfslnREHGTTLILVTHDLQ 208
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-231 |
1.64e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.21 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARlqqdpprnvtgTVYDFVAEGIAeqaaYLKG 100
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAL-----------STAQRLARGLV----YLPE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 101 YHDVSQLVMTDPSDKNLNELARlqeqlDNLGLWQLDSRINEVLEQ----LNL---DPNAELSSLSGGWLRKAALGRALVS 173
Cdd:PRK15439 346 DRQSSGLYLDAPLAWNVCALTH-----NRRGFWIKPARENAVLERyrraLNIkfnHAEQAARTLSGGNQQKVLIAKCLEA 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765469 174 GPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK15439 421 SPQLLIVDEPTRGVDVSARNDIYQLIRSIAAqnvAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
335-516 |
1.79e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 50.08 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 335 IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIhvgtklEVAYFDQHraeldpDKTVMDNLAEGKQEVMVn 414
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI------EWIFKDEK------NKKKTKEKEKVLEKLVI- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 415 GKPRH---------------VLGY----------LQDFMFHP-----------KRAMTPVR--------------ALSGG 444
Cdd:PRK13651 90 QKTRFkkikkikeirrrvgvVFQFaeyqlfeqtiEKDIIFGPvsmgvskeeakKRAAKYIElvgldesylqrspfELSGG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765469 445 ERNRLLLARLFLKPSNLLILDEPTNDLD---VETLELLEELVDGYQGTVMLVSHDrqfVDNTV--TECWIFEGEGRI 516
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD---LDNVLewTKRTIFFKDGKI 243
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
332-501 |
2.39e-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: 48.76 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 332 KVLIKDF-----SAQIQRGDKIALI-GPNGCGKTTLLKlmlgqlkadsgrihvgtKLEVAYFDQHRAELDPDKTVMDNLA 405
Cdd:cd03240 3 KLSIRNIrsfheRSEIEFFSPLTLIvGQNGAGKTTIIE-----------------ALKYALTGELPPNSKGGAHDPKLIR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 406 EGKQEVMV-------NGKPRHVLGYL----------QDFMFHPkrAMTPVRALSGGERN------RLLLARLFLKPSNLL 462
Cdd:cd03240 66 EGEVRAQVklafenaNGKKYTITRSLailenvifchQGESNWP--LLDMRGRCSGGEKVlasliiRLALAETFGSNCGIL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695765469 463 ILDEPTNDLDVETLELL-EELVDGYQGT----VMLVSHDRQFVD 501
Cdd:cd03240 144 ALDEPTTNLDEENIEESlAEIIEERKSQknfqLIVITHDEELVD 187
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
339-468 |
2.66e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.11 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 339 SAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLEVAYFDQHRAELDPD-------KTVMDNLAEG 407
Cdd:PRK11614 25 SLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgkdiTDWQTAKIMREAVAIVPEgrrvfsrMTVEENLAMG 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765469 408 KQEVMVNGKPRHVLGYLQDFMFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPT 468
Cdd:PRK11614 105 GFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| HemX |
COG2959 |
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis ... |
517-621 |
3.21e-06 |
|
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis HemX, COG0755, no evidence of involvement in heme biosynthesis) [General function prediction only];
Pssm-ID: 442199 [Multi-domain] Cd Length: 361 Bit Score: 49.58 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 517 GQYVGGYHDARGQQAQY--LAQKQQISKKAVEAAQpkaESVKRASGKLSyNLQRELEQLPQRLEELETQLQTLQEQVADP 594
Cdd:COG2959 46 GGYYLGWQQLQQQQAELaqLAQQLAALQQQAQELR---ALAQQLQELLQ-QLAARLAQLEQRLAELQQQLAALQQLLQSL 121
|
90 100
....*....|....*....|....*..
gi 695765469 595 SffGQSHDHTQqvlaqLAEAEQALETA 621
Cdd:COG2959 122 S--GSSRDDWL-----LAEAEYLLRLA 141
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
134-226 |
3.70e-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: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 134 QLDSRINEVLEQLNLdpNAELSSLSGGWLRKAALGRALVSGPR--VLLLDEPTNHLDIETIDWLEGFLKTF---KGTIIF 208
Cdd:cd03238 67 QLQFLIDVGLGYLTL--GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLidlGNTVIL 144
|
90
....*....|....*...
gi 695765469 209 ISHDRSFIRNmATRIVDL 226
Cdd:cd03238 145 IEHNLDVLSS-ADWIIDF 161
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-232 |
3.71e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 49.65 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLVVARLQQDPPRNVTGTVYDFVAEGIAEQaaylkg 100
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLID-GVDIAKISDAELREVRRKKIAMVFQSFALM------ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 101 yhdvsqlvmtdPSDKNLNELArLQEQLDNLGLWQLDSRINEVLEQLNLDPNAE--LSSLSGGWLRKAALGRALVSGPRVL 178
Cdd:PRK10070 119 -----------PHMTVLDNTA-FGMELAGINAEERREKALDALRQVGLENYAHsyPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695765469 179 LLDEPTNHLD----IETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK10070 187 LMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-232 |
4.28e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 48.93 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiYEQDLVVARLQQD-PPRNVTGTVYD-----FVAEGIA 92
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV-YVDGLDTSDEENLwDIRNKAGMVFQnpdnqIVATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 93 EQAAYlkgyhdvsqlvmtDPsdknlnelarlqeqlDNLGLWQLD--SRINEVLEQLNL------DPNAelssLSGGWLRK 164
Cdd:PRK13633 105 EDVAF-------------GP---------------ENLGIPPEEirERVDESLKKVGMyeyrrhAPHL----LSGGQKQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695765469 165 AALGRALVSGPRVLLLDEPTNHLD----IETIDWLEGFLKTFKGTIIFISHdrsFIRNM--ATRIVDLDRGKLV 232
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH---YMEEAveADRIIVMDSGKVV 223
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
331-473 |
4.59e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 49.75 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 331 GKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLmLGQL---------KADSGRIH---------VGT-KLEVAYFDqhR 391
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRI-LGELwpvyggrltKPAKGKLFyvpqrpymtLGTlRDQIIYPD--S 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 392 AELDPDKTVMDNLAEgkqEVMVNGKPRHVL----GY--LQDFMfhpkramtpvRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:TIGR00954 541 SEDMKRRGLSDKDLE---QILDNVQLTHILeregGWsaVQDWM----------DVLSGGEKQRIAMARLFYHKPQFAILD 607
|
....*...
gi 695765469 466 EPTNDLDV 473
Cdd:TIGR00954 608 ECTSAVSV 615
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
149-232 |
4.79e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.64 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 149 DPNAELSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTF--KGT-IIFISHDRSFIRNMATRIVD 225
Cdd:COG3845 395 GPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELrdAGAaVLLISEDLDEILALSDRIAV 474
|
....*..
gi 695765469 226 LDRGKLV 232
Cdd:COG3845 475 MYEGRIV 481
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
337-471 |
5.05e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 337 DFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKlEVAyFDQHRAELD-------------PDKTVMDN 403
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-EMR-FASTTAALAagvaiiyqelhlvPEMTVAEN 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695765469 404 LAEGK---QEVMVNGKP--RHVLGYLQ--DFMFHPKramTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
Cdd:PRK11288 100 LYLGQlphKGGIVNRRLlnYEAREQLEhlGVDIDPD---TPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
17-224 |
5.93e-06 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 48.32 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlvvaRLQQDPprnVTG--------------- 81
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI---------TLDGVP---VTGpgadrgvvfqkdall 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 82 ---TVYDFVAEGIAeqaayLKGyhdvsqlvmtdpsdknLNELARLQEQLDNLGLWQLDSRINevleqlnldpnAELSSLS 158
Cdd:COG4525 89 pwlNVLDNVAFGLR-----LRG----------------VPKAERRARAEELLALVGLADFAR-----------RRIWQLS 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765469 159 GGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFL-----KTFKGtIIFISHDRSFIRNMATRIV 224
Cdd:COG4525 137 GGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLldvwqRTGKG-VFLITHSVEEALFLATRLV 206
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
319-473 |
6.01e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.16 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 319 VFEMENVNYQVDGkVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKAD----SGRIHV-GTKLE--------VA 385
Cdd:PRK10418 4 QIELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLdGKPVApcalrgrkIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 386 YFDQH-RAELDPDKTVMDNlaeGKQEVMVNGKPRHVlgylqDFMFHPKRAM---TPVRAL-------SGGERNRLLLARL 454
Cdd:PRK10418 83 TIMQNpRSAFNPLHTMHTH---ARETCLALGKPADD-----ATLTAALEAVgleNAARVLklypfemSGGMLQRMMIALA 154
|
170
....*....|....*....
gi 695765469 455 FLKPSNLLILDEPTNDLDV 473
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDV 173
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
319-472 |
6.61e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 48.26 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 319 VFEMENVNYQVDGKV-LIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLEVAYFDQHRAEL-- 394
Cdd:PRK13652 3 LIETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIREVRKFVgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 ---DPDKTVMDNLAE----------GKQEVMVNGKPR---HVLGyLQDFmfhpkRAMTPvRALSGGERNRLLLARLFLKP 458
Cdd:PRK13652 83 vfqNPDDQIFSPTVEqdiafgpinlGLDEETVAHRVSsalHMLG-LEEL-----RDRVP-HHLSGGEKKRVAIAGVIAME 155
|
170
....*....|....
gi 695765469 459 SNLLILDEPTNDLD 472
Cdd:PRK13652 156 PQVLVLDEPTAGLD 169
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-245 |
9.13e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 47.92 E-value: 9.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqglddGRIIyeqdlvvarlqqdpPRNVTGTVYDFvaegiaeqaaYL 98
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFN-------GLIK--------------SKYGTIQVGDI----------YI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 99 KGYHDVSQLVMTDPSDK--NLNELARL--------QEQL-------D------NLGLWQLDSR--INEVLEQLNLD-PNA 152
Cdd:PRK13631 91 GDKKNNHELITNPYSKKikNFKELRRRvsmvfqfpEYQLfkdtiekDimfgpvALGVKKSEAKklAKFYLNKMGLDdSYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 153 ELS--SLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIVDLD 227
Cdd:PRK13631 171 ERSpfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITHTMEHVLEVADEVIVMD 250
|
250 260
....*....|....*....|..
gi 695765469 228 RGKLVTYPGNY----DQYLLDK 245
Cdd:PRK13631 251 KGKILKTGTPYeiftDQHIINS 272
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
139-189 |
9.85e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.39 E-value: 9.85e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 695765469 139 INEVLEQLNL---DPNAELSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDI 189
Cdd:PRK13549 385 ILESIQRLKVktaSPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
335-501 |
1.03e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.16 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 335 IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLgqlkADSGRIHVGTKLEVAYfdqhraeldPDKTVM-DNLaegkQEVMV 413
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLISFLPKFS---------RNKLIFiDQL----QFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 414 NGkprhvLGYLQdfmfhPKRAMTpvrALSGGERNRLLLAR-LFLKPSN-LLILDEPTNDLDVETLELLEELVDGY--QG- 488
Cdd:cd03238 74 VG-----LGYLT-----LGQKLS---TLSGGELQRVKLASeLFSEPPGtLFILDEPSTGLHQQDINQLLEVIKGLidLGn 140
|
170
....*....|...
gi 695765469 489 TVMLVSHDRQFVD 501
Cdd:cd03238 141 TVILIEHNLDVLS 153
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-212 |
1.10e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.45 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 1 MSLISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVA--RLQQDPPRN 78
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 79 VTGTVYD----FVAEGIAEQAAYlkgyhdvsqlvmtdPsdknLNELARLQEQLdnlglwqLDSRINEVLEQLNLDPNAEL 154
Cdd:PRK11831 85 RMSMLFQsgalFTDMNVFDNVAY--------------P----LREHTQLPAPL-------LHSTVMMKLEAVGLRGAAKL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765469 155 --SSLSGGWLRKAALGRALVSGPRVLLLDEP-------TNHLDIETIDWLEGFLKTfkgTIIFISHD 212
Cdd:PRK11831 140 mpSELSGGMARRAALARAIALEPDLIMFDEPfvgqdpiTMGVLVKLISELNSALGV---TCVVVSHD 203
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
322-472 |
1.11e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 47.67 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 322 MENVNYQV-DGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV------------GTKLEVAYFD 388
Cdd:PRK13644 4 LENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidtgdfsklqGIRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 389 QHRAELDPDKTVMDNLAEGKQEVMVngKP----RHVLGYLQDFMFHPKRAMTPvRALSGGERNRLLLARLFLKPSNLLIL 464
Cdd:PRK13644 84 QNPETQFVGRTVEEDLAFGPENLCL--PPieirKRVDRALAEIGLEKYRHRSP-KTLSGGQGQCVALAGILTMEPECLIF 160
|
....*...
gi 695765469 465 DEPTNDLD 472
Cdd:PRK13644 161 DEVTSMLD 168
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
330-473 |
1.17e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.51 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 330 DGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQHRAELDPD-----KTVMDNL 404
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTLNGEPLAAIDAPrlarlRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 405 AE-----GKQEVMVNGKPRHVL---------GYLQDFMFHPKRAMTPVR----ALSGGERNRLLLARLFLK--------- 457
Cdd:PRK13547 92 AQpafafSAREIVLLGRYPHARragalthrdGEIAWQALALAGATALVGrdvtTLSGGELARVQFARVLAQlwpphdaaq 171
|
170
....*....|....*.
gi 695765469 458 PSNLLILDEPTNDLDV 473
Cdd:PRK13547 172 PPRYLLLDEPTAALDL 187
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-232 |
1.35e-05 |
|
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: 48.21 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 14 SDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL---------------------NREQGlddGRII-YeqdlvvarL 71
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvgvwpptagsvrldgadlsqwDREEL---GRHIgY--------L 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 72 QQDpprnVT---GTVydfvAEGIA----------EQAAYLKGYHDvsqLVMTDPsdknlnelarlqeqldnLGLwqlDSR 138
Cdd:COG4618 412 PQD----VElfdGTI----AENIArfgdadpekvVAAAKLAGVHE---MILRLP-----------------DGY---DTR 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 139 INEvleqlnldpnaELSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLD-------IETIDwlegFLKTFKGTIIFISH 211
Cdd:COG4618 461 IGE-----------GGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalAAAIR----ALKARGATVVVITH 525
|
250 260
....*....|....*....|.
gi 695765469 212 DRSFIrNMATRIVDLDRGKLV 232
Cdd:COG4618 526 RPSLL-AAVDKLLVLRDGRVQ 545
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
19-187 |
1.40e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 47.69 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 19 LDNAELHIEDNeRVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQDPPRNVTGTVYDFVAEgIAEQAAYL 98
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELTFGSLLSR-LLRLLLKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 99 KGYHDVSQLVmtDPSDKNLNE-LARLQEQLDNLGLWQLD----------SRINEVLEQLNL----DPNAELSSLSGG--W 161
Cdd:COG3593 92 EDKEELEEAL--EELNEELKEaLKALNELLSEYLKELLDgldlelelslDELEDLLKSLSLriedGKELPLDRLGSGfqR 169
|
170 180 190
....*....|....*....|....*....|.
gi 695765469 162 LRKAALGRALV-----SGPRVLLLDEPTNHL 187
Cdd:COG3593 170 LILLALLSALAelkraPANPILLIEEPEAHL 200
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
318-472 |
1.56e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.10 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 318 IVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADS---GRIHV-GTKLEVAYFDQHRAE 393
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVdGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 L-----DPDK-----TVMDNLAEGKQEVMVngkPRH-----VLGYLQDFMFHPKRAMTPVRaLSGGERNRLLLARLFLKP 458
Cdd:PRK13640 86 VgivfqNPDNqfvgaTVGDDVAFGLENRAV---PRPemikiVRDVLADVGMLDYIDSEPAN-LSGGQKQRVAIAGILAVE 161
|
170
....*....|....
gi 695765469 459 SNLLILDEPTNDLD 472
Cdd:PRK13640 162 PKIIILDESTSMLD 175
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
333-496 |
1.56e-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: 46.87 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 333 VLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKlEVAYFD----------------QHRAeLDP 396
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQ-DIAAMSrkelrelrrkkismvfQSFA-LLP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 397 DKTVMDNLAEGKQEVMVNGKPRHvlgylqdfmfhpKRAMTPVRA-------------LSGGERNRLLLAR-LFLKPSnLL 462
Cdd:cd03294 116 HRTVLENVAFGLEVQGVPRAERE------------ERAAEALELvglegwehkypdeLSGGMQQRVGLARaLAVDPD-IL 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 695765469 463 ILDEPTNDLD----VETLELLEELVDGYQGTVMLVSHD 496
Cdd:cd03294 183 LMDEAFSALDplirREMQDELLRLQAELQKTIVFITHD 220
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
302-472 |
1.68e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 302 MGSAKMQVEEAARSGKIVfemENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRihVGTK 381
Cdd:PTZ00243 646 GHEATPTSERSAKTPKMK---TDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR--VWAE 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 382 LEVAYFDQHRAELdpDKTVMDNLaegkqevmvngkprhvlgylqdFMFHPKRA---MTPVRA------------------ 440
Cdd:PTZ00243 721 RSIAYVPQQAWIM--NATVRGNI----------------------LFFDEEDAarlADAVRVsqleadlaqlgggletei 776
|
170 180 190
....*....|....*....|....*....|....*...
gi 695765469 441 ------LSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PTZ00243 777 gekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-232 |
1.92e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.94 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 26 IEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYEQDLVVARLQQD---PPRNVTGTVYDFVAEGIAEQAaylk 99
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLN---GLlqpTSGTVTIGERVITAGKKNKklkPLRKKVGIVFQFPEHQLFEET---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 100 gyhdVSQLVMTDPSDKNLNE---LARLQEQLDNLGLWQldsrinEVLEQLNLDpnaelssLSGGWLRKAALGRALVSGPR 176
Cdd:PRK13634 103 ----VEKDICFGPMNFGVSEedaKQKAREMIELVGLPE------ELLARSPFE-------LSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 177 VLLLDEPTNHLD----IETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13634 166 VLVLDEPTAGLDpkgrKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-223 |
2.21e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.67 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 29 NERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYeqdlvvarlqqdpprnvtgtvydfvaegiaeqaaylkgyhdvsqlv 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 109 mTDPSDKNLNELARLQEQLDNLGLWQLDSRinEVLEQlnldpnaelsslsggwlrkaALGRALVSGPRVLLLDEPTNHLD 188
Cdd:smart00382 36 -IDGEDILEEVLDQLLLIIVGGKKASGSGE--LRLRL--------------------ALALARKLKPDVLILDEITSLLD 92
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695765469 189 IET---------IDWLEGFLKTFKGTIIFISHDRSFIRNMATRI 223
Cdd:smart00382 93 AEQeallllleeLRLLLLLKSEKNLTVILTTNDEKDLGPALLRR 136
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
319-496 |
2.30e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 46.62 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 319 VFEMENVNYQVDGKVLIKDF---SAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLEVAYFDQHRAEL 394
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 -----DPDK-----TVMDNLAEGKQ------EVMVNGKPRHVLGY-LQDFmfhpkRAMTPVRaLSGGERNRLLLARLFLK 457
Cdd:PRK13642 84 gmvfqNPDNqfvgaTVEDDVAFGMEnqgiprEEMIKRVDEALLAVnMLDF-----KTREPAR-LSGGQKQRVAVAGIIAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695765469 458 PSNLLILDEPTNDLDVETLELLEELV----DGYQGTVMLVSHD 496
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIheikEKYQLTVLSITHD 200
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
139-231 |
2.42e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.13 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 139 INEVLEQLNL---DPNAELSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIET---IDWLEGFLKTFKGTIIFISHD 212
Cdd:TIGR02633 383 IGSAIQRLKVktaSPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSE 462
|
90
....*....|....*....
gi 695765469 213 RSFIRNMATRIVDLDRGKL 231
Cdd:TIGR02633 463 LAEVLGLSDRVLVIGEGKL 481
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-230 |
2.43e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 46.14 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILN---REQG----LDDGRIIYEQDLVVARLqqdpprnvtGTVYDFvaegia 92
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTgfyKPTGgtilLRGQHIEGLPGHQIARM---------GVVRTF------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 93 eQAAYL-KGYHDVSQLVMTDPSDKNLNELARL----------QEQLDNLGLWqldsrinevLEQLNLDP--NAELSSLSG 159
Cdd:PRK11300 87 -QHVRLfREMTVIENLLVAQHQQLKTGLFSGLlktpafrraeSEALDRAATW---------LERVGLLEhaNRQAGNLAY 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695765469 160 GWLRKAALGRALVSGPRVLLLDEPTNHLD-IETID---WLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNpKETKEldeLIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
39-231 |
2.60e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 39 GAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQDPPRNvtGTVYdfvaegIAEQAaylKGyhDVSQLVMTDPSDKNLN 118
Cdd:PRK10762 288 GAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN--GIVY------ISEDR---KR--DGLVLGMSVKENMSLT 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 119 ELarlqEQLDNLGLwqldsRINEVLEQLNLD----------PNAE--LSSLSGGWLRKAALGRALVSGPRVLLLDEPTNH 186
Cdd:PRK10762 355 AL----RYFSRAGG-----SLKHADEQQAVSdfirlfniktPSMEqaIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695765469 187 LDIETIDWLEGFLKTFKG---TIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK10762 426 VDVGAKKEIYQLINQFKAeglSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
30-232 |
2.81e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.16 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 30 ERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQ---DLVVARLQQDPPRNVtgtvydfvaegiaeqaaylkgyhdvsQ 106
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqriDTLSPGKLQALRRDI--------------------------Q 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 107 LVMTDPS---DKNLNELARLQEQLDNLGLWQLD---SRINEVLEQLNLDPNAELS---SLSGGWLRKAALGRALVSGPRV 177
Cdd:PRK10261 405 FIFQDPYaslDPRQTVGDSIMEPLRVHGLLPGKaaaARVAWLLERVGLLPEHAWRyphEFSGGQRQRICIARALALNPKV 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 178 LLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK10261 485 IIADEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-191 |
3.00e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 45.72 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqglddGRIIYEQDLVVARLQQDP-PRNVTGtVYDFVAEGIAEQA 95
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA-------GALKGTPVAGCVDVPDNQfGREASL-IDAIGRKGDFKDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 96 AYLkgyhdvsqlvmtdpsdknlnelarlqeqLDNLGLwqldsriNEVleQLNLDPNAELSSlsgGWLRKAALGRALVSGP 175
Cdd:COG2401 116 VEL----------------------------LNAVGL-------SDA--VLWLRRFKELST---GQKFRFRLALLLAERP 155
|
170
....*....|....*.
gi 695765469 176 RVLLLDEPTNHLDIET 191
Cdd:COG2401 156 KLLVIDEFCSHLDRQT 171
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
18-250 |
3.35e-05 |
|
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: 46.00 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNReqglddgriiyeqdlvvarlqqdpprnVTGTVYDFVAEGIAEQAAY 97
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLR---------------------------LLNTEGDIQIDGVSWNSVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 98 L----KGYHDVSQ--LVMTDPSDKNLNELARLQEQldnlGLWQ------LDSRINEVLEQLNLDPNAELSSLSGGWLRKA 165
Cdd:cd03289 72 LqkwrKAFGVIPQkvFIFSGTFRKNLDPYGKWSDE----EIWKvaeevgLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 166 ALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLK-TFKGTIIFISHDRSFIRNMATRIVDLDRGKLVTYpgNYDQYLLD 244
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKqAFADCTVILSEHRIEAMLECQRFLVIEENKVRQY--DSIQKLLN 225
|
....*.
gi 695765469 245 KEEALR 250
Cdd:cd03289 226 EKSHFK 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
318-472 |
3.79e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 45.78 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 318 IVFEMENVNYQVDG---KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAYFDQhrael 394
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKN----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 dpdktvmDNLAEGKQEV-MVNGKPRHVL---GYLQDFMFHP-----------KRAMTPVR--------------ALSGGE 445
Cdd:PRK13634 78 -------KKLKPLRKKVgIVFQFPEHQLfeeTVEKDICFGPmnfgvseedakQKAREMIElvglpeellarspfELSGGQ 150
|
170 180
....*....|....*....|....*..
gi 695765469 446 RNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
317-473 |
3.85e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.79 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 317 KIVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGqlkadsgriHVGTKL---EVAYFDQHRAE 393
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG---------HPAYKIlegDILFKGESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 LDPDK-------------------TVMDNL-----AEGKQEVMVNGKPRHVLGYLQDFMfhPKRAMTPV-------RALS 442
Cdd:CHL00131 76 LEPEErahlgiflafqypieipgvSNADFLrlaynSKRKFQGLPELDPLEFLEIINEKL--KLVGMDPSflsrnvnEGFS 153
|
170 180 190
....*....|....*....|....*....|.
gi 695765469 443 GGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDI 184
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
342-376 |
4.11e-05 |
|
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: 46.71 E-value: 4.11e-05
10 20 30
....*....|....*....|....*....|....*
gi 695765469 342 IQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRI 376
Cdd:COG4615 355 IRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
307-471 |
4.24e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.58 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 307 MQVEEAArsGKIVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKL 382
Cdd:PRK15439 1 MQTSDTT--APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGgnpcARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 383 EVA-------YFDQHRAELDPDKTVMDNLAEGKQEVMVNGKPRHVLgyLQDFMFHPKRAMtPVRALSGGERNRLLLARLF 455
Cdd:PRK15439 79 TPAkahqlgiYLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQL--LAALGCQLDLDS-SAGSLEVADRQIVEILRGL 155
|
170
....*....|....*.
gi 695765469 456 LKPSNLLILDEPTNDL 471
Cdd:PRK15439 156 MRDSRILILDEPTASL 171
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
12-232 |
4.61e-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: 46.35 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFS---DSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLvvARLQQDPPRNVTGTV---- 83
Cdd:COG5265 364 SFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlIDGQDI--RDVTQASLRAAIGIVpqdt 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 84 ---YDFVAEGIA-----------EQAAYLKGYHDVsqlvmtdpsdknlneLARLQEQLDNL----GLwqldsrinevleq 145
Cdd:COG5265 442 vlfNDTIAYNIAygrpdaseeevEAAARAAQIHDF---------------IESLPDGYDTRvgerGL------------- 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 146 lnldpnaelsSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIET---IdwLEGFLKTFKG-TIIFISHDRSFIRNmAT 221
Cdd:COG5265 494 ----------KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTeraI--QAALREVARGrTTLVIAHRLSTIVD-AD 560
|
250
....*....|.
gi 695765469 222 RIVDLDRGKLV 232
Cdd:COG5265 561 EILVLEAGRIV 571
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
321-496 |
4.62e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 45.59 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNY--------QVDGkvlIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAyfdqhra 392
Cdd:PRK13641 4 KFENVDYiyspgtpmEKKG---LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 393 eldpdKTVMDNLAEGKQEV-MVNGKPRHVL---GYLQDFMFHPK-----------RAMTPVRA--------------LSG 443
Cdd:PRK13641 74 -----ETGNKNLKKLRKKVsLVFQFPEAQLfenTVLKDVEFGPKnfgfsedeakeKALKWLKKvglsedliskspfeLSG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 444 GERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDGYQG---TVMLVSHD 496
Cdd:PRK13641 149 GQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHN 204
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-268 |
4.71e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 46.24 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 14 SDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYeQDLVVARLQQDPPRN----VTGTVY---DF 86
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF-HDIPLTKLQLDSWRSrlavVSQTPFlfsDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 87 VAEGIA-----------EQAAYLKGYHDvsqlvmtdpsdknlnELARLQEQLDnlglwqldsriNEVLEQLNLdpnaels 155
Cdd:PRK10789 405 VANNIAlgrpdatqqeiEHVARLASVHD---------------DILRLPQGYD-----------TEVGERGVM------- 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 156 sLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTF-KGTIIFISHDRSFIRNMATRIVDLDRG----- 229
Cdd:PRK10789 452 -LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWgEGRTVIISAHRLSALTEASEILVMQHGhiaqr 530
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 695765469 230 ----KLVTYPGNY-DQYlldkeealRVEELQNAEFDRKLAQEEV 268
Cdd:PRK10789 531 gnhdQLAQQSGWYrDMY--------RYQQLEAALDDAPEIREEA 566
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
315-472 |
5.58e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 45.38 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 315 SGKIVfeMENVNYQVDGKV-----LIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGT--------- 380
Cdd:PRK13645 4 SKDII--LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 381 -------KLEVAY-FDQHRAELDPDKTVMD------NLAEGKQEVMvnGKPRHVLGYLQDFMFHPKRamTPVRaLSGGER 446
Cdd:PRK13645 82 ikevkrlRKEIGLvFQFPEYQLFQETIEKDiafgpvNLGENKQEAY--KKVPELLKLVQLPEDYVKR--SPFE-LSGGQK 156
|
170 180
....*....|....*....|....*.
gi 695765469 447 NRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLD 182
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-63 |
5.62e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 5.62e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 695765469 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILN--REQGLDDGRIIYE 63
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvYPHGSYEGEILFD 63
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-189 |
5.67e-05 |
|
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: 45.05 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 34 LVGRNGAGKSTLMKILNREQGLDDGRiiyeqdlvvarlQQDPPrNVTGTVYDFVAEGIAEQAAYLKGyHDVS-----QLV 108
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGK------------FDDPP-DWDEILDEFRGSELQNYFTKLLE-GDVKvivkpQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 109 MTDPS--DKNLNELARLQEQLDNLglwqldsriNEVLEQLNLDP--NAELSSLSGGWLRKAALGRALVSGPRVLLLDEPT 184
Cdd:cd03236 97 DLIPKavKGKVGELLKKKDERGKL---------DELVDQLELRHvlDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
....*
gi 695765469 185 NHLDI 189
Cdd:cd03236 168 SYLDI 172
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-216 |
6.31e-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: 44.63 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 14 SDSPLLDNAELHIEDNERVCLVGRNGAGKSTLM-KILNREQGLDdGRIIYEQDLVVARLQQDPPRNVTGTVydfvaeGIA 92
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLE-GKVHWSNKNESEPSFEATRSRNRYSV------AYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 93 EQAAYLKGYHDVSQLVMTDPSDKNlnelarlqeqldnlglwqldsRINEVLEQLNLDPNAEL-------------SSLSG 159
Cdd:cd03290 85 AQKPWLLNATVEENITFGSPFNKQ---------------------RYKAVTDACSLQPDIDLlpfgdqteigergINLSG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695765469 160 GWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWL--EGFLKTF---KGTIIFISHDRSFI 216
Cdd:cd03290 144 GQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLmqEGILKFLqddKRTLVLVTHKLQYL 205
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-229 |
6.38e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 45.08 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 3 LISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVAR-------LQQD- 74
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaergvvFQNEg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 75 --PPRNVTgtvyDFVAEGIaeqaaylkgyhdvsQLVMTDPSDKnlneLARLQEQLDNLGLWQLDSRInevleqlnldpna 152
Cdd:PRK11248 81 llPWRNVQ----DNVAFGL--------------QLAGVEKMQR----LEIAHQMLKKVGLEGAEKRY------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 153 eLSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWL-EGFLKTFKGT---IIFISHDRSFIRNMATRIVDLDR 228
Cdd:PRK11248 126 -IWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMqTLLLKLWQETgkqVLLITHDIEEAVFMATELVLLSP 204
|
.
gi 695765469 229 G 229
Cdd:PRK11248 205 G 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
332-472 |
7.04e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 45.00 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 332 KVLIKDFSAQIQRGdkiaLIGPNGCGKTTLLKLMLGQLKADSGRI-HVGTKLEVA-----YFDQHRAEL--DPDKTV--- 400
Cdd:PRK13638 18 KGLNLDFSLSPVTG----LVGANGCGKSTLFMNLSGLLRPQKGAVlWQGKPLDYSkrgllALRQQVATVfqDPEQQIfyt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 401 ---------MDNLAEGKQEVMVNGKPRHVLGYLQDFMFHpkramtPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
Cdd:PRK13638 94 didsdiafsLRNLGVPEAEITRRVDEALTLVDAQHFRHQ------PIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
.
gi 695765469 472 D 472
Cdd:PRK13638 168 D 168
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
34-262 |
1.14e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 34 LVGRNGAGKSTLMKILNREQGLDDGRIIYE-----QDL-------VVARLQQDP-------PRNVTGTVYDFvaegiaEQ 94
Cdd:PTZ00265 416 FVGESGCGKSTILKLIERLYDPTEGDIIINdshnlKDInlkwwrsKIGVVSQDPllfsnsiKNNIKYSLYSL------KD 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 95 AAYLKGYHDVSQLVMTDPSD-------KNLNELARLQEQLDNLGLWQL--------DSRINEVLEQLNLD------PN-- 151
Cdd:PTZ00265 490 LEALSNYYNEDGNDSQENKNkrnscraKCAGDLNDMSNTTDSNELIEMrknyqtikDSEVVDVSKKVLIHdfvsalPDky 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 152 -----AELSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKGT----IIFISHDRSFIRNMATR 222
Cdd:PTZ00265 570 etlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNenriTIIIAHRLSTIRYANTI 649
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 695765469 223 IVDLDRGKlvtypGNYDQYLLDKEEALRVEELQNAEFDRK 262
Cdd:PTZ00265 650 FVLSNRER-----GSTVDVDIIGEDPTKDNKENNNKNNKD 684
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
328-472 |
1.35e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.87 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 328 QVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADS--GRIHVGTK------LEVAYFDQHRAELDPDKT 399
Cdd:PLN03211 77 QIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRkptkqiLKRTGFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 400 VMDNLAEGKQEVMVNGKPRHVLGYLQDFMFhPKRAMTP----------VRALSGGERNRLLLARLFLKPSNLLILDEPTN 469
Cdd:PLN03211 157 VRETLVFCSLLRLPKSLTKQEKILVAESVI-SELGLTKcentiignsfIRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
...
gi 695765469 470 DLD 472
Cdd:PLN03211 236 GLD 238
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
341-472 |
1.61e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.11 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 341 QIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRiHVGTKLEVAYFDQhrAELDPDKTVMDNLAEGKQ-EVMVNGKPRH 419
Cdd:PLN03130 639 DVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA-SVVIRGTVAYVPQ--VSWIFNATVRDNILFGSPfDPERYERAID 715
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 695765469 420 VLGYLQDFMFHPKRAMTPV--RA--LSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PLN03130 716 VTALQHDLDLLPGGDLTEIgeRGvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-188 |
1.99e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 44.62 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 14 SDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGriiyeqDLVVArlqqdpPRNVTGTVYDfvaegIAE 93
Cdd:TIGR01257 1950 TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG------DATVA------GKSILTNISD-----VHQ 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 94 QAAYLKGYHDVSQLVMtdpSDKNLNELARLQ----EQLDNLGLWQLDSRinevleQLNLDPNAELSSLSGGWLRKAALGR 169
Cdd:TIGR01257 2013 NMGYCPQFDAIDDLLT---GREHLYLYARLRgvpaEEIEKVANWSIQSL------GLSLYADRLAGTYSGGNKRKLSTAI 2083
|
170
....*....|....*....
gi 695765469 170 ALVSGPRVLLLDEPTNHLD 188
Cdd:TIGR01257 2084 ALIGCPPLVLLDEPTTGMD 2102
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
134-229 |
2.08e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.06 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 134 QLDSRINEV-----LEQLnLD--PNAelssLSGGWLRKAALGRALVSGPRVLLLDEPTNHLD--------IEtIDWLEGF 198
Cdd:PRK11650 110 EIEERVAEAarileLEPL-LDrkPRE----LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDaklrvqmrLE-IQRLHRR 183
|
90 100 110
....*....|....*....|....*....|.
gi 695765469 199 LKTfkgTIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:PRK11650 184 LKT---TSLYVTHDQVEAMTLADRVVVMNGG 211
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
302-472 |
2.65e-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: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 302 MGSAKMQVEEAAR---SGKIvfEMENVNYQV-DGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIH 377
Cdd:PRK10790 322 MDGPRQQYGNDDRplqSGRI--DIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 378 VGTK----LEVAYFDQHRAELDPDKTVM-----DNLAEGKQevMVNGKPRHVLGYLQ--DFMfhpkRAM-----TPV--- 438
Cdd:PRK10790 400 LDGRplssLSHSVLRQGVAMVQQDPVVLadtflANVTLGRD--ISEEQVWQALETVQlaELA----RSLpdglyTPLgeq 473
|
170 180 190
....*....|....*....|....*....|....*
gi 695765469 439 -RALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK10790 474 gNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
523-629 |
2.92e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 523 YHDARGQQAQyLAQKQQISKKAVEAAQPKAESVKRASGKLSY-----NLQRELEQLPQRLEELETQLQTLQEQVADPSFF 597
Cdd:COG4717 90 YAELQEELEE-LEEELEELEAELEELREELEKLEKLLQLLPLyqeleALEAELAELPERLEELEERLEELRELEEELEEL 168
|
90 100 110
....*....|....*....|....*....|....*..
gi 695765469 598 GQSHDHTQQVLAQL-----AEAEQALETAFERWEYLE 629
Cdd:COG4717 169 EAELAELQEELEELleqlsLATEEELQDLAEELEELQ 205
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
321-580 |
3.53e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 42.81 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 321 EMENVNYQ------VDGKVLIkDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKLEVAyfDQHRAEL 394
Cdd:PRK13649 4 NLQNVSYTyqagtpFEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITS--TSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 395 DP-----------------DKTVMDNLAEGKQEVMVNGKPR--------HVLGYLQDFmfhpkRAMTPVRaLSGGERNRL 449
Cdd:PRK13649 81 KQirkkvglvfqfpesqlfEETVLKDVAFGPQNFGVSQEEAealareklALVGISESL-----FEKNPFE-LSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 450 LLARLFLKPSNLLILDEPTNDLDVETLELLEELVDG-YQG--TVMLVSHDRQFVDNTVTECWIFEgEGRIgqYVGGYHDA 526
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKlHQSgmTIVLVTHLMDDVANYADFVYVLE-KGKL--VLSGKPKD 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 695765469 527 RGQQAQYLAQKQQISKKAVEAAQPKAESvkrasgklSYNLQReleqLPQRLEEL 580
Cdd:PRK13649 232 IFQDVDFLEEKQLGVPKITKFAQRLADR--------GISFSS----LPITIEEF 273
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
439-549 |
3.65e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 439 RALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELV----DGYQGTVMLVSHDRQFVDNTvTECWIFEGEG 514
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKADKTIITIAHRIASIKRS-DKIVVFNNPD 1435
|
90 100 110
....*....|....*....|....*....|....*
gi 695765469 515 RIGQYVggyhDARGQQAQYLAQKQQISKKAVEAAQ 549
Cdd:PTZ00265 1436 RTGSFV----QAHGTHEELLSVQDGVYKKYVKLAK 1466
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-201 |
4.04e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.14 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 3 LISMHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlvvarlQQDPPRNVTGT 82
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI-----------QIDGKTATRGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 83 VYDFVA-----EGIAEQAAYLKGYHDVSQLVMTDPSDKNLNELA--RLQEQLDNLglwqldsrinevleqlnldpnaeLS 155
Cdd:PRK13543 80 RSRFMAylghlPGLKADLSTLENLHFLCGLHGRRAKQMPGSALAivGLAGYEDTL-----------------------VR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695765469 156 SLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKT 201
Cdd:PRK13543 137 QLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISA 182
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
137-261 |
4.05e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.19 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 137 SRINEVLEQLNLDPNA--ELSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETID--WLEGFLKTFKG-TIIFISH 211
Cdd:NF000106 123 ARADELLERFSLTEAAgrAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNevWDEVRSMVRDGaTVLLTTQ 202
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 695765469 212 DRSFIRNMATRIVDLDRGKLVTyPGNYDQYLLD-KEEALRVEELQNAEFDR 261
Cdd:NF000106 203 YMEEAEQLAHELTVIDRGRVIA-DGKVDELKTKvGGRTLQIRPAHAAELDR 252
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
158-220 |
4.94e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 42.64 E-value: 4.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765469 158 SGGWLRKAALGRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIFISHDRSFIRNMA 220
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVsvqaQVLNLMMDLQQELGLSYVFISHDLSVVEHIA 222
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-232 |
5.04e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 6 MHGAWLSFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLVVARLQQDPPRNVTGTVY- 84
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 85 --DFVAEGIAEQAAYLKGYHDVSQLVmtdPSDKNLNELARLQEQLDnlglwqldsrinevleqLNLDPNAELSSLSGGWL 162
Cdd:PRK10982 81 elNLVLQRSVMDNMWLGRYPTKGMFV---DQDKMYRDTKAIFDELD-----------------IDIDPRAKVATLSVSQM 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695765469 163 RKAALGRALVSGPRVLLLDEPTNHLDIETIDWLEGFLKTFKGT---IIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK10982 141 QMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERgcgIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
335-496 |
5.72e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 42.71 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 335 IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG----TKLEVAYFDQHRAE----------LDPDKTV 400
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiAKISDAELREVRRKkiamvfqsfaLMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 401 MDNLAEGKQEVMVNGKPRH--VLGYLQDFMFHPKRAMTPvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLEL 478
Cdd:PRK10070 124 LDNTAFGMELAGINAEERRekALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180
....*....|....*....|..
gi 695765469 479 LEELV----DGYQGTVMLVSHD 496
Cdd:PRK10070 203 MQDELvklqAKHQRTIVFISHD 224
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
154-231 |
6.42e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 154 LSSLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGtIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:PRK10982 389 IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVgakfEIYQLIAELAKKDKG-IIIISSEMPELLGITDRILVMSNG 467
|
..
gi 695765469 230 KL 231
Cdd:PRK10982 468 LV 469
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-472 |
7.91e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 41.44 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 349 ALIGPNGCGKTTLLKLM--LGQLKAD---SGRIHVGT----KLEVAYFdQHRAEL-------DPDKTVMDNLAEG-KQEV 411
Cdd:PRK14247 33 ALMGPSGSGKSTLLRVFnrLIELYPEarvSGEVYLDGqdifKMDVIEL-RRRVQMvfqipnpIPNLSIFENVALGlKLNR 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765469 412 MVNGKP------RHVLGYLQDFMFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK14247 112 LVKSKKelqervRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
322-471 |
8.92e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 322 MENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKlEVAYFDQHRA--------- 392
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK-EIDFKSSKEAlengismvh 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 393 -ELD--PDKTVMDNLAEGKQevmvngkPRHVLGYLQDFMFHPKRAM-----------TPVRALSGGERNRLLLARLFLKP 458
Cdd:PRK10982 80 qELNlvLQRSVMDNMWLGRY-------PTKGMFVDQDKMYRDTKAIfdeldididprAKVATLSVSQMQMIEIAKAFSYN 152
|
170
....*....|...
gi 695765469 459 SNLLILDEPTNDL 471
Cdd:PRK10982 153 AKIVIMDEPTSSL 165
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-192 |
8.95e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.09 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 13 FSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMK----ILNREQG--------LDDGRIIYEQDLVVARLQQDPPRNVT 80
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKliagLLNPEKGeilferqsIKKDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 81 gtvydfvaegIAEQAaylkgYHDVSqlvmTDPSDKNLNELARLQEqldnlglwqldsrinevLEQLnLDPNAELssLSGG 160
Cdd:PRK13540 91 ----------LRENC-----LYDIH----FSPGAVGITELCRLFS-----------------LEHL-IDYPCGL--LSSG 131
|
170 180 190
....*....|....*....|....*....|....*
gi 695765469 161 WLRKAALGRALVSGPRVLLLDEPTNHLD---IETI 192
Cdd:PRK13540 132 QKRQVALLRLWMSKAKLWLLDEPLVALDelsLLTI 166
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-242 |
1.12e-03 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 41.11 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 24 LHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLVVArlqqdPP--RNVTgtvydfvaegIAEQAAYLKG 100
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtLNGQDHTTT-----PPsrRPVS----------MLFQENNLFS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 101 YHDVSQ---LVMtDPSDK-NLNELARLQEQLDNLGLWQLDSRInevleqlnldPnaelSSLSGGWLRKAALGRALVSGPR 176
Cdd:PRK10771 85 HLTVAQnigLGL-NPGLKlNAAQREKLHAIARQMGIEDLLARL----------P----GQLSGGQRQRVALARCLVREQP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 177 VLLLDEPTNHLD----IETIDWLEGFLKTFKGTIIFISHDRSFIRNMATRIVDLDRGKLVtYPGNYDQYL 242
Cdd:PRK10771 150 ILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA-WDGPTDELL 218
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
316-500 |
1.24e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 41.05 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 316 GKIVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIhVGTKLEVAYFDQH----- 390
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKI-VIDGIDISKLPLHtlrsr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 391 ---------------RAELDPDKTVMDN-----LAEGKQEVMVNGKPrhvlGYLQDFMFHPKRAmtpvraLSGGERNRLL 450
Cdd:cd03288 97 lsiilqdpilfsgsiRFNLDPECKCTDDrlweaLEIAQLKNMVKSLP----GGLDAVVTEGGEN------FSVGQRQLFC 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695765469 451 LARLFLKPSNLLILDEPTNDLDVETLELLeelvdgyQGTVMLVSHDRQFV 500
Cdd:cd03288 167 LARAFVRKSSILIMDEATASIDMATENIL-------QKVVMTAFADRTVV 209
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
12-211 |
1.49e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.78 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 12 SFSDSPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLD--DGRIIYEQDLVvarLQQDP-------------- 75
Cdd:CHL00131 16 SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESI---LDLEPeerahlgiflafqy 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 76 PRNVTG-TVYDFVaegiaeQAAYlkgyhdvsqlvmtdpsdkNLNELARLQEQLDNLGLWQLdsrINEVLEQLNLDPNAeL 154
Cdd:CHL00131 93 PIEIPGvSNADFL------RLAY------------------NSKRKFQGLPELDPLEFLEI---INEKLKLVGMDPSF-L 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695765469 155 S-----SLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIETIDWL-EGF--LKTFKGTIIFISH 211
Cdd:CHL00131 145 SrnvneGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIaEGInkLMTSENSIILITH 209
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
138-232 |
2.58e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.50 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 138 RINEVLEQLNL-DPNAELS----SLSGGWLRKAALGRALVSGPRVLLLDEPTNHLDI----ETIDWLEGFLKTFKGTIIF 208
Cdd:PRK11022 130 RAIDLLNQVGIpDPASRLDvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELLLELQQKENMALVL 209
|
90 100
....*....|....*....|....
gi 695765469 209 ISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK11022 210 ITHDLALVAEAAHKIIVMYAGQVV 233
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
349-473 |
3.17e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 40.24 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 349 ALIGPNGCGKTTLLKLMLGQLKADSGRIHVGT---------------KLEVAY-FDQHRaeLDPDKTVMDNLAEGKQEVM 412
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaekgiclppeKRRIGYvFQDAR--LFPHYKVRGNLRYGMAKSM 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765469 413 VNGKPRHV--LG---YLQDFmfhpkramtPvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK11144 106 VAQFDKIValLGiepLLDRY---------P-GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
331-468 |
3.50e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.49 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 331 GKVL-IKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHV-GTKLEVAyfdQHRAE--------------- 393
Cdd:NF033858 12 GKTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlGGDMADA---RHRRAvcpriaympqglgkn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 LDPDKTVMDNL-----------AEGKQEVmvngkpRHVL---GyLQDFmfhPKRamtPVRALSGGERNRL-LLARLFLKP 458
Cdd:NF033858 89 LYPTLSVFENLdffgrlfgqdaAERRRRI------DELLratG-LAPF---ADR---PAGKLSGGMKQKLgLCCALIHDP 155
|
170
....*....|
gi 695765469 459 sNLLILDEPT 468
Cdd:NF033858 156 -DLLILDEPT 164
|
|
| 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
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
341-500 |
5.99e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 38.82 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 341 QIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRI-------------HVGTKLEVAYFdQHrAELDPDKTVMDNLaeg 407
Cdd:PRK11300 27 EVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIllrgqhieglpghQIARMGVVRTF-QH-VRLFREMTVIENL--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 408 kqevMVnGKPRHV-LGYLQDFMFHP----------KRAMT-------------PVRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK11300 102 ----LV-AQHQQLkTGLFSGLLKTPafrraesealDRAATwlervgllehanrQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695765469 464 LDEPTNDLDVETLELLEELVDG----YQGTVMLVSHDRQFV 500
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIAElrneHNVTVLLIEHDMKLV 217
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
437-500 |
6.20e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 6.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765469 437 PVRALSGGERNRLLLARLFLKPS---NLLILDEPTNDL---DVETLELLEELVDgYQG-TVMLVSHDRQFV 500
Cdd:PRK00635 806 PLSSLSGGEIQRLKLAYELLAPSkkpTLYVLDEPTTGLhthDIKALIYVLQSLT-HQGhTVVIIEHNMHVV 875
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
335-498 |
6.24e-03 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 39.71 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 335 IKDFSAQIQRGDKIALIGPNGCGKTTLLKLmLGQL-KADSGRIHVGtklevayfDQHRAELDPDKT-------------- 399
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNI-LGCLdKPTSGTYRVA--------GQDVATLDADALaqlrrehfgfifqr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 400 --VMDNL-AEGKQEV--MVNGKPRHV-----------LGYLQDFMFHPKRamtpvraLSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK10535 95 yhLLSHLtAAQNVEVpaVYAGLERKQrllraqellqrLGLEDRVEYQPSQ-------LSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 695765469 464 LDEPTNDLDVETLELLEELVDGY--QG-TVMLVSHDRQ 498
Cdd:PRK10535 168 ADEPTGALDSHSGEEVMAILHQLrdRGhTVIIVTHDPQ 205
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
349-472 |
6.33e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 38.99 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 349 ALIGPNGCGKTTLLKLM--LGQLKAD---SGRI-HVGTKLEVAYFD--QHRAEL-----DPDK---TVMDNLAEGkqeVM 412
Cdd:PRK14239 35 ALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIvYNGHNIYSPRTDtvDLRKEIgmvfqQPNPfpmSIYENVVYG---LR 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695765469 413 VNG-KPRHVLGYLQDFMFHPKRAMTPVR--------ALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK14239 112 LKGiKDKQVLDEAVEKSLKGASIWDEVKdrlhdsalGLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
315-507 |
6.35e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.96 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 315 SGKIVFEMENVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVgTKLEVAYF---DQHR 391
Cdd:PLN03232 1232 RGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMI-DDCDVAKFgltDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 392 A-ELDPDKTVM---------DNLAEGKQEVMVNGKPRhvlGYLQDFMFHPKRAMTPV-----RALSGGERNRLLLARLFL 456
Cdd:PLN03232 1311 VlSIIPQSPVLfsgtvrfniDPFSEHNDADLWEALER---AHIKDVIDRNPFGLDAEvseggENFSVGQRQLLSLARALL 1387
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695765469 457 KPSNLLILDEPTNDLDVETLELLEELV-DGYQGTVMLVSHDRQfvdNTVTEC 507
Cdd:PLN03232 1388 RRSKILVLDEATASVDVRTDSLIQRTIrEEFKSCTMLVIAHRL---NTIIDC 1436
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
350-406 |
6.55e-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: 6.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765469 350 LIGPNGCGKTTLLKLM----------LGQLKADSGRIHVGTKLE----VAYFDQHRAELDPDKTVMDNLAE 406
Cdd:COG3950 30 LVGENGSGKTTLLEAIalalsgllsrLDDVKFRKLLIRNGEFGDsaklILYYGTSRLLLDGPLKKLERLKE 100
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
437-471 |
7.06e-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: 39.61 E-value: 7.06e-03
10 20 30
....*....|....*....|....*....|....*...
gi 695765469 437 PVRALSGGERNRLLLARLFLKPSN---LLILDEPTNDL 471
Cdd:TIGR00630 826 PATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGL 863
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
332-504 |
8.09e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 38.61 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 332 KVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVG-----TKLEVAYFDQHRAELD-----PDKTVM 401
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDdititHKTKDKYIRPVRKRIGmvfqfPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 402 DNLAEgkQEVMVNGKPRHV---------------LGYLQDFMfhpkrAMTPVRaLSGGERNRLLLARLFLKPSNLLILDE 466
Cdd:PRK13646 100 EDTVE--REIIFGPKNFKMnldevknyahrllmdLGFSRDVM-----SQSPFQ-MSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695765469 467 PTNDLDVETLELLEELVDGYQ----GTVMLVSHDR----QFVDNTV 504
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHDMnevaRYADEVI 217
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
157-223 |
8.66e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 38.63 E-value: 8.66e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765469 157 LSGGWLRKAALGRALVSGPRVLLLDEPTNHLDIET----IDWLEGFLKTFKGTIIFISHDRSFIRNMATRI 223
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTqaqiFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-496 |
8.80e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 38.54 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 324 NVNYQVDGKVLIKDFSAQIQRGDKIALIGPNGCGKTTLLKLMLGQLKADSGRIHVGTKL----------EVAYFDQHRAE 393
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLlggrsifnyrDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 394 L--DPDK---TVMDNLAEG--------KQEVMVNGKPRHVLGYLQDFMfHPKRAMTPVRaLSGGERNRLLLARLFLKPSN 460
Cdd:PRK14271 106 LfqRPNPfpmSIMDNVLAGvrahklvpRKEFRGVAQARLTEVGLWDAV-KDRLSDSPFR-LSGGQQQLLCLARTLAVNPE 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 695765469 461 LLILDEPTNDLDVETLELLEELVDGYQG--TVMLVSHD 496
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
529-629 |
9.13e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765469 529 QQAQYLAQKQQISKKAVEAAQPKAESVKRA----SGKLSYNLQRELEQLPQRLEELETQLQTLQEQVADpsfFGQSHDHT 604
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQirgnGGDRLEQLEREIERLERELEERERRRARLEALLAA---LGLPLPAS 378
|
90 100
....*....|....*....|....*.
gi 695765469 605 QQVLAQL-AEAEQALETAFERWEYLE 629
Cdd:COG4913 379 AEEFAALrAEAAALLEALEEELEALE 404
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
153-219 |
9.53e-03 |
|
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: 37.97 E-value: 9.53e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695765469 153 ELSSLSGGWLRKA------ALGRALVSGPRVLLLDEPTNHLDIETIDW-----LEGFLKTFKGTIIFISHDRSFIRNM 219
Cdd:cd03240 112 MRGRCSGGEKVLAsliirlALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVDAA 189
|
|
| |
