|
Name |
Accession |
Description |
Interval |
E-value |
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-608 |
0e+00 |
|
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: 717.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPE-YARVSGSIRLHGKELLGLS 79
Cdd:COG4172 3 SMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpAAHPSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 80 DHAMSQIRGRMIGTVFQDPMSALTPVYTIGDQIAEAIEIHsREISRADARRRAVELLELVGIAQPERRARAFPHELSGGE 159
Cdd:COG4172 83 ERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLH-RGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 160 RQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAV 239
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 240 DELYRDRRMPYTVGLLGSVPRLDAAqgtrlipipgapptmtslspgactfaprcplaideclsaepdlvrvadghwaaci 319
Cdd:COG4172 242 AELFAAPQHPYTRKLLAAEPRGDPR------------------------------------------------------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 320 rtddvagrsaadvfgvstqPPPNNAaggqpPVVLRVSDLTKTYRLTKGvVVRRRVGEVRAVDGISFTLEQGRTLGIVGES 399
Cdd:COG4172 267 -------------------PVPPDA-----PPLLEARDLKVWFPIKRG-LFRRTVGHVKAVDGVSLTLRRGETLGLVGES 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 400 GSGKSTTLNQILELTKPEaGSIEILGTDVAVLDAAARRRLRTELQVVFQDPVASLDPRLPVYDVIAEPLRANGFH--RHE 477
Cdd:COG4172 322 GSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGlsAAE 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 478 CEERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYL 557
Cdd:COG4172 401 RRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYL 480
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 558 FVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLAAVPR 608
Cdd:COG4172 481 FISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPL 531
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-610 |
0e+00 |
|
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: 640.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETEDieVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYARVSGSIRLHGKELLGLSD 80
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGD--VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 hamsQIRGRMIGTVFQDPMSALTPVyTIGDQIAEAIEIhsREISRADARRRAVELLELVGIaqpERRARAFPHELSGGER 160
Cdd:COG1123 79 ----ALRGRRIGMVFQDPMTQLNPV-TVGDQIAEALEN--LGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 161 QRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVD 240
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 241 ELYRDRRMpytvglLGSVPRLDAAQGTRLIPIPGAPPtmtslspgactfaprcplaideclsaepdlvrvadghwaacir 320
Cdd:COG1123 229 EILAAPQA------LAAVPRLGAARGRAAPAAAAAEP------------------------------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 321 tddvagrsaadvfgvstqpppnnaaggqppvVLRVSDLTKTYRLTKGVVVRRRvgevravDGISFTLEQGRTLGIVGESG 400
Cdd:COG1123 260 -------------------------------LLEVRNLSKRYPVRGKGGVRAV-------DDVSLTLRRGETLGLVGESG 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 401 SGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRTELQVVFQDPVASLDPRLPVYDVIAEPLRANGFH-RHECE 479
Cdd:COG1123 302 SGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLsRAERR 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 480 ERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFV 559
Cdd:COG1123 382 ERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFI 461
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 560 SHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLAAVPRAH 610
Cdd:COG1123 462 SHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAAVPSLD 512
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-325 |
2.18e-172 |
|
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: 492.26 E-value: 2.18e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYARVSGSIRLHGKELLGLSDHAM 83
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 SQIRGRMIGTVFQDPMSALTPVYTIGDQIAEAIEIHsREISRADARRRAVELLELVGIAQPERRARAFPHELSGGERQRV 163
Cdd:COG0444 81 RKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIH-GGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 164 VIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELY 243
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 244 RDRRMPYTVGLLGSVPRLDAAqGTRLIPIPGAPPTMTSLSPGaCTFAPRCPLAIDECLSAEPDLVRVADGHWAACIRTDD 323
Cdd:COG0444 240 ENPRHPYTRALLSSIPRLDPD-GRRLIPIPGEPPSLLNPPSG-CRFHPRCPYAMDRCREEEPPLREVGPGHRVACHLYEE 317
|
..
gi 1424538268 324 VA 325
Cdd:COG0444 318 EA 319
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-609 |
1.78e-158 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 468.57 E-value: 1.78e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYARV--SGSIRLHGK-----ELL 76
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLvqCDKMLLRRRsrqviELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 77 GLSDHAMSQIRGRMIGTVFQDPMSALTPVYTIGDQIAEAIEIHsREISRADARRRAVELLELVGIAQPERRARAFPHELS 156
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLH-QGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 157 GGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEI 236
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 237 AAVDELYRDRRMPYTVGLLGSVPRLDAAQGTRLipipgapptmtslspgactfAPRCPL-AIDECLSAEPdlvrvadghw 315
Cdd:PRK10261 251 GSVEQIFHAPQHPYTRALLAAVPQLGAMKGLDY--------------------PRRFPLiSLEHPAKQEP---------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 316 aacirtddvagrsaadvfgvstQPPPNNAAGGQPpvVLRVSDLTKTYRLTKGVVVRRRVGEVRAvDGISFTLEQGRTLGI 395
Cdd:PRK10261 301 ----------------------PIEQDTVVDGEP--ILQVRNLVTRFPLRSGLLNRVTREVHAV-EKVSFDLWPGETLSL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 396 VGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRTELQVVFQDPVASLDPRLPVYDVIAEPLRANGF-H 474
Cdd:PRK10261 356 VGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLlP 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 475 RHECEERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGL 554
Cdd:PRK10261 436 GKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGI 515
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 555 SYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLAAVPRA 609
Cdd:PRK10261 516 AYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVA 570
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-604 |
4.01e-151 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 446.07 E-value: 4.01e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 2 TAVLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYARV--SGSIRLHGKELLGLS 79
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVypSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 80 DHAMSQIRGRMIGTVFQDPMSALTPVYTIGDQIAEAIEIHsREISRADARRRAVELLELVGIAQPERRARAFPHELSGGE 159
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLH-RGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 160 RQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAV 239
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 240 DELYRDRRMPYTVGLLGSVPRldaaqgtrlipipGAPPtmtslspgactfaprcPLAIDEclsaepdlvrvadghwaaci 319
Cdd:PRK15134 242 ATLFSAPTHPYTQKLLNSEPS-------------GDPV----------------PLPEPA-------------------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 320 rtddvagrsaadvfgvstqpppnnaaggqpPVVLRVSDLTKTYRLTKGVVVRRRVGEVRAVDgISFTLEQGRTLGIVGES 399
Cdd:PRK15134 273 ------------------------------SPLLDVEQLQVAFPIRKGILKRTVDHNVVVKN-ISFTLRPGETLGLVGES 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 400 GSGKSTTLNQILELTKPEaGSIEILGTDVAVLDAAARRRLRTELQVVFQDPVASLDPRLPVYDVIAEPLRAN--GFHRHE 477
Cdd:PRK15134 322 GSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHqpTLSAAQ 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 478 CEERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYL 557
Cdd:PRK15134 401 REQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYL 480
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1424538268 558 FVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLA 604
Cdd:PRK15134 481 FISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
346-610 |
1.36e-131 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 388.71 E-value: 1.36e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 346 GGQPPVVLRVSDLTKTYRLTKGVVVRRRVGEVRAvDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILG 425
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAV-DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 426 TDVAVLDAAARRRLRTELQVVFQDPVASLDPRLPVYDVIAEPLRANGFH-RHECEERVAELLAVVGLDHSDASRYPAEFS 504
Cdd:COG4608 80 QDITGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLAsKAERRERVAELLELVGLRPEHADRYPHEFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 505 GGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQ 584
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEI 239
|
250 260
....*....|....*....|....*.
gi 1424538268 585 GESDQVFTNPQHEYTRRLLAAVPRAH 610
Cdd:COG4608 240 APRDELYARPLHPYTQALLSAVPVPD 265
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
352-612 |
9.79e-114 |
|
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: 342.42 E-value: 9.79e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 352 VLRVSDLTKTYRLTKGVVVRRrvgevravDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEA---GSIEILGTDV 428
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAV--------DGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 429 AVLDAAARRRLR-TELQVVFQDPVASLDPRLPVYDVIAEPLRA-NGFHRHECEERVAELLAVVGLDHSD--ASRYPAEFS 504
Cdd:COG0444 73 LKLSEKELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPErrLDRYPHELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 505 GGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQ 584
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEE 232
|
250 260
....*....|....*....|....*...
gi 1424538268 585 GESDQVFTNPQHEYTRRLLAAVPRAHSD 612
Cdd:COG0444 233 GPVEELFENPRHPYTRALLSSIPRLDPD 260
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-320 |
1.39e-110 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 334.77 E-value: 1.39e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYARVSGSIRLHGKELLGLSD 80
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 HAMSQIRGRMIGTVFQDPMSALTPVYTIGDQIAEAIEIHSReISRADARRRAVELLELVGIAQPERRARAFPHELSGGER 160
Cdd:PRK09473 89 KELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKG-MSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 161 QRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVD 240
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNAR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 241 ELYRDRRMPYTVGLLGSVPRLDaAQGTRLIPIPGAPPTMTSLsPGACTFAPRCPLAIDECLSAePDLVRVADGHWAACIR 320
Cdd:PRK09473 248 DVFYQPSHPYSIGLLNAVPRLD-AEGESLLTIPGNPPNLLRL-PKGCPFQPRCPHAMEICSSA-PPLEEFGPGRLRACFK 324
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-326 |
1.22e-107 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 327.07 E-value: 1.22e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFE-------TEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlpeYARVSGSIRLHGK 73
Cdd:COG4608 4 AEPLLEVRDLKKHFPvrgglfgRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRL---EEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 74 ELLGLSDHAMSQIRgRMIGTVFQDPMSALTPVYTIGDQIAEAIEIHsREISRADARRRAVELLELVGIAqPERRARaFPH 153
Cdd:COG4608 81 DITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIH-GLASKAERRERVAELLELVGLR-PEHADR-YPH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 154 ELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRP 233
Cdd:COG4608 157 EFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 234 VEIAAVDELYRDRRMPYTVGLLGSVPRLDAAQGTRLIPIPGAPPTMTSLSPGaCTFAPRCPLAIDECLSAEPDLVRVADG 313
Cdd:COG4608 237 VEIAPRDELYARPLHPYTQALLSAVPVPDPERRRERIVLEGDVPSPLNPPSG-CRFHTRCPYAQDRCATEEPPLREVGPG 315
|
330
....*....|...
gi 1424538268 314 HWAACIRTDDVAG 326
Cdd:COG4608 316 HQVACHLAEEGSG 328
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-237 |
3.24e-107 |
|
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: 322.15 E-value: 3.24e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLpeyARVSGSIRLHGKELLGLSDhAM 83
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL---KPTSGSIIFDGKDLLKLSR-RL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 SQIRGRMIGTVFQDPMSALTPVYTIGDQIAEAIEIHSREISRADARRRAVELLELVGiaQPERRARAFPHELSGGERQRV 163
Cdd:cd03257 77 RKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVG--LPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 164 VIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIA 237
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
348-612 |
1.21e-101 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 311.90 E-value: 1.21e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 348 QPPVVLRVSDLTKTYRLTKGVVVRRRVGEVRavDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTD 427
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRGLFKPERLVKAL--DGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 428 VAVLDAAARRRLRTELQVVFQDPVASLDPRLPVYDVIAEPLRAN-GFHRHECEERVAELLAVVGLDHSDASRYPAEFSGG 506
Cdd:PRK11308 79 LLKADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINtSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 507 QKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGE 586
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGT 238
|
250 260
....*....|....*....|....*.
gi 1424538268 587 SDQVFTNPQHEYTRRLLAAVPRAHSD 612
Cdd:PRK11308 239 KEQIFNNPRHPYTQALLSATPRLNPD 264
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
352-585 |
3.86e-101 |
|
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: 306.74 E-value: 3.86e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 352 VLRVSDLTKTYRLTKGVVVRRrvgevravDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVL 431
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKAL--------DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 432 DAAARRRLRTELQVVFQDPVASLDPRLPVYDVIAEPLRANGFHRHECE--ERVAELLAVVGLDHSDASRYPAEFSGGQKQ 509
Cdd:cd03257 73 SRRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEArkEAVLLLLVGVGLPEEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 510 RIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQG 585
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
353-608 |
3.00e-98 |
|
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: 300.18 E-value: 3.00e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRltkgvvvrRRVGEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAvld 432
Cdd:COG1124 2 LEVRNLSVSYG--------QGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 433 AAARRRLRTELQVVFQDPVASLDPRLPVYDVIAEPLRANGFHRHEceERVAELLAVVGLDHSDASRYPAEFSGGQKQRIG 512
Cdd:COG1124 71 RRRRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDRE--ERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 513 IARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFT 592
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
250
....*....|....*.
gi 1424538268 593 NPQHEYTRRLLAAVPR 608
Cdd:COG1124 229 GPKHPYTRELLAASLA 244
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
381-607 |
2.57e-97 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 300.85 E-value: 2.57e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRTELQVVFQDPVASLDPRLPV 460
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRAngFH----RHECEERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVS 536
Cdd:PRK15079 118 GEIIAEPLRT--YHpklsRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 537 IQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLAAVP 607
Cdd:PRK15079 196 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVP 266
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-264 |
3.21e-92 |
|
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: 293.73 E-value: 3.21e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 2 TAVLEVTDLNVTFETEDI-EVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeyaRVSGSIRLHGKELLGLSD 80
Cdd:COG1123 258 EPLLEVRNLSKRYPVRGKgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR---PTSGSILFDGKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 HAMSQIRgRMIGTVFQDPMSALTPVYTIGDQIAEAIEIHsREISRADARRRAVELLELVGIaqPERRARAFPHELSGGER 160
Cdd:COG1123 335 RSLRELR-RRVQMVFQDPYSSLNPRMTVGDIIAEPLRLH-GLLSRAERRERVAELLERVGL--PPDLADRYPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 161 QRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVD 240
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
250 260
....*....|....*....|....
gi 1424538268 241 ELYRDRRMPYTVGLLGSVPRLDAA 264
Cdd:COG1123 491 EVFANPQHPYTRALLAAVPSLDPA 514
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
3-327 |
1.12e-88 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 278.16 E-value: 1.12e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 3 AVLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYARVSG-SIRLHGKELLGLSDH 81
Cdd:PRK11022 2 ALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAeKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 82 AMSQIRGRMIGTVFQDPMSALTPVYTIGDQIAEAIEIHSREiSRADARRRAVELLELVGIAQPERRARAFPHELSGGERQ 161
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGG-NKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 162 RVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDE 241
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 242 LYRDRRMPYTVGLLGSVPRLdAAQGTRLIPIPGAPPTMTSlSPGACTFAPRCPLAIDECLSAEPDLvRVADGHWAACIRT 321
Cdd:PRK11022 241 IFRAPRHPYTQALLRALPEF-AQDKARLASLPGVVPGKYD-RPNGCLLNPRCPYATDRCRAEEPAL-NMLAGRQSKCHYP 317
|
....*.
gi 1424538268 322 DDVAGR 327
Cdd:PRK11022 318 LDDAGR 323
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-264 |
4.75e-81 |
|
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: 255.50 E-value: 4.75e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSDHAMs 84
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPW---SGEVTFDGRPVTRRRRKAF- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 qiRGRmIGTVFQDPMSALTPVYTIGDQIAEAIEIHSReisrADARRRAVELLELVGIaqPERRARAFPHELSGGERQRVV 164
Cdd:COG1124 78 --RRR-VQMVFQDPYASLHPRHTVDRILAEPLRIHGL----PDREERIAELLEQVGL--PPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 165 IAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYR 244
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
250 260
....*....|....*....|
gi 1424538268 245 DRRMPYTVGLLGSVPRLDAA 264
Cdd:COG1124 229 GPKHPYTRELLAASLAFERA 248
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
353-605 |
4.00e-80 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 253.61 E-value: 4.00e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRLTKGVVVRRRVGEVravDGISFTLEQGRTLGIVGESGSGKSTtLNQILE-LTKPEAGSIEILGTDVAVL 431
Cdd:COG4167 5 LEVRNLSKTFKYRTGLFRRQQFEAV---KPVSFTLEAGQTLAIIGENGSGKST-LAKMLAgIIEPTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 432 DAAARRRLrteLQVVFQDPVASLDPRLPVYDVIAEPLRAN-GFHRHECEERVAELLAVVGL--DHsdASRYPAEFSGGQK 508
Cdd:COG4167 81 DYKYRCKH---IRMIFQDPNTSLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLlpEH--ANFYPHMLSSGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 509 QRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESD 588
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTA 235
|
250
....*....|....*..
gi 1424538268 589 QVFTNPQHEYTRRLLAA 605
Cdd:COG4167 236 EVFANPQHEVTKRLIES 252
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-262 |
5.97e-80 |
|
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: 261.93 E-value: 5.97e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFET-------EDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeyarVSGSIRLHGKELL 76
Cdd:COG4172 275 LLEARDLKVWFPIkrglfrrTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP----SEGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 77 GLSDHAMSQIRGRM-IgtVFQDPMSALTPVYTIGDQIAEAIEIHSREISRADARRRAVELLELVGIAqPERRARaFPHEL 155
Cdd:COG4172 351 GLSRRALRPLRRRMqV--VFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAERRARVAEALEEVGLD-PAARHR-YPHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 156 SGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVE 235
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
250 260
....*....|....*....|....*..
gi 1424538268 236 IAAVDELYRDRRMPYTVGLLGSVPRLD 262
Cdd:COG4172 507 QGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-324 |
2.11e-77 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 249.24 E-value: 2.11e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETED---------IEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKE 74
Cdd:PRK15079 8 LLEVADLKVHFDIKDgkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKA---TDGEVAWLGKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 75 LLGLSDHAMSQIRgRMIGTVFQDPMSALTPVYTIGDQIAEAIEIHSREISRADARRRAVELLELVGIAqPERRARaFPHE 154
Cdd:PRK15079 85 LLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLL-PNLINR-YPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 155 LSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPV 234
Cdd:PRK15079 162 FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 235 EIAAVDELYRDRRMPYTVGLLGSV----PRLDAAQGTRL----IPIPGAPPTmtslspgACTFAPRCPLAIDECLSAEPD 306
Cdd:PRK15079 242 ELGTYDEVYHNPLHPYTKALMSAVpipdPDLERNKTIQLlegeLPSPINPPS-------GCVFRTRCPIAGPECAKTRPV 314
|
330
....*....|....*...
gi 1424538268 307 LvRVADGHWAACIRTDDV 324
Cdd:PRK15079 315 L-EGSFRHAVSCLKVDPL 331
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
3-318 |
1.24e-75 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 244.43 E-value: 1.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 3 AVLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYARVSGS-IRLHGKELLGLSDH 81
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADrFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 82 AMSQIRGRMIGTVFQDPMSALTPVYTIGDQIAEAI---EIHSREISRADAR-RRAVELLELVGIAQPERRARAFPHELSG 157
Cdd:COG4170 82 ERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIpswTFKGKWWQRFKWRkKRAIELLHRVGIKDHKDIMNSYPHELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 158 GERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIA 237
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 238 AVDELYRDRRMPYTVGLLGSVP--RLDAAQGTRLIPIPGAPPTMTSLsPGACTFAPRCPLAIDECLSAePDLVRVaDGHW 315
Cdd:COG4170 242 PTEQILKSPHHPYTKALLRSMPdfRQPLPHKSRLNTLPGSIPPLQHL-PIGCRLGPRCPYAQKKCVET-PRLRKI-KGHE 318
|
...
gi 1424538268 316 AAC 318
Cdd:COG4170 319 FAC 321
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-329 |
2.03e-75 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 243.72 E-value: 2.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFE------TEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIglLPEyARVSGSIRLHGKE 74
Cdd:PRK11308 2 QQPLLQAIDLKKHYPvkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLT--MIE-TPTGGELYYQGQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 75 LLGLSDHAMSQIRgRMIGTVFQDPMSALTPVYTIGDQIAEAIEIHSrEISRADARRRAVELLELVGIaQPERRARaFPHE 154
Cdd:PRK11308 79 LLKADPEAQKLLR-QKIQIVFQNPYGSLNPRKKVGQILEEPLLINT-SLSAAERREKALAMMAKVGL-RPEHYDR-YPHM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 155 LSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPV 234
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 235 EIAAVDELYRDRRMPYTVGLLGSVPRLDAAQGTRLIPIPGAPPTMTSLSPGaCTFAPRCPLAIDECLSAEPDLvRVADGH 314
Cdd:PRK11308 235 EKGTKEQIFNNPRHPYTQALLSATPRLNPDDRRERIKLTGELPSPLNPPPG-CAFNARCPRAFGRCRQEQPQL-RDYDGR 312
|
330
....*....|....*
gi 1424538268 315 WAACIRTDDVAGRSA 329
Cdd:PRK11308 313 LVACFAVEQDENPQA 327
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
353-608 |
9.67e-73 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 236.90 E-value: 9.67e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRLTKGVVVRRrvgevravDGISFTLEQGRTLGIVGESGSGKST---TLNQiLEltKPEAGSIEILGTDVA 429
Cdd:COG1135 2 IELENLSKTFPTKGGPVTAL--------DDVSLTIEKGEIFGIIGYSGAGKSTlirCINL-LE--RPTSGSVLVDGVDLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 430 VLDAAARRRLRTELQVVFQDpvASLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGL-DHSDAsrYPAEFSGGQK 508
Cdd:COG1135 71 ALSERELRAARRKIGMIFQH--FNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLsDKADA--YPSQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 509 QRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESD 588
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVL 226
|
250 260
....*....|....*....|
gi 1424538268 589 QVFTNPQHEYTRRLLAAVPR 608
Cdd:COG1135 227 DVFANPQSELTRRFLPTVLN 246
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
352-595 |
4.55e-69 |
|
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: 223.61 E-value: 4.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 352 VLRVSDLTKTYRLTKGVVVRRrvgevravDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVL 431
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTAL--------KDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 432 DAAARRRLRTELQVVFQDpvASLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRI 511
Cdd:cd03258 73 SGKELRKARRRIGMIFQH--FNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDK-ADAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 512 GIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVF 591
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
....
gi 1424538268 592 TNPQ 595
Cdd:cd03258 230 ANPQ 233
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
352-610 |
5.08e-69 |
|
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: 224.68 E-value: 5.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 352 VLRVSDLTKTYRlTKGVVVRRRVGEVRavDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVL 431
Cdd:TIGR02769 2 LLEVRDVTHTYR-TGGLFGAKQRAPVL--TNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 432 DAAARRRLRTELQVVFQDPVASLDPRLPVYDVIAEPLR-ANGFHRHECEERVAELLAVVGLDHSDASRYPAEFSGGQKQR 510
Cdd:TIGR02769 79 DRKQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 511 IGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQV 590
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQL 238
|
250 260
....*....|....*....|
gi 1424538268 591 FTNpQHEYTRRLLAAVPRAH 610
Cdd:TIGR02769 239 LSF-KHPAGRNLQSAVLPEH 257
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-256 |
6.55e-69 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 223.40 E-value: 6.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 23 AVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEYARVSGSIRLHGKELLGLSdhamsqIRGRMIGTVFQDPMSA 101
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLpPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 102 LTPVYTIGDQIAEAIEIHsrEISRADARRRAVELLELVGIAQPERRARAFPHELSGGERQRVVIAIAIANDPDLLICDEP 181
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSL--GKLSKQARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 182 TTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDRRMPYTVGLLG 256
Cdd:TIGR02770 153 TTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
352-611 |
2.42e-68 |
|
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: 230.95 E-value: 2.42e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 352 VLRVSDLTKTYRltkgvvvrrrVGEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEA---GSIEILGTDV 428
Cdd:COG1123 4 LLEVRDLSVRYP----------GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 429 AVLDAAARRRlrtELQVVFQDPVASLDPrLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQK 508
Cdd:COG1123 74 LELSEALRGR---RIGMVFQDPMTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERR-LDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 509 QRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESD 588
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
250 260
....*....|....*....|...
gi 1424538268 589 QVFTNPQheytrrLLAAVPRAHS 611
Cdd:COG1123 229 EILAAPQ------ALAAVPRLGA 245
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
352-606 |
3.80e-67 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 219.68 E-value: 3.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 352 VLRVSDLTKTYrltkgvvvRRRVGEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILG-----T 426
Cdd:COG4107 8 LLSVRGLSKRY--------GPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDrdggpR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 427 DVAVLDAAARRRL-RTELQVVFQDPVASLDPRLPVYDVIAEPLRANGfHRH--ECEERVAELLAVVGLDHSDASRYPAEF 503
Cdd:COG4107 80 DLFALSEAERRRLrRTDWGMVYQNPRDGLRMDVSAGGNIAERLMAAG-ERHygDIRARALEWLERVEIPLERIDDLPRTF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 504 SGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVE 583
Cdd:COG4107 159 SGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVE 238
|
250 260
....*....|....*....|...
gi 1424538268 584 QGESDQVFTNPQHEYTRRLLAAV 606
Cdd:COG4107 239 SGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-238 |
1.16e-66 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 217.22 E-value: 1.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIGLL--PEyarvSGSIRLHGKELLGL 78
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTL-LNILGGLdrPT----SGEVLIDGQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 79 SDHAMSQIRGRMIGTVFQDPmsALTPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGIAQperRARAFPHELSGG 158
Cdd:COG1136 76 SERELARLRRRHIGFVFQFF--NLLPELTALENVALPLLL--AGVSRKERRERARELLERVGLGD---RLDHRPSQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 159 ERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLgVVSEFADRALVMYAGRPVEIAA 238
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVSDER 227
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-318 |
3.73e-65 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 216.98 E-value: 3.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYARVSGS-IRLHGKELLGLSDHA 82
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADrMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 83 MSQIRGRMIGTVFQDPMSALTPVYTIGDQIAEAI---EIHSREISRADAR-RRAVELLELVGIAQPERRARAFPHELSGG 158
Cdd:PRK15093 83 RRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgwTYKGRWWQRFGWRkRRAIELLHRVGIKDHKDAMRSFPYELTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 159 ERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAA 238
Cdd:PRK15093 163 ECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 239 VDELYRDRRMPYTVGLLGSVPRLDAA--QGTRLIPIPGAPPTMTSLsPGACTFAPRCPLAIDECLSAEPdlVRVADGHWA 316
Cdd:PRK15093 243 SKELVTTPHHPYTQALIRAIPDFGSAmpHKSRLNTLPGAIPLLEHL-PIGCRLGPRCPYAQRECIETPR--LTGAKNHLY 319
|
..
gi 1424538268 317 AC 318
Cdd:PRK15093 320 AC 321
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
381-603 |
2.94e-62 |
|
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: 205.98 E-value: 2.94e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRTELQVVFQDPvASLDpRLPV 460
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRRIGMLFQGG-ALFD-SLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRAN-GFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQA 539
Cdd:COG1127 100 FENVAFPLREHtDLSEAEIRELVLEKLELVGLPGA-ADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 540 GIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPqHEYTRRLL 603
Cdd:COG1127 179 VIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
353-606 |
5.45e-62 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 206.46 E-value: 5.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRltkGVVVRRRVGEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLD 432
Cdd:PRK10419 4 LNVSGLSHHYA---HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 433 AAARRRLRTELQVVFQDPVASLDPRLPVYDVIAEPLR-ANGFHRHECEERVAELLAVVGLDHSDASRYPAEFSGGQKQRI 511
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 512 GIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEqgesDQVF 591
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE----TQPV 236
|
250
....*....|....*...
gi 1424538268 592 TNPQ---HEYTRRLLAAV 606
Cdd:PRK10419 237 GDKLtfsSPAGRVLQNAV 254
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
354-606 |
8.61e-62 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 208.50 E-value: 8.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 354 RVSDLTKTYRLTKGVVVRRrvgevravDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDA 433
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHAL--------NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 434 AARRRLRTELQVVFQDpvASLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGL-DHSDasRYPAEFSGGQKQRIG 512
Cdd:PRK11153 75 KELRKARRQIGMIFQH--FNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLsDKAD--RYPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 513 IARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFT 592
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFS 230
|
250
....*....|....
gi 1424538268 593 NPQHEYTRRLLAAV 606
Cdd:PRK11153 231 HPKHPLTREFIQST 244
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-232 |
1.68e-59 |
|
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: 198.10 E-value: 1.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIGLL--PeyarVSGSIRLHGKELLGLSDHA 82
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILGGLdrP----TSGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 83 MSQIRGRMIGTVFQDPmsALTPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGIAQperRARAFPHELSGGERQR 162
Cdd:cd03255 76 LAAFRRRHIGFVFQSF--NLLPDLTALENVELPLLL--AGVPKKERRERAEELLERVGLGD---RLNHYPSELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 163 VVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVsEFADRALVMYAGR 232
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGK 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
381-595 |
5.21e-59 |
|
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: 197.34 E-value: 5.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRTELQVVFQDpvASLDPRLPV 460
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQS--GALFDSLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANG-FHRHECEERVAELLAVVGLDHsDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDvSIQA 539
Cdd:cd03261 95 FENVAFPLREHTrLSEEEIREIVLEKLEAVGLRG-AEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLD-PIAS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 540 G-IVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVF--TNPQ 595
Cdd:cd03261 173 GvIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDPL 231
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-268 |
4.08e-57 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 195.68 E-value: 4.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTaaLA-VIGLLPEYArvSGSIRLHGKELLGLSDHAM 83
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKST--LIrCINLLERPT--SGSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 SQIRgRMIGTVFQDP--MSALTpVYtigDQIAEAIEIHsrEISRADARRRAVELLELVGIaqpERRARAFPHELSGGERQ 161
Cdd:COG1135 78 RAAR-RKIGMIFQHFnlLSSRT-VA---ENVALPLEIA--GVPKAEIRKRVAELLELVGL---SDKADAYPSQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 162 RVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDE 241
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLD 227
|
250 260
....*....|....*....|....*..
gi 1424538268 242 LYRDRRMPYTVGLLGSVPRLDAAQGTR 268
Cdd:COG1135 228 VFANPQSELTRRFLPTVLNDELPEELL 254
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
381-606 |
5.00e-57 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 192.13 E-value: 5.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKST---TLNQileLTKPEAGSIEILGTDVAvLDAAARRRLRTELQVVFQDpvASLDPR 457
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTllrCINL---LEEPDSGTITVDGEDLT-DSKKDINKLRRKVGMVFQQ--FNLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 458 LPVYDVIAE-PLRANGFHRHECEERVAELLAVVGL-DHSDAsrYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDV 535
Cdd:COG1126 92 LTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLaDKADA--YPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 536 SIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLAAV 606
Cdd:COG1126 170 ELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
353-581 |
1.68e-56 |
|
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: 190.01 E-value: 1.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRLTKgvvvrrrvGEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLD 432
Cdd:cd03255 1 IELKNLSKTYGGGG--------EKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 433 AAARRRLR-TELQVVFQDPvaSLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRI 511
Cdd:cd03255 73 EKELAAFRrRHIGFVFQSF--NLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDR-LNHYPSELSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 512 GIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHlAHRVAVMYRGMI 581
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
352-605 |
3.31e-55 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 188.46 E-value: 3.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 352 VLRVSDLTKTYRLTKGVVVRRRVGEVRAvdgISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVL 431
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRRQTVEAVKP---LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 432 DAAAR-RRLRtelqVVFQDPVASLDPRLPVYDVIAEPLRAN-GFHRHECEERVAELLAVVGLDHSDASRYPAEFSGGQKQ 509
Cdd:PRK15112 81 DYSYRsQRIR----MIFQDPSTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 510 RIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQ 589
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTAD 236
|
250
....*....|....*.
gi 1424538268 590 VFTNPQHEYTRRLLAA 605
Cdd:PRK15112 237 VLASPLHELTKRLIAG 252
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
381-614 |
3.46e-55 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 190.34 E-value: 3.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELT----KPEAGSIEILGTDVAVLDAAARRRL-RTELQVVFQDPVASLD 455
Cdd:PRK11022 24 DRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKERRNLvGAEVAMIFQDPMTSLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 456 PRLPVYDVIAEPLRAN-GFHRHECEERVAELLAVVGLDhSDASR---YPAEFSGGQKQRIGIARALALQPKILALDEPVS 531
Cdd:PRK11022 104 PCYTVGFQIMEAIKVHqGGNKKTRRQRAIDLLNQVGIP-DPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 532 ALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLAAVPRAHS 611
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRALPEFAQ 262
|
...
gi 1424538268 612 DVA 614
Cdd:PRK11022 263 DKA 265
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
341-608 |
3.86e-55 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 190.32 E-value: 3.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 341 PNNAAGGQPPVVLRVSDLTKTYRLTKGVVVRRrvgevravDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPE--- 417
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRVTFSTPDGDVTAV--------NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgri 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 418 AGSIEILGTDVAVLDAAARRRLRTE-LQVVFQDPVASLDPRLPVYDVIAEPLRAN-GFHRHEC-EERVAELLAV-VGLDH 493
Cdd:PRK09473 73 GGSATFNGREILNLPEKELNKLRAEqISMIFQDPMTSLNPYMRVGEQLMEVLMLHkGMSKAEAfEESVRMLDAVkMPEAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 494 SDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRV 573
Cdd:PRK09473 153 KRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKV 232
|
250 260 270
....*....|....*....|....*....|....*
gi 1424538268 574 AVMYRGMIVEQGESDQVFTNPQHEYTRRLLAAVPR 608
Cdd:PRK09473 233 LVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVPR 267
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
353-606 |
4.25e-55 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 187.83 E-value: 4.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRLTKGVvvrrrvgevravDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILG-----TD 427
Cdd:PRK11701 7 LSVRGLTKLYGPRKGC------------RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 428 VAVLDAAARRRL-RTELQVVFQDPVASLDPRLPVYDVIAEPLRANGfHRH--ECEERVAELLAVVGLDHSDASRYPAEFS 504
Cdd:PRK11701 75 LYALSEAERRRLlRTEWGFVHQHPRDGLRMQVSAGGNIGERLMAVG-ARHygDIRATAGDWLERVEIDAARIDDLPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 505 GGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQ 584
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
250 260
....*....|....*....|..
gi 1424538268 585 GESDQVFTNPQHEYTRRLLAAV 606
Cdd:PRK11701 234 GLTDQVLDDPQHPYTQLLVSSV 255
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
350-584 |
4.90e-55 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 186.40 E-value: 4.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 350 PVVLRVSDLTKTYRLTKGVVVRRrvgevravDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVA 429
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTAL--------RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 430 VLDAAARRRLR-TELQVVFQDPvaSLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQK 508
Cdd:COG1136 74 SLSERELARLRrRHIGFVFQFF--NLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDR-LDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 509 QRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQ 584
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
349-598 |
2.38e-54 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 188.77 E-value: 2.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 349 PPVVLRVSDLTKTYrltkgvvvrrrvGEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDV 428
Cdd:COG3842 2 AMPALELENVSKRY------------GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 429 AVLdAAARRRLRTelqvVFQDPvaSLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQK 508
Cdd:COG3842 70 TGL-PPEKRNVGM----VFQDY--ALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGL-ADRYPHQLSGGQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 509 QRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHD----LSvvkhLAHRVAVMYRGMIVEQ 584
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRIAVMNDGRIEQV 217
|
250
....*....|....
gi 1424538268 585 GESDQVFTNPQHEY 598
Cdd:COG3842 218 GTPEEIYERPATRF 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-243 |
3.58e-54 |
|
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: 184.32 E-value: 3.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIGLLPEYArvSGSIRLHGKELLGLSDHAM 83
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTL-IRCINGLERPT--SGSVLVDGTDLTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 SQIRgRMIGTVFQ--DPMSALTpVYtigDQIAEAIEIHSreISRADARRRAVELLELVGIAQperRARAFPHELSGGERQ 161
Cdd:cd03258 78 RKAR-RRIGMIFQhfNLLSSRT-VF---ENVALPLEIAG--VPKAEIEERVLELLELVGLED---KADAYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 162 RVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDE 241
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
..
gi 1424538268 242 LY 243
Cdd:cd03258 228 VF 229
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
353-585 |
1.18e-53 |
|
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: 182.33 E-value: 1.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRltkgvvvrrrvgEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLd 432
Cdd:cd03259 1 LELKGLSKTYG------------SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 433 AAARRRLRtelqVVFQDPvaSLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHsDASRYPAEFSGGQKQRIG 512
Cdd:cd03259 68 PPERRNIG----MVFQDY--ALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEG-LLNRYPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 513 IARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQG 585
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
353-590 |
5.70e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 181.03 E-value: 5.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRltkgvvvrrrvgEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLD 432
Cdd:COG1131 1 IEVRGLTKRYG------------DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 433 AAARRRlrteLQVVFQDPvaSLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHsDASRYPAEFSGGQKQRIG 512
Cdd:COG1131 69 AEVRRR----IGYVPQEP--ALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTD-AADRKVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 513 IARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQV 590
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
383-609 |
8.18e-53 |
|
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: 182.07 E-value: 8.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLR-TELQVVFQDpvASLDPRLPVY 461
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRrKKISMVFQS--FALLPHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 DVIAEPLRANGFHRHECEERVAELLAVVGLdHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGI 541
Cdd:cd03294 121 ENVAFGLEVQGVPRAEREERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 542 VNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLAAVPRA 609
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVDRA 267
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-232 |
1.84e-52 |
|
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: 178.81 E-value: 1.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSDHAmsqiRGRM 90
Cdd:cd03225 4 NLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPT---SGEVLVDGKDLTKLSLKE----LRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 91 IGTVFQDPMSAL-TPvyTIGDQIAEAIEihSREISRADARRRAVELLELVGIAqpERRARaFPHELSGGERQRVVIAIAI 169
Cdd:cd03225 77 VGLVFQNPDDQFfGP--TVEEEVAFGLE--NLGLPEEEIEERVEEALELVGLE--GLRDR-SPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 170 ANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-247 |
1.77e-51 |
|
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: 177.14 E-value: 1.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEdieVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELlglSDHAMS 84
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPT---SGEVLVDGKDI---TKKNLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 QIRgRMIGTVFQDPMSAL-TPvyTIGDQIAEAIEihSREISRADARRRAVELLELVGIAQPERRArafPHELSGGERQRV 163
Cdd:COG1122 72 ELR-RKVGLVFQNPDDQLfAP--TVEEDVAFGPE--NLGLPREEIRERVEEALELVGLEHLADRP---PHELSGGQKQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 164 VIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELY 243
Cdd:COG1122 144 AIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
....
gi 1424538268 244 RDRR 247
Cdd:COG1122 223 SDYE 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
348-576 |
1.18e-50 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 175.66 E-value: 1.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 348 QPPVVLRVSDLTKTYRLTKGVVVRRrvgevravDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTD 427
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTAL--------DDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 428 VAvlDAAARRRlrtelqVVFQDPvaSLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQ 507
Cdd:COG1116 75 VT--GPGPDRG------VVFQEP--ALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGF-EDAYPHQLSGGM 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 508 KQRIGIARALALQPKILALDEPVSALDV----SIQagivNLLLDLQRRFGLSYLFVSHDLS--VVkhLAHRVAVM 576
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALDAltreRLQ----DELLRLWQETGKTVLFVTHDVDeaVF--LADRVVVL 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
353-576 |
1.34e-50 |
|
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: 174.20 E-value: 1.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRLTKGVVVRRrvgevravDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVavld 432
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTAL--------EDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 433 aaarRRLRTELQVVFQDPvaSLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIG 512
Cdd:cd03293 69 ----TGPGPDRGYVFQQD--ALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGF-ENAYPHQLSGGMRQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 513 IARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVM 576
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-255 |
1.83e-50 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 175.27 E-value: 1.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 21 VPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPE-YARVSGSIRLHGKELlglsdhAMSQIRGRMIGTVFQDPM 99
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgVRQTAGRVLLDGKPV------APCALRGRKIATIMQNPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 100 SALTPVYTIGDqiaeaieiHSREISRA----DARRRAVELLELVGIAQPERRARAFPHELSGGERQRVVIAIAIANDPDL 175
Cdd:PRK10418 90 SAFNPLHTMHT--------HARETCLAlgkpADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 176 LICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDRRMPYTVGLL 255
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLV 241
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-242 |
1.64e-49 |
|
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: 172.09 E-value: 1.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHGKELLGLS 79
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVV----LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLrPD----SGEILVDGQDITGLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 80 DHAMSQIRGRMiGTVFQDpmSALTPVYTIGDQIAEAIEIHSReISRADARRRAVELLELVGIAQPERRaraFPHELSGGE 159
Cdd:COG1127 74 EKELYELRRRI-GMLFQG--GALFDSLTVFENVAFPLREHTD-LSEAEIRELVLEKLELVGLPGAADK---MPSELSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 160 RQRVVIAIAIANDPDLLICDEPTTALD-VTVqAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAA 238
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
....
gi 1424538268 239 VDEL 242
Cdd:COG1127 226 PEEL 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-239 |
2.15e-49 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 172.58 E-value: 2.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLsd 80
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPT---SGEVLVDGKPVTGP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 hamsqirGRMIGTVFQDPmsALTPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGIAQperRARAFPHELSGGER 160
Cdd:COG1116 79 -------GPDRGVVFQEP--ALLPWLTVLDNVALGLEL--RGVPKAERRERARELLELVGLAG---FEDAYPHQLSGGMR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 161 QRVVIAIAIANDPDLLICDEPTTALDV----TVQAQILDVLRTardvTGAAVLIITHDlgvVSE---FADRALVMyAGRP 233
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDAltreRLQDELLRLWQE----TGKTVLFVTHD---VDEavfLADRVVVL-SARP 216
|
....*.
gi 1424538268 234 VEIAAV 239
Cdd:COG1116 217 GRIVEE 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
353-605 |
3.51e-49 |
|
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: 171.33 E-value: 3.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRltkgvvvrrrvGEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLD 432
Cdd:cd03295 1 IEFENVTKRYG-----------GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 433 AAarrRLRTELQVVFQDpvASLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLD-HSDASRYPAEFSGGQKQRI 511
Cdd:cd03295 70 PV---ELRRKIGYVIQQ--IGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpAEFADRYPHELSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 512 GIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVF 591
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
250
....*....|....
gi 1424538268 592 TNPQHEYTRRLLAA 605
Cdd:cd03295 225 RSPANDFVAEFVGA 238
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
353-616 |
8.35e-49 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 173.79 E-value: 8.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRLTKgvvvrrrvgevrAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVlD 432
Cdd:COG1118 3 IEVRNISKRFGSFT------------LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT-N 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 433 AAARRRlrtelQV--VFQDPvaSLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQR 510
Cdd:COG1118 70 LPPRER-----RVgfVFQHY--ALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGL-ADRYPSQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 511 IGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQV 590
Cdd:COG1118 142 VALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
250 260
....*....|....*....|....*.
gi 1424538268 591 FTNPQHEYTRRLLAAVPRAHSDVASG 616
Cdd:COG1118 222 YDRPATPFVARFLGCVNVLRGRVIGG 247
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
381-595 |
1.34e-48 |
|
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: 169.05 E-value: 1.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVavlDAAARRRLRTELQVVFQDP----VASLdp 456
Cdd:COG1122 18 DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELRRKVGLVFQNPddqlFAPT-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 457 rlpVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVS 536
Cdd:COG1122 93 ---VEEDVAFGPENLGLPREEIRERVEEALELVGLEHL-ADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 537 IQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQ 595
Cdd:COG1122 169 GRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
381-595 |
2.79e-48 |
|
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: 168.57 E-value: 2.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRrlrteLQVVFQDpvASLDPRLPV 460
Cdd:cd03300 17 DGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP-----VNTVFQN--YALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGFHRHECEERVAELLAVVGLDhSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:cd03300 90 FENIAFGLRLKKLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 541 IVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQ 595
Cdd:cd03300 169 MQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
350-606 |
6.36e-48 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 168.47 E-value: 6.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 350 PVVLRVSDLTKTYRLTKGVVVrrrvgevravdgISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVA 429
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCRD------------VSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 430 VLD-----AAARRRL-RTELQVVFQDPVASLDPRLPVYDVIAEPLRANGfHRHECEERVA--ELLAVVGLDHSDASRYPA 501
Cdd:TIGR02323 69 ELElyqlsEAERRRLmRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIG-ARHYGNIRATaqDWLEEVEIDPTRIDDLPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 502 EFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMI 581
Cdd:TIGR02323 148 AFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
250 260
....*....|....*....|....*
gi 1424538268 582 VEQGESDQVFTNPQHEYTRRLLAAV 606
Cdd:TIGR02323 228 VESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-239 |
8.43e-48 |
|
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: 166.88 E-value: 8.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGlsdhams 84
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT---SGEVLVDGEPVTG------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 qiRGRMIGTVFQDPmsALTPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGIaqpERRARAFPHELSGGERQRVV 164
Cdd:cd03293 71 --PGPDRGYVFQQD--ALLPWLTVLDNVALGLEL--QGVPKAEARERAEELLELVGL---SGFENAYPHQLSGGMRQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 165 IAIAIANDPDLLICDEPTTALDV----TVQAQILDVLRTardvTGAAVLIITHDLGVVSEFADRALVMyAGRPVEIAAV 239
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDAltreQLQEELLDIWRE----TGKTVLLVTHDIDEAVFLADRVVVL-SARPGRIVAE 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
381-586 |
9.18e-48 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 166.77 E-value: 9.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRTELQVVFQDpvASLDPRLPV 460
Cdd:COG2884 19 SDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQD--FRLLPDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:COG2884 97 YENVALPLRVTGKSRKEIRRRVREVLDLVGLSDK-AKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1424538268 541 IVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGE 586
Cdd:COG2884 176 IMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
381-608 |
1.46e-47 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 174.89 E-value: 1.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILEL--TKP---EAGSIEILGTDVAVLDAAARRRLR-TELQVVFQDPVASL 454
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSVTALSILRLlpSPPvvyPSGDIRFHGESLLHASEQTLRGVRgNKIAMIFQEPMVSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 455 DPRLPVYDVIAEPLRAN-GFHRHECEERVAELLAVVGLDHSdASR---YPAEFSGGQKQRIGIARALALQPKILALDEPV 530
Cdd:PRK15134 106 NPLHTLEKQLYEVLSLHrGMRREAARGEILNCLDRVGIRQA-AKRltdYPHQLSGGERQRVMIAMALLTRPELLIADEPT 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 531 SALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLAAVPR 608
Cdd:PRK15134 185 TALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLNSEPS 262
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
381-605 |
1.22e-46 |
|
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: 164.05 E-value: 1.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRrlrteLQVVFQDpvASLDPRLPV 460
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD-----ISYVPQN--YALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHL-LNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 541 IVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLAA 605
Cdd:cd03299 168 LREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGF 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-265 |
2.57e-46 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 173.12 E-value: 2.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 20 EVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYArvsGSIRLHGKELLGLSDHAMSQIRgRMIGTVFQDPM 99
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG---GEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDPY 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 100 SALTPVYTIGDQIAEAIEIHSREISRAdARRRAVELLELVGIaQPERRARaFPHELSGGERQRVVIAIAIANDPDLLICD 179
Cdd:PRK10261 412 ASLDPRQTVGDSIMEPLRVHGLLPGKA-AAARVAWLLERVGL-LPEHAWR-YPHEFSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 180 EPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDRRMPYTVGLLGSVP 259
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVP 568
|
....*.
gi 1424538268 260 RLDAAQ 265
Cdd:PRK10261 569 VADPSR 574
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
381-607 |
3.88e-46 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 165.85 E-value: 3.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPE----AGSIEILGTDVAVLDAAARRRL-RTELQVVFQDPVASLD 455
Cdd:COG4170 24 DRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRERRKIiGREIAMIFQEPSSCLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 456 PRLPVYDVIAEPLRANGF---------HRHEceeRVAELLAVVGL-DHSDASR-YPAEFSGGQKQRIGIARALALQPKIL 524
Cdd:COG4170 104 PSAKIGDQLIEAIPSWTFkgkwwqrfkWRKK---RAIELLHRVGIkDHKDIMNsYPHELTEGECQKVMIAMAIANQPRLL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 525 ALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLA 604
Cdd:COG4170 181 IADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKALLR 260
|
...
gi 1424538268 605 AVP 607
Cdd:COG4170 261 SMP 263
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
381-595 |
4.07e-46 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 164.16 E-value: 4.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRTELQVVFQDPVASLDPRLpV 460
Cdd:TIGR04521 22 DDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQFPEHQLFEET-V 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGFHRHECEERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:TIGR04521 101 YKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 541 IVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQ 595
Cdd:TIGR04521 181 ILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
21-235 |
4.65e-46 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 162.14 E-value: 4.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 21 VPAVRGTSYHIDPGEVLAIVGESGCGKTTaalaVIGLLpeYARV---SGSIRLHGKELLGLSDHAMSQIRgRMIGTVFQD 97
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKST----LLKLL--YGEErptSGQVLVNGQDLSRLKRREIPYLR-RRIGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 98 pmSALTPVYTIGDQIAEAIEIHsrEISRADARRRAVELLELVGIAQperRARAFPHELSGGERQRVVIAIAIANDPDLLI 177
Cdd:COG2884 88 --FRLLPDRTVYENVALPLRVT--GKSRKEIRRRVREVLDLVGLSD---KAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 178 CDEPTTALDVTVQAQILDVLRTARDVtGAAVLIITHDLGVVSEFADRALVMYAGRPVE 235
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-244 |
8.43e-46 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 165.66 E-value: 8.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHGKELLGLS 79
Cdd:COG3842 2 AMPALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFEtPD----SGRILLDGRDVTGLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 80 DHAmsqirgRMIGTVFQDPmsALTPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGIAQperRARAFPHELSGGE 159
Cdd:COG3842 74 PEK------RNVGMVFQDY--ALFPHLTVAENVAFGLRM--RGVPKAEIRARVAELLELVGLEG---LADRYPHQLSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 160 RQRVVIAIAIANDPDLLICDEPTTALD----VTVQAQILDVLRTardvTGAAVLIITHDLgvvSE---FADRALVMYAGR 232
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRE----LGITFIYVTHDQ---EEalaLADRIAVMNDGR 213
|
250
....*....|..
gi 1424538268 233 PVEIAAVDELYR 244
Cdd:COG3842 214 IEQVGTPEEIYE 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-242 |
9.18e-46 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 161.70 E-value: 9.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIGLLPEYArvSGSIRLHGKELlGLSDHAM 83
Cdd:COG1126 1 MIEIENLHKSFG----DLEVLKGISLDVEKGEVVVIIGPSGSGKSTL-LRCINLLEEPD--SGTITVDGEDL-TDSKKDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 SQIRGRmIGTVFQDPmsALTPVYTIGDQIAEAIeIHSREISRADARRRAVELLELVGIAQperRARAFPHELSGGERQRV 163
Cdd:COG1126 73 NKLRRK-VGMVFQQF--NLFPHLTVLENVTLAP-IKVKKMSKAEAEERAMELLERVGLAD---KADAYPAQLSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 164 VIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRT-ARDvtGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDEL 242
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDlAKE--GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-582 |
9.85e-46 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 169.04 E-value: 9.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETedieVPAVRGTSYHIDPGEVLAIVGESGCGKTT--AALAviGLlpeYARVSGSIRLHGKELLGL 78
Cdd:COG1129 1 AEPLLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTlmKILS--GV---YQPDSGEILLDGEPVRFR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 79 SDHAmSQIRGrmIGTVFQDPmsALTPVYTIGDQIAEAIEIHSRE-ISRADARRRAVELLELVGIA-QPERRARafphELS 156
Cdd:COG1129 72 SPRD-AQAAG--IAIIHQEL--NLVPNLSVAENIFLGREPRRGGlIDWRAMRRRARELLARLGLDiDPDTPVG----DLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 157 GGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVEI 236
Cdd:COG1129 143 VAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKA-QGVAIIYISHRLDEVFEIADRVTVLRDGRLVGT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 237 AAVDELYRDrrmpytvgllgsvprldaaqgtrlipipgapptmtslspgactfaprcplaideclsaepDLVRvadghwa 316
Cdd:COG1129 222 GPVAELTED------------------------------------------------------------ELVR------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 317 acirtdDVAGRSAADVFgvstqPPPNNAAGgqpPVVLRVSDLTKTYRLtkgvvvrrrvgevravDGISFTLEQGRTLGIV 396
Cdd:COG1129 235 ------LMVGRELEDLF-----PKRAAAPG---EVVLEVEGLSVGGVV----------------RDVSFSVRAGEILGIA 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 397 GESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLR----TE---LQVVFQDpvasldprLPVYDVIA---- 465
Cdd:COG1129 285 GLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGiayvPEdrkGEGLVLD--------LSIRENITlasl 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 466 EPLRANGF-HRHECEERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNL 544
Cdd:COG1129 357 DRLSRGGLlDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRL 436
|
570 580 590
....*....|....*....|....*....|....*...
gi 1424538268 545 LLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIV 582
Cdd:COG1129 437 IRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
352-590 |
1.10e-45 |
|
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: 161.95 E-value: 1.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 352 VLRVSDLTKTYRLTKGVvvrrrvgevravDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVL 431
Cdd:COG4555 1 MIEVENLSKKYGKVPAL------------KDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 432 DAAARRRLrtelQVVFQDPvaSLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDhSDASRYPAEFSGGQKQRI 511
Cdd:COG4555 69 PREARRQI----GVLPDER--GLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 512 GIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLqRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQV 590
Cdd:COG4555 142 ALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
381-603 |
1.62e-45 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 163.34 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRlrtelQV--VFQDpvASLDPRL 458
Cdd:COG1125 19 DDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRR-----RIgyVIQQ--IGLFPHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 459 PVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSD-ASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSI 537
Cdd:COG1125 92 TVAENIATVPRLLGWDKERIRARVDELLELVGLDPEEyRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALDPIT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 538 QAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLL 603
Cdd:COG1125 172 REQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFV 237
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-242 |
3.30e-44 |
|
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: 157.66 E-value: 3.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeyaRVSGSIRLHGKELLGLSDHAMS 84
Cdd:cd03261 1 IELRGLTKSFGGRTV----LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR---PDSGEVLIDGEDISGLSEAELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 QIRGRMiGTVFQDpmSALTPVYTIGDQIAEAIEIHSREiSRADARRRAVELLELVGIAQperRARAFPHELSGGERQRVV 164
Cdd:cd03261 74 RLRRRM-GMLFQS--GALFDSLTVFENVAFPLREHTRL-SEEEIREIVLEKLEAVGLRG---AEDLYPAELSGGMKKRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 165 IAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDEL 242
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
381-592 |
3.62e-44 |
|
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: 157.90 E-value: 3.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRTelqVVFQDPVASLDprLPV 460
Cdd:COG1120 18 DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA---YVPQEPPAPFG--LTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIA---EP-LRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVS 536
Cdd:COG1120 93 RELVAlgrYPhLGLFGRPSAEDREAVEEALERTGLEHL-ADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 537 IQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFT 592
Cdd:COG1120 172 HQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
353-579 |
4.38e-44 |
|
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: 155.42 E-value: 4.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYrltkgvvvrrrvGEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLD 432
Cdd:cd03229 1 LELKNVSKRY------------GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 433 AAaRRRLRTELQVVFQDPvaSLDPRLPVYDVIAEPLrangfhrheceervaellavvgldhsdasrypaefSGGQKQRIG 512
Cdd:cd03229 69 DE-LPPLRRRIGMVFQDF--ALFPHLTVLENIALGL-----------------------------------SGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 513 IARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRG 579
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-263 |
4.43e-44 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 160.70 E-value: 4.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEdievPAVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVI-GLlpEYARvSGSIRLHGKELLglSDHAm 83
Cdd:COG1118 3 IEVRNISKRFGSF----TLLDDVSLEIASGELVALLGPSGSGKTTL-LRIIaGL--ETPD-SGRIVLNGRDLF--TNLP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 sqIRGRMIGTVFQDPmsALTPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGIAQPERRaraFPHELSGGERQRV 163
Cdd:COG1118 72 --PRERRVGFVFQHY--ALFPHMTVAENIAFGLRV--RPPSKAEIRARVEELLELVQLEGLADR---YPSQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 164 VIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELY 243
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
250 260
....*....|....*....|
gi 1424538268 244 RDRRMPYTVGLLGSVPRLDA 263
Cdd:COG1118 223 DRPATPFVARFLGCVNVLRG 242
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
381-579 |
8.34e-44 |
|
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: 155.70 E-value: 8.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRlrtELQVVFQDP----VASLdp 456
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR---KVGLVFQNPddqfFGPT-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 457 rlpVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHsDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVS 536
Cdd:cd03225 93 ---VEEEVAFGLENLGLPEEEIEERVEEALELVGLEG-LRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1424538268 537 IQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRG 579
Cdd:cd03225 169 GRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
381-581 |
1.76e-43 |
|
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: 154.99 E-value: 1.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAvLDAAARRRLRTELQVVFQDpvASLDPRLPV 460
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELRQKVGMVFQQ--FNLFPHLTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAE-PLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQA 539
Cdd:cd03262 94 LENITLaPIKVKGMSKAEAEERALELLEKVGLADK-ADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1424538268 540 GIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMI 581
Cdd:cd03262 173 EVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-242 |
1.89e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 155.61 E-value: 1.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSDHAMs 84
Cdd:COG1131 1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT---SGEVRVLGEDVARDPAEVR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 qirgRMIGTVFQDPmsALTPVYTIgdqiAEAIEIHSR--EISRADARRRAVELLELVGIaqpERRARAFPHELSGGERQR 162
Cdd:COG1131 73 ----RRIGYVPQEP--ALYPDLTV----RENLRFFARlyGLPRKEARERIDELLELFGL---TDAADRKVGTLSGGMKQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 163 VVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDEL 242
Cdd:COG1131 140 LGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
381-595 |
2.83e-43 |
|
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: 154.90 E-value: 2.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRL---RTelqvvFQDPvaSLDPR 457
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgigRT-----FQIP--RLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 458 LPVYD--VIAEPLRANGF--------HRHECEERVAELLAVVGLDHsDASRYPAEFSGGQKQRIGIARALALQPKILALD 527
Cdd:cd03219 90 LTVLEnvMVAAQARTGSGlllararrEEREARERAEELLERVGLAD-LADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 528 EPVSALDVSIQAGIVNLLLDLqRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQ 595
Cdd:cd03219 169 EPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-252 |
3.19e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 155.25 E-value: 3.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeyaRVSGSIRLHGKELlglsd 80
Cdd:COG1121 3 MMPAIELENLTVSYG----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP---PTSGTVRLFGKPP----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 hamsQIRGRMIGTVFQDPMSALT-PVyTIGDQIAEAIEIHS---REISRADaRRRAVELLELVGIAqpERRARAFpHELS 156
Cdd:COG1121 71 ----RRARRRIGYVPQRAEVDWDfPI-TVRDVVLMGRYGRRglfRRPSRAD-REAVDEALERVGLE--DLADRPI-GELS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 157 GGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVM-----YAG 231
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLLnrglvAHG 220
|
250 260
....*....|....*....|.
gi 1424538268 232 RPVEIAAVDELYRDRRMPYTV 252
Cdd:COG1121 221 PPEEVLTPENLSRAYGGPVAL 241
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
352-590 |
8.04e-43 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 154.06 E-value: 8.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 352 VLRVSDLTKTYRltkgvvvrrrvGEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVL 431
Cdd:COG3638 2 MLELRNLSKRYP-----------GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 432 DAAARRRLRTELQVVFQDPvaSLDPRLPVYD-VIAEPLRANGFHRH-------ECEERVAELLAVVGLDHsDASRYPAEF 503
Cdd:COG3638 71 RGRALRRLRRRIGMIFQQF--NLVPRLSVLTnVLAGRLGRTSTWRSllglfppEDRERALEALERVGLAD-KAYQRADQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 504 SGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVE 583
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVF 227
|
....*..
gi 1424538268 584 QGESDQV 590
Cdd:COG3638 228 DGPPAEL 234
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
381-598 |
8.93e-43 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 157.16 E-value: 8.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRrlrteLQVVFQDPVasLDPRLPV 460
Cdd:COG3839 20 KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRN-----IAMVFQSYA--LYPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:COG3839 93 YENIAFPLKLRKVPKAEIDRRVREAAELLGLEDL-LDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 541 IVNLLLDLQRRFGLSYLFVSHD----LSvvkhLAHRVAVMYRGMIVEQGESDQVFTNPQHEY 598
Cdd:COG3839 172 MRAEIKRLHRRLGTTTIYVTHDqveaMT----LADRIAVMNDGRIQQVGTPEELYDRPANLF 229
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
381-529 |
1.09e-42 |
|
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: 150.49 E-value: 1.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDaaaRRRLRTELQVVFQDPvaSLDPRLPV 460
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE---RKSLRKEIGYVFQDP--QLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 461 YDVIAEPLRANGFHRHECEERVAELLAVVGLDHSDASR---YPAEFSGGQKQRIGIARALALQPKILALDEP 529
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
381-608 |
7.92e-42 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 151.11 E-value: 7.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAaaRRRlrtELQVVFQDpvASLDPRLPV 460
Cdd:TIGR00968 17 DDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHA--RDR---KIGFVFQH--YALFKHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:TIGR00968 90 RDNIAFGLEIRKHPKAKIKARVEELLELVQLEGL-GDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKVRKE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 541 IVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLAAVPR 608
Cdd:TIGR00968 169 LRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNV 236
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-237 |
1.19e-41 |
|
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: 149.98 E-value: 1.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELLGLSdhams 84
Cdd:cd03259 1 LELKGLSKTYG----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERP---DSGEILIDGRDVTGVP----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 qIRGRMIGTVFQDPmsALTPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGIAQPERRaraFPHELSGGERQRVV 164
Cdd:cd03259 69 -PERRNIGMVFQDY--ALFPHLTVAENIAFGLKL--RGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 165 IAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIA 237
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
353-581 |
2.00e-41 |
|
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: 147.93 E-value: 2.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRLTKGVvvrrrvgevravDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLD 432
Cdd:cd03230 1 IEVRNLSKRYGKKTAL------------DDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 433 AAARRRLRtelqVVFQDPvaSLDPRLPVYDVIaeplrangfhrheceervaellavvgldhsdasrypaEFSGGQKQRIG 512
Cdd:cd03230 69 EEVKRRIG----YLPEEP--SLYENLTVRENL-------------------------------------KLSGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 513 IARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMI 581
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
24-242 |
2.04e-41 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 150.99 E-value: 2.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 24 VRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlpeYARVSGSIRLHGKELLGLSDHAMSQIRgRMIGTVFQDPMSALT 103
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL---ESPSQGNVSWRGEPLAKLNRAQRKAFR-RDIQMVFQDSISAVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 104 PVYTIGDQIAEAIEiHSREISRADARRRAVELLELVGIaqPERRARAFPHELSGGERQRVVIAIAIANDPDLLICDEPTT 183
Cdd:PRK10419 104 PRKTVREIIREPLR-HLLSLDKAERLARASEMLRAVDL--DDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 184 ALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDEL 242
Cdd:PRK10419 181 NLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDK 239
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
349-595 |
3.83e-41 |
|
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: 149.80 E-value: 3.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 349 PPVVLRVSDLTKTYR-LTkgvvvrrrvgevrAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTD 427
Cdd:COG0411 1 SDPLLEVRGLTKRFGgLV-------------AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 428 VAVLDAAARRRL---RTelqvvFQdpVASLDPRLPVYD-------------VIAEPLRANGFHR--HECEERVAELLAVV 489
Cdd:COG0411 68 ITGLPPHRIARLgiaRT-----FQ--NPRLFPELTVLEnvlvaaharlgrgLLAALLRLPRARReeREARERAEELLERV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 490 GLDHsDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHL 569
Cdd:COG0411 141 GLAD-RADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGL 219
|
250 260
....*....|....*....|....*.
gi 1424538268 570 AHRVAVMYRGMIVEQGESDQVFTNPQ 595
Cdd:COG0411 220 ADRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-282 |
4.98e-41 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 150.17 E-value: 4.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHGKELlglSDHAMSQIRgR 89
Cdd:PRK13635 10 HISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLlPE----AGTITVGGMVL---SEETVWDVR-R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 90 MIGTVFQDPMSALTPVyTIGDQIAEAIEihSREISRADARRRAVELLELVGIAQPERRArafPHELSGGERQRVVIAIAI 169
Cdd:PRK13635 82 QVGMVFQNPDNQFVGA-TVQDDVAFGLE--NIGVPREEMVERVDQALRQVGMEDFLNRE---PHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 170 ANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSeFADRALVMYAGRPVEIAAVDELYRDRRMP 249
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAA-QADRVIVMNKGEILEEGTPEEIFKSGHML 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 1424538268 250 YTVGLlgSVP---RLDAAQGTRLIPIPGAPPTMTSL 282
Cdd:PRK13635 235 QEIGL--DVPfsvKLKELLKRNGILLPNTYLTMESL 268
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-241 |
5.54e-41 |
|
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: 148.74 E-value: 5.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 2 TAVLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTT--AALAviGL-LPEyarvSGSIRLHGKELLGL 78
Cdd:COG4181 6 APIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTllGLLA--GLdRPT----SGTVRLAGQDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 79 SDHAMSQIRGRMIGTVFQD----P-MSALtpvytigDQIAEAIEIHSReisrADARRRAVELLELVGIAQperRARAFPH 153
Cdd:COG4181 80 DEDARARLRARHVGFVFQSfqllPtLTAL-------ENVMLPLELAGR----RDARARARALLERVGLGH---RLDHYPA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 154 ELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEfADRALVMYAGRP 233
Cdd:COG4181 146 QLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRL 224
|
....*...
gi 1424538268 234 VEIAAVDE 241
Cdd:COG4181 225 VEDTAATA 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
383-597 |
6.01e-41 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 149.01 E-value: 6.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKST---TLNqILELtkPEAGSIEILGTDV---AVLDAAARRRLRTELQVVFQDpvASLDP 456
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSllrVLN-LLEM--PRSGTLNIAGNHFdfsKTPSDKAIRELRRNVGMVFQQ--YNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 457 RLPVYD-VIAEPLRANGFHRHECEERVAELLAVVGL-DHSDasRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALD 534
Cdd:PRK11124 96 HLTVQQnLIEAPCRVLGLSKDQALARAEKLLERLRLkPYAD--RFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 535 VSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQvFTNPQHE 597
Cdd:PRK11124 174 PEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTE 234
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-232 |
6.59e-41 |
|
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: 147.68 E-value: 6.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEdievPAVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIGLLPEYArvSGSIRLHGKELLGlSDHAMS 84
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKSTL-LRCINLLEEPD--SGTIIIDGLKLTD-DKKNIN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 QIRGRmIGTVFQDpmSALTPVYTIGDQIAEAIeIHSREISRADARRRAVELLELVGIAQperRARAFPHELSGGERQRVV 164
Cdd:cd03262 73 ELRQK-VGMVFQQ--FNLFPHLTVLENITLAP-IKVKGMSKAEAEERALELLEKVGLAD---KADAYPAQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 165 IAIAIANDPDLLICDEPTTALDVTVQAQILDVLRT-ARDvtGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlAEE--GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
381-590 |
6.80e-41 |
|
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: 148.10 E-value: 6.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKST---TLNQILELTK--PEAGSIEILGTDVAVLDAAaRRRLRTELQVVFQDPvaslD 455
Cdd:cd03260 17 KDISLDIPKGEITALIGPSGCGKSTllrLLNRLNDLIPgaPDEGEVLLDGKDIYDLDVD-VLELRRRVGMVFQKP----N 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 456 P-RLPVYDVIAEPLRANGFHRHEC-EERVAELLAVVGLDHSDASRYPA-EFSGGQKQRIGIARALALQPKILALDEPVSA 532
Cdd:cd03260 92 PfPGSIYDNVAYGLRLHGIKLKEElDERVEEALRKAALWDEVKDRLHAlGLSGGQQQRLCLARALANEPEVLLLDEPTSA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 533 LDVSIQAGIVNLLLDLQRRFGLsyLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQV 590
Cdd:cd03260 172 LDPISTAKIEELIAELKKEYTI--VIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-262 |
7.31e-41 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 151.88 E-value: 7.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 6 EVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIGLLPEYArvSGSIRLHGKELLGLSDHAMSQ 85
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTL-IRCINLLERPT--SGRVLVDGQDLTALSEKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 86 IRgRMIGTVFQ--DPMSAltpvYTIGDQIAEAIEIHSreISRADARRRAVELLELVGIAQperRARAFPHELSGGERQRV 163
Cdd:PRK11153 80 AR-RQIGMIFQhfNLLSS----RTVFDNVALPLELAG--TPKAEIKARVTELLELVGLSD---KADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 164 VIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELY 243
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVF 229
|
250
....*....|....*....
gi 1424538268 244 RDRRMPYTVGLLGSVPRLD 262
Cdd:PRK11153 230 SHPKHPLTREFIQSTLHLD 248
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-242 |
1.10e-40 |
|
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: 148.65 E-value: 1.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSDHAm 83
Cdd:COG1120 1 MLEAENLSVGYGGRPV----LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS---SGEVLLDGRDLASLSRRE- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 sqiRGRMIGTVFQDPMSA--LTpvytigdqIAEAIEI----HSREISRADA--RRRAVELLELVGIAqpERRARAFpHEL 155
Cdd:COG1120 73 ---LARRIAYVPQEPPAPfgLT--------VRELVALgrypHLGLFGRPSAedREAVEEALERTGLE--HLADRPV-DEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 156 SGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVE 235
Cdd:COG1120 139 SGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
|
....*..
gi 1424538268 236 IAAVDEL 242
Cdd:COG1120 219 QGPPEEV 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
381-592 |
1.34e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.93 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAvldaAARRRL-----RtelqvvfqdpvASLD 455
Cdd:COG1121 23 EDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR----RARRRIgyvpqR-----------AEVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 456 PRLP--VYDVIA----EPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEP 529
Cdd:COG1121 88 WDFPitVRDVVLmgryGRRGLFRRPSRADREAVDEALERVGLEDL-ADRPIGELSGGQQQRVLLARALAQDPDLLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 530 VSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGmIVEQGESDQVFT 592
Cdd:COG1121 167 FAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLT 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-582 |
1.74e-40 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 154.41 E-value: 1.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETedieVPAVRGTSYHIDPGEVLAIVGESGCGKTTaaLAVI--GLL-PEyarvSGSIRLHGKEL-L 76
Cdd:COG3845 2 MPPALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKST--LMKIlyGLYqPD----SGEILIDGKPVrI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 77 GLSDHAMSqiRGrmIGTVFQDPMsaLTPVYTIGDQIAEAIEIHSRE-ISRADARRRAVELLELVGIA-QPERRArafpHE 154
Cdd:COG3845 72 RSPRDAIA--LG--IGMVHQHFM--LVPNLTVAENIVLGLEPTKGGrLDRKAARARIRELSERYGLDvDPDAKV----ED 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 155 LSGGERQRVVIAIAIANDPDLLICDEPTTALdvTVQ--AQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:COG3845 142 LSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAA-EGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 233 PVEIAAVDElyrdrrmpytvgllgsvprLDAAQGTRLipipgapptMtslspgactfaprcplaideclsaepdlvrvad 312
Cdd:COG3845 219 VVGTVDTAE-------------------TSEEELAEL---------M--------------------------------- 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 313 ghwaacirtddvagrsaadvFGVSTQPPPNNAAGGQPPVVLRVSDLTktyrltkgvvvRRRVGEVRAVDGISFTLEQGRT 392
Cdd:COG3845 238 --------------------VGREVLLRVEKAPAEPGEVVLEVENLS-----------VRDDRGVPALKDVSLEVRAGEI 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 393 LGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRteLQVVFQDPVAS-LDPRLPVYDVIA------ 465
Cdd:COG3845 287 LGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLG--VAYIPEDRLGRgLVPDMSVAENLIlgryrr 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 466 EPLRANGF-HRHECEERVAELLA---VVGLDHSDASRypaEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGI 541
Cdd:COG3845 365 PPFSRGGFlDRKAIRAFAEELIEefdVRTPGPDTPAR---SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFI 441
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1424538268 542 VNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIV 582
Cdd:COG3845 442 HQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
381-585 |
1.91e-40 |
|
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: 146.63 E-value: 1.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARrrlrtELQVVFQDpvASLDPRLPV 460
Cdd:cd03301 17 DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR-----DIAMVFQN--YALYPHMTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:cd03301 90 YDNIAFGLKLRKVPKDEIDERVREVAELLQIEHL-LDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1424538268 541 IVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQG 585
Cdd:cd03301 169 MRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
383-597 |
4.70e-40 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 146.31 E-value: 4.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKST---TLNqILELtkPEAGSIEILGTDV---AVLDAAARRRLRTELQVVFQDpvASLDP 456
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSllrVLN-LLET--PDSGQLNIAGHQFdfsQKPSEKAIRLLRQKVGMVFQQ--YNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 457 RLPVYD-VIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDV 535
Cdd:COG4161 96 HLTVMEnLIEAPCKVLGLSKEQAREKAMKLLARLRLTDK-ADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 536 SIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDqVFTNPQHE 597
Cdd:COG4161 175 EITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQPQTE 234
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-232 |
4.79e-40 |
|
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: 145.57 E-value: 4.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIGLL--PeyarVSGSIRLHGKELLGLSDH 81
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTL-LHLLGGLdnP----TSGEVLFNGQSLSKLSSN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 82 AMSQIRGRMIGTVFQdpMSALTPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGIaqpERRARAFPHELSGGERQ 161
Cdd:TIGR02211 76 ERAKLRNKKLGFIYQ--FHHLLPDFTALENVAMPLLI--GKKSVKEAKERAYEMLEKVGL---EHRINHRPSELSGGERQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 162 RVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFaDRALVMYAGR 232
Cdd:TIGR02211 149 RVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQ 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
382-603 |
9.34e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 146.05 E-value: 9.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSI-----EILGTDVAVLDAAARRRLRTELQVVFQDpvASLDP 456
Cdd:PRK11264 21 GIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSLSQQKGLIRQLRQHVGFVFQN--FNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 457 -RLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSDASrYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDV 535
Cdd:PRK11264 99 hRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETS-YPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 536 SIQAGIVNLLLDL--QRRfglSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLL 603
Cdd:PRK11264 178 ELVGEVLNTIRQLaqEKR---TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFL 244
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
382-604 |
9.39e-40 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 146.27 E-value: 9.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVA----------VLDAAARRRLRTELQVVFQDpv 451
Cdd:PRK10619 23 GVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLRLLRTRLTMVFQH-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 452 ASLDPRLPVYDVIAE-PLRANGFHRHECEERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPV 530
Cdd:PRK10619 101 FNLWSHMTVLENVMEaPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 531 SALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLA 604
Cdd:PRK10619 181 SALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
381-593 |
1.78e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 146.35 E-value: 1.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAvlDAAAR-RRLRTELQVVFQDPVASLDPRlP 459
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT--DKKVKlSDIRKKVGLVFQYPEYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 460 VYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSD-ASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQ 538
Cdd:PRK13637 101 IEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 539 AGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTN 593
Cdd:PRK13637 181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
348-605 |
2.00e-39 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 145.33 E-value: 2.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 348 QPPVVLRVSDLTKTYrltkgvvvrrrvGEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTD 427
Cdd:COG4598 4 TAPPALEVRDLHKSF------------GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 428 VA----------VLDAAARRRLRTELQVVFQDpvASLDPRLPVYD-VIAEPLRANGFHRHECEERVAELLAVVGLDHSdA 496
Cdd:COG4598 72 IRlkpdrdgelvPADRRQLQRIRTRLGMVFQS--FNLWSHMTVLEnVIEAPVHVLGRPKAEAIERAEALLAKVGLADK-R 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 497 SRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVM 576
Cdd:COG4598 149 DAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFL 227
|
250 260
....*....|....*....|....*....
gi 1424538268 577 YRGMIVEQGESDQVFTNPQHEYTRRLLAA 605
Cdd:COG4598 228 HQGRIEEQGPPAEVFGNPKSERLRQFLSS 256
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
381-605 |
2.48e-39 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 144.84 E-value: 2.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKP----EAGSIEILGTDVAvldaAARRRLRTeLQVVFQDPVASLDP 456
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVA----PCALRGRK-IATIMQNPRSAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 457 RLPVYDVIAEPLRANGfhRHECEERVAELLAVVGLDHSD--ASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALD 534
Cdd:PRK10418 95 LHTMHTHARETCLALG--KPADDATLTAALEAVGLENAArvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 535 VSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLAA 605
Cdd:PRK10418 173 VVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
381-598 |
3.07e-39 |
|
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: 144.02 E-value: 3.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARrrlrtELQVVFQDpvASLDPRLPV 460
Cdd:cd03296 19 DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER-----NVGFVFQH--YALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGFHRH----ECEERVAELLAVVGLDhSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVS 536
Cdd:cd03296 92 FDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLD-WLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 537 IQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEY 598
Cdd:cd03296 171 VRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
21-232 |
7.36e-39 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 142.39 E-value: 7.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 21 VPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYArvsGSIRLHGKELLGLSDHAMSQIRgRMIGTVFQDpmS 100
Cdd:TIGR02673 15 VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSR---GQVRIAGEDVNRLRGRQLPLLR-RRIGVVFQD--F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 101 ALTPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGIaqpERRARAFPHELSGGERQRVVIAIAIANDPDLLICDE 180
Cdd:TIGR02673 89 RLLPDRTVYENVALPLEV--RGKKEREIQRRVGAALRQVGL---EHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 181 PTTALDVTVQAQILDVLRTARDVtGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:TIGR02673 164 PTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
381-593 |
7.67e-39 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 143.72 E-value: 7.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTT---LNQILeltKPEAGSIEILGTDVavLDAAARRRLRTELQVVFQDP----VAS 453
Cdd:TIGR04520 19 KNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLL---LPTSGKVTVDGLDT--LDEENLWEIRKKVGMVFQNPdnqfVGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 454 LdprlpVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSAL 533
Cdd:TIGR04520 94 T-----VEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDF-RDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSML 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 534 DVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVkHLAHRVAVMYRGMIVEQGESDQVFTN 593
Cdd:TIGR04520 168 DPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-258 |
1.07e-38 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 143.14 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETEDievpAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYArvsGSIRLHGKELLGLSD 80
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRK----GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDA---GEVHYRMRDGQLRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 HAMSQIRGRMI-----GTVFQDPMSALTPVYTIGDQIAEAI----EIHSREIsradaRRRAVELLELVGIaqPERRARAF 151
Cdd:PRK11701 76 YALSEAERRRLlrtewGFVHQHPRDGLRMQVSAGGNIGERLmavgARHYGDI-----RATAGDWLERVEI--DAARIDDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 152 PHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAG 231
Cdd:PRK11701 149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
250 260
....*....|....*....|....*..
gi 1424538268 232 RPVEIAAVDELYRDRRMPYTVGLLGSV 258
Cdd:PRK11701 229 RVVESGLTDQVLDDPQHPYTQLLVSSV 255
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
383-585 |
1.10e-38 |
|
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: 141.66 E-value: 1.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTlGIVGESGSGKSTTLNQILELTKPEAGSIEILGT---DVAV-LDAAARRRlrtELQVVFQDpvASLDPRL 458
Cdd:cd03297 17 IDFDLNEEVT-GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkINLPPQQR---KIGLVFQQ--YALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 459 PVYDVIAEPLRanGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQ 538
Cdd:cd03297 91 NVRENLAFGLK--RKRNREDRISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1424538268 539 AGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQG 585
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
381-581 |
1.24e-38 |
|
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: 141.78 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRTELQVVFQDpvASLDPRLPV 460
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:cd03292 96 YENVAFALEVTGVPPREIRKRVPAALELVGLSHK-HRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1424538268 541 IVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMI 581
Cdd:cd03292 175 IMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-228 |
2.12e-38 |
|
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: 140.75 E-value: 2.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 6 EVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSDHA--M 83
Cdd:cd03235 1 EVEDLTVSYG----GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPT---SGSIRVFGKPLEKERKRIgyV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 SQIRG---RMIGTVFQDPMSALTPvyTIGdqiaeaieiHSREISRADaRRRAVELLELVGIAQPERRARAfphELSGGER 160
Cdd:cd03235 74 PQRRSidrDFPISVRDVVLMGLYG--HKG---------LFRRLSKAD-KAKVDEALERVGLSELADRQIG---ELSGGQQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 161 QRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVM 228
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
383-603 |
2.15e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 141.43 E-value: 2.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARrrlrtELQVVFQDpvASLDPRLPVYD 462
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER-----PVSMLFQE--NNLFPHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 463 VIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIV 542
Cdd:COG3840 91 NIGLGLRPGLKLTAEQRAQVEQALERVGLAGL-LDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEML 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 543 NLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLL 603
Cdd:COG3840 170 DLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
350-576 |
2.17e-38 |
|
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: 141.42 E-value: 2.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 350 PVVLRVSDLTKTYRL-TKGVVVRRRVgevravDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEIL--GT 426
Cdd:COG4778 2 TTLLEVENLSKTFTLhLQGGKRLPVL------DGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 427 DVAVLDAAARR--RLRTE--------LQVVfqdpvasldPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSDA 496
Cdd:COG4778 76 WVDLAQASPREilALRRRtigyvsqfLRVI---------PRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 497 SRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVM 576
Cdd:COG4778 147 DLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDV 225
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
4-232 |
2.37e-38 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 140.92 E-value: 2.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIGLLpeyARV-SGSIRLHGKELLGLSDHA 82
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTL-LTLIGGL---RSVqEGSLKVLGQELHGASKKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 83 MSQIRgRMIGTVFQDpmSALTPVYTIGDQIAEAIEIHsREISRADARRRAVELLELVGIaqpERRARAFPHELSGGERQR 162
Cdd:TIGR02982 77 LVQLR-RRIGYIFQA--HNLLGFLTARQNVQMALELQ-PNLSYQEARERARAMLEAVGL---GDHLNYYPHNLSGGQKQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 163 VVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRT-ARDvTGAAVLIITHD---LGVvsefADRALVMYAGR 232
Cdd:TIGR02982 150 VAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKlAKE-QGCTILMVTHDnriLDV----ADRILQMEDGK 218
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
395-606 |
3.09e-38 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 143.79 E-value: 3.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 395 IVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAvlDAAARRRlrtELQVVFQDpvASLDPRLPVYDVIAEPLRANGFH 474
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT--NVPPHLR---HINMVFQS--YALFPHMTVEENVAFGLKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 475 RHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGL 554
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEF-ADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 555 SYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLAAV 606
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-282 |
4.83e-38 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 141.80 E-value: 4.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHGKELLglSDHAMSQIRgR 89
Cdd:TIGR04520 5 NVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLlPT----SGKVTVDGLDTL--DEENLWEIR-K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 90 MIGTVFQDP----MSAltpvyTIGDQIAEAIEihSREISRADARRRAVELLELVGIAQPERRArafPHELSGGERQRVVI 165
Cdd:TIGR04520 78 KVGMVFQNPdnqfVGA-----TVEDDVAFGLE--NLGVPREEMRKRVDEALKLVGMEDFRDRE---PHLLSGGQKQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 166 AIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEfADRALVMYAGRPVEIAAVDELYRD 245
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1424538268 246 RRMPYTVGLlgSVP---RLDAAQGTRLIPIPGAPPTMTSL 282
Cdd:TIGR04520 227 VELLKEIGL--DVPfitELAKALKKRGIPLPPDILTEEEL 264
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
382-600 |
9.54e-38 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 140.56 E-value: 9.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKST---TLNQILELTkPEA---GSIEILGTDV--AVLDAAArrrLRTELQVVFQDPVas 453
Cdd:COG1117 29 DINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLI-PGArveGEILLDGEDIydPDVDVVE---LRRRVGMVFQKPN-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 454 ldPrLP--VYDVIAEPLRANGFH-RHECEERVAELLAVVGL-----DHSDASryPAEFSGGQKQRIGIARALALQPKILA 525
Cdd:COG1117 103 --P-FPksIYDNVAYGLRLHGIKsKSELDEIVEESLRKAALwdevkDRLKKS--ALGLSGGQQQRLCIARALAVEPEVLL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 526 LDEPVSALD-VSIQAgIVNLLLDLQRRFglSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTR 600
Cdd:COG1117 178 MDEPTSALDpISTAK-IEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTE 250
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-257 |
9.85e-38 |
|
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: 139.78 E-value: 9.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 22 PAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlpEYARvSGSIRLHGKELLGLSdhamsqIRGRMIGTVFQDpmSA 101
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL--ERPD-SGTILFGGEDATDVP------VQERNVGFVFQH--YA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 102 LTPVYTIGDQIAEAIEIH--SREISRADARRRAVELLELVGIAQPERRaraFPHELSGGERQRVVIAIAIANDPDLLICD 179
Cdd:cd03296 85 LFRHMTVFDNVAFGLRVKprSERPPEAEIRAKVHELLKLVQLDWLADR---YPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 180 EPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDRRMPYTVGLLGS 257
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-242 |
1.04e-37 |
|
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: 139.62 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDievpAVRGTSYHIDPGEVLAIVGESGCGKTT--AALAVIGLLPEYARVSGSIRLHGKELLGLSDHA 82
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTllRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 83 MSqIRgRMIGTVFQDPMSALTPVYtigDQIAEAIEIHsREISRADARRRAVELLELVGIAqPERRARAFPHELSGGERQR 162
Cdd:cd03260 77 LE-LR-RRVGMVFQKPNPFPGSIY---DNVAYGLRLH-GIKLKEELDERVEEALRKAALW-DEVKDRLHALGLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 163 VVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTgaAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDEL 242
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
22-244 |
1.08e-37 |
|
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: 139.68 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 22 PAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGL-LPEyarvSGSIRLHGKELLGLSDHAmsqirgRMIGTVFQDpmS 100
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFeTPT----SGEILLDGKDITNLPPHK------RPVNTVFQN--Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 101 ALTPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGIAQPERRaraFPHELSGGERQRVVIAIAIANDPDLLICDE 180
Cdd:cd03300 82 ALFPHLTVFENIAFGLRL--KKLPKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 181 PTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYR 244
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
381-581 |
1.19e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 138.80 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRlrtelQV--VFQDPVASLDPrl 458
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRR-----QVayVPQEPALWGGT-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 459 pVYDVIAEPLRANgfHRHECEERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQ 538
Cdd:COG4619 90 -VRDNLPFPFQLR--ERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1424538268 539 AGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMI 581
Cdd:COG4619 167 RRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-245 |
2.34e-37 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 139.04 E-value: 2.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 3 AVLEVTDLNVTFETEdieVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSDHA 82
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPT---SGEILVDGQDVTALRGRA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 83 MSQIRGRmIGTVFQDP-----MSALTPVYT--IGDqiaeaieiHS------REISRADaRRRAVELLELVGIA-QPERRA 148
Cdd:COG3638 75 LRRLRRR-IGMIFQQFnlvprLSVLTNVLAgrLGR--------TStwrsllGLFPPED-RERALEALERVGLAdKAYQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 149 rafpHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVM 228
Cdd:COG3638 145 ----DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGL 220
|
250 260
....*....|....*....|....*
gi 1424538268 229 YAGR------PVEI--AAVDELYRD 245
Cdd:COG3638 221 RDGRvvfdgpPAELtdAVLREIYGG 245
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
381-584 |
2.83e-37 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 139.23 E-value: 2.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGtdVAVLDAAARRrlrtelQVVFQDpvASLDPRLPV 460
Cdd:COG4525 24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG--VPVTGPGADR------GVVFQK--DALLPWLNV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDV----S 536
Cdd:COG4525 94 LDNVAFGLRLRGVPKAERRARAEELLALVGLADF-ARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAltreQ 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1424538268 537 IQAgivnLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVM--YRGMIVEQ 584
Cdd:COG4525 173 MQE----LLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVER 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
381-606 |
4.57e-37 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 138.30 E-value: 4.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGsiEILGTDVAVLDAAARRRL-RTELQVVFQDpvASLDPRLP 459
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSG--DLIVDGLKVNDPKVDERLiRQEAGMVFQQ--FYLFPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 460 VYDVIA-EPLRANGFHRHECEERVAELLAVVGLDhSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQ 538
Cdd:PRK09493 94 ALENVMfGPLRVRGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 539 AGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLAAV 606
Cdd:PRK09493 173 HEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-242 |
6.01e-37 |
|
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: 138.55 E-value: 6.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 21 VPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELLGLSDHAMSQIRGRMIGTVFQDpmS 100
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEP---TSGKVLIDGQDIAAMSRKELRELRRKKISMVFQS--F 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 101 ALTPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGIAQPERRaraFPHELSGGERQRVVIAIAIANDPDLLICDE 180
Cdd:cd03294 112 ALLPHRTVLENVAFGLEV--QGVPRAEREERAAEALELVGLEGWEHK---YPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 181 PTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDEL 242
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-232 |
6.22e-37 |
|
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: 135.78 E-value: 6.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeyaRVSGSIRLHGKELLGLSDhaMS 84
Cdd:cd03229 1 LELKNVSKRYG----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE---PDSGSILIDGEDLTDLED--EL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 QIRGRMIGTVFQDPmsALTPVYTIGDQIAEAieihsreisradarrravellelvgiaqperrarafpheLSGGERQRVV 164
Cdd:cd03229 72 PPLRRRIGMVFQDF--ALFPHLTVLENIALG---------------------------------------LSGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 165 IAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-590 |
1.31e-36 |
|
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: 143.79 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEVpaVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIGLLPEYARVSGSIRLH------------------- 71
Cdd:TIGR03269 5 NLTKKFDGKEV--LKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQYEPTSGRIIYHvalcekcgyverpskvgep 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 72 ----GKEL-------LGLSDHAMSQIRGRmIGTVFQDPMsALTPVYTIGDQIAEAIeiHSREISRADARRRAVELLELVg 140
Cdd:TIGR03269 82 cpvcGGTLepeevdfWNLSDKLRRRIRKR-IAIMLQRTF-ALYGDDTVLDNVLEAL--EEIGYEGKEAVGRAVDLIEMV- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 141 iaQPERRARAFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSE 220
Cdd:TIGR03269 157 --QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 221 FADRALVMYAGRPVEIAAVDELyrdrrmpyTVGLLGSVPRLDAAQgtrlipipgapptmtslspgactfaprcplaidEC 300
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGTPDEV--------VAVFMEGVSEVEKEC---------------------------------EV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 301 LSAEPdlvrvadghwaacirtddvagrsaadvfgvstqpppnnaaggqppvVLRVSDLTKTY-RLTKGVVVRRrvgevra 379
Cdd:TIGR03269 274 EVGEP----------------------------------------------IIKVRNVSKRYiSVDRGVVKAV------- 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 380 vDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEIL----GTDVAVLDAAARRRLRTELQVVFQDpvASLD 455
Cdd:TIGR03269 301 -DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdeWVDMTKPGPDGRGRAKRYIGILHQE--YDLY 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 456 PRLPVYDVIAEPLRANgFHRHECEERVAELLAVVGLDHSDA----SRYPAEFSGGQKQRIGIARALALQPKILALDEPVS 531
Cdd:TIGR03269 378 PHRTVLDNLTEAIGLE-LPDELARMKAVITLKMVGFDEEKAeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 532 ALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQV 590
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
21-232 |
1.51e-36 |
|
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: 136.00 E-value: 1.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 21 VPAVRGTSYHIDPGEVLAIVGESGCGKTTaalaVIGLLPEYAR-VSGSIRLHGKELLGLSDHAMSQIRgRMIGTVFQDpm 99
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKST----LLKLIYKEELpTSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQD-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 100 SALTPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGIAQperRARAFPHELSGGERQRVVIAIAIANDPDLLICD 179
Cdd:cd03292 87 FRLLPDRNVYENVAFALEV--TGVPPREIRKRVPAALELVGLSH---KHRALPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 180 EPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
381-585 |
1.70e-36 |
|
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: 134.49 E-value: 1.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRTelqVVFQdpvasldprlpv 460
Cdd:cd03214 16 DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIA---YVPQ------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 ydviaeplrangfhrheceervaeLLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:cd03214 81 ------------------------ALELLGLAHL-ADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1424538268 541 IVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQG 585
Cdd:cd03214 136 LLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
383-594 |
2.21e-36 |
|
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: 139.47 E-value: 2.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVavLDAAARRRLRTE---LQVVFQDpvASLDPRLP 459
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSARGIFLPPHrrrIGYVFQE--ARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 460 VydviaeplRAN---GFHRHECEERVAELLAVV---GLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSAL 533
Cdd:COG4148 94 V--------RGNllyGRKRAPRAERRISFDEVVellGIGHL-LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 534 DVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNP 594
Cdd:COG4148 165 DLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-232 |
3.58e-36 |
|
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: 135.64 E-value: 3.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSDHams 84
Cdd:cd03219 1 LEVRGLTKRFG----GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT---SGSVLFDGEDITGLPPH--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 QIRGRMIGTVFQDP-----MSALTPVYtIGDQIA--EAIEIHSREISRADARRRAVELLELVGIAqpeRRARAFPHELSG 157
Cdd:cd03219 71 EIARLGIGRTFQIPrlfpeLTVLENVM-VAAQARtgSGLLLARARREEREARERAEELLERVGLA---DLADRPAGELSY 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 158 GERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
353-590 |
3.66e-36 |
|
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: 135.77 E-value: 3.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRLTKgvvvrrrvgevRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLD 432
Cdd:cd03256 1 IEVENLSKTYPNGK-----------KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 433 AAARRRLRTELQVVFQDPvaSLDPRLPVYDVI-------AEPLRA--NGFHRHEcEERVAELLAVVGLDHsDASRYPAEF 503
Cdd:cd03256 70 GKALRQLRRQIGMIFQQF--NLIERLSVLENVlsgrlgrRSTWRSlfGLFPKEE-KQRALAALERVGLLD-KAYQRADQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 504 SGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVE 583
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVF 225
|
....*..
gi 1424538268 584 QGESDQV 590
Cdd:cd03256 226 DGPPAEL 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
383-601 |
5.40e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 135.56 E-value: 5.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKST---TLNQILELTKPEA---GSIEILGTDVAVLDAAarrRLRTELQVVFQDPvaSLDP 456
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTllkVLNRLIEIYDSKIkvdGKVLYFGKDIFQIDAI---KLRKEVGMVFQQP--NPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 457 RLPVYDVIAEPLRANGF-HRHECEERVAELLAVVGL--DHSDASRYPA-EFSGGQKQRIGIARALALQPKILALDEPVSA 532
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIkEKREIKKIVEECLRKVGLwkEVYDRLNSPAsQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 533 LDVSIQAGIVNLLLDLQRRfgLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRR 601
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-243 |
5.78e-36 |
|
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: 135.00 E-value: 5.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEdieVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELLGLSDHAMS 84
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP---TSGSVLIDGTDINKLKGKALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 QIRGRmIGTVFQDP-----MSALTPVytigdqIAEAIEIHS------REISRADaRRRAVELLELVGIA-QPERRARafp 152
Cdd:cd03256 75 QLRRQ-IGMIFQQFnlierLSVLENV------LSGRLGRRStwrslfGLFPKEE-KQRALAALERVGLLdKAYQRAD--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 153 hELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:cd03256 144 -QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
250
....*....|....*....
gi 1424538268 233 ------PVEI--AAVDELY 243
Cdd:cd03256 223 ivfdgpPAELtdEVLDEIY 241
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-232 |
6.05e-36 |
|
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: 132.94 E-value: 6.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 6 EVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSdhamSQ 85
Cdd:cd03214 1 EVENLSVGYGGRTV----LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS---SGEILLDGKDLASLS----PK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 86 IRGRMIGTVFQdpmsaltpvytigdqiaeaieihsreisradarrraveLLELVGIAqpERRARAFpHELSGGERQRVVI 165
Cdd:cd03214 70 ELARKIAYVPQ--------------------------------------ALELLGLA--HLADRPF-NELSGGERQRVLL 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 166 AIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:cd03214 109 ARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
382-581 |
6.48e-36 |
|
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: 134.20 E-value: 6.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVavldaaarRRLRTELQVVFQdpVASLDPRLP-- 459
Cdd:cd03235 17 DVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL--------EKERKRIGYVPQ--RRSIDRDFPis 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 460 VYDVIAEPL--RANGFHR--HECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDV 535
Cdd:cd03235 87 VRDVVLMGLygHKGLFRRlsKADKAKVDEALERVGLSEL-ADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1424538268 536 SIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMI 581
Cdd:cd03235 166 KTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
383-613 |
1.01e-35 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 137.52 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRrlrteLQVVFQDpvASLDPRLPVYD 462
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK-----VGFVFQH--YALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 463 VIAEPL----RANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQ 538
Cdd:PRK10851 94 NIAFGLtvlpRRERPNAAAIKAKVTQLLEMVQLAHL-ADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 539 AGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLAAVPRAHSDV 613
Cdd:PRK10851 173 KELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNRLQGTI 247
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
381-607 |
1.02e-35 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 136.86 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPE----AGSIEILGTDVAVLDAAARRRL-RTELQVVFQDPVASLD 455
Cdd:PRK15093 24 DRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDIDLLRLSPRERRKLvGHNVSMIFQEPQSCLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 456 PRLPVYDVIAEPL-----RANGFHRHECEERVA-ELLAVVGL-DHSDASR-YPAEFSGGQKQRIGIARALALQPKILALD 527
Cdd:PRK15093 104 PSERVGRQLMQNIpgwtyKGRWWQRFGWRKRRAiELLHRVGIkDHKDAMRsFPYELTEGECQKVMIAIALANQPRLLIAD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 528 EPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLAAVP 607
Cdd:PRK15093 184 EPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQALIRAIP 263
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
381-590 |
1.02e-35 |
|
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: 143.05 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLrteLQVVFQDPVasldprlPV 460
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ---IGVVLQDVF-------LF 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRanGFHRHECEERVAELLAVVGLdHSDASRYP-----------AEFSGGQKQRIGIARALALQPKILALDEP 529
Cdd:COG2274 562 SGTIRENIT--LGDPDATDEEIIEAARLAGL-HDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEA 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 530 VSALDVSIQAGIVNLLLDLQRRFGLsyLFVSHDLSVVKHlAHRVAVMYRGMIVEQGESDQV 590
Cdd:COG2274 639 TSALDAETEAIILENLRRLLKGRTV--IIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
11-244 |
1.09e-35 |
|
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: 134.35 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEvPAVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIGLLPEYArvSGSIRLHGKELLGLSDhamSQIRgRM 90
Cdd:cd03295 5 NVTKRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTT-MKMINRLIEPT--SGEIFIDGEDIREQDP---VELR-RK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 91 IGTVFQDpmSALTPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGIAQPERRARaFPHELSGGERQRVVIAIAIA 170
Cdd:cd03295 77 IGYVIQQ--IGLFPHMTVEENIALVPKL--LKWPKEKIRERADELLALVGLDPAEFADR-YPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 171 NDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYR 244
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-232 |
2.13e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 132.25 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELlglSDHAMS 84
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT---SGEIYLDGKPL---SAMPPP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 QIRgRMIGTVFQDPmsALTPvYTIGDQIAEAIEIHSREISRADARrravELLELVGIAQP--ERRArafpHELSGGERQR 162
Cdd:COG4619 71 EWR-RQVAYVPQEP--ALWG-GTVRDNLPFPFQLRERKFDRERAL----ELLERLGLPPDilDKPV----ERLSGGERQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 163 VVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:COG4619 139 LALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-183 |
2.60e-35 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 130.08 E-value: 2.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 24 VRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSDHamsqIRGRMIGTVFQDPmsALT 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT---EGTILLDGQDLTDDERK----SLRKEIGYVFQDP--QLF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 104 PVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGI-AQPERRARAFPHELSGGERQRVVIAIAIANDPDLLICDEPT 182
Cdd:pfam00005 72 PRLTVRENLRLGLLL--KGLSKREKDARAEEALEKLGLgDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 1424538268 183 T 183
Cdd:pfam00005 150 A 150
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
349-583 |
3.79e-35 |
|
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: 132.56 E-value: 3.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 349 PPVVLRVSDLTKTYRLTKGVVVRRrvgevravDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDV 428
Cdd:COG4181 5 SAPIIELRGLTKTVGTGAGELTIL--------KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 429 AVLDAAARRRLRTE-LQVVFQdpvaS--LDPRLPVYDVIAEPLRANGfhRHECEERVAELLAVVGLDHSdASRYPAEFSG 505
Cdd:COG4181 77 FALDEDARARLRARhVGFVFQ----SfqLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHR-LDHYPAQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 506 GQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLsvvkHLA---HRVAVMYRGMIV 582
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDP----ALAarcDRVLRLRAGRLV 225
|
.
gi 1424538268 583 E 583
Cdd:COG4181 226 E 226
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
352-590 |
4.62e-35 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 132.81 E-value: 4.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 352 VLRVSDLTKTYRLTKgvvvrrrvgevRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVL 431
Cdd:TIGR02315 1 MLEVENLSKVYPNGK-----------QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 432 DAAARRRLRTELQVVFQDpvASLDPRLpvyDVIAEPLRA------------NGFHRHEcEERVAELLAVVGLDHSDASRy 499
Cdd:TIGR02315 70 RGKKLRKLRRRIGMIFQH--YNLIERL---TVLENVLHGrlgykptwrsllGRFSEED-KERALSALERVGLADKAYQR- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 500 PAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRG 579
Cdd:TIGR02315 143 ADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAG 222
|
250
....*....|.
gi 1424538268 580 MIVEQGESDQV 590
Cdd:TIGR02315 223 EIVFDGAPSEL 233
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
381-589 |
9.21e-35 |
|
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: 130.95 E-value: 9.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVaVLDAaarRRLRTELQVVFQDPvaSLDPRLPV 460
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREP---REVRRRIGIVFQDL--SVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:cd03265 91 WENLYIHARLYGVPGAERRERIDELLDFVGLLEA-ADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAH 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1424538268 541 IVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQ 589
Cdd:cd03265 170 VWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
23-261 |
9.31e-35 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 131.46 E-value: 9.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 23 AVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGL-LPEyarvSGSIRLHGKellglsDHAMSQIRGRMIGTVFQDpmSA 101
Cdd:TIGR00968 15 ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLeQPD----SGRIRLNGQ------DATRVHARDRKIGFVFQH--YA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 102 LTPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGIAQPERRaraFPHELSGGERQRVVIAIAIANDPDLLICDEP 181
Cdd:TIGR00968 83 LFKHLTVRDNIAFGLEI--RKHPKAKIKARVEELLELVQLEGLGDR---YPNQLSGGQRQRVALARALAVEPQVLLLDEP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 182 TTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDRRMPYTVGLLGSVPRL 261
Cdd:TIGR00968 158 FGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNVL 237
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-242 |
1.09e-34 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 132.29 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 3 AVLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELLGlsdha 82
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAP---SSGEITLDGVPVTG----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 83 msqiRGRMIGTVFQDpmSALTPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGIAQPERRaraFPHELSGGERQR 162
Cdd:COG4525 74 ----PGADRGVVFQK--DALLPWLNVLDNVAFGLRL--RGVPKAERRARAEELLALVGLADFARR---RIWQLSGGMRQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 163 VVIAIAIANDPDLLICDEPTTALDV----TVQAQILDVLRTardvTGAAVLIITHDlgvVSE---FADRALVMyAGRPVE 235
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDAltreQMQELLLDVWQR----TGKGVFLITHS---VEEalfLATRLVVM-SPGPGR 214
|
....*..
gi 1424538268 236 IAAVDEL 242
Cdd:COG4525 215 IVERLEL 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
339-601 |
1.25e-34 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 135.07 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 339 PPPNNAAGGQPPVVLRVSDLTKTYRLTKgvvvrrrvgevrAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEA 418
Cdd:PRK09452 1 SKKLNKQPSSLSPLVELRGISKSFDGKE------------VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 419 GSIEILGTDVAVLDAAARrrlrtELQVVFQDpvASLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASR 498
Cdd:PRK09452 69 GRIMLDGQDITHVPAENR-----HVNTVFQS--YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEF-AQR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 499 YPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYR 578
Cdd:PRK09452 141 KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRD 220
|
250 260
....*....|....*....|...
gi 1424538268 579 GMIVEQGESDQVFTNPQHEYTRR 601
Cdd:PRK09452 221 GRIEQDGTPREIYEEPKNLFVAR 243
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
381-579 |
2.07e-34 |
|
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: 128.27 E-value: 2.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRTelqVVFQDPVasldprlpv 460
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA---YVPQDPF--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 ydVIAEPLRANgfhrheceervaeLLavvgldhsdasrypaefSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:cd03228 87 --LFSGTIREN-------------IL-----------------SGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 1424538268 541 IVNLLLDLQRrfGLSYLFVSHDLSVVKHlAHRVAVMYRG 579
Cdd:cd03228 135 ILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
384-585 |
2.48e-34 |
|
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: 129.54 E-value: 2.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 384 SFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARrrlrtELQVVFQDpvASLDPRLPVYDV 463
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR-----PVSMLFQE--NNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 464 IAEPLRANGFHRHECEERVAELLAVVGLDHSDAsRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVN 543
Cdd:cd03298 91 VGLGLSPGLKLTAEDRQAIEVALARVGLAGLEK-RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1424538268 544 LLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQG 585
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
381-598 |
2.71e-34 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 133.69 E-value: 2.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAvlDAAARRRlrtELQVVFQDpvASLDPRLPV 460
Cdd:PRK11432 23 DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQR---DICMVFQS--YALFPHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGFHRHECEERVAELLAVVGLDhSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:PRK11432 96 GENVGYGLKMLGVPKEERKQRVKEALELVDLA-GFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 541 IVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEY 598
Cdd:PRK11432 175 MREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
381-579 |
4.03e-34 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 126.98 E-value: 4.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRlrtELQVVFQdpvasldprlpv 460
Cdd:cd00267 16 DNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR---RIGYVPQ------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 ydviaeplrangfhrheceervaellavvgldhsdasrypaeFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:cd00267 81 ------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRER 118
|
170 180 190
....*....|....*....|....*....|....*....
gi 1424538268 541 IVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRG 579
Cdd:cd00267 119 LLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-242 |
4.48e-34 |
|
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: 129.98 E-value: 4.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTTA--ALAviGLLPEYarvSGSIRLHGKELLGLSDH 81
Cdd:COG4555 1 MIEVENLSKKYG----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLlrMLA--GLLKPD---SGSILIDGEDVRKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 82 AMSQIrgrmiGTVFQDPMsaLTPVYTIGDQIAEAIEIHsrEISRADARRRAVELLELVGIAQP-ERRArafpHELSGGER 160
Cdd:COG4555 72 ARRQI-----GVLPDERG--LYDRLTVRENIRYFAELY--GLFDEELKKRIEELIELLGLEEFlDRRV----GELSTGMK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 161 QRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVD 240
Cdd:COG4555 139 KKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLD 217
|
..
gi 1424538268 241 EL 242
Cdd:COG4555 218 EL 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
381-591 |
4.97e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.91 E-value: 4.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTdvaVLDAAARRRLRTELQVVFQDP----VASldp 456
Cdd:PRK13635 24 KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVRRQVGMVFQNPdnqfVGA--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 457 rlPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDhSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVS 536
Cdd:PRK13635 98 --TVQDDVAFGLENIGVPREEMVERVDQALRQVGME-DFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 537 IQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQGESDQVF 591
Cdd:PRK13635 175 GRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
383-594 |
5.20e-34 |
|
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: 132.93 E-value: 5.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLE-QGRTlGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAvlDAAARRRLRTE---LQVVFQDpvASLDPRL 458
Cdd:TIGR02142 16 ADFTLPgQGVT-AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF--DSRKGIFLPPEkrrIGYVFQE--ARLFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 459 PVydviAEPL-----RANGFHRHECEERVAELLavvGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSAL 533
Cdd:TIGR02142 91 SV----RGNLrygmkRARPSERRISFERVIELL---GIGHL-LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 534 DVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNP 594
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-244 |
5.28e-34 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 129.73 E-value: 5.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEDIevpAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELLGLSDHAM 83
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQ---ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEP---SSGSILLEGTDITKLRGKKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 SQIRgRMIGTVFQD-----PMSALTPVYTIGDQIAEAIEIHSREISRADaRRRAVELLELVGIA-QPERRARafphELSG 157
Cdd:TIGR02315 75 RKLR-RRIGMIFQHynlieRLTVLENVLHGRLGYKPTWRSLLGRFSEED-KERALSALERVGLAdKAYQRAD----QLSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 158 GERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRAL------VMYAG 231
Cdd:TIGR02315 149 GQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVglkageIVFDG 228
|
250
....*....|....*
gi 1424538268 232 RPVEI--AAVDELYR 244
Cdd:TIGR02315 229 APSELddEVLRHIYG 243
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-231 |
5.70e-34 |
|
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: 128.53 E-value: 5.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 6 EVTDLNVTFEtEDIEVpaVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKEllglsdhAMSQ 85
Cdd:cd03226 1 RIENISFSYK-KGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES---SGSILLNGKP-------IKAK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 86 IRGRMIGTVFQDPMSALTpvytiGDQIAEAIEIHSREISraDARRRAVELLELVGIAQPERRaraFPHELSGGERQRVVI 165
Cdd:cd03226 68 ERRKSIGYVMQDVDYQLF-----TDSVREELLLGLKELD--AGNEQAETVLKDLDLYALKER---HPLSLSGGQKQRLAI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 166 AIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAG 231
Cdd:cd03226 138 AAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAA-QGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
23-258 |
5.77e-34 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 129.95 E-value: 5.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 23 AVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSDHAMSQIRGRMI-----GTVFQD 97
Cdd:TIGR02323 18 GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPD---HGTATYIMRSGAELELYQLSEAERRRLmrtewGFVHQN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 98 PMSALTPVYTIGDQIAE-AIEIHSREIsrADARRRAVELLELVGIaqPERRARAFPHELSGGERQRVVIAIAIANDPDLL 176
Cdd:TIGR02323 95 PRDGLRMRVSAGANIGErLMAIGARHY--GNIRATAQDWLEEVEI--DPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 177 ICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDRRMPYTVGLLG 256
Cdd:TIGR02323 171 FMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVS 250
|
..
gi 1424538268 257 SV 258
Cdd:TIGR02323 251 SI 252
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
384-606 |
6.39e-34 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 133.62 E-value: 6.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 384 SFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVA-VLDAAARRRLRTELQVVFQDpvASLDPRLPVYD 462
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkISDAELREVRRKKIAMVFQS--FALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 463 VIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIV 542
Cdd:PRK10070 126 NTAFGMELAGINAEERREKALDALRQVGLENY-AHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 543 NLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLAAV 606
Cdd:PRK10070 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
381-595 |
1.21e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 129.95 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDV-AVLDAAARRRLRTELQVVFQDPVASLDPRLP 459
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLRKKVSLVFQFPEAQLFENTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 460 VYDVIAEPLRAnGFHRHECEERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQA 539
Cdd:PRK13641 104 LKDVEFGPKNF-GFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 540 GIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQ 595
Cdd:PRK13641 183 EMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-232 |
1.83e-33 |
|
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: 125.57 E-value: 1.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSDHAMSqirgRM 90
Cdd:cd03228 5 NVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT---SGEILIDGVDLRDLDLESLR----KN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 91 IGTVFQDP--MSAltpvyTIGDQIaeaieihsreisradarrravellelvgiaqperrarafpheLSGGERQRVVIAIA 168
Cdd:cd03228 78 IAYVPQDPflFSG-----TIRENI------------------------------------------LSGGQRQRIAIARA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 169 IANDPDLLICDEPTTALDVTVQAQILDVLRTARDvtGAAVLIITHDLGVVsEFADRALVMYAGR 232
Cdd:cd03228 111 LLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-232 |
1.94e-33 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 125.05 E-value: 1.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 6 EVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSDHAmsq 85
Cdd:cd00267 1 EIENLSFRYG----GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT---SGEILIDGKDIAKLPLEE--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 86 iRGRMIGTVFQdpmsaltpvytigdqiaeaieihsreisradarrravellelvgiaqperrarafpheLSGGERQRVVI 165
Cdd:cd00267 71 -LRRRIGYVPQ----------------------------------------------------------LSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 166 AIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
353-573 |
3.20e-33 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 126.74 E-value: 3.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRLTKgvvvrRRVGEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEI--LGTDVAV 430
Cdd:TIGR02324 2 LEVEDLSKTFTLHQ-----QGGVRLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVrhEGAWVDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 431 LDAAARRRL---RTELQVVFQdpvaSLD--PRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSDASRYPAEFSG 505
Cdd:TIGR02324 77 AQASPREVLevrRKTIGYVSQ----FLRviPRVSALEVVAEPLLERGVPREAARARARELLARLNIPERLWHLPPATFSG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 506 GQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRV 573
Cdd:TIGR02324 153 GEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRV 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-232 |
3.58e-33 |
|
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: 126.78 E-value: 3.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTF---ETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGllpEYARVSGSIRLHGKE--- 74
Cdd:COG4778 1 MTTLLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG---NYLPDSGSILVRHDGgwv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 75 -LLGLSDHAMSQIRGRMIGTVFQ----DP-MSALtpvytigDQIAEAIEihSREISRADARRRAVELLELVGIaqPERRA 148
Cdd:COG4778 78 dLAQASPREILALRRRTIGYVSQflrvIPrVSAL-------DVVAEPLL--ERGVDREEARARARELLARLNL--PERLW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 149 RAFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVM 228
Cdd:COG4778 147 DLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKA-RGTAIIGIFHDEEVREAVADRVVDV 225
|
....
gi 1424538268 229 YAGR 232
Cdd:COG4778 226 TPFS 229
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
383-573 |
3.93e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 126.85 E-value: 3.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRT-ELQVVFQdpVASLDPRLPVY 461
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNqKLGFIYQ--FHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 DVIAEPLRANGFHRHECEERVAELLAVVGLDHSDASRyPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGI 541
Cdd:PRK11629 106 ENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180 190
....*....|....*....|....*....|..
gi 1424538268 542 VNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRV 573
Cdd:PRK11629 185 FQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-244 |
4.38e-33 |
|
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: 133.73 E-value: 4.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDievPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSDHAms 84
Cdd:COG4988 337 IELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY---SGSILINGVDLSDLDPAS-- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 qiRGRMIGTVFQDPmsaltpvYTIGDQIAEAIEIHSREISRADARR--RAVELLELV-----GIAQP--ERRARafpheL 155
Cdd:COG4988 409 --WRRQIAWVPQNP-------YLFAGTIRENLRLGRPDASDEELEAalEAAGLDEFVaalpdGLDTPlgEGGRG-----L 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 156 SGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvtGAAVLIITHDLGVVsEFADRALVMYAGRPVE 235
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALL-AQADRILVLDDGRIVE 551
|
....*....
gi 1424538268 236 IAAVDELYR 244
Cdd:COG4988 552 QGTHEELLA 560
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
353-589 |
4.86e-33 |
|
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: 126.08 E-value: 4.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRltkgvvvrrrVGEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVavld 432
Cdd:cd03263 1 LQIRNLTKTYK----------KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 433 AAARRRLRTELQVVFQDPVasLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGL-DHSDasRYPAEFSGGQKQRI 511
Cdd:cd03263 67 RTDRKAARQSLGYCPQFDA--LFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLtDKAN--KRARTLSGGMKRKL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 512 GIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRrfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQ 589
Cdd:cd03263 143 SLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
325-589 |
5.96e-33 |
|
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: 133.34 E-value: 5.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 325 AGRSAAD-VFGVSTQPPPNNAAGGQP-----PVVLRVSDLTKTYrltkgvvvrrrVGEVRAVDGISFTLEQGRTLGIVGE 398
Cdd:COG4988 303 NGIAAAEkIFALLDAPEPAAPAGTAPlpaagPPSIELEDVSFSY-----------PGGRPALDGLSLTIPPGERVALVGP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 399 SGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLrteLQVVFQDPVasldprlpvydVIAEPLRAN-GFHRHE 477
Cdd:COG4988 372 SGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ---IAWVPQNPY-----------LFAGTIRENlRLGRPD 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 478 C-EERVAELLAVVGLDHsDASRYP-----------AEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLL 545
Cdd:COG4988 438 AsDEELEAALEAAGLDE-FVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL 516
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1424538268 546 LDLQRrfGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQGESDQ 589
Cdd:COG4988 517 RRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
381-595 |
7.63e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 127.50 E-value: 7.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTT---LNQILeltKPEAGSIEILGTDVAvLDAAARRRLRTELQVVFQDPVASLDPR 457
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLflhFNGIL---KPTSGEVLIKGEPIK-YDKKSLLEVRKTVGIVFQNPDDQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 458 LPVYDVIAEPLRAnGFHRHECEERVAELLAVVGLDHSDaSRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSI 537
Cdd:PRK13639 95 TVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFE-NKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 538 QAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQ 595
Cdd:PRK13639 173 ASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
339-606 |
9.49e-33 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 129.96 E-value: 9.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 339 PPPNNAAGGQPPVVLRVSDLTKTYrltkgvvvrrrvGEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEA 418
Cdd:PRK11607 6 PRPQAKTRKALTPLLEIRNLTKSF------------DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 419 GSIEILGTDVAVLDAAARrrlrtELQVVFQDpvASLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASR 498
Cdd:PRK11607 74 GQIMLDGVDLSHVPPYQR-----PINMMFQS--YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEF-AKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 499 YPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYR 578
Cdd:PRK11607 146 KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNR 225
|
250 260
....*....|....*....|....*...
gi 1424538268 579 GMIVEQGESDQVFTNPQHEYTRRLLAAV 606
Cdd:PRK11607 226 GKFVQIGEPEEIYEHPTTRYSAEFIGSV 253
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-232 |
1.13e-32 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 123.66 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETedieVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSDHAMs 84
Cdd:cd03230 1 IEVRNLSKRYGK----KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD---SGEIKVLGKDIKKEPEEVK- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 qirgRMIGTVFQDPMsaLTPVYTIGDQIaeaieihsreisradarrravellelvgiaqperrarafphELSGGERQRVV 164
Cdd:cd03230 73 ----RRIGYLPEEPS--LYENLTVRENL-----------------------------------------KLSGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 165 IAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-224 |
1.43e-32 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 124.26 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 7 VTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIGLLPEYArvSGSIRLHGKELLGLSDHAMSQI 86
Cdd:TIGR03608 1 LKNISKKFGDKVI----LDDLNLTIEKGKMYAIIGESGSGKSTL-LNIIGLLEKFD--SGQVYLNGQETPPLNSKKASKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 87 RGRMIGTVFQDpmSALTPVYTIGDQIAEAIeIHSReISRADARRRAVELLELVGIAQPERRaraFPHELSGGERQRVVIA 166
Cdd:TIGR03608 74 RREKLGYLFQN--FALIENETVEENLDLGL-KYKK-LSKKEKREKKKEALEKVGLNLKLKQ---KIYELSGGEQQRVALA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 167 IAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLgVVSEFADR 224
Cdd:TIGR03608 147 RAILKPPPLILADEPTGSLDPKNRDEVLDLLLELND-EGKTIIIVTHDP-EVAKQADR 202
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
353-585 |
1.83e-32 |
|
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: 124.40 E-value: 1.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRLTKGVVVRRrvgevravDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLD 432
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAV--------DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 433 AAARRRLRtelqvVFQDPVAsLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIG 512
Cdd:cd03266 74 AEARRRLG-----FVSDSTG-LYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEEL-LDRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 513 IARALALQPKILALDEPVSALDVSIQAGIVNLLLDLqRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQG 585
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-243 |
2.81e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 126.00 E-value: 2.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTdlNVTFE-TEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHGKELlgl 78
Cdd:PRK13650 1 MSNIIEVK--NLTFKyKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLeAE----SGQIIIDGDLL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 79 SDHAMSQIRgRMIGTVFQDPMSALTPVyTIGDQIAEAIEihSREISRADARRRAVELLELVGIAQPERRArafPHELSGG 158
Cdd:PRK13650 72 TEENVWDIR-HKIGMVFQNPDNQFVGA-TVEDDVAFGLE--NKGIPHEEMKERVNEALELVGMQDFKERE---PARLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 159 ERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSeFADRALVMYAGRPVEIAA 238
Cdd:PRK13650 145 QKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTST 223
|
....*
gi 1424538268 239 VDELY 243
Cdd:PRK13650 224 PRELF 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
381-601 |
3.49e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 124.64 E-value: 3.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTL---NQILELTkPEA---GSIEILGTDVAVLDAAarrRLRTELQVVFQDPvaSL 454
Cdd:PRK14247 20 DGVNLEIPDNTITALMGPSGSGKSTLLrvfNRLIELY-PEArvsGEVYLDGQDIFKMDVI---ELRRRVQMVFQIP--NP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 455 DPRLPVYDVIAEPLRANGF--HRHECEERVAELLAVVGL-----DHSDAsryPA-EFSGGQKQRIGIARALALQPKILAL 526
Cdd:PRK14247 94 IPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwdevkDRLDA---PAgKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 527 DEPVSALDVSIQAGIVNLLLDLQRRfgLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRR 601
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEK 243
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
383-595 |
3.94e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 125.90 E-value: 3.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEIlGTDV--AVLDAAARRRLRTELQVVFQDPVASLDPRLPV 460
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitAGKKNKKLKPLRKKVGIVFQFPEHQLFEETVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLraN-GFHRHECEERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQA 539
Cdd:PRK13634 105 KDICFGPM--NfGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 540 GIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQ 595
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-258 |
4.77e-32 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 127.08 E-value: 4.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETedieVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGL-LPEyarvSGSIRLHGKELLGLS 79
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLeRQT----AGTIYQGGRDITRLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 80 DHAmsqirgRMIGTVFQDpmSALTPVYTIGDQIAEAIeiHSREISRADARRRAVELLELVGIAQPERRaraFPHELSGGE 159
Cdd:TIGR03265 73 PQK------RDYGIVFQS--YALFPNLTVADNIAYGL--KNRGMGRAEVAERVAELLDLVGLPGSERK---YPGQLSGGQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 160 RQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAV 239
Cdd:TIGR03265 140 QQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTP 219
|
250
....*....|....*....
gi 1424538268 240 DELYRDRRMPYTVGLLGSV 258
Cdd:TIGR03265 220 QEIYRHPATPFVADFVGEV 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-242 |
4.84e-32 |
|
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: 131.88 E-value: 4.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSdhaMSQIRgRM 90
Cdd:COG2274 478 NVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT---SGRILIDGIDLRQID---PASLR-RQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 91 IGTVFQDPmsaltpvYTIGDQIAEAIEIHSREISRADArrraVELLELVGIAQperRARAFPH-----------ELSGGE 159
Cdd:COG2274 551 IGVVLQDV-------FLFSGTIRENITLGDPDATDEEI----IEAARLAGLHD---FIEALPMgydtvvgeggsNLSGGQ 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 160 RQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARdvTGAAVLIITHDLGVVsEFADRALVMYAGRPVEIAAV 239
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTH 693
|
...
gi 1424538268 240 DEL 242
Cdd:COG2274 694 EEL 696
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
382-606 |
1.22e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 123.41 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKST---TLNQILELTkPEA---GSIEILGTDVAVLDAAARRrLRTELQVVFQDPvaSLD 455
Cdd:PRK14267 22 GVDLKIPQNGVFALMGPSGCGKSTllrTFNRLLELN-EEArveGEVRLFGRNIYSPDVDPIE-VRREVGMVFQYP--NPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 456 PRLPVYDVIAEPLRANGF--HRHECEERVAELLAVVGLDHSDASR---YPAEFSGGQKQRIGIARALALQPKILALDEPV 530
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 531 SALDVSIQAGIVNLLLDLQRRFglSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLAAV 606
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGA 251
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
381-581 |
2.02e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 123.30 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILG---TDVAVLDaaarrrLRTELQVVFQDPvaslDPR 457
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllTEENVWD------IRHKIGMVFQNP----DNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 458 L---PVYDVIAEPLRANGFHRHECEERVAELLAVVGLdhSD-ASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSAL 533
Cdd:PRK13650 94 FvgaTVEDDVAFGLENKGIPHEEMKERVNEALELVGM--QDfKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSML 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1424538268 534 DVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKhLAHRVAVMYRGMI 581
Cdd:PRK13650 172 DPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
381-592 |
2.50e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 122.57 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAA--ARRR--LRTELQVVFqdpvasldP 456
Cdd:PRK13548 19 DDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelARRRavLPQHSSLSF--------P 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 457 rLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSDASRYPaEFSGGQKQRIGIARALA------LQPKILALDEPV 530
Cdd:PRK13548 91 -FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 531 SALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFT 592
Cdd:PRK13548 169 SALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
340-594 |
2.53e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 124.19 E-value: 2.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 340 PPNNAAGGqppVVLRVSDLTKTYRltkgvvvRRRVGEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAG 419
Cdd:PRK13631 12 VPNPLSDD---IILRVKNLYCVFD-------EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 420 SIEI----LGTDVAVLDAAAR---------RRLRTELQVVFQDPVASLDPRLPVYDVIAEPLrANGFHRHECEERVAELL 486
Cdd:PRK13631 82 TIQVgdiyIGDKKNNHELITNpyskkiknfKELRRRVSMVFQFPEYQLFKDTIEKDIMFGPV-ALGVKKSEAKKLAKFYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 487 AVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVV 566
Cdd:PRK13631 161 NKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHV 239
|
250 260
....*....|....*....|....*...
gi 1424538268 567 KHLAHRVAVMYRGMIVEQGESDQVFTNP 594
Cdd:PRK13631 240 LEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-245 |
2.59e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.19 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 3 AVLEVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVI-GLLpeyaRVS-GSIRLHGKELLGLSd 80
Cdd:COG3839 2 ASLELENVSKSYG----GVEALKDIDLDIEDGEFLVLLGPSGCGKSTL-LRMIaGLE----DPTsGEILIGGRDVTDLP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 hamsqIRGRMIGTVFQDPmsALTPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGIAQ-PERRarafPHELSGGE 159
Cdd:COG3839 72 -----PKDRNIAMVFQSY--ALYPHMTVYENIAFPLKL--RKVPKAEIDRRVREAAELLGLEDlLDRK----PKQLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 160 RQRVVIAIAIANDPDLLICDEPTTALD----VTVQAQILDVLRTardvTGAAVLIITHDLgvvSE---FADRALVMYAGR 232
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRR----LGTTTIYVTHDQ---VEamtLADRIAVMNDGR 211
|
250
....*....|...
gi 1424538268 233 PVEIAAVDELYRD 245
Cdd:COG3839 212 IQQVGTPEELYDR 224
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
4-275 |
6.22e-31 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 123.84 E-value: 6.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIGLLPEYArvSGSIRLHGKELLGLSDHAM 83
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTL-IRCVNLLERPT--SGSVIVDGQDLTTLSNSEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 SQIRgRMIGTVFQDpmSALTPVYTIGDQIAEAIEIHSReiSRADARRRAVELLELVGIAQperRARAFPHELSGGERQRV 163
Cdd:TIGR02314 78 TKAR-RQIGMIFQH--FNLLSSRTVFGNVALPLELDNT--PKDEIKRKVTELLALVGLGD---KHDSYPSNLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 164 VIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELY 243
Cdd:TIGR02314 150 AIARALASNPKVLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIF 229
|
250 260 270
....*....|....*....|....*....|....
gi 1424538268 244 RDRRMPYTVGLLGSVPRLDAAQG--TRLIPIPGA 275
Cdd:TIGR02314 230 SHPKTPLAQKFIRSTLHLSIPEDyqERLQATPFA 263
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
381-585 |
8.15e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 127.20 E-value: 8.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAArrrLRTELQVVFQDPVasldprlpv 460
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES---LRRQIGVVPQDTF--------- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 ydVIAEPLRAN-GFHRHEC-EERVAELLAVVGLdHSDASRYP-----------AEFSGGQKQRIGIARALALQPKILALD 527
Cdd:COG1132 425 --LFSGTIRENiRYGRPDAtDEEVEEAAKAAQA-HEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILD 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 528 EPVSALDV----SIQAGIVNLlldLQRRfglSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQG 585
Cdd:COG1132 502 EATSALDTeteaLIQEALERL---MKGR---TTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-232 |
1.56e-30 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 119.54 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIGLLPEyaRVSGSIRLHGKELLGLSDHAM 83
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTL-LHLLGGLDT--PTSGDVIFNGQPMSKLSSAAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 SQIRGRMIGTVFQdpMSALTPVYTIGDQIAEAIEIHSREisRADARRRAVELLELVGIaqpERRARAFPHELSGGERQRV 163
Cdd:PRK11629 82 AELRNQKLGFIYQ--FHHLLPDFTALENVAMPLLIGKKK--PAEINSRALEMLAAVGL---EHRANHRPSELSGGERQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 164 VIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFaDRALVMYAGR 232
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGR 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
381-596 |
1.64e-30 |
|
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: 119.49 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVavlDAAARRRLrtelqVVFQDpvASLDPRLPV 460
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI---TEPGPDRM-----VVFQN--YSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGFHRHECEER--VAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQ 538
Cdd:TIGR01184 72 RENIALAVDRVLPDLSKSERRaiVEEHIALVGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 539 AGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQV-FTNPQH 596
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
381-563 |
1.79e-30 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 120.19 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGtdVAVLDAAARRrlrtelQVVFQDpvASLDPRLPV 460
Cdd:PRK11248 18 EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG--KPVEGPGAER------GVVFQN--EGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGFHRHECEERVAELLAVVGLDHSDAsRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:PRK11248 88 QDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEK-RYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|...
gi 1424538268 541 IVNLLLDLQRRFGLSYLFVSHDL 563
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHDI 189
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-214 |
3.78e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 117.58 E-value: 3.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 22 PAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYARVSGSIRLHGKELLGLSDHAmsqirgRMIGTVFQDPMsa 101
Cdd:COG4136 15 PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASGEVLLNGRRLTALPAEQ------RRIGILFQDDL-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 102 LTPVYTIGDQIAEAIeihSREISRADARRRAVELLELVGIAQperRARAFPHELSGGERQRVVIAIAIANDPDLLICDEP 181
Cdd:COG4136 87 LFPHLSVGENLAFAL---PPTIGRAQRRARVEQALEEAGLAG---FADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190
....*....|....*....|....*....|...
gi 1424538268 182 TTALDVTVQAQILDVLRTARDVTGAAVLIITHD 214
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
353-585 |
3.83e-30 |
|
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: 117.70 E-value: 3.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRltkgvvvrrrvgEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLD 432
Cdd:cd03268 1 LKTNDLTKTYG------------KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 433 AAARRrlrtelqvvfqdpVASLDPRLPVYDVIA--EPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQR 510
Cdd:cd03268 69 EALRR-------------IGALIEAPGFYPNLTarENLRLLARLLGIRKKRIDEVLDVVGLKDS-AKKKVKGFSLGMKQR 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 511 IGIARALALQPKILALDEPVSALDvsiQAGIV---NLLLDLqRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQG 585
Cdd:cd03268 135 LGIALALLGNPDLLILDEPTNGLD---PDGIKelrELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-242 |
4.02e-30 |
|
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: 117.92 E-value: 4.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeyaRVSGSIRLHGKELLGLSDHAMS 84
Cdd:cd03224 1 LEVENLNAGYG----KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP---PRSGSIRFDGRDITGLPPHERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 QiRGrmIGTVFQDPM--SALTpvytigdqIAEAIEIHSREISRADARRRAVELLELVGIAQPERRARAfpHELSGGERQR 162
Cdd:cd03224 74 R-AG--IGYVPEGRRifPELT--------VEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLA--GTLSGGEQQM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 163 VVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDEL 242
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-243 |
5.09e-30 |
|
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: 118.10 E-value: 5.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTaalaVIGLLPEYARV-SGSIRLHGKELlglSDHAMSQIRgR 89
Cdd:cd03251 5 NVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKST----LVNLIPRFYDVdSGRILIDGHDV---RDYTLASLR-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 90 MIGTVFQDpmsaltpVYTIGDQIAEAIEIHSREISRADARR--RAVELLELV-----GIAQP--ERRARafpheLSGGER 160
Cdd:cd03251 77 QIGLVSQD-------VFLFNDTVAENIAYGRPGATREEVEEaaRAANAHEFImelpeGYDTVigERGVK-----LSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 161 QRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVL-RTARDVTgaaVLIITHDLGVVsEFADRALVMYAGRPVEIAAV 239
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALeRLMKNRT---TFVIAHRLSTI-ENADRIVVLEDGKIVERGTH 220
|
....
gi 1424538268 240 DELY 243
Cdd:cd03251 221 EELL 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
381-590 |
5.81e-30 |
|
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: 117.97 E-value: 5.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRlrtELQVVFQ----------DP 450
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRR---QVGVVLQenvlfnrsirDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 451 VASLDPRLPVYDVIaEPLRANGFHRHECEERvaellavVGLDHSDASRyPAEFSGGQKQRIGIARALALQPKILALDEPV 530
Cdd:cd03252 96 IALADPGMSMERVI-EAAKLAGAHDFISELP-------EGYDTIVGEQ-GAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 531 SALDVSIQAGIVNLLLDLQRrfGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQGESDQV 590
Cdd:cd03252 167 SALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-236 |
6.48e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.94 E-value: 6.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHGKELlglSDHAMSQIRGR 89
Cdd:PRK13632 12 NVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQ----SGEIKIDGITI---SKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 90 mIGTVFQDPMSALTPVyTIGDQIAEAIEihSREISRADARRRAVELLELVGIAQPERRArafPHELSGGERQRVVIAIAI 169
Cdd:PRK13632 85 -IGIIFQNPDNQFIGA-TVEDDIAFGLE--NKKVPPKKMKDIIDDLAKKVGMEDYLDKE---PQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 170 ANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEfADRALVM------YAGRPVEI 236
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFsegkliAQGKPKEI 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
293-585 |
1.21e-29 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 123.72 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 293 CPLAIDECLSAEPDLVRvadgHWAACIRtddvagrSAADVFGVSTQPP----PNNAAGGQPPVVLRVSDLTKTYRltkgv 368
Cdd:COG4987 281 AALALFEALAPLPAAAQ----HLGRVRA-------AARRLNELLDAPPavtePAEPAPAPGGPSLELEDVSFRYP----- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 369 vvrrrVGEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLrteLQVVFQ 448
Cdd:COG4987 345 -----GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR---IAVVPQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 449 DPvasldprlpvyDVIAEPLRAN-GFHRHEC-EERVAELLAVVGLDHsDASRYP-----------AEFSGGQKQRIGIAR 515
Cdd:COG4987 417 RP-----------HLFDTTLRENlRLARPDAtDEELWAALERVGLGD-WLAALPdgldtwlgeggRRLSGGERRRLALAR 484
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 516 ALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLsyLFVSHDLSVVKHlAHRVAVMYRGMIVEQG 585
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV--LLITHRLAGLER-MDRILVLEDGRIVEQG 551
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
381-589 |
1.31e-29 |
|
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: 117.26 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAaarRRLRTELQVVFQDPVasldprlpV 460
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNL---RWLRSQIGLVSQEPV--------L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YD-VIAEPLRANGFHRHECEERVAELLA-----VVGLDH---SDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVS 531
Cdd:cd03249 89 FDgTIAENIRYGKPDATDEEVEEAAKKAnihdfIMSLPDgydTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 532 ALDvSIQAGIVNLLLDlQRRFGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQGESDQ 589
Cdd:cd03249 169 ALD-AESEKLVQEALD-RAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
24-243 |
1.34e-29 |
|
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: 117.05 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 24 VRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHGKELLGLSDHAmsqirgRMIGTVFQDpmSAL 102
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIkPD----SGKILLNGKDITNLPPEK------RDISYVPQN--YAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 103 TPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGIAQPERRArafPHELSGGERQRVVIAIAIANDPDLLICDEPT 182
Cdd:cd03299 83 FPHMTVYKNIAYGLKK--RKVDKKEIERKVLEIAEMLGIDHLLNRK---PETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 183 TALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELY 243
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
28-263 |
1.49e-29 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 120.19 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 28 SYHIDPGEVLAIVGESGCGKTTAaLAVIGLLPEYArvSGSIRLHGKELLGLsdHAmsqiRGRMIGTVFQDpmSALTPVYT 107
Cdd:PRK10851 22 SLDIPSGQMVALLGPSGSGKTTL-LRIIAGLEHQT--SGHIRFHGTDVSRL--HA----RDRKVGFVFQH--YALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 108 IGDQIAEAIEIHSRE--ISRADARRRAVELLELVgiaQPERRARAFPHELSGGERQRVVIAIAIANDPDLLICDEPTTAL 185
Cdd:PRK10851 91 VFDNIAFGLTVLPRRerPNAAAIKAKVTQLLEMV---QLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 186 DVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDRRMPYTVGLLGSVPRLDA 263
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNRLQG 245
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-237 |
1.84e-29 |
|
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: 115.86 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 33 PGEVLAIVGESGCGKTTAALAVIGLLPEYArvsGSIRLHGKELLGLSDHAMSQIRGRMIGTVFQDpmSALTPVYTIgdqi 112
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDG---GTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQ--YALFPHLNV---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 113 AEAIEIHSREISRADARRRAVELLELVGIAQPERRaraFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQ 192
Cdd:cd03297 93 RENLAFGLKRKRNREDRISVDELLDLLGLDHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1424538268 193 ILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIA 237
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
353-585 |
2.38e-29 |
|
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: 115.37 E-value: 2.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRLTKGVvvrrrvgevravDGISFTLEQGrTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAvld 432
Cdd:cd03264 1 LQLENLTKRYGKKRAL------------DGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 433 aAARRRLRTELQVVFQDPvaSLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGL-DHsdASRYPAEFSGGQKQRI 511
Cdd:cd03264 65 -KQPQKLRRRIGYLPQEF--GVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLgDR--AKKKIGSLSGGMRRRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 512 GIARALALQPKILALDEPVSALDVSIQAGIVNLLLDL--QRRFGLSylfvSHDLSVVKHLAHRVAVMYRGMIVEQG 585
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELgeDRIVILS----THIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
381-595 |
3.10e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.01 E-value: 3.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTtLNQILE-LTKPEAGSIEILGTdvaVLDAAARRRLRTELQVVFQDPvaslDPR-- 457
Cdd:PRK13632 26 KNVSFEINEGEYVAILGHNGSGKST-ISKILTgLLKPQSGEIKIDGI---TISKENLKEIRKKIGIIFQNP----DNQfi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 458 -LPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDhSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVS 536
Cdd:PRK13632 98 gATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 537 IQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKhLAHRVAVMYRGMIVEQGESDQVFTNPQ 595
Cdd:PRK13632 177 GKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-254 |
3.15e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 117.12 E-value: 3.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETEDiEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELlglSD 80
Cdd:PRK13642 1 MNKILEVENLVFKYEKES-DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEF---EGKVKIDGELL---TA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 HAMSQIRgRMIGTVFQDPMSALTPVyTIGDQIAEAIEihSREISRADARRRAVELLELVGIAQPERRArafPHELSGGER 160
Cdd:PRK13642 74 ENVWNLR-RKIGMVFQNPDNQFVGA-TVEDDVAFGME--NQGIPREEMIKRVDEALLAVNMLDFKTRE---PARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 161 QRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEfADRALVMYAGRPVEIAAVD 240
Cdd:PRK13642 147 QRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPS 225
|
250
....*....|....
gi 1424538268 241 ELYRDRRMPYTVGL 254
Cdd:PRK13642 226 ELFATSEDMVEIGL 239
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-245 |
3.91e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 122.20 E-value: 3.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDiEVPAVRGTSYHIDPGEVLAIVGESGCGKTTaalaVIGLLPEYARV-SGSIRLHGKELlglSDHAMSQIRgR 89
Cdd:COG1132 344 NVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKST----LVNLLLRFYDPtSGRILIDGVDI---RDLTLESLR-R 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 90 MIGTVFQDPM--SAltpvyTIGDQIAeaieihsreISRADARRRAVEllELVGIAQPERRARAFPH-----------ELS 156
Cdd:COG1132 415 QIGVVPQDTFlfSG-----TIRENIR---------YGRPDATDEEVE--EAAKAAQAHEFIEALPDgydtvvgergvNLS 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 157 GGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARdvTGAAVLIITHDLGVVsEFADRALVMYAGRPVEI 236
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM--KGRTTIVIAHRLSTI-RNADRILVLDDGRIVEQ 555
|
250
....*....|....*
gi 1424538268 237 ------AAVDELYRD 245
Cdd:COG1132 556 gtheelLARGGLYAR 570
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
31-242 |
3.95e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 115.96 E-value: 3.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 31 IDPGEVLAIVGESGCGKTTAaLAVIGLLPEYArvSGSIRLHGKELLGlSDHAMSQIRgRMIGTVFQD----P-MSALTPV 105
Cdd:PRK09493 24 IDQGEVVVIIGPSGSGKSTL-LRCINKLEEIT--SGDLIVDGLKVND-PKVDERLIR-QEAGMVFQQfylfPhLTALENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 106 yTIGdqiaeaiEIHSREISRADARRRAVELLELVGIAQperRARAFPHELSGGERQRVVIAIAIANDPDLLICDEPTTAL 185
Cdd:PRK09493 99 -MFG-------PLRVRGASKEEAEKQARELLAKVGLAE---RAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 186 DVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDEL 242
Cdd:PRK09493 168 DPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-251 |
6.15e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 115.62 E-value: 6.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVlEVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIGLL--PEYARVS-GSIRLHGKELLG 77
Cdd:PRK11264 1 MSAI-EVKNLVKKFHGQTV----LHGIDLEVKPGEVVAIIGPSGSGKTTL-LRCINLLeqPEAGTIRvGDITIDTARSLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 78 LSDHAMSQIRgRMIGTVFQDpmSALTPVYTIGDQIAEAIEIHSREiSRADARRRAVELLELVGIAQPERrarAFPHELSG 157
Cdd:PRK11264 75 QQKGLIRQLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGE-PKEEATARARELLAKVGLAGKET---SYPRRLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 158 GERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVlIITHDLGVVSEFADRALVMYAGRPVEIA 237
Cdd:PRK11264 148 GQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMV-IVTHEMSFARDVADRAIFMDQGRIVEQG 226
|
250
....*....|....
gi 1424538268 238 AVDELYRDRRMPYT 251
Cdd:PRK11264 227 PAKALFADPQQPRT 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-255 |
8.96e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 120.13 E-value: 8.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTfetEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeyaRVSGSIRLHGKELLGLSDHam 83
Cdd:COG3845 257 VLEVENLSVR---DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP---PASGSIRLDGEDITGLSPR-- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 sQIRGRMIGTVFQDPMS-ALTPVYTIGDQIAeaIEIHSRE-------ISRADARRRAVELLELVGI--AQPERRARAfph 153
Cdd:COG3845 329 -ERRRLGVAYIPEDRLGrGLVPDMSVAENLI--LGRYRRPpfsrggfLDRKAIRAFAEELIEEFDVrtPGPDTPARS--- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 154 eLSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRP 233
Cdd:COG3845 403 -LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRD-AGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
250 260
....*....|....*....|..
gi 1424538268 234 VEIAAVDELYRDRrmpytVGLL 255
Cdd:COG3845 481 VGEVPAAEATREE-----IGLL 497
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-263 |
1.01e-28 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 116.82 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 39 IVGESGCGKTTaalaVIGLLPEYARVS-GSIRLHGKELLGLSDHAmsqirgRMIGTVFQDpmSALTPVYTIGDQIAEAIE 117
Cdd:TIGR01187 1 LLGPSGCGKTT----LLRLLAGFEQPDsGSIMLDGEDVTNVPPHL------RHINMVFQS--YALFPHMTVEENVAFGLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 118 IhsREISRADARRRAVELLELVgiaQPERRARAFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVL 197
Cdd:TIGR01187 69 M--RKVPRAEIKPRVLEALRLV---QLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 198 RTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDRRMPYTVGLLGSVPRLDA 263
Cdd:TIGR01187 144 KTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEA 209
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
382-562 |
1.36e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 113.35 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEA---GSIEILGTDVAVLDAAARRrlrteLQVVFQDPVasLDPRL 458
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTALPAEQRR-----IGILFQDDL--LFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 459 PVYDVIAEPLrANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQ 538
Cdd:COG4136 92 SVGENLAFAL-PPTIGRAQRRARVEQALEEAGLAGF-ADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALR 169
|
170 180
....*....|....*....|....
gi 1424538268 539 AGIVNLLLDLQRRFGLSYLFVSHD 562
Cdd:COG4136 170 AQFREFVFEQIRQRGIPALLVTHD 193
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-234 |
2.11e-28 |
|
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: 111.37 E-value: 2.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETedieVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlpeYARVSGSIRLHGKELLGLSDHAMS 84
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGL---YKPDSGEILVDGKEVSFASPRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 QiRGrmIGTVFQdpmsaltpvytigdqiaeaieihsreisradarrravellelvgiaqperrarafpheLSGGERQRVV 164
Cdd:cd03216 74 R-AG--IAMVYQ----------------------------------------------------------LSVGERQMVE 92
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 165 IAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPV 234
Cdd:cd03216 93 IARALARNARLLILDEPTAALTPAEVERLFKVIRRLRA-QGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
382-562 |
2.14e-28 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 113.19 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRTELQVVFQ--DPVASLDPRLP 459
Cdd:TIGR02982 23 DINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLRRRIGYIFQahNLLGFLTARQN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 460 VydVIAEPLRANgFHRHECEERVAELLAVVGL-DHSDAsrYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQ 538
Cdd:TIGR02982 103 V--QMALELQPN-LSYQEARERARAMLEAVGLgDHLNY--YPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSG 177
|
170 180
....*....|....*....|....
gi 1424538268 539 AGIVNLLLDLQRRFGLSYLFVSHD 562
Cdd:TIGR02982 178 RDVVELMQKLAKEQGCTILMVTHD 201
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-245 |
3.53e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 113.67 E-value: 3.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTT--AALAviGLLPEYarvSGSIRLHGKELLGLSDHA 82
Cdd:COG4559 2 LEAENLSVRLGGRTL----LDDVSLTLRPGELTAIIGPNGAGKSTllKLLT--GELTPS---SGEVRLNGRPLAAWSPWE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 83 MSQIRGRMIgtvfQDpmSALTPVYTIGDQIAEAIEIHSReiSRADARRRAVELLELVGIAqpERRARAFPhELSGGERQR 162
Cdd:COG4559 73 LARRRAVLP----QH--SSLAFPFTVEEVVALGRAPHGS--SAAQDRQIVREALALVGLA--HLAGRSYQ-TLSGGEQQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 163 VVIAIAIA-------NDPDLLICDEPTTALDVTVQaqiLDVLRTARDVT--GAAVLIITHDLGVVSEFADRALVMYAGRP 233
Cdd:COG4559 142 VQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQ---HAVLRLARQLArrGGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
250
....*....|..
gi 1424538268 234 VEIAAVDELYRD 245
Cdd:COG4559 219 VAQGTPEEVLTD 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
15-242 |
4.48e-28 |
|
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: 112.08 E-value: 4.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 15 ETEDI-----EVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELLGLSDhamsQIRgR 89
Cdd:cd03265 2 EVENLvkkygDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKP---TSGRATVAGHDVVREPR----EVR-R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 90 MIGTVFQDPmsaltpvyTIGDQIA--EAIEIHSR--EISRADARRRAVELLELVGIAQ-PERRARAFphelSGGERQRVV 164
Cdd:cd03265 74 RIGIVFQDL--------SVDDELTgwENLYIHARlyGVPGAERRERIDELLDFVGLLEaADRLVKTY----SGGMRRRLE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 165 IAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDEL 242
Cdd:cd03265 142 IARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-242 |
4.90e-28 |
|
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: 112.71 E-value: 4.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDiEVPAVRGTSYHIDPGEVLAIVGESGCGKTTaalaVIGLLPEYARV-SGSIRLHGKELlglSDHAMSQIRgR 89
Cdd:cd03253 5 NVTFAYDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKST----ILRLLFRFYDVsSGSILIDGQDI---REVTLDSLR-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 90 MIGTVFQDpmsalTPVY--TIGDQIAEAieihsreisRADARRRAVEllELVGIAQPERRARAFPH-----------ELS 156
Cdd:cd03253 76 AIGVVPQD-----TVLFndTIGYNIRYG---------RPDATDEEVI--EAAKAAQIHDKIMRFPDgydtivgerglKLS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 157 GGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARdvTGAAVLIITHDLGVVSEfADRALVMYAGRPVEI 236
Cdd:cd03253 140 GGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVER 216
|
....*.
gi 1424538268 237 AAVDEL 242
Cdd:cd03253 217 GTHEEL 222
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-246 |
5.31e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 118.72 E-value: 5.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 3 AVLEVTDLNVTFETEDieVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSDHA 82
Cdd:COG4987 332 PSLELEDVSFRYPGAG--RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ---SGSITLGGVDLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 83 MSqirgRMIGTVFQDPmsaltpvYTIGDQIAEAIEIHSREISRADARR--RAVELLELVGiAQPER-------RARAfph 153
Cdd:COG4987 407 LR----RRIAVVPQRP-------HLFDTTLRENLRLARPDATDEELWAalERVGLGDWLA-ALPDGldtwlgeGGRR--- 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 154 eLSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvtGAAVLIITHDLGVVsEFADRALVMYAGRP 233
Cdd:COG4987 472 -LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGL-ERMDRILVLEDGRI 547
|
250
....*....|...
gi 1424538268 234 VEIAAVDELYRDR 246
Cdd:COG4987 548 VEQGTHEELLAQN 560
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-274 |
5.47e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 114.05 E-value: 5.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELlglSDHAM 83
Cdd:COG4152 1 MLELKGLTKRFG----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD---SGEVLWDGEPL---DPEDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 SQI------RGrmigtvfqdpmsaLTPVYTIGDQIAEAIEIHSreISRADARRRAVELLELVGIAqpERRARAFpHELSG 157
Cdd:COG4152 71 RRIgylpeeRG-------------LYPKMKVGEQLVYLARLKG--LSKAEAKRRADEWLERLGLG--DRANKKV-EELSK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 158 GERQRVVIAIAIANDPDLLICDEPTTALD-VTVQAqILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVEI 236
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDpVNVEL-LKDVIRELAA-KGTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
250 260 270
....*....|....*....|....*....|....*....
gi 1424538268 237 AAVDELYRDRRMP-YTVGLLGSVPRLDAAQGTRLIPIPG 274
Cdd:COG4152 211 GSVDEIRRQFGRNtLRLEADGDAGWLRALPGVTVVEEDG 249
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
31-276 |
7.52e-28 |
|
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: 115.20 E-value: 7.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 31 IDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHGKELLglsDHAMSQ---IRGRMIGTVFQDPmsALTPVY 106
Cdd:COG4148 22 LPGRGVTALFGPSGSGKTTLLRAIAGLErPD----SGRIRLGGEVLQ---DSARGIflpPHRRRIGYVFQEA--RLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 107 TIGDQIAEAIeihsreiSRADARRRAV---ELLELVGIAQPERRaraFPHELSGGERQRVVIAIAIANDPDLLICDEPTT 183
Cdd:COG4148 93 SVRGNLLYGR-------KRAPRAERRIsfdEVVELLGIGHLLDR---RPATLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 184 ALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDRRMPYTVG-------LLG 256
Cdd:COG4148 163 ALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGgeeagsvLEA 242
|
250 260
....*....|....*....|
gi 1424538268 257 SVPRLDAAQGTRLIPIPGAP 276
Cdd:COG4148 243 TVAAHDPDYGLTRLALGGGR 262
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
382-582 |
1.33e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 111.12 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRTELQVVFQDPVASLDPrlPVY 461
Cdd:PRK10908 20 GVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMDR--TVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 DVIAEPLRANGFHRHECEERVAELLAVVGLdHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGI 541
Cdd:PRK10908 98 DNVAIPLIIAGASGDDIRRRVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1424538268 542 VNLLLDLQrRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIV 582
Cdd:PRK10908 177 LRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
11-232 |
2.12e-27 |
|
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: 108.84 E-value: 2.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKEL--LGLSDHamsqirG 88
Cdd:cd03246 5 NVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRP---TSGRVRLDGADIsqWDPNEL------G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 89 RMIGTVFQDpmsaltpVYTIGDQIAEAIeihsreisradarrravellelvgiaqperrarafpheLSGGERQRVVIAIA 168
Cdd:cd03246 76 DHVGYLPQD-------DELFSGSIAENI--------------------------------------LSGGQRQRLGLARA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 169 IANDPDLLICDEPTTALDVTVQAQILDVLRTARdVTGAAVLIITHDLGVVSEfADRALVMYAGR 232
Cdd:cd03246 111 LYGNPRILVLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
349-590 |
2.72e-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: 2.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 349 PPVVLRVSDLTKTYRLTKgvvvrrrvgevrAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDV 428
Cdd:COG1129 1 AEPLLEMRGISKSFGGVK------------ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 429 AVLDAAARRRLRteLQVVFQDPvaSLDPRLPVYDVIA---EPLRANGFHRHECEERVAELLAVVGLDHsDASRYPAEFSG 505
Cdd:COG1129 69 RFRSPRDAQAAG--IAIIHQEL--NLVPNLSVAENIFlgrEPRRGGLIDWRAMRRRARELLARLGLDI-DPDTPVGDLSV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 506 GQKQRIGIARALALQPKILALDEPVSALDvsiqAGIVNLLLDLQRRF---GLSYLFVSHDLSVVKHLAHRVAVMYRGMIV 582
Cdd:COG1129 144 AQQQLVEIARALSRDARVLILDEPTASLT----EREVERLFRIIRRLkaqGVAIIYISHRLDEVFEIADRVTVLRDGRLV 219
|
....*...
gi 1424538268 583 EQGESDQV 590
Cdd:COG1129 220 GTGPVAEL 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-215 |
3.12e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 110.94 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 22 PAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYArvsGSIRLHGKELLGlsdhamsqiRGRMIGTVFQDpmSA 101
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQH---GSITLDGKPVEG---------PGAERGVVFQN--EG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 102 LTPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGIAQPERRaraFPHELSGGERQRVVIAIAIANDPDLLICDEP 181
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQL--AGVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190
....*....|....*....|....*....|....
gi 1424538268 182 TTALDVTVQAQILDVLRTARDVTGAAVLIITHDL 215
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-242 |
3.15e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 116.60 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 6 EVTDLNVTFETeDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAalavIGLLpeyARV----SGSIRLHGKELLGLSdh 81
Cdd:PRK13657 334 AVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL----INLL---QRVfdpqSGRILIDGTDIRTVT-- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 82 aMSQIRgRMIGTVFQDPMSAltpVYTIGDQIaeaieihsrEISRADARRraVELLELVGIAQP----ERRARAFP----- 152
Cdd:PRK13657 404 -RASLR-RNIAVVFQDAGLF---NRSIEDNI---------RVGRPDATD--EEMRAAAERAQAhdfiERKPDGYDtvvge 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 153 --HELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARdvTGAAVLIITHDLGVVSEfADRALVMYA 230
Cdd:PRK13657 468 rgRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRN-ADRILVFDN 544
|
250
....*....|..
gi 1424538268 231 GRPVEIAAVDEL 242
Cdd:PRK13657 545 GRVVESGSFDEL 556
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-245 |
3.30e-27 |
|
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: 115.67 E-value: 3.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 21 VPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLH-GKELLGLSDHAMSQiRGRM---IGTVFQ 96
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEP---TSGEVNVRvGDEWVDMTKPGPDG-RGRAkryIGILHQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 97 DpmSALTPVYTIGDQIAEAIEIhsrEISRADARRRAVELLELVGIAqpERRARA----FPHELSGGERQRVVIAIAIAND 172
Cdd:TIGR03269 373 E--YDLYPHRTVLDNLTEAIGL---ELPDELARMKAVITLKMVGFD--EEKAEEildkYPDELSEGERHRVALAQVLIKE 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 173 PDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRD 245
Cdd:TIGR03269 446 PRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
383-607 |
3.54e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 111.41 E-value: 3.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEIlgTDVAVLDAAAR---RRLRTELQVVFQDPVASLDPRLP 459
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDITITHKTKDkyiRPVRKRIGMVFQFPESQLFEDTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 460 VYDVIAEPlRANGFHRHECEERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQA 539
Cdd:PRK13646 104 EREIIFGP-KNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKR 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 540 GIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTnpQHEYTRRLLAAVP 607
Cdd:PRK13646 183 QVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK--DKKKLADWHIGLP 248
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
353-594 |
4.49e-27 |
|
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: 109.55 E-value: 4.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRLTKgvvvrrrvgevrAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLD 432
Cdd:cd03218 1 LRAENLSKRYGKRK------------VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 433 AAARRRLrtELQVVFQDpvASLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIG 512
Cdd:cd03218 69 MHKRARL--GIGYLPQE--ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHL-RKSKASSLSGGERRRVE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 513 IARALALQPKILALDEPVSALD---VS-IQAGIVNLlldlqRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESD 588
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDpiaVQdIQKIIKIL-----KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPE 218
|
....*.
gi 1424538268 589 QVFTNP 594
Cdd:cd03218 219 EIAANE 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
381-593 |
4.59e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 111.25 E-value: 4.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIeILGtDVAVLDAAAR----RRLRTELQVVFQDPVASLDP 456
Cdd:PRK13645 28 NNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-IVG-DYAIPANLKKikevKRLRKEIGLVFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 457 RLPVYDVIAEPLRAnGFHRHECEERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVS 536
Cdd:PRK13645 106 ETIEKDIAFGPVNL-GENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 537 IQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTN 593
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
381-591 |
5.92e-27 |
|
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: 109.24 E-value: 5.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDaaaRRRLRTELQVVFQDPVasLDPrlpv 460
Cdd:cd03254 20 KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLRSMIGVVLQDTF--LFS---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 yDVIAEPLRANgfHRHECEERVAELLAVVGLDH------SDASRYPAE----FSGGQKQRIGIARALALQPKILALDEPV 530
Cdd:cd03254 91 -GTIMENIRLG--RPNATDEEVIEAAKEAGAHDfimklpNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 531 SALDVSIQAGIVNLLLDLQRrfGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQGESDQVF 591
Cdd:cd03254 168 SNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-248 |
6.61e-27 |
|
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: 109.30 E-value: 6.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 2 TAVLEVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeyaRVSGSIRLHGKELLGLSDH 81
Cdd:COG0410 1 MPMLEVENLHAGYG----GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP---PRSGSIRFDGEDITGLPPH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 82 AMSQiRGrmIGTVFQDPM--SALTpvytigdqIAEAIEIHSREISRADARRRAVE-LLELVGIAQPERRARAfpHELSGG 158
Cdd:COG0410 74 RIAR-LG--IGYVPEGRRifPSLT--------VEENLLLGAYARRDRAEVRADLErVYELFPRLKERRRQRA--GTLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 159 ERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAA 238
Cdd:COG0410 141 EQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVLERGRIVLEGT 219
|
250
....*....|
gi 1424538268 239 VDELYRDRRM 248
Cdd:COG0410 220 AAELLADPEV 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-234 |
6.67e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.86 E-value: 6.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 3 AVLEVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTT--AALAviGLLPEYarvSGSIRLHGKELLGLSD 80
Cdd:PRK13548 1 AMLEARNLSVRLGGRTL----LDDVSLTLRPGEVVAILGPNGAGKSTllRALS--GELSPD---SGEVRLNGRPLADWSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 HAMSQIRGRMigtvfqdPM-SALTPVYTIGDQIAEAIEIHSReiSRADARRRAVELLELVGIAqpERRARAFPhELSGGE 159
Cdd:PRK13548 72 AELARRRAVL-------PQhSSLSFPFTVEEVVAMGRAPHGL--SRAEDDALVAAALAQVDLA--HLAGRDYP-QLSGGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 160 RQRVVIAIAIA------NDPDLLICDEPTTALDVtvqAQILDVLRTARDVT---GAAVLIITHDLGVVSEFADRALVMYA 230
Cdd:PRK13548 140 QQRVQLARVLAqlwepdGPPRWLLLDEPTSALDL---AHQHHVLRLARQLAherGLAVIVVLHDLNLAARYADRIVLLHQ 216
|
....
gi 1424538268 231 GRPV 234
Cdd:PRK13548 217 GRLV 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
381-589 |
7.26e-27 |
|
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: 109.24 E-value: 7.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAArrrLRTELQVVFQDPVAsldprlpV 460
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS---LRRQIGLVSQDVFL-------F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLR--ANGFHRHECEE--RVAELLAVV-----GLDHSDASRyPAEFSGGQKQRIGIARALALQPKILALDEPVS 531
Cdd:cd03251 89 NDTVAENIAygRPGATREEVEEaaRAANAHEFImelpeGYDTVIGER-GVKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 532 ALDVS----IQAGIVNLlldLQRRFGLSylfVSHDLSVVKHlAHRVAVMYRGMIVEQGESDQ 589
Cdd:cd03251 168 ALDTEserlVQAALERL---MKNRTTFV---IAHRLSTIEN-ADRIVVLEDGKIVERGTHEE 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-235 |
9.04e-27 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 109.88 E-value: 9.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETED-----IEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKEL 75
Cdd:PRK15112 1 VETLLEVRNLSKTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEP---TSGELLIDDHPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 76 lGLSDHAMSQIRGRMIgtvFQDPMSALTPVYTIGdQIAEAIEIHSREISRADARRRAVELLELVGIaQPERrARAFPHEL 155
Cdd:PRK15112 78 -HFGDYSYRSQRIRMI---FQDPSTSLNPRQRIS-QILDFPLRLNTDLEPEQREKQIIETLRQVGL-LPDH-ASYYPHML 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 156 SGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVE 235
Cdd:PRK15112 151 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-232 |
9.07e-27 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 108.36 E-value: 9.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDieVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELLglSDhaMS 84
Cdd:cd03263 1 LQIRNLTKTYKKGT--KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRP---TSGTAYINGYSIR--TD--RK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 QIRgRMIGTVFQDPM--SALTPvytigdqiAEAIEIHSR--EISRADARRRAVELLELVGIAQPE-RRARafphELSGGE 159
Cdd:cd03263 72 AAR-QSLGYCPQFDAlfDELTV--------REHLRFYARlkGLPKSEIKEEVELLLRVLGLTDKAnKRAR----TLSGGM 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 160 RQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARdvTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:cd03263 139 KRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR--KGRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
381-562 |
1.07e-26 |
|
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: 107.95 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLrtelqvvfqdpvASLDPRLPV 460
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRL------------AYLGHADGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVI--AEPLR--ANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVS 536
Cdd:COG4133 87 KPELtvRENLRfwAALYGLRADREAIDEALEAVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
170 180
....*....|....*....|....*.
gi 1424538268 537 IQAGIVNLLLDLQRRfGLSYLFVSHD 562
Cdd:COG4133 166 GVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
33-275 |
1.07e-26 |
|
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: 111.74 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 33 PG-EVLAIVGESGCGKTTAALAVIGLLPEYArvsGSIRLHGKELLGLSDHAMSQIRGRMIGTVFQDpmSALTPVYTIGDQ 111
Cdd:TIGR02142 21 PGqGVTAIFGRSGSGKTTLIRLIAGLTRPDE---GEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQE--ARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 112 IaeaieIHSREISRADARR-RAVELLELVGIAQPERRaraFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQ 190
Cdd:TIGR02142 96 L-----RYGMKRARPSERRiSFERVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 191 AQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDRRMPY------TVGLLGSVPRLDAA 264
Cdd:TIGR02142 168 YEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWlaredqGSLIEGVVAEHDQH 247
|
250
....*....|.
gi 1424538268 265 QGTRLIPIPGA 275
Cdd:TIGR02142 248 YGLTALRLGGG 258
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
7-254 |
1.27e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.89 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 7 VTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYARVSGSIRLHGKELlglSDHAMSQI 86
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITL---TAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 87 RGRmIGTVFQDPMSALTPVyTIGDQIAEAIEihSREISRADARRRAVELLELVGIAQperRARAFPHELSGGERQRVVIA 166
Cdd:PRK13640 83 REK-VGIVFQNPDNQFVGA-TVGDDVAFGLE--NRAVPRPEMIKIVRDVLADVGMLD---YIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 167 IAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGvVSEFADRALVMYAGRPVEIAAVDELYRDR 246
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
....*...
gi 1424538268 247 RMPYTVGL 254
Cdd:PRK13640 235 EMLKEIGL 242
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-258 |
1.28e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 111.85 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETEdievPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELLGLSD 80
Cdd:PRK11607 16 LTPLLEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP---TAGQIMLDGVDLSHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 HAmsqirgRMIGTVFQDpmSALTPVYTIGDQIAEAIEihSREISRADARRRAVELLELVGIAQPERRArafPHELSGGER 160
Cdd:PRK11607 89 YQ------RPINMMFQS--YALFPHMTVEQNIAFGLK--QDKLPKAEIASRVNEMLGLVHMQEFAKRK---PHQLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 161 QRVVIAIAIANDPDLLICDEPTTALDVTV----QAQILDVLrtarDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEI 236
Cdd:PRK11607 156 QRVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQI 231
|
250 260
....*....|....*....|..
gi 1424538268 237 AAVDELYRDRRMPYTVGLLGSV 258
Cdd:PRK11607 232 GEPEEIYEHPTTRYSAEFIGSV 253
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-237 |
1.55e-26 |
|
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: 107.73 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlpeYARVSGSIRLHGKellglsDHAMS 84
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL---EEPTSGRIYIGGR------DVTDL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 QIRGRMIGTVFQDpmSALTPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVGIAQPERRaraFPHELSGGERQRVV 164
Cdd:cd03301 68 PPKDRDIAMVFQN--YALYPHMTVYDNIAFGLKL--RKVPKDEIDERVREVAELLQIEHLLDR---KPKQLSGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 165 IAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIA 237
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-242 |
1.76e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 108.59 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTTaalavigLL----------PEyARVSGSIRL 70
Cdd:COG1117 8 LEPKIEVRNLNVYYG----DKQALKDINLDIPENKVTALIGPSGCGKST-------LLrclnrmndliPG-ARVEGEILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 71 HGKELLGlSDHAMSQIRgRMIGTVFQDP----MSaltpvytIGDQIAEAIEIHSReisradaRRRAvELLELVgiaqpE- 145
Cdd:COG1117 76 DGEDIYD-PDVDVVELR-RRVGMVFQKPnpfpKS-------IYDNVAYGLRLHGI-------KSKS-ELDEIV-----Ee 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 146 --RRA----------RAFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRT-ARDVTgaaVLIIT 212
Cdd:COG1117 134 slRKAalwdevkdrlKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILElKKDYT---IVIVT 210
|
250 260 270
....*....|....*....|....*....|
gi 1424538268 213 HDLGVVSEFADRALVMYAGRPVEIAAVDEL 242
Cdd:COG1117 211 HNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
381-594 |
2.66e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 108.74 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAvldAAARRRLRTELQVVFQDPVASLDPRLPV 460
Cdd:PRK13652 21 NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT---KENIREVRKFVGLVFQNPDDQIFSPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRAnGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:PRK13652 98 QDIAFGPINL-GLDEETVAHRVSSALHMLGLEEL-RDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 541 IVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNP 594
Cdd:PRK13652 176 LIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
33-235 |
3.09e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 107.41 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 33 PGEVLAIVGESGCGKTTAaLAVIGLLpEYARvSGSIRLHGKEL---LGLSDHAMSQIRgRMIGTVFQDpmSALTPVYTIG 109
Cdd:COG4161 27 SGETLVLLGPSGAGKSSL-LRVLNLL-ETPD-SGQLNIAGHQFdfsQKPSEKAIRLLR-QKVGMVFQQ--YNLWPHLTVM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 110 DQIAEAiEIHSREISRADARRRAVELLELVGIAQperRARAFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTV 189
Cdd:COG4161 101 ENLIEA-PCKVLGLSKEQAREKAMKLLARLRLTD---KADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1424538268 190 QAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVE 235
Cdd:COG4161 177 TAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-228 |
3.78e-26 |
|
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: 112.77 E-value: 3.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDievPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELlglsDHAMS 84
Cdd:TIGR02857 322 LEFSGVSVAYPGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT---EGSIAVNGVPL----ADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 QIRGRMIGTVFQDPmsaltpvYTIGDQIAEAIEIHSREISRADARR--RAVELLELV-----GIAQPERRArafPHELSG 157
Cdd:TIGR02857 392 DSWRDQIAWVPQHP-------FLFAGTIAENIRLARPDASDAEIREalERAGLDEFVaalpqGLDTPIGEG---GAGLSG 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 158 GERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvtGAAVLIITHDLGVVsEFADRALVM 228
Cdd:TIGR02857 462 GQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA-ALADRIVVL 529
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
352-590 |
3.93e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 107.47 E-value: 3.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 352 VLRVSDLTKTYRLTKGVVVRRRVGEVRAV----------DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSI 421
Cdd:COG1134 4 MIEVENVSKSYRLYHEPSRSLKELLLRRRrtrreefwalKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 422 EILGTDVAVLdaaarrrlrtELQVVFqdpvaslDPRLPVYD---VIAeplRANGFHRHECEERVAELLAVVGL-DHSDA- 496
Cdd:COG1134 84 EVNGRVSALL----------ELGAGF-------HPELTGREniyLNG---RLLGLSRKEIDEKFDEIVEFAELgDFIDQp 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 497 -SRYpaefSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAV 575
Cdd:COG1134 144 vKTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIW 218
|
250
....*....|....*
gi 1424538268 576 MYRGMIVEQGESDQV 590
Cdd:COG1134 219 LEKGRLVMDGDPEEV 233
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
381-593 |
4.94e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 108.63 E-value: 4.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAAR---------------------RRL 439
Cdd:PRK13651 24 DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEkekvleklviqktrfkkikkiKEI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 440 RTELQVVFQDPVASLDPRLPVYDVIAEPlRANGFHRHECEERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALAL 519
Cdd:PRK13651 104 RRRVGVVFQFAEYQLFEQTIEKDIIFGP-VSMGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAM 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 520 QPKILALDEPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTN 593
Cdd:PRK13651 183 EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
381-585 |
5.63e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 107.90 E-value: 5.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVavlDAAARRRLRTELQVVFQDPvaslDPRL-- 458
Cdd:PRK13647 22 KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV---NAENEKWVRSKVGLVFQDP----DDQVfs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 459 -PVYDVIAEPLRANGFHRHECEERVAELLAVVGL-DHSDasRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVS 536
Cdd:PRK13647 95 sTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMwDFRD--KPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1424538268 537 IQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQG 585
Cdd:PRK13647 173 GQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
381-590 |
7.14e-26 |
|
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: 105.98 E-value: 7.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAvlDAAARRRLRTELQVVFQDPvaSLDPRLPV 460
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT--GLPPHERARAGIGYVPEGR--RIFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YdviaEPLRANGFHRHEC--EERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQ 538
Cdd:cd03224 93 E----ENLLLGAYARRRAkrKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 539 AGIVNLLLDLqRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQV 590
Cdd:cd03224 169 EEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
381-595 |
7.33e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.58 E-value: 7.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTT---LNQILELTKPEAGSIEILGTDvavLDAAARRRLRTELQVVFQDPvaslDPR 457
Cdd:PRK13640 24 NDISFSIPRGSWTALIGHNGSGKSTIsklINGLLLPDDNPNSKITVDGIT---LTAKTVWDIREKVGIVFQNP----DNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 458 L---PVYDVIAEPLRANGFHRHECEERVAELLAVVG-LDHSDASryPAEFSGGQKQRIGIARALALQPKILALDEPVSAL 533
Cdd:PRK13640 97 FvgaTVGDDVAFGLENRAVPRPEMIKIVRDVLADVGmLDYIDSE--PANLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 534 DVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQGESDQVFTNPQ 595
Cdd:PRK13640 175 DPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
381-595 |
8.23e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.49 E-value: 8.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDvavLDAAARRRLRTELQVVFQDPVASLdPRLPV 460
Cdd:PRK13642 24 NGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEL---LTAENVWNLRRKIGMVFQNPDNQF-VGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGFHRHECEERVAE-LLAVVGLDHSdaSRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQA 539
Cdd:PRK13642 100 EDDVAFGMENQGIPREEMIKRVDEaLLAVNMLDFK--TREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 540 GIVNLLLDLQRRFGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQGESDQVFTNPQ 595
Cdd:PRK13642 178 EIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
31-235 |
9.18e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 106.25 E-value: 9.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 31 IDPGEVLAIVGESGCGKTTAaLAVIGLLpEYARvSGSIRLHGKEL---LGLSDHAMSQIRgRMIGTVFQDpmSALTPVYT 107
Cdd:PRK11124 25 CPQGETLVLLGPSGAGKSSL-LRVLNLL-EMPR-SGTLNIAGNHFdfsKTPSDKAIRELR-RNVGMVFQQ--YNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 108 IGDQIAEAiEIHSREISRADARRRAVELLELVGIAQperRARAFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDV 187
Cdd:PRK11124 99 VQQNLIEA-PCRVLGLSKDQALARAEKLLERLRLKP---YADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1424538268 188 TVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVE 235
Cdd:PRK11124 175 EITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-214 |
1.19e-25 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 104.87 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 3 AVLEVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTT--AALAviGLLPeyaRVSGSIRLHGKELlglsD 80
Cdd:COG4133 1 MMLEAENLSCRRG----ERLLFSGLSFTLAAGEALALTGPNGSGKTTllRILA--GLLP---PSAGEVLWNGEPI----R 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 HAMSQIRGRmIGTVFQDPM--SALTPvytigdqiAEAIEIHSREISRADARRRAVELLELVGIAqpeRRARAFPHELSGG 158
Cdd:COG4133 68 DAREDYRRR-LAYLGHADGlkPELTV--------RENLRFWAALYGLRADREAIDEALEAVGLA---GLADLPVRQLSAG 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 159 ERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHD 214
Cdd:COG4133 136 QKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLA-RGGAVLLTTHQ 190
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
28-256 |
1.25e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.61 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 28 SYHIDPGEVLAIVGESGCGKTTAaLAVI-GLLPEYarvSGSIRLHGKELLGLSDHAmsqirgRMIGTVFQDpmSALTPVY 106
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTL-LNLIaGFLPPD---SGRILWNGQDLTALPPAE------RPVSMLFQE--NNLFPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 107 TIGDQIAeaIEIHSREISRADARRRAVELLELVGIAQPERRaraFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALD 186
Cdd:COG3840 87 TVAQNIG--LGLRPGLKLTAEQRAQVEQALERVGLAGLLDR---LPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 187 VTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDRRMPYTVGLLG 256
Cdd:COG3840 162 PALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
353-585 |
1.99e-25 |
|
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: 104.28 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRLTKgvvvrrrvgevrAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGtdvAVLD 432
Cdd:cd03269 1 LEVENVTKRFGRVT------------ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 433 AAARRR---LRTElqvvfqdpvASLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQ 509
Cdd:cd03269 66 IAARNRigyLPEE---------RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEY-ANKRVEELSKGNQQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 510 RIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQG 585
Cdd:cd03269 136 KVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
381-590 |
2.28e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 106.35 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDvavLDAAARRRL------RtelqvvfqdpvaSL 454
Cdd:COG4152 18 DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP---LDPEDRRRIgylpeeR------------GL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 455 DPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSDASRYpAEFSGGQKQRIGIARALALQPKILALDEPVSALD 534
Cdd:COG4152 83 YPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKV-EELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 535 -VSIQAgIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQV 590
Cdd:COG4152 162 pVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-234 |
2.51e-25 |
|
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: 103.90 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETedieVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSDHAMS 84
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD---SGEVLFDGKPLDIAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 QI---RGrmigtvfqdpmsaLTPVYTIGDQIAEAIEIHSreISRADARRRAVELLELVGIAQ-PERRARafphELSGGER 160
Cdd:cd03269 74 YLpeeRG-------------LYPKMKVIDQLVYLAQLKG--LKKEEARRRIDEWLERLELSEyANKRVE----ELSKGNQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 161 QRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPV 234
Cdd:cd03269 135 QKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-245 |
2.59e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 105.93 E-value: 2.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFE--TEdievpAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHGKELlGLSD 80
Cdd:PRK13639 1 ILETRDLKYSYPdgTE-----ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkPT----SGEVLIKGEPI-KYDK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 HAMSQIRgRMIGTVFQDPMSAL-TPvyTIGDQIAeaIEIHSREISRADARRRAVELLELVGIAQPERRArafPHELSGGE 159
Cdd:PRK13639 71 KSLLEVR-KTVGIVFQNPDDQLfAP--TVEEDVA--FGPLNLGLSKEEVEKRVKEALKAVGMEGFENKP---PHHLSGGQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 160 RQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAV 239
Cdd:PRK13639 143 KKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
....*.
gi 1424538268 240 DELYRD 245
Cdd:PRK13639 222 KEVFSD 227
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
381-600 |
2.63e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 105.50 E-value: 2.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKST---TLNQILEL---TKPEaGSIEILGTDVAvldaaARR----RLRTELQVVFQDP 450
Cdd:PRK14258 24 EGVSMEIYQSKVTAIIGPSGCGKSTflkCLNRMNELeseVRVE-GRVEFFNQNIY-----ERRvnlnRLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 451 vaSLDPrLPVYDVIAEPLRANGFH-RHECEERVAELLAVVGL-DH--SDASRYPAEFSGGQKQRIGIARALALQPKILAL 526
Cdd:PRK14258 98 --NLFP-MSVYDNVAYGVKIVGWRpKLEIDDIVESALKDADLwDEikHKIHKSALDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 527 DEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYR-----GMIVEQGESDQVFTNPQHEYTR 600
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTR 253
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
11-235 |
2.72e-25 |
|
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: 110.19 E-value: 2.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTaalaVIGLLPE-YARVSGSIRLHGKELlglSDHAMSQIRgR 89
Cdd:TIGR02203 335 NVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKST----LVNLIPRfYEPDSGQILLDGHDL---ADYTLASLR-R 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 90 MIGTVFQDpmsaltpVYTIGDQIAEAIEI-HSREISRADARR--RAVELLELV-----GIAQP--ERRARafpheLSGGE 159
Cdd:TIGR02203 407 QVALVSQD-------VVLFNDTIANNIAYgRTEQADRAEIERalAAAYAQDFVdklplGLDTPigENGVL-----LSGGQ 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 160 RQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRtaRDVTGAAVLIITHDLGVVsEFADRALVMYAGRPVE 235
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALDNESERLVQAALE--RLMQGRTTLVIAHRLSTI-EKADRIVVMDDGRIVE 547
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
382-562 |
2.85e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 104.48 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRTE-LQVVFQDPVasLDPRLPV 460
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKhVGFVFQSFM--LIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGFHRHECEERVAELLAVVGL----DHsdasrYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVS 536
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLgkrlDH-----LPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180
....*....|....*....|....*.
gi 1424538268 537 IQAGIVNLLLDLQRRFGLSYLFVSHD 562
Cdd:PRK10584 181 TGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
353-582 |
3.24e-25 |
|
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: 102.12 E-value: 3.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRLTKgvvvrrrvgevrAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLD 432
Cdd:cd03216 1 LELRGITKRFGGVK------------ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 433 AAARRRLRteLQVVFQdpvasldprlpvydviaeplrangfhrheceervaellavvgldhsdasrypaeFSGGQKQRIG 512
Cdd:cd03216 69 PRDARRAG--IAMVYQ------------------------------------------------------LSVGERQMVE 92
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 513 IARALALQPKILALDEPVSALDVSiqagIVNLLLDLQRRF---GLSYLFVSHDLSVVKHLAHRVAVMYRGMIV 582
Cdd:cd03216 93 IARALARNARLLILDEPTAALTPA----EVERLFKVIRRLraqGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-232 |
4.96e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 103.42 E-value: 4.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 23 AVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYArvsGSIRLHGKELLGLSDHAMSQIRgRMIGTVFQDpmSAL 102
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSA---GKIWFSGHDITRLKNREVPFLR-RQIGMIFQD--HHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 103 TPVYTIGDQIAEAIEIHSreISRADARRRAVELLELVGIAQperRARAFPHELSGGERQRVVIAIAIANDPDLLICDEPT 182
Cdd:PRK10908 91 LMDRTVYDNVAIPLIIAG--ASGDDIRRRVSAALDKVGLLD---KAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1424538268 183 TALDVTVQAQILDVLRTARDVtGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:PRK10908 166 GNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
382-604 |
1.14e-24 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 102.60 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLdaAARRRLRTELQVVFQDpvASLDPRLPVY 461
Cdd:TIGR03410 18 GVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKL--PPHERARAGIAYVPQG--REIFPRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 DVIAEPLRANGFHRHECEERVAELLAVVgldHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGI 541
Cdd:TIGR03410 94 ENLLTGLAALPRRSRKIPDEIYELFPVL---KEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 542 VNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVftnpQHEYTRRLLA 604
Cdd:TIGR03410 171 GRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DEDKVRRYLA 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
11-242 |
1.14e-24 |
|
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: 102.69 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEvPAVRGTSYHIDPGEVLAIVGESGCGKTTaalaVIGLLPEYARVS-GSIRLHGKELLGLSdhaMSQIRgR 89
Cdd:cd03254 7 NVNFSYDEKK-PVLKDINFSIKPGETVAIVGPTGAGKTT----LINLLMRFYDPQkGQILIDGIDIRDIS---RKSLR-S 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 90 MIGTVFQDPmsaltpvYTIGDQIAEAIEIhSREISRADarrRAVELLELVGIAQ-PERRARAFPHE-------LSGGERQ 161
Cdd:cd03254 78 MIGVVLQDT-------FLFSGTIMENIRL-GRPNATDE---EVIEAAKEAGAHDfIMKLPNGYDTVlgenggnLSQGERQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 162 RVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvtGAAVLIITHDLGVVsEFADRALVMYAGRPVEIAAVDE 241
Cdd:cd03254 147 LLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHDE 223
|
.
gi 1424538268 242 L 242
Cdd:cd03254 224 L 224
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
381-589 |
1.27e-24 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 102.48 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAvldaaaRRRLRTelqvvfqdpVASLDPRLPV 460
Cdd:TIGR03740 17 NNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT------RKDLHK---------IGSLIESPPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIA--EPLRANGFHRHECEERVAELLAVVGLDHSDASRyPAEFSGGQKQRIGIARALALQPKILALDEPVSALD-VSI 537
Cdd:TIGR03740 82 YENLTarENLKVHTTLLGLPDSRIDEVLNIVDLTNTGKKK-AKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDpIGI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 538 QAgivnlLLDLQRRF---GLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQ 589
Cdd:TIGR03740 161 QE-----LRELIRSFpeqGITVILSSHILSEVQQLADHIGIISEGVLGYQGKINK 210
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
381-590 |
1.41e-24 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 108.68 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRlrtELQVVFQ----------DP 450
Cdd:TIGR01846 474 SNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRR---QMGVVLQenvlfsrsirDN 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 451 VASLDPRLPVYDVIAEPLRANGfhrHECEERVAEllavvGLDhSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPV 530
Cdd:TIGR01846 551 IALCNPGAPFEHVIHAAKLAGA---HDFISELPQ-----GYN-TEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEAT 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 531 SALDVSIQAGIVNLLLDLQRrfGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQGESDQV 590
Cdd:TIGR01846 622 SALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEEL 678
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-232 |
1.67e-24 |
|
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: 100.58 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 3 AVLEVTDLNVTfetedievPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeyaRVSGSIRLHGKELLGLSDHA 82
Cdd:cd03215 3 PVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP---PASGEITLDGKPVTRRSPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 83 MsqiRGRMIGTVFQDPMS-ALTPVYTIGDQIAeaieihsreisradarrravellelvgiaqperraraFPHELSGGERQ 161
Cdd:cd03215 72 A---IRAGIAYVPEDRKReGLVLDLSVAENIA-------------------------------------LSSLLSGGNQQ 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 162 RVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:cd03215 112 KVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
353-585 |
1.86e-24 |
|
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: 101.84 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRLTKGVVVRRRVGEVRAV----------DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIE 422
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKLGILGRkgevgefwalKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 423 ILGTDVAVLDAAarrrlrtelqvvfqdpvASLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGL-DHSDasrYP- 500
Cdd:cd03220 81 VRGRVSSLLGLG-----------------GGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELgDFID---LPv 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 501 AEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGM 580
Cdd:cd03220 141 KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
....*
gi 1424538268 581 IVEQG 585
Cdd:cd03220 220 IRFDG 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
383-609 |
2.16e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 103.66 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEIlgTDVAVLDAAARRRL---RTELQVVFQDPVASLDPRLP 459
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV--GDIVVSSTSKQKEIkpvRKKVGVVFQFPESQLFEETV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 460 VYDVIAEPlRANGFHRHECEERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQA 539
Cdd:PRK13643 103 LKDVAFGP-QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 540 GIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTnpQHEYTRRLLAAVPRA 609
Cdd:PRK13643 182 EMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ--EVDFLKAHELGVPKA 248
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
382-594 |
2.44e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 107.89 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDaaaRRRLRTELQVVFQDPVASldpRLPVY 461
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD---HHYLHRQVALVGQEPVLF---SGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 DVIAEPLRangfhrhECEERVAELLAVVGLDHSDASRYP-----------AEFSGGQKQRIGIARALALQPKILALDEPV 530
Cdd:TIGR00958 573 ENIAYGLT-------DTPDEEIMAAAKAANAHDFIMEFPngydtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 531 SALDVSIQAgivnLLLDLQRRFGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQGESDQVFTNP 594
Cdd:TIGR00958 646 SALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
382-608 |
3.49e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.62 E-value: 3.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKST---TLNQILeltKPEAGSIEILGTDVavlDAAAR--RRLRTELQVVFQDPvaslDP 456
Cdd:PRK13636 24 GININIKKGEVTAILGGNGAGKSTlfqNLNGIL---KPSSGRILFDGKPI---DYSRKglMKLRESVGMVFQDP----DN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 457 RL---PVYDVIAEPLRANGFHRHECEERVAELLAVVGLDH-SDASRYPAEFsgGQKQRIGIARALALQPKILALDEPVSA 532
Cdd:PRK13636 94 QLfsaSVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHlKDKPTHCLSF--GQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 533 LDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTnpQHEYTRRLLAAVPR 608
Cdd:PRK13636 172 LDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA--EKEMLRKVNLRLPR 245
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-214 |
3.99e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 101.01 E-value: 3.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIGLLPEYArvSGSIRLHGKELLGLSDHAM 83
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTL-LAILAGLDDGS--SGEVSLVGQPLHQMDEEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 SQIRGRMIGTVFQDPMsaLTPVYTIgdqiAEAIEIHS--REISRADARRRAVELLELVGIAQperRARAFPHELSGGERQ 161
Cdd:PRK10584 83 AKLRAKHVGFVFQSFM--LIPTLNA----LENVELPAllRGESSRQSRNGAKALLEQLGLGK---RLDHLPAQLSGGEQQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 162 RVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHD 214
Cdd:PRK10584 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
381-585 |
4.00e-24 |
|
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: 101.03 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDaaaRRRLRTELQVVFQDPV-------AS 453
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSRISIIPQDPVlfsgtirSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 454 LDPrlpvydviaeplrangFHRHEcEERVAELLAVVGLD-----HSDASRYPAE-----FSGGQKQRIGIARALALQPKI 523
Cdd:cd03244 98 LDP----------------FGEYS-DEELWQALERVGLKefvesLPGGLDTVVEeggenLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 524 LALDEPVSALDVSIQAGIVNLlldLQRRF-GLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQG 585
Cdd:cd03244 161 LVLDEATASVDPETDALIQKT---IREAFkDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
381-591 |
4.51e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 102.14 E-value: 4.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGsiEILGTDVAVlDAAARRRLRTELQVVFQDPVASLDPRLPV 460
Cdd:PRK13648 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--EIFYNNQAI-TDDNFEKLRKHIGIVFQNPDNQFVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDViAEPLRANGFHRHECEERVAELLAVVG-LDHSDASryPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQA 539
Cdd:PRK13648 103 YDV-AFGLENHAVPYDEMHRRVSEALKQVDmLERADYE--PNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 540 GIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHrVAVMYRGMIVEQGESDQVF 591
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDLSEAMEADH-VIVMNKGTVYKEGTPTEIF 230
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
381-593 |
4.80e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 102.47 E-value: 4.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAvlDAAARRRLRTELQVVFQDPVASLDPRLPV 460
Cdd:PRK13633 27 DDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS--DEENLWDIRNKAGMVFQNPDNQIVATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPlrAN-GFHRHECEERVAELLAVVGLdhSDASRY-PAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQ 538
Cdd:PRK13633 105 EDVAFGP--ENlGIPPEEIRERVDESLKKVGM--YEYRRHaPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 539 AGIVNLLLDLQRRFGLSYLFVSHDL-SVVKhlAHRVAVMYRGMIVEQGESDQVFTN 593
Cdd:PRK13633 181 REVVNTIKELNKKYGITIILITHYMeEAVE--ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-232 |
6.23e-24 |
|
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: 100.13 E-value: 6.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIrlhgkELLGLSDHAM 83
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePD----AGFA-----TVDGFDVVKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 SQIRGRMIGTVFQDpmSALTPVYTIGDQIAEAIEIHSreISRADARRRAVELLELVGIAQ-PERRARAFphelSGGERQR 162
Cdd:cd03266 73 PAEARRRLGFVSDS--TGLYDRLTARENLEYFAGLYG--LKGDELTARLEELADRLGMEElLDRRVGGF----STGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 163 VVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVtGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-249 |
7.08e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 101.20 E-value: 7.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIGLLPEYARvsGSIRLHGKEL--------- 75
Cdd:PRK10619 6 LNVIDLHKRYGEHEV----LKGVSLQANAGDVISIIGSSGSGKSTF-LRCINFLEKPSE--GSIVVNGQTInlvrdkdgq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 76 LGLSD-HAMSQIRGRMIgTVFQDpmSALTPVYTIGDQIAEAiEIHSREISRADARRRAVELLELVGIAqpERRARAFPHE 154
Cdd:PRK10619 79 LKVADkNQLRLLRTRLT-MVFQH--FNLWSHMTVLENVMEA-PIQVLGLSKQEARERAVKYLAKVGID--ERAQGKYPVH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 155 LSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPV 234
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
250
....*....|....*
gi 1424538268 235 EIAAVDELYRDRRMP 249
Cdd:PRK10619 232 EEGAPEQLFGNPQSP 246
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
382-591 |
7.09e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 101.74 E-value: 7.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAAR-RRLRTELQVVFQDPVASLDPRLPV 460
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDiKQIRKKVGLVFQFPESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPlRANGFHRHECEERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:PRK13649 105 KDVAFGP-QNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 541 IVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVF 591
Cdd:PRK13649 184 LMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
352-599 |
9.16e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.62 E-value: 9.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 352 VLRVSDLTKTYRLTKgvvvrrrvgevrAVDGISFTLEQGRTLGIVGESGSGKST---TLNQILELTkPE---AGSIEILG 425
Cdd:PRK14239 5 ILQVSDLSVYYNKKK------------ALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLN-PEvtiTGSIVYNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 426 TDVAvldaaARR----RLRTELQVVFQDPvaslDP-RLPVYDVIAEPLRANGFH-RHECEERVAELLAVVGL-----DHS 494
Cdd:PRK14239 72 HNIY-----SPRtdtvDLRKEIGMVFQQP----NPfPMSIYENVVYGLRLKGIKdKQVLDEAVEKSLKGASIwdevkDRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 495 DASryPAEFSGGQKQRIGIARALALQPKILALDEPVSALDvSIQAG-IVNLLLDLQRRFGLsyLFVSHDLSVVKHLAHRV 573
Cdd:PRK14239 143 HDS--ALGLSGGQQQRVCIARVLATSPKIILLDEPTSALD-PISAGkIEETLLGLKDDYTM--LLVTRSMQQASRISDRT 217
|
250 260
....*....|....*....|....*.
gi 1424538268 574 AVMYRGMIVEQGESDQVFTNPQHEYT 599
Cdd:PRK14239 218 GFFLDGDLIEYNDTKQMFMNPKHKET 243
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
381-582 |
1.08e-23 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 99.25 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDvavldAAARRRLRTeLQVVFQDPvaslDPRLPV 460
Cdd:cd03226 17 DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP-----IKAKERRKS-IGYVMQDV----DYQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGfHRHECEERVAELLAVVGLdHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:cd03226 87 DSVREELLLGLK-ELDAGNEQAETVLKDLDL-YALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1424538268 541 IVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIV 582
Cdd:cd03226 165 VGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
384-589 |
1.20e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 99.66 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 384 SFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAvLDAAARRrlrtELQVVFQDpvASLDPRLPVYDV 463
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT-TTPPSRR----PVSMLFQE--NNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 464 IA---EP-LRANGFHRHECEERVAEllavVGLDhSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQA 539
Cdd:PRK10771 92 IGlglNPgLKLNAAQREKLHAIARQ----MGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1424538268 540 GIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQ 589
Cdd:PRK10771 167 EMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-242 |
1.24e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 103.57 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 23 AVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIGLLPEYARvsGSIRLHGKELLGLSDHAMSQIRGRMIGTVFQDpmSAL 102
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTM-VRLLNRLIEPTR--GQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 103 TPVYTIGDQIAEAIEIHSreISRADARRRAVELLELVGIaqpERRARAFPHELSGGERQRVVIAIAIANDPDLLICDEPT 182
Cdd:PRK10070 118 MPHMTVLDNTAFGMELAG--INAEERREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 183 TALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDEL 242
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-250 |
1.26e-23 |
|
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: 99.87 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlpeYARVSGSIRLHGKELlGLSDHAMSQirgRM 90
Cdd:cd03252 5 HVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF---YVPENGRVLVDGHDL-ALADPAWLR---RQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 91 IGTVFQDpmsALTPVYTIGDQIAEAIEIHSRE-----ISRADARRRAVELLELVGIAQPERRArafphELSGGERQRVVI 165
Cdd:cd03252 78 VGVVLQE---NVLFNRSIRDNIALADPGMSMErvieaAKLAGAHDFISELPEGYDTIVGEQGA-----GLSGGQRQRIAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 166 AIAIANDPDLLICDEPTTALDVTVQAQIldvLRTARDV-TGAAVLIITHDLGVVSEfADRALVMYAGRPVEIAAVDELYR 244
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAI---MRNMHDIcAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
....*.
gi 1424538268 245 DRRMPY 250
Cdd:cd03252 226 ENGLYA 231
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
14-261 |
1.42e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 100.89 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 14 FETEdievpAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELLGLSDHaMSQIRGRmIGT 93
Cdd:PRK13637 18 FEKK-----ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKP---TSGKIIIDGVDITDKKVK-LSDIRKK-VGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 94 VFQDPMSALtpvytIGDQIAEAIEIHSRE--ISRADARRRAVELLELVGIAQPERRARAfPHELSGGERQRVVIAIAIAN 171
Cdd:PRK13637 88 VFQYPEYQL-----FEETIEKDIAFGPINlgLSEEEIENRVKRAMNIVGLDYEDYKDKS-PFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 172 DPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDRRMPYT 251
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLES 241
|
250
....*....|
gi 1424538268 252 VGLlgSVPRL 261
Cdd:PRK13637 242 IGL--AVPQV 249
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
381-594 |
1.42e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 102.61 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARrrlrtELQVVFQDpvASLDPRLPV 460
Cdd:PRK11650 21 KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADR-----DIAMVFQN--YALYPHMSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:PRK11650 94 RENMAYGLKIRGMPKAEIEERVAEAARILELEPL-LDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 541 IVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIvEQ-GESDQVFTNP 594
Cdd:PRK11650 173 MRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA-EQiGTPVEVYEKP 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-232 |
1.46e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 100.55 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDI-EVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELLGLSDHAm 83
Cdd:COG1101 2 LELKNLSKTFNPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPP---DSGSILIDGKDVTKLPEYK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 sqiRGRMIGTVFQDPMSALTPVYTIGDQIAEAI-EIHSREISRA-DARRRAV--ELLELVGIAQpERRARAFPHELSGGE 159
Cdd:COG1101 78 ---RAKYIGRVFQDPMMGTAPSMTIEENLALAYrRGKRRGLRRGlTKKRRELfrELLATLGLGL-ENRLDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 160 RQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVlrTARDVT--GAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLEL--TEKIVEenNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-243 |
1.71e-23 |
|
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: 99.54 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 20 EVPAVRGTSYHIDPGEVLAIVGESGCGKTTaalaVIGLLPE-YARVSGSIRLHGKELlglSDHAMSQIRgRMIGTVFQDP 98
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLERfYDPTSGEILLDGVDI---RDLNLRWLR-SQIGLVSQEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 99 MSALTpvyTIGDQIA----EAIEIHSREISRADARRRAVELL-----ELVGiaqperrARAFphELSGGERQRVVIAIAI 169
Cdd:cd03249 87 VLFDG---TIAENIRygkpDATDEEVEEAAKKANIHDFIMSLpdgydTLVG-------ERGS--QLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 170 ANDPDLLICDEPTTALDVTVQAQILDVLRTARdvTGAAVLIITHDLGVVSEfADRALVMYAGRPVEIAAVDELY 243
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELM 225
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
381-590 |
1.88e-23 |
|
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: 105.21 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDaaaRRRLRTELQVVFQDPVasldprlpV 460
Cdd:TIGR01193 491 SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID---RHTLRQFINYLPQEPY--------I 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YD-VIAEPLRAnGFHRHECEERVAELLAVVGLD----------HSDASRYPAEFSGGQKQRIGIARALALQPKILALDEP 529
Cdd:TIGR01193 560 FSgSILENLLL-GAKENVSQDEIWAACEIAEIKddienmplgyQTELSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 530 VSALDVSIQAGIVNLLLDLQRRfglSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQGESDQV 590
Cdd:TIGR01193 639 TSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
1.95e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 100.20 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLnvTFETEDiEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlpeYARVSGSIRLHGKELlglSD 80
Cdd:PRK13647 1 MDNIIEVEDL--HFRYKD-GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGI---YLPQRGRVKVMGREV---NA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 HAMSQIRGrMIGTVFQDPMSALTPVyTIGDQIAeaIEIHSREISRADARRRAVELLELVGIAQPERRArafPHELSGGER 160
Cdd:PRK13647 72 ENEKWVRS-KVGLVFQDPDDQVFSS-TVWDDVA--FGPVNMGLDKDEVERRVEEALKAVRMWDFRDKP---PYHLSYGQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 161 QRVVIAIAIANDPDLLICDEPTTALDVTVQA---QILDVLRTArdvtGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:PRK13647 145 KRVAIAGVLAMDPDVIVLDEPMAYLDPRGQEtlmEILDRLHNQ----GKTVIVATHDVDLAAEWADQVIVLKEGR 215
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-246 |
2.09e-23 |
|
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: 99.08 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 24 VRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGL-LPeyarVSGSIRLHGKELlglsdhamsQIRG--RMIgtVFQDpmS 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQP----TSGGVILEGKQI---------TEPGpdRMV--VFQN--Y 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 101 ALTPVYTIGDQIAEAIEIHSREISRADARRRAVELLELVGIaqpERRARAFPHELSGGERQRVVIAIAIANDPDLLICDE 180
Cdd:TIGR01184 64 SLLPWLTVRENIALAVDRVLPDLSKSERRAIVEEHIALVGL---TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 181 PTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDR 246
Cdd:TIGR01184 141 PFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVPFPR 206
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
28-246 |
2.39e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.29 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 28 SYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHGKEL-LGLSDHAMSQIRgRMIGTVFQDPMSALtpv 105
Cdd:PRK13641 27 SFELEEGSFVALVGHTGSGKSTLMQHFNALLkPS----SGTITIAGYHItPETGNKNLKKLR-KKVSLVFQFPEAQL--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 106 ytIGDQIAEAIEIHSRE--ISRADARRRAVELLELVGIaqPERRARAFPHELSGGERQRVVIAIAIANDPDLLICDEPTT 183
Cdd:PRK13641 99 --FENTVLKDVEFGPKNfgFSEDEAKEKALKWLKKVGL--SEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 184 ALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDR 246
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQK-AGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
381-591 |
2.59e-23 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 104.40 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDaaaRRRLRTELQVVFQDPV-----ASLD 455
Cdd:TIGR02204 357 DGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLD---PAELRARMALVPQDPVlfaasVMEN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 456 PRLPVYDVIAEPLR--ANGFHRHECEERVAEllavvGLDHSDASRyPAEFSGGQKQRIGIARALALQPKILALDEPVSAL 533
Cdd:TIGR02204 434 IRYGRPDATDEEVEaaARAAHAHEFISALPE-----GYDTYLGER-GVTLSGGQRQRIAIARAILKDAPILLLDEATSAL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 534 DVSIQAGIVNLLLDLQRrfGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQGESDQVF 591
Cdd:TIGR02204 508 DAESEQLVQQALETLMK--GRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAELI 562
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-234 |
2.62e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 104.42 E-value: 2.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIGLLPEYArvSGSIRLHGKELLGLSD 80
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTL-MNILGCLDKPT--SGTYRVAGQDVATLDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 HAMSQIRGRMIGTVFQ--DPMSALTPvytigdqiAEAIEIHS--REISRADARRRAVELLELVGIAQperRARAFPHELS 156
Cdd:PRK10535 78 DALAQLRREHFGFIFQryHLLSHLTA--------AQNVEVPAvyAGLERKQRLLRAQELLQRLGLED---RVEYQPSQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 157 GGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEfADRALVMYAGRPV 234
Cdd:PRK10535 147 GGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD-RGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
383-598 |
2.84e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.06 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAvlDAAARRRLRTELQVVFQDPVASLDPRLPVYD 462
Cdd:PRK13644 21 INLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG--DFSKLQGIRKLVGIVFQNPETQFVGRTVEED 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 463 VIAEPLRAnGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIV 542
Cdd:PRK13644 99 LAFGPENL-CLPPIEIRKRVDRALAEIGLEKY-RHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 543 NLLLDLQRRfGLSYLFVSHDLSVVkHLAHRVAVMYRGMIVEQGESDQVFTNPQHEY 598
Cdd:PRK13644 177 ERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-235 |
3.96e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 98.60 E-value: 3.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlPEYARVSGSIRLHGKELLGLSDHAms 84
Cdd:COG0396 1 LEIKNLHVSVEGKEI----LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH-PKYEVTSGSILLDGEDILELSPDE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 qiRGRM-IGTVFQDPMSalTPVYTIGDQIAEAI-EIHSREISRADARRRAVELLELVGIAqPERRARAFPHELSGGERQR 162
Cdd:COG0396 74 --RARAgIFLAFQYPVE--IPGVSVSNFLRTALnARRGEELSAREFLKLLKEKMKELGLD-EDFLDRYVNEGFSGGEKKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 163 VVIAIAIANDPDLLICDEPTTALDVtvqaqilDVLRTARDV------TGAAVLIITH-----DLGVvsefADRALVMYAG 231
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLDI-------DALRIVAEGvnklrsPDRGILIITHyqrilDYIK----PDFVHVLVDG 217
|
....
gi 1424538268 232 RPVE 235
Cdd:COG0396 218 RIVK 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
11-234 |
5.46e-23 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 97.66 E-value: 5.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlpeYARVSGSIRLHGKELLGLSdhaMSQIRgRM 90
Cdd:cd03245 7 NVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL---YKPTSGSVLLDGTDIRQLD---PADLR-RN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 91 IGTVFQDPmsalTPVY-TIGDQIAEAIEIHSREisradarrRAVELLELVGIAQperRARAFPH-----------ELSGG 158
Cdd:cd03245 80 IGYVPQDV----TLFYgTLRDNITLGAPLADDE--------RILRAAELAGVTD---FVNKHPNgldlqigergrGLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 159 ERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRT-ARDVTgaaVLIITHDLGVVSeFADRALVMYAGRPV 234
Cdd:cd03245 145 QRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQlLGDKT---LIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-232 |
5.60e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 99.78 E-value: 5.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETE-DIEVPAVRGTSYHIDPGEVLAIVGESGCGKTT-----AALavigLLPEyarvSGSIRL-----HGK 73
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTfiehlNAL----LLPD----TGTIEWifkdeKNK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 74 ELLGLSDHAMS----------------QIRgRMIGTVFQDPMSALTPVYTIGDQIAEAIeihSREISRADARRRAVELLE 137
Cdd:PRK13651 75 KKTKEKEKVLEklviqktrfkkikkikEIR-RRVGVVFQFAEYQLFEQTIEKDIIFGPV---SMGVSKEEAKKRAAKYIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 138 LVGIaqPERRARAFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGV 217
Cdd:PRK13651 151 LVGL--DESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDN 227
|
250
....*....|....*
gi 1424538268 218 VSEFADRALVMYAGR 232
Cdd:PRK13651 228 VLEWTKRTIFFKDGK 242
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-242 |
6.32e-23 |
|
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: 98.23 E-value: 6.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 2 TAVLEVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTaalaVIGLLP--EYARVSGSIRLHGKELLGLS 79
Cdd:COG1119 1 DPLLELRNVTVRRGGKTI----LDDISWTVKPGEHWAILGPNGAGKST----LLSLITgdLPPTYGNDVRLFGERRGGED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 80 dhaMSQIRGRmIGTVFQDPMSALTPVYTIGDQIAEA----IEIHsREISRADaRRRAVELLELVGIAqpERRARAFpHEL 155
Cdd:COG1119 73 ---VWELRKR-IGLVSPALQLRFPRDETVLDVVLSGffdsIGLY-REPTDEQ-RERARELLELLGLA--HLADRPF-GTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 156 SGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVE 235
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVA 223
|
....*..
gi 1424538268 236 IAAVDEL 242
Cdd:COG1119 224 AGPKEEV 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
381-589 |
6.79e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 103.12 E-value: 6.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLdaaARRRLRTELQVVFQDpvASLDPRlpv 460
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV---TRASLRRNIAVVFQD--AGLFNR--- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 ydVIAEPLRANGFHRHECE-ERVAELLAVVGLDHSDASRYPA-------EFSGGQKQRIGIARALALQPKILALDEPVSA 532
Cdd:PRK13657 424 --SIEDNIRVGRPDATDEEmRAAAERAQAHDFIERKPDGYDTvvgergrQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 533 LDVSIQAGiVNLLLDLQRRfGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQGESDQ 589
Cdd:PRK13657 502 LDVETEAK-VKAALDELMK-GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDE 555
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-245 |
7.29e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.79 E-value: 7.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 2 TAVLEVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlpEYARvSGSIRLHGKELLGLSDH 81
Cdd:PRK09452 12 SPLVELRGISKSFDGKEV----ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF--ETPD-SGRIMLDGQDITHVPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 82 AmsqirgRMIGTVFQDpmSALTPVYTIGDQIAEAIEIhsREISRADARRRAVELLELVgiaQPERRARAFPHELSGGERQ 161
Cdd:PRK09452 85 N------RHVNTVFQS--YALFPHMTVFENVAFGLRM--QKTPAAEITPRVMEALRMV---QLEEFAQRKPHQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 162 RVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDE 241
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
....
gi 1424538268 242 LYRD 245
Cdd:PRK09452 232 IYEE 235
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
381-585 |
7.45e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 97.83 E-value: 7.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQIL--ELTKPEAGSIEILGTDVavLDAAARRRLRTELQVVFQDPVASldPRL 458
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDI--LELSPDERARAGIFLAFQYPVEI--PGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 459 PVYDVI--------AEPLRANGFHRheceeRVAELLAVVGLDHSDASRYPAE-FSGGQKQRIGIARALALQPKILALDEP 529
Cdd:COG0396 93 SVSNFLrtalnarrGEELSAREFLK-----LLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDET 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 530 VSALDV---SIQAGIVNLLLDLQRrfglSYLFVSHDLSVVKHL-AHRVAVMYRGMIVEQG 585
Cdd:COG0396 168 DSGLDIdalRIVAEGVNKLRSPDR----GILIITHYQRILDYIkPDFVHVLVDGRIVKSG 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-228 |
8.64e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.15 E-value: 8.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 22 PAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGkellglsdhamsqirGRMIGTVFQdpMSA 101
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRP---TSGTVRRAG---------------GARVAYVPQ--RSE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 102 LTPVYTIgdQIAEAIEI-------HSREISRADaRRRAVELLELVGIAQPERRARafpHELSGGERQRVVIAIAIANDPD 174
Cdd:NF040873 66 VPDSLPL--TVRDLVAMgrwarrgLWRRLTRDD-RAAVDDALERVGLADLAGRQL---GELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 175 LLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEfADRALVM 228
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
381-585 |
9.85e-23 |
|
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: 97.30 E-value: 9.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAArrrLRTELQVVFQDPVAsldprlpV 460
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS---LRRAIGVVPQDTVL-------F 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLR-----ANgfhrhecEERVAELlAVVGLDHSDASRYPAEF-----------SGGQKQRIGIARALALQPKIL 524
Cdd:cd03253 88 NDTIGYNIRygrpdAT-------DEEVIEA-AKAAQIHDKIMRFPDGYdtivgerglklSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 525 ALDEPVSALDVSIQAGIVNLLLDLQRrfGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQG 585
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-581 |
9.96e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 101.93 E-value: 9.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETedieVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeYARVSGSIRLHGKELL--GL 78
Cdd:PRK13549 2 MEYLLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP-HGTYEGEIIFEGEELQasNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 79 SDhamSQIRGrmIGTVFQDPMsaLTPVYTIGDQIAEAIEIHSREISRADA-RRRAVELLELVGIA-QPERRARafphELS 156
Cdd:PRK13549 77 RD---TERAG--IAIIHQELA--LVKELSVLENIFLGNEITPGGIMDYDAmYLRAQKLLAQLKLDiNPATPVG----NLG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 157 GGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVEI 236
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKA-HGIACIYISHKLNEVKAISDTICVIRDGRHIGT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 237 AAVDELYRDRRMPYTVGllgsvpRldaaqgtrlipipgappTMTSLspgactfAPRCPLAIDEclsaepdlvrvadghwa 316
Cdd:PRK13549 225 RPAAGMTEDDIITMMVG------R-----------------ELTAL-------YPREPHTIGE----------------- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 317 acirtddvagrsaadvfgvstqpppnnaaggqppVVLRVSDLT---KTYRLTKgvvvrrrvgevrAVDGISFTLEQGRTL 393
Cdd:PRK13549 258 ----------------------------------VILEVRNLTawdPVNPHIK------------RVDDVSFSLRRGEIL 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 394 GIVGESGSGKsTTLNQILELTKPEA--GSIEILGTDVAVldAAARRRLRTELQVVFQD-------PVASL--DPRLPVYD 462
Cdd:PRK13549 292 GIAGLVGAGR-TELVQCLFGAYPGRweGEIFIDGKPVKI--RNPQQAIAQGIAMVPEDrkrdgivPVMGVgkNITLAALD 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 463 VIAEPLRANGFHRHEC-EERVAEL--------LAVVGLdhsdasrypaefSGGQKQRIGIARALALQPKILALDEPVSAL 533
Cdd:PRK13549 369 RFTGGSRIDDAAELKTiLESIQRLkvktaspeLAIARL------------SGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1424538268 534 DVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMI 581
Cdd:PRK13549 437 DVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
381-582 |
1.37e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 102.49 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRTE-LQVVFQDpvASLDPRLP 459
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREhFGFIFQR--YHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 460 VYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQA 539
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDR-VEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1424538268 540 GIVNLLLDLQRRfGLSYLFVSHDLSVVKHlAHRVAVMYRGMIV 582
Cdd:PRK10535 182 EVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-261 |
1.55e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.00 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFE--TEdievpAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELlGLSDH 81
Cdd:PRK13636 5 ILKVEELNYNYSdgTH-----ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP---SSGRILFDGKPI-DYSRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 82 AMSQIRgRMIGTVFQDPMSALTPVYTIGDQIAEAIEIhsrEISRADARRRAVELLELVGIAQPERRArafPHELSGGERQ 161
Cdd:PRK13636 76 GLMKLR-ESVGMVFQDPDNQLFSASVYQDVSFGAVNL---KLPEDEVRKRVDNALKRTGIEHLKDKP---THCLSFGQKK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 162 RVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDE 241
Cdd:PRK13636 149 RVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKE 228
|
250 260
....*....|....*....|
gi 1424538268 242 LYRDRRMPYTVGLlgSVPRL 261
Cdd:PRK13636 229 VFAEKEMLRKVNL--RLPRI 246
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
353-585 |
1.57e-22 |
|
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: 96.63 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 353 LRVSDLTKTYRLTKGVVVRRRVGEV---------RAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEI 423
Cdd:cd03267 1 IEVSNLSKSYRVYSKEPGLIGSLKSlfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 424 LGtdvaVLDAAARRRLRTELQVVF-QDPVASLDprLPV---YDVIAEPLRANGFHRHECEERVAELLAVVGLDHSDASRy 499
Cdd:cd03267 81 AG----LVPWKRRKKFLRRIGVVFgQKTQLWWD--LPVidsFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQ- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 500 paeFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRG 579
Cdd:cd03267 154 ---LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
....*.
gi 1424538268 580 MIVEQG 585
Cdd:cd03267 231 RLLYDG 236
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
381-595 |
1.72e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 97.11 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRL---RTelqvvFQDPvaSLDPR 457
Cdd:COG4674 27 NDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLgigRK-----FQKP--TVFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 458 LPVYD--VIAEP----LRANGFHRH--ECEERVAELLAVVGLDHsDASRYPAEFSGGQKQRIGIARALALQPKILALDEP 529
Cdd:COG4674 100 LTVFEnlELALKgdrgVFASLFARLtaEERDRIEEVLETIGLTD-KADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 530 VSALDVSIQAGIVNLLLDLQRRFglSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQ 595
Cdd:COG4674 179 VAGMTDAETERTAELLKSLAGKH--SVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQADPR 242
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-235 |
1.75e-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: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETedieVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlpeYARVSGSIRLHGKELLGLSDhAMS 84
Cdd:cd03268 1 LKTNDLTKTYGK----KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGL---IKPDSGEITFDGKSYQKNIE-ALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 QIrGRMI-GTVFQDPMSALtpvytigdqiaEAIEIHSREISRADarRRAVELLELVGIAQ-PERRARAFphelSGGERQR 162
Cdd:cd03268 73 RI-GALIeAPGFYPNLTAR-----------ENLRLLARLLGIRK--KRIDEVLDVVGLKDsAKKKVKGF----SLGMKQR 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 163 VVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVE 235
Cdd:cd03268 135 LGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
381-586 |
2.08e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 97.06 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGsiEILGTDVAVLDAaarrrlRTELQVVFQDpvASLDPRLPV 460
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--ELLAGTAPLAEA------REDTRLMFQD--ARLLPWKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANgfhrheCEERVAELLAVVGLDhSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:PRK11247 99 IDNVGLGLKGQ------WRDAALQALAAVGLA-DRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1424538268 541 IVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVavmyrgMIVEQGE 586
Cdd:PRK11247 172 MQDLIESLWQQHGFTVLLVTHDVSEAVAMADRV------LLIEEGK 211
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
328-585 |
2.10e-22 |
|
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: 101.33 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 328 SAADVFGVSTQPPPNNAAGGQPPVV---LRVSDLTKTYRltkgvvvrrrVGEVRAVDGISFTLEQGRTLGIVGESGSGKS 404
Cdd:TIGR02203 303 AAESLFTLLDSPPEKDTGTRAIERArgdVEFRNVTFRYP----------GRDRPALDSISLVIEPGETVALVGRSGSGKS 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 405 TTLNQILELTKPEAGSIEILGTDVAVLdaaARRRLRTELQVVFQDpVASLDprlpvyDVIAEPL---RANGFHRHECEE- 480
Cdd:TIGR02203 373 TLVNLIPRFYEPDSGQILLDGHDLADY---TLASLRRQVALVSQD-VVLFN------DTIANNIaygRTEQADRAEIERa 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 481 -RVAELLAVV-----GLDH---SDASRypaeFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRr 551
Cdd:TIGR02203 443 lAAAYAQDFVdklplGLDTpigENGVL----LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ- 517
|
250 260 270
....*....|....*....|....*....|....
gi 1424538268 552 fGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQG 585
Cdd:TIGR02203 518 -GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERG 549
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
381-592 |
2.12e-22 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 101.87 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRlrtELQVVFQDPV---ASLdpr 457
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRR---NIGYVPQDPRlfyGTL--- 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 458 lpvYDVIAepLRAngfhRHECEERVAELLAVVGLdHSDASRYPAEF-----------SGGQKQRIGIARALALQPKILAL 526
Cdd:TIGR03375 556 ---RDNIA--LGA----PYADDEEILRAAELAGV-TEFVRRHPDGLdmqigergrslSGGQRQAVALARALLRDPPILLL 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 527 DEPVSALDVSIQAgivnLLLDLQRRF--GLSYLFVSHDLSVVKhLAHRVAVMYRGMIVEQGESDQVFT 592
Cdd:TIGR03375 626 DEPTSAMDNRSEE----RFKDRLKRWlaGKTLVLVTHRTSLLD-LVDRIIVMDNGRIVADGPKDQVLE 688
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-562 |
2.50e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 7 VTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVI-GLLPEYarvSGSIRLHGkellglsdhamsQ 85
Cdd:COG0488 1 LENLSKSFGGRPL----LDDVSLSINPGDRIGLVGRNGAGKSTL-LKILaGELEPD---SGEVSIPK------------G 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 86 IRgrmIGTVFQDP------------MSALTPVYTIGDQIAEA---IEIHSREISRA-------------DARRRAVELLE 137
Cdd:COG0488 61 LR---IGYLPQEPpldddltvldtvLDGDAELRALEAELEELeakLAEPDEDLERLaelqeefealggwEAEARAEEILS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 138 LVGIAQPERRARAfpHELSGGERQRVVIAIAIANDPDLLICDEPTTALDV-TVQ--AQILdvlrtaRDVTGAaVLIITHD 214
Cdd:COG0488 138 GLGFPEEDLDRPV--SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIEwlEEFL------KNYPGT-VLVVSHD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 215 ---L-GVVS---EFADRALVMYAG---------------RPVEIAAVDELYRD-----RRMpytvgllgsvpRLDAAQGT 267
Cdd:COG0488 209 ryfLdRVATrilELDRGKLTLYPGnysayleqraerleqEAAAYAKQQKKIAKeeefiRRF-----------RAKARKAK 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 268 RlipipgapptMTSlspgactfaprcplaideclsaepdlvRVADghwAACIRTDDVAGRSAADVFGVSTQPPPnnaagg 347
Cdd:COG0488 278 Q----------AQS---------------------------RIKA---LEKLEREEPPRRDKTVEIRFPPPERL------ 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 348 qPPVVLRVSDLTKTYrltkgvvvrrrvGEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEIlGTD 427
Cdd:COG0488 312 -GKKVLELEGLSKSY------------GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GET 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 428 V--AVLDaaarrrlrtelqvvfQDpVASLDPRLPVYDVIAEplrangFHRHECEERVAELLAVVGLDHSDASRYPAEFSG 505
Cdd:COG0488 378 VkiGYFD---------------QH-QEELDPDKTVLDELRD------GAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSG 435
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 506 GQKQRIGIARALALQPKILALDEPVSALDV-SIQAgIVNLLLDlqrrFGLSYLFVSHD 562
Cdd:COG0488 436 GEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA-LEEALDD----FPGTVLLVSHD 488
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
11-261 |
2.55e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.08 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTF----ETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHGKELLGLSDhaMSQ 85
Cdd:PRK13633 9 NVSYkyesNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLiPS----EGKVYVDGLDTSDEEN--LWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 86 IRGRMiGTVFQDPMSALtpVYTIGDQ-IA---EAIEIHSREIsradaRRRAVELLELVGIAQPERRArafPHELSGGERQ 161
Cdd:PRK13633 83 IRNKA-GMVFQNPDNQI--VATIVEEdVAfgpENLGIPPEEI-----RERVDESLKKVGMYEYRRHA---PHLLSGGQKQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 162 RVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEfADRALVMYAGRPVEIAAVDE 241
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKE 230
|
250 260
....*....|....*....|
gi 1424538268 242 LYRDRRMPYTVGLlgSVPRL 261
Cdd:PRK13633 231 IFKEVEMMKKIGL--DVPQV 248
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
234-318 |
2.84e-22 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 91.27 E-value: 2.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 234 VEIAAVDELYRDRRMPYTVGLLGSVPRLdAAQGTRLIPIPGAPPTMTSLSPGaCTFAPRCPLAIDECLSAEPDLVRVADG 313
Cdd:TIGR01727 3 VETGPAEEIFKNPLHPYTKALLSAIPTI-KKRDRKLISIPGEVPSLINLPSG-CRFYPRCPYAQDECRKEPPALVEIAEG 80
|
....*
gi 1424538268 314 HWAAC 318
Cdd:TIGR01727 81 HRVAC 85
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
31-244 |
3.25e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 98.25 E-value: 3.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 31 IDPGEVLAIVGESGCGKTTAALAVIGLlpeYARVSGSIRLHGKellglsDHAMSQIRGRMIGTVFQDpmSALTPVYTIGD 110
Cdd:PRK11432 29 IKQGTMVTLLGPSGCGKTTVLRLVAGL---EKPTEGQIFIDGE------DVTHRSIQQRDICMVFQS--YALFPHMSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 111 QIAEAIEIHSReiSRADARRRAVELLELVGIAQPERRaraFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQ 190
Cdd:PRK11432 98 NVGYGLKMLGV--PKEERKQRVKEALELVDLAGFEDR---YVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 191 AQILDVLRTARDVTGAAVLIITHDLgvvSE-FA--DRALVMYAGRPVEIAAVDELYR 244
Cdd:PRK11432 173 RSMREKIRELQQQFNITSLYVTHDQ---SEaFAvsDTVIVMNKGKIMQIGSPQELYR 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
381-592 |
3.82e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 95.92 E-value: 3.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAA--ARRrlrteLQVVFQDPvaSLDPRL 458
Cdd:COG4604 18 DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRelAKR-----LAILRQEN--HINSRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 459 PVYDVIaeplranGFHRH---------ECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEP 529
Cdd:COG4604 91 TVRELV-------AFGRFpyskgrltaEDREIIDEAIAYLDLEDL-ADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 530 VSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFT 592
Cdd:COG4604 163 LNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIIT 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-246 |
3.99e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 97.61 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTF-ETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEYARVSGS---IRLHGKELLGL 78
Cdd:PRK13631 21 ILRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIkSKYGTIQVGdiyIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 79 SDHAMSQIRG-----RMIGTVFQDPMSALtpvytIGDQIAEAIEIH--SREISRADARRRAVELLELVGIAQP--ERRar 149
Cdd:PRK13631 101 TNPYSKKIKNfkelrRRVSMVFQFPEYQL-----FKDTIEKDIMFGpvALGVKKSEAKKLAKFYLNKMGLDDSylERS-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 150 afPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMY 229
Cdd:PRK13631 174 --PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKA-NNKTVFVITHTMEHVLEVADEVIVMD 250
|
250
....*....|....*..
gi 1424538268 230 AGRPVEIAAVDELYRDR 246
Cdd:PRK13631 251 KGKILKTGTPYEIFTDQ 267
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
382-595 |
4.21e-22 |
|
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: 95.43 E-value: 4.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRL---------RtelqvVFqdpva 452
Cdd:COG0410 21 GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgigyvpegrR-----IF----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 453 sldPRLPVYD--VIAEPLRANGFHRHECEERVAELlavvgldhsdasrYP--AEF--------SGGQKQRIGIARALALQ 520
Cdd:COG0410 91 ---PSLTVEEnlLLGAYARRDRAEVRADLERVYEL-------------FPrlKERrrqragtlSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 521 PKILALDEPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQ 595
Cdd:COG0410 155 PKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
395-595 |
4.98e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 98.02 E-value: 4.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 395 IVGESGSGKSTTLNQILELTKPEAGSIeILGTDVAVlDAAARRRLRTELQ---VVFQDPvasldpRL-PVYDViaeplRA 470
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRI-VLNGRVLF-DAEKGICLPPEKRrigYVFQDA------RLfPHYKV-----RG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 471 N---GFhRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLD 547
Cdd:PRK11144 96 NlryGM-AKSMVAQFDKIVALLGIEPL-LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1424538268 548 LQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQ 595
Cdd:PRK11144 174 LAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-245 |
5.04e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.39 E-value: 5.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 20 EVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEYARVS-GSIRLHGKEllglSDHAMSQIRGRmIGTVFQD 97
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLkPTTGTVTvDDITITHKT----KDKYIRPVRKR-IGMVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 98 PMSALtpvytIGDQIAEAIEIHSRE--ISRADARRRAVELLELVGIaqPERRARAFPHELSGGERQRVVIAIAIANDPDL 175
Cdd:PRK13646 94 PESQL-----FEDTVEREIIFGPKNfkMNLDEVKNYAHRLLMDLGF--SRDVMSQSPFQMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 176 LICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRD 245
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
22-244 |
5.69e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 95.10 E-value: 5.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 22 PAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSDHAmsqiRGRM-IG------TV 94
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPD---SGRIFLDGEDITHLPMHK----RARLgIGylpqeaSI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 95 FQDpmsaLTpvytIGDQIAEAIEIhsREISRADARRRAVELLELVGIaQPERRARAfpHELSGGERQRVVIAIAIANDPD 174
Cdd:COG1137 90 FRK----LT----VEDNILAVLEL--RKLSKKEREERLEELLEEFGI-THLRKSKA--YSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 175 LLICDEPTTALD-VTVqAQILDVLRTARDvTGAAVLIITHD----LGVVsefaDRALVMYAGR------PVEIAAvDELY 243
Cdd:COG1137 157 FILLDEPFAGVDpIAV-ADIQKIIRHLKE-RGIGVLITDHNvretLGIC----DRAYIISEGKvlaegtPEEILN-NPLV 229
|
.
gi 1424538268 244 R 244
Cdd:COG1137 230 R 230
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
11-241 |
6.79e-22 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 99.82 E-value: 6.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELlglsDHAMSQIRGRM 90
Cdd:COG4618 335 NLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPP---TAGSVRLDGADL----SQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 91 IGTVFQDPmsALTPVyTIGDQIAEAIEIHSREISRAdARRRAV-EL-LEL-------VGiaqpERRARafpheLSGGERQ 161
Cdd:COG4618 408 IGYLPQDV--ELFDG-TIAENIARFGDADPEKVVAA-AKLAGVhEMiLRLpdgydtrIG----EGGAR-----LSGGQRQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 162 RVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEfADRALVMYAGRPVEIAAVDE 241
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKA-RGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDE 552
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-593 |
7.41e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 99.47 E-value: 7.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 21 VPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlpeYARVSGSIRLHGKELLGLsDHAMSQIRGrmIGTVFQ---- 96
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI---HEPTKGTITINNINYNKL-DHKLAAQLG--IGIIYQelsv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 97 -DPMSALTPVYtIGDQIAE---AIEIhsreISRADARRRAVELLELVGIaqpERRARAFPHELSGGERQRVVIAIAIAND 172
Cdd:PRK09700 92 iDELTVLENLY-IGRHLTKkvcGVNI----IDWREMRVRAAMMLLRVGL---KVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 173 PDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDrrmpytv 252
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRK-EGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND------- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 253 gllgsvprldaaqgtrlipipgapptmtslspgactfaprcplaideclsaepDLVRVadghwaacirtddVAGRSAADV 332
Cdd:PRK09700 236 -----------------------------------------------------DIVRL-------------MVGRELQNR 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 333 FgVSTQPPPNNAAGgqpPVVLRVSDLTKTYRltkgvvvrrrvgevRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILE 412
Cdd:PRK09700 250 F-NAMKENVSNLAH---ETVFEVRNVTSRDR--------------KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFG 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 413 LTKPEAGSIEILGTDVAvldaaarrrlrtelqvvfqdPVASLDPRLPVYDVIAEPLRANG-FHRHECEERVA-------- 483
Cdd:PRK09700 312 VDKRAGGEIRLNGKDIS--------------------PRSPLDAVKKGMAYITESRRDNGfFPNFSIAQNMAisrslkdg 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 484 ELLAVVGL-DHSDASRYP------------------AEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNL 544
Cdd:PRK09700 372 GYKGAMGLfHEVDEQRTAenqrellalkchsvnqniTELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKV 451
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1424538268 545 LLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIveqgesDQVFTN 593
Cdd:PRK09700 452 MRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL------TQILTN 493
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-263 |
8.55e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.08 E-value: 8.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTaalavigLLPEYARV----SGSIRLHGKELLGLSD 80
Cdd:PRK11231 3 LRTENLTVGYGTKRI----LNDLSLSLPTGKITALIGPNGCGKST-------LLKCFARLltpqSGTVFLGDKPISMLSS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 HAMSqirgRMIGTVFQDPmsaLTPvytigdqiaEAIEIhsREI---------------SRADARR--RAVELLELVGIAq 143
Cdd:PRK11231 72 RQLA----RRLALLPQHH---LTP---------EGITV--RELvaygrspwlslwgrlSAEDNARvnQAMEQTRINHLA- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 144 pERRARafphELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFAD 223
Cdd:PRK11231 133 -DRRLT----DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNT-QGKTVVTVLHDLNQASRYCD 206
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1424538268 224 RALVMYAGRPVEIAAVDELyrdrrmpYTVGLLGSVPRLDA 263
Cdd:PRK11231 207 HLVVLANGHVMAQGTPEEV-------MTPGLLRTVFDVEA 239
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-256 |
9.24e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.91 E-value: 9.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGL--LPEYARVSGSIRLHGKELLGL 78
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHV----IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEARVEGEVRLFGRNIYSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 79 SDHAMsQIRgRMIGTVFQDPMSalTPVYTIGDQIAEAIEIHSREISRADARRRAVELLELVGI-AQPERRARAFPHELSG 157
Cdd:PRK14267 77 DVDPI-EVR-REVGMVFQYPNP--FPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALwDEVKDRLNDYPSNLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 158 GERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVL-RTARDVTgaaVLIITHDLGVVSEFADRALVMYAGRPVEI 236
Cdd:PRK14267 153 GQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLfELKKEYT---IVLVTHSPAQAARVSDYVAFLYLGKLIEV 229
|
250 260
....*....|....*....|....
gi 1424538268 237 AAVDELYRDRRMP----YTVGLLG 256
Cdd:PRK14267 230 GPTRKVFENPEHEltekYVTGALG 253
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-234 |
9.27e-22 |
|
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: 94.26 E-value: 9.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 17 EDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYARVSGSIRLHGKELlglSDHAMSQIrgrmIGTVFQ 96
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPR---KPDQFQKC----VAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 97 DpmSALTPVYTIGDQIAEAIEIHSREISRaDARRR---AVELLELVGIaqpERRARAFPHELSGGERQRVVIAIAIANDP 173
Cdd:cd03234 89 D--DILLPGLTVRETLTYTAILRLPRKSS-DAIRKkrvEDVLLRDLAL---TRIGGNLVKGISGGERRRVSIAVQLLWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 174 DLLICDEPTTALDVTVQAQILDVLR-TARdvTGAAVLIITHDLGV-VSEFADRALVMYAGRPV 234
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSqLAR--RNRIVILTIHQPRSdLFRLFDRILLLSSGEIV 223
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-242 |
1.06e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.03 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLpeyARVSGSIRLHGKELLGLSD 80
Cdd:PRK13537 4 SVAPIDFRNVEKRYG----DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLT---HPDAGSISLCGEPVPSRAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 HAmsqiRGRmIGTVFQdpMSALTPVYTIgdqiAEAIEIHSRE--ISRADARRRAVELLELvgiAQPERRARAFPHELSGG 158
Cdd:PRK13537 77 HA----RQR-VGVVPQ--FDNLDPDFTV----RENLLVFGRYfgLSAAAARALVPPLLEF---AKLENKADAKVGELSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 159 ERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRT--ARdvtGAAVLIITHDLGVVSEFADRALVMYAGRPVEI 236
Cdd:PRK13537 143 MKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR---GKTILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
|
....*.
gi 1424538268 237 AAVDEL 242
Cdd:PRK13537 220 GAPHAL 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
381-581 |
1.07e-21 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 92.28 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLrteLQVVFQDpvaslDPRLPv 460
Cdd:cd03246 19 RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH---VGYLPQD-----DELFS- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 yDVIAEPLrangfhrheceervaellavvgldhsdasrypaeFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:cd03246 90 -GSIAENI----------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1424538268 541 IVNLLLDLQRRfGLSYLFVSHDLSVVKhLAHRVAVMYRGMI 581
Cdd:cd03246 135 LNQAIAALKAA-GATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
384-585 |
1.17e-21 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 93.77 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 384 SFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEIlgTDVAVLDAAARRRlrtELQVVFQDpvASLDPRLPVYDV 463
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKV--NDQSHTGLAPYQR---PVSMLFQE--NNLFAHLTVRQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 464 IAEPLRANGFHRHECEERVAELLAVVGLDHSDAsRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVN 543
Cdd:TIGR01277 91 IGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLD-RLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1424538268 544 LLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQG 585
Cdd:TIGR01277 170 LVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
381-585 |
1.33e-21 |
|
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: 93.42 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRlrtELQVVFQDPVasldprlpv 460
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR---NIGYVPQDVT--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 ydVIAEPLRAN--GFHRHECEERVAELLAVVGLDhSDASRYPAEF-----------SGGQKQRIGIARALALQPKILALD 527
Cdd:cd03245 89 --LFYGTLRDNitLGAPLADDERILRAAELAGVT-DFVNKHPNGLdlqigergrglSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 528 EPVSALDVSIQAGIVNLLLDLQRrfGLSYLFVSHDLSVVKhLAHRVAVMYRGMIVEQG 585
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
350-581 |
1.42e-21 |
|
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: 92.50 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 350 PVVLRVSDLTKTYRLtkgvvvrrrvgevravDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVA 429
Cdd:cd03215 2 EPVLEVRGLSVKGAV----------------RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 430 VLDAAARRRLRteLQVVFQDP-VASLDPRLPVYDVIAeplrangfhrheceerVAELLavvgldhsdasrypaefSGGQK 508
Cdd:cd03215 66 RRSPRDAIRAG--IAYVPEDRkREGLVLDLSVAENIA----------------LSSLL-----------------SGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 509 QRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMI 581
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-244 |
1.56e-21 |
|
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: 92.98 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVtfETEDIEVpaVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlPEYARVSGSIRLHGKELLGLSDHAms 84
Cdd:cd03217 1 LEIKDLHV--SVGGKEI--LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEVTEGEILFKGEDITDLPPEE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 qiRGRM-IGTVFQDPmsaltpvytigdqiaeaIEIHsreisradarrrAVELLELVgiaqperraRAFPHELSGGERQRV 163
Cdd:cd03217 74 --RARLgIFLAFQYP-----------------PEIP------------GVKNADFL---------RYVNEGFSGGEKKRN 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 164 VIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVtGAAVLIITHdLGVVSEF--ADRALVMYAGR-----PVEI 236
Cdd:cd03217 114 EILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITH-YQRLLDYikPDRVHVLYDGRivksgDKEL 191
|
....*...
gi 1424538268 237 AavDELYR 244
Cdd:cd03217 192 A--LEIEK 197
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
381-568 |
1.57e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.63 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRlrtelQV--VFQDPVASLDPrl 458
Cdd:PRK10247 24 NNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ-----QVsyCAQTPTLFGDT-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 459 pVYDVIAEP--LRangfHRHECEERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVS 536
Cdd:PRK10247 97 -VYDNLIFPwqIR----NQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190
....*....|....*....|....*....|..
gi 1424538268 537 IQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKH 568
Cdd:PRK10247 172 NKHNVNEIIHRYVREQNIAVLWVTHDKDEINH 203
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
382-592 |
1.60e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 94.14 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTkPEAGSIEILGTDVAVLDAAARRRLRTEL--QvvfQDPVASLdprlP 459
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLsqQ---QSPPFAM----P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 460 VYDVIAEPLRANGfHRHECEERVAELLAVVGLDhSDASRYPAEFSGGQKQRIGIARALaLQ--------PKILALDEPVS 531
Cdd:COG4138 86 VFQYLALHQPAGA-SSEAVEQLLAQLAEALGLE-DKLSRPLTQLSGGEWQRVRLAAVL-LQvwptinpeGQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 532 ALDVSIQAgivnLLLDLQRRF---GLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFT 592
Cdd:COG4138 163 SLDVAQQA----ALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-232 |
1.85e-21 |
|
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: 93.55 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 14 FETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHG-------KELLglsdhamsq 85
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqPT----SGEVRVAGlvpwkrrKKFL--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 86 irgRMIGTVF--QDPMSALTPVytigdqiAEAIEIHSR--EISRADARRRAVELLELVGIA----QPERRarafpheLSG 157
Cdd:cd03267 94 ---RRIGVVFgqKTQLWWDLPV-------IDSFYLLAAiyDLPPARFKKRLDELSELLDLEelldTPVRQ-------LSL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 158 GERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
11-254 |
2.15e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 94.43 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlpEYARvSGSIRLhgkELLGLSDHAMSQIRgRM 90
Cdd:PRK13648 12 NVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI--EKVK-SGEIFY---NNQAITDDNFEKLR-KH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 91 IGTVFQDPMSALTPVyTIGDQIAEAIEIHSreISRADARRRAVELLELVGIAQperRARAFPHELSGGERQRVVIAIAIA 170
Cdd:PRK13648 85 IGIVFQNPDNQFVGS-IVKYDVAFGLENHA--VPYDEMHRRVSEALKQVDMLE---RADYEPNALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 171 NDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEfADRALVMYAGRPVEIAAVDELYRDRRMPY 250
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELT 237
|
....
gi 1424538268 251 TVGL 254
Cdd:PRK13648 238 RIGL 241
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-614 |
2.16e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 97.77 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETedieVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlpeYARVSGSIRLHGKELlGLSD 80
Cdd:PRK10762 1 MQALLQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGI---YTRDAGSILYLGKEV-TFNG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 HAMSQIRGrmIGTVFQDpmSALTPVYTIGDQIAEAIEIHSR--EISRADARRRAVELLELVGIAQPERRARAfphELSGG 158
Cdd:PRK10762 73 PKSSQEAG--IGIIHQE--LNLIPQLTIAENIFLGREFVNRfgRIDWKKMYAEADKLLARLNLRFSSDKLVG---ELSIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 159 ERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAA 238
Cdd:PRK10762 146 EQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKS-QGRGIVYISHRLKEIFEICDDVTVFRDGQFIAERE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 239 VDELYRDRRMPYTVG--LLGSVPRLDAAQGtrlipipgapptmtslspgactfaprcplaideclsaepdlvrvadghwa 316
Cdd:PRK10762 225 VADLTEDSLIEMMVGrkLEDQYPRLDKAPG-------------------------------------------------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 317 acirtddvagrsaadvfgvstqpppnnaaggqpPVVLRVSDLTktyrltkgvvvrrrvgeVRAVDGISFTLEQGRTLGIV 396
Cdd:PRK10762 255 ---------------------------------EVRLKVDNLS-----------------GPGVNDVSFTLRKGEILGVS 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 397 GESGSGKsTTLNQILELTKP-EAGSIEILGTDVAVL---DAAA---------RRR--LRTELQVVFQDPVASLDprlpvy 461
Cdd:PRK10762 285 GLMGAGR-TELMKVLYGALPrTSGYVTLDGHEVVTRspqDGLAngivyisedRKRdgLVLGMSVKENMSLTALR------ 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 dviaEPLRANGFHRHECE-ERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:PRK10762 358 ----YFSRAGGSLKHADEqQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKE 433
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 541 IVNLLldlqRRF---GLSYLFVSHDLSVVKHLAHRVAVMYRGMIveQGEsdqvFTNPQHEYTRRLLAAVPRAHSDVA 614
Cdd:PRK10762 434 IYQLI----NQFkaeGLSIILVSSEMPEVLGMSDRILVMHEGRI--SGE----FTREQATQEKLMAAAVGKLNRVNQ 500
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
381-594 |
2.21e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.90 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVL--DAAARR---------RLRTELQVVFQD 449
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpgHQIARMgvvrtfqhvRLFREMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 450 PVASldPRLPVYDVIAEPLRANGFHRHECE--ERVAELLAVVGLdHSDASRYPAEFSGGQKQRIGIARALALQPKILALD 527
Cdd:PRK11300 102 LVAQ--HQQLKTGLFSGLLKTPAFRRAESEalDRAATWLERVGL-LEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 528 EPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNP 594
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-242 |
2.30e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.78 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTfetedievPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeyaRVSGSIRLHGKELLGLS-DHA 82
Cdd:COG1129 256 VLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADP---ADSGEIRLDGKPVRIRSpRDA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 83 MSQirGrmIGTVFQD--------PMSaltpvytigdqIAE-----AIEIHSRE--ISRADARRRAVELLELVGI--AQPE 145
Cdd:COG1129 325 IRA--G--IAYVPEDrkgeglvlDLS-----------IREnitlaSLDRLSRGglLDRRRERALAEEYIKRLRIktPSPE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 146 RRARafphELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRA 225
Cdd:COG1129 390 QPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAA-EGKAVIVISSELPELLGLSDRI 464
|
250
....*....|....*..
gi 1424538268 226 LVMYAGRPVEIAAVDEL 242
Cdd:COG1129 465 LVMREGRIVGELDREEA 481
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
381-582 |
2.47e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 94.00 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRL--RtelqvVFQDPVASLDPRL 458
Cdd:COG1101 23 DGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYigR-----VFQDPMMGTAPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 459 pvydVIAEPL-------RANGFHR---HECEERVAELLAVVGL---DHSDAsryPAEF-SGGQKQrigiarALAL----- 519
Cdd:COG1101 98 ----TIEENLalayrrgKRRGLRRgltKKRRELFRELLATLGLgleNRLDT---KVGLlSGGQRQ------ALSLlmatl 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 520 -QPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIV 582
Cdd:COG1101 165 tKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-593 |
2.65e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.43 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETedieVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSD 80
Cdd:PRK15439 8 APPLLCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD---SGTLEIGGNPCARLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 ---HAMSqirgrmIGTVFQDPMsaLTPVYTIGDQIAEAIEIHsreisrADARRRAVELLELVGIA-QPERRARAfpheLS 156
Cdd:PRK15439 81 akaHQLG------IYLVPQEPL--LFPNLSVKENILFGLPKR------QASMQKMKQLLAALGCQlDLDSSAGS----LE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 157 GGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGrpvei 236
Cdd:PRK15439 143 VADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDG----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 237 aavdelyrdrrmpyTVGLLGSVPRLDAAQgtrlipipgappTMTSLSPGActfaprcplaIDECLSAEPDLvrvadghWA 316
Cdd:PRK15439 217 --------------TIALSGKTADLSTDD------------IIQAITPAA----------REKSLSASQKL-------WL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 317 ACirtddvagrsaadvfgvstqppPNN---AAGGQPpvVLRVSDLTktyrltkgvvvrrrvgevraVDG---ISFTLEQG 390
Cdd:PRK15439 254 EL----------------------PGNrrqQAAGAP--VLTVEDLT--------------------GEGfrnISLEVRAG 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 391 RTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARrrLRTELQVVFQDPVAS---LDPRLpVYDVIAEP 467
Cdd:PRK15439 290 EILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQR--LARGLVYLPEDRQSSglyLDAPL-AWNVCALT 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 468 LRANGFHRHECEER--VAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLL 545
Cdd:PRK15439 367 HNRRGFWIKPARENavLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLI 446
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1424538268 546 LDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTN 593
Cdd:PRK15439 447 RSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVD 493
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
31-246 |
2.82e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 94.32 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 31 IDPGEVLAIVGESGCGKTTAALAVIGLL-PeyarVSGSIRLhGKELL--GLSDHAMSQIRgRMIGTVFQDPMSALtpvyt 107
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLNGLLqP----TSGTVTI-GERVItaGKKNKKLKPLR-KKVGIVFQFPEHQL----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 108 igdqIAEAIEihsREI---------SRADARRRAVELLELVGIAqPERRARAfPHELSGGERQRVVIAIAIANDPDLLIC 178
Cdd:PRK13634 99 ----FEETVE---KDIcfgpmnfgvSEEDAKQKAREMIELVGLP-EELLARS-PFELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 179 DEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDR 246
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-251 |
4.06e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.05 E-value: 4.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 3 AVLEVTDLNVTFEteDIEVpaVRGTSYHIDPGEVLAIVGESGCGKTTAALA---VIGLLPEyARVSGSIRLHGKELLGLS 79
Cdd:PRK14247 2 NKIEIRDLKVSFG--QVEV--LDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPE-ARVSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 80 dhaMSQIRgRMIGTVFQDPMSalTPVYTIGDQIAEAIEIHSREISRADARRRAVELLELVGI-AQPERRARAFPHELSGG 158
Cdd:PRK14247 77 ---VIELR-RRVQMVFQIPNP--IPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLwDEVKDRLDAPAGKLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 159 ERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDV-LRTARDVTgaaVLIITHDLGVVSEFADRALVMYAGRPVEIA 237
Cdd:PRK14247 151 QQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLfLELKKDMT---IVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
250
....*....|....
gi 1424538268 238 AVDELYRDRRMPYT 251
Cdd:PRK14247 228 PTREVFTNPRHELT 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-284 |
4.59e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 95.68 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYArvsGSIRLHGKELLGLSDHAMS 84
Cdd:PRK09536 4 IDVSDLSVEFG----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA---GTVLVAGDDVEALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 qirgRMIGTVFQDpmSALTPVYTIGDQIAEAIEIHSREISRAD-ARRRAVE-LLELVGIAQPERRARAfphELSGGERQR 162
Cdd:PRK09536 77 ----RRVASVPQD--TSLSFEFDVRQVVEMGRTPHRSRFDTWTeTDRAAVErAMERTGVAQFADRPVT---SLSGGERQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 163 VVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMY------AGRPVEI 236
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVD-DGKTAVAAIHDLDLAARYCDELVLLAdgrvraAGPPADV 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1424538268 237 AAVDELyRDRRMPYTVglLGSVPRLDAAQGTrliPIPGAPPTMTSLSP 284
Cdd:PRK09536 227 LTADTL-RAAFDARTA--VGTDPATGAPTVT---PLPDPDRTEAAADT 268
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
23-232 |
4.75e-21 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 91.87 E-value: 4.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 23 AVRGTSYHIDPGeVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELLGlsdhAMSQIRgRMIGTVFQDPMsaL 102
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPP---SSGTIRIDGQDVLK----QPQKLR-RRIGYLPQEFG--V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 103 TPVYTIGDQIAEAIEIHsrEISRADARRRAVELLELVGIAQperRARAFPHELSGGERQRVVIAIAIANDPDLLICDEPT 182
Cdd:cd03264 84 YPNFTVREFLDYIAWLK--GIPSKEVKARVDEVLELVNLGD---RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 183 TALDVTVQAQILDVL-RTARDVTgaaVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:cd03264 159 AGLDPEERIRFRNLLsELGEDRI---VILSTHIVEDVESLCNQVAVLNKGK 206
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
381-585 |
4.86e-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: 90.84 E-value: 4.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAarrrLRTELQVVFQDPVasldprlpv 460
Cdd:cd03247 19 KNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LSSLISVLNQRPY--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 ydVIAEPLRANgfhrheceervaellavVGldhsdasrypAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:cd03247 86 --LFDTTLRNN-----------------LG----------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1424538268 541 IVNLLLDLQRrfGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQG 585
Cdd:cd03247 137 LLSLIFEVLK--DKTLIWITHHLTGIEH-MDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
382-591 |
5.34e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 93.15 E-value: 5.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTdvaVLDAAAR--RRLRTELQVVFQDPvaslDPRLP 459
Cdd:PRK13638 19 GLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK---PLDYSKRglLALRQQVATVFQDP----EQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 460 VYDV---IAEPLRANGFHRHECEERVAELLAVVgldhsDASRYPAE----FSGGQKQRIGIARALALQPKILALDEPVSA 532
Cdd:PRK13638 92 YTDIdsdIAFSLRNLGVPEAEITRRVDEALTLV-----DAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 533 LDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVF 591
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
342-585 |
6.93e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 94.13 E-value: 6.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 342 NNAAGGQPPVVLRVSDLTKTYRltkgvvvrrrvgEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSI 421
Cdd:PRK13536 31 ASIPGSMSTVAIDLAGVSKSYG------------DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 422 EILGTDVAVLDAAARRRlrteLQVVFQdpVASLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDhSDASRYPA 501
Cdd:PRK13536 99 TVLGVPVPARARLARAR----IGVVPQ--FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLE-SKADARVS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 502 EFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMI 581
Cdd:PRK13536 172 DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRK 250
|
....
gi 1424538268 582 VEQG 585
Cdd:PRK13536 251 IAEG 254
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
352-595 |
9.60e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 91.63 E-value: 9.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 352 VLRVSDLTKTYRLTKgvvvrrrvgevrAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVL 431
Cdd:COG1137 3 TLEAENLVKSYGKRT------------VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 432 DAAARRR-----LRTElqvvfqdpvASLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGG 506
Cdd:COG1137 71 PMHKRARlgigyLPQE---------ASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHL-RKSKAYSLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 507 QKQRIGIARALALQPKILALDEPVSALD-VSIqAGIVNLLLDLQRRfGLSYLFVSHD----LSVVkhlaHRVAVMYRGMI 581
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLKER-GIGVLITDHNvretLGIC----DRAYIISEGKV 214
|
250
....*....|....
gi 1424538268 582 VEQGESDQVFTNPQ 595
Cdd:COG1137 215 LAEGTPEEILNNPL 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
381-616 |
1.03e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 92.47 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAG---SIEILGTDVAVLDAAARRRLRTELQVVFQDPvaslDP- 456
Cdd:PRK14271 38 DQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrySGDVLLGGRSIFNYRDVLEFRRRVGMLFQRP----NPf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 457 RLPVYDVIAEPLRANGF-HRHECEERVAELLAVVGLDHSDASRY---PAEFSGGQKQRIGIARALALQPKILALDEPVSA 532
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 533 LDVSIQAGIVNLLLDLQRRfgLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLAAVPRAHSD 612
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSGDVKD 271
|
....
gi 1424538268 613 VASG 616
Cdd:PRK14271 272 AKRG 275
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-274 |
1.06e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 93.23 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 20 EVPAVRGTSYHIDPGEVLAIVGESGCGKTTAalavI----GLL-PEyarvSGSIRLHG-------KELLglsdhamsqir 87
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTT----IkmltGILvPT----SGEVRVLGyvpfkrrKEFA----------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 88 gRMIGTVF-Q------DpmsaLTPVytigdqiaEAIEIHSR--EISRADARRRAVELLELVGIA----QPERrarafphE 154
Cdd:COG4586 95 -RRIGVVFgQrsqlwwD----LPAI--------DSFRLLKAiyRIPDAEYKKRLDELVELLDLGelldTPVR-------Q 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 155 LSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPV 234
Cdd:COG4586 155 LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1424538268 235 EIAAVDELyRDRRMPY---TVGLLGSVPRLDAAQGTRLIPIPG 274
Cdd:COG4586 235 YDGSLEEL-KERFGPYktiVLELAEPVPPLELPRGGEVIEREG 276
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
381-585 |
1.16e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.95 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVavldAAARRRLRTELQVVFQdpVASLDPRLPV 460
Cdd:PRK13537 24 DGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRARHARQRVGVVPQ--FDNLDPDFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGFHRHECEERVAELLAVVGLDhSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:PRK13537 98 RENLLVFGRYFGLSAAAARALVPPLLEFAKLE-NKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1424538268 541 IVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQG 585
Cdd:PRK13537 177 MWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
328-576 |
1.17e-20 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 95.82 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 328 SAADVFGV---STQPPPNNA-AGGQPPVVLRVSDLTKTYRLTkgvvvrrrvgeVRAVDGISFTLEQGRTLGIVGESGSGK 403
Cdd:TIGR02857 293 AAEALFAVldaAPRPLAGKApVTAAPASSLEFSGVSVAYPGR-----------RPALRPVSFTVPPGERVALVGPSGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 404 STTLNQILELTKPEAGSIEILGTDVAVLDAAARRRlrtELQVVFQDPVAsldprlpVYDVIAEPLRangFHRHEC-EERV 482
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD---QIAWVPQHPFL-------FAGTIAENIR---LARPDAsDAEI 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 483 AELLAVVGLD----------HSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRrf 552
Cdd:TIGR02857 429 REALERAGLDefvaalpqglDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-- 506
|
250 260
....*....|....*....|....
gi 1424538268 553 GLSYLFVSHDLSVVkHLAHRVAVM 576
Cdd:TIGR02857 507 GRTVLLVTHRLALA-ALADRIVVL 529
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
22-243 |
1.61e-20 |
|
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: 90.80 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 22 PAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeyaRVSGSIRLHGKELLGLSDHamsqIRGRM-IGTVFQDPms 100
Cdd:TIGR04406 15 KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVR---PDAGKILIDGQDITHLPMH----ERARLgIGYLPQEA-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 101 ALTPVYTIGDQIAEAIEIhSREISRADARRRAVELLELVGIAQpERRARAFphELSGGERQRVVIAIAIANDPDLLICDE 180
Cdd:TIGR04406 86 SIFRKLTVEENIMAVLEI-RKDLDRAEREERLEALLEEFQISH-LRDNKAM--SLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 181 PTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGR------PVEIAA---VDELY 243
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKE-RGIGVLITDHNVRETLDICDRAYIISDGKvlaegtPAEIVAnekVRRVY 232
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
382-592 |
2.57e-20 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 94.72 E-value: 2.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDaaaRRRLRTELQVVFQD----------PV 451
Cdd:TIGR01842 336 GISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWD---RETFGKHIGYLPQDvelfpgtvaeNI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 452 ASLDpRLPVYDVIAEPLRANGFHrheceervaELLAVV--GLDhSDASRYPAEFSGGQKQRIGIARALALQPKILALDEP 529
Cdd:TIGR01842 413 ARFG-ENADPEKIIEAAKLAGVH---------ELILRLpdGYD-TVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEP 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 530 VSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKhLAHRVAVMYRGMIVEQGESDQVFT 592
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLG-CVDKILVLQDGRIARFGERDEVLA 542
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
382-581 |
3.40e-20 |
|
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: 89.84 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDaaaRRRLRTELQVVFQDPVasLDPRlPVY 461
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE---HKYLHSKVSLVGQEPV--LFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 DVIAEPLRANGFhrheceERVAELlAVVGLDHSDASRYP-----------AEFSGGQKQRIGIARALALQPKILALDEPV 530
Cdd:cd03248 106 DNIAYGLQSCSF------ECVKEA-AQKAHAHSFISELAsgydtevgekgSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 531 SALDVSIQAGIVNLLLD-LQRRfglSYLFVSHDLSVVKHlAHRVAVMYRGMI 581
Cdd:cd03248 179 SALDAESEQQVQQALYDwPERR---TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-242 |
4.53e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.45 E-value: 4.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEdievPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHGKELlGLSDHA 82
Cdd:PRK13638 1 MLATSDLWFRYQDE----PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQ----KGAVLWQGKPL-DYSKRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 83 MSQIRgRMIGTVFQDPMSALtpVYT-IGDQIAeaIEIHSREISRADARRRAVELLELVGiaqperrARAFPHE----LSG 157
Cdd:PRK13638 72 LLALR-QQVATVFQDPEQQI--FYTdIDSDIA--FSLRNLGVPEAEITRRVDEALTLVD-------AQHFRHQpiqcLSH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 158 GERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRtaRDVT-GAAVLIITHDLGVVSEFAD------RALVMYA 230
Cdd:PRK13638 140 GQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIR--RIVAqGNHVIISSHDIDLIYEISDavyvlrQGQILTH 217
|
250
....*....|..
gi 1424538268 231 GRPVEIAAVDEL 242
Cdd:PRK13638 218 GAPGEVFACTEA 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
11-235 |
6.32e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 93.54 E-value: 6.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAAlaviGLLPEYARV-SGSIRLHGkelLGLSDHAMSQIRgR 89
Cdd:PRK11176 346 NVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIA----NLLTRFYDIdEGEILLDG---HDLRDYTLASLR-N 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 90 MIGTVFQDpmsaltpVYTIGDQIAEAI-----EIHSRE-ISRADARRRAVELLE--------LVGiaqpERRArafphEL 155
Cdd:PRK11176 418 QVALVSQN-------VHLFNDTIANNIayartEQYSREqIEEAARMAYAMDFINkmdngldtVIG----ENGV-----LL 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 156 SGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQI---LDVLRTARdvtgaAVLIITHDLGVVsEFADRALVMYAGR 232
Cdd:PRK11176 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIqaaLDELQKNR-----TSLVIAHRLSTI-EKADEILVVEDGE 555
|
...
gi 1424538268 233 PVE 235
Cdd:PRK11176 556 IVE 558
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
381-596 |
7.76e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 89.82 E-value: 7.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLdaaARRRL---RTELQVVFQDpvASLDPR 457
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAM---SRSRLytvRKRMSMLFQS--GALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 458 LPVYDVIAEPLRAngfHRHECEE----RVAELLAVVGLdHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSAL 533
Cdd:PRK11831 99 MNVFDNVAYPLRE---HTQLPAPllhsTVMMKLEAVGL-RGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 534 DVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQH 596
Cdd:PRK11831 175 DPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDP 237
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
381-592 |
9.99e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.92 E-value: 9.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAaarRRLRTELQVVFQDPVASLDprLPV 460
Cdd:PRK11231 19 NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS---RQLARRLALLPQHHLTPEG--ITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIA---EP-LRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVS 536
Cdd:PRK11231 94 RELVAygrSPwLSLWGRLSAEDNARVNQAMEQTRINHL-ADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDIN 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 537 IQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFT 592
Cdd:PRK11231 173 HQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
34-234 |
1.39e-19 |
|
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: 87.55 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 34 GEVLAIVGESGCGKTTAALAVIG-LLPEyarvSGSIRLHGKellglsDHAMSQIRGRMIGTVFQDpmSALTPVYTIGDQI 112
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGfETPQ----SGRVLINGV------DVTAAPPADRPVSMLFQE--NNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 113 AEAIEIHSReiSRADARRRAVELLELVGIAQPERRaraFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQ 192
Cdd:cd03298 92 GLGLSPGLK--LTAEDRQAIEVALARVGLAGLEKR---LPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1424538268 193 ILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPV 234
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
381-585 |
1.55e-19 |
|
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: 92.58 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAArrrLRTELQVVFQDPVAsldprlpV 460
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS---LRAAIGIVPQDTVL-------F 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRangFHRHECEErvAELLAVVGLDHSDA--SRYPAEF-----------SGGQKQRIGIARALALQPKILALD 527
Cdd:COG5265 445 NDTIAYNIA---YGRPDASE--EEVEAAARAAQIHDfiESLPDGYdtrvgerglklSGGEKQRVAIARTLLKNPPILIFD 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 528 EPVSALDVSIQAGIVNLLLDLQRrfGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQG 585
Cdd:COG5265 520 EATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-247 |
2.34e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.12 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETedieVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlpeYARVSGSIRLHGKELLGLSD 80
Cdd:PRK11300 2 SQPLLSVSGLMMRFGG----LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGF---YKPTGGTILLRGQHIEGLPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 HAMSqirgRMiGTV--FQD-----PMSAL---------------------TPVYtigdqiaeaieihsREiSRADARRRA 132
Cdd:PRK11300 75 HQIA----RM-GVVrtFQHvrlfrEMTVIenllvaqhqqlktglfsgllkTPAF--------------RR-AESEALDRA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 133 VELLELVGIAQPERRARAfphELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIIT 212
Cdd:PRK11300 135 ATWLERVGLLEHANRQAG---NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIE 211
|
250 260 270
....*....|....*....|....*....|....*
gi 1424538268 213 HDLGVVSEFADRALVMYAGRPVEIAAVDELYRDRR 247
Cdd:PRK11300 212 HDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
381-592 |
2.94e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 87.45 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQIL-ELTKPEAGSIEILG-----TDVavldaaarRRLRTELQVVFQDPVASL 454
Cdd:COG1119 20 DDISWTVKPGEHWAILGPNGAGKSTLLSLITgDLPPTYGNDVRLFGerrggEDV--------WELRKRIGLVSPALQLRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 455 DPRLPVYDVIAEPLRAN-GFHRH---ECEERVAELLAVVGLDHsDASRYPAEFSGGQKQRIGIARALALQPKILALDEPV 530
Cdd:COG1119 92 PRDETVLDVVLSGFFDSiGLYREptdEQRERARELLELLGLAH-LADRPFGTLSQGEQRRVLIARALVKDPELLILDEPT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 531 SALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFT 592
Cdd:COG1119 171 AGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLT 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-234 |
3.22e-19 |
|
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: 86.07 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 3 AVLEVTDLNVTFETEDIEV--PAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLpEYARVSGSIRLHGKELlglsd 80
Cdd:cd03213 2 VTLSFRNLTVTVKSSPSKSgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRR-TGLGVSGEVLINGRPL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 hAMSQIRgRMIGTVFQDPM--SALTpvytigdqIAEAIEIHSreisradarrravellELVGIaqperrarafphelSGG 158
Cdd:cd03213 76 -DKRSFR-KIIGYVPQDDIlhPTLT--------VRETLMFAA----------------KLRGL--------------SGG 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 159 ERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDL-GVVSEFADRALVMYAGRPV 234
Cdd:cd03213 116 ERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-266 |
4.43e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.84 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 36 VLAIVGESGCGKTTAALAVIGLLPEYA--RVSGSIRLHGKELLGLSDhaMSQIRgRMIGTVFQDPmsalTPV-YTIGDQI 112
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSgyRYSGDVLLGGRSIFNYRD--VLEFR-RRVGMLFQRP----NPFpMSIMDNV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 113 AEAIEIHsREISRADARRRAVELLELVGIAQPER-RARAFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQA 191
Cdd:PRK14271 122 LAGVRAH-KLVPRKEFRGVAQARLTEVGLWDAVKdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTE 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 192 QILDVLRTARDVTgaAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDRRMP----YTVGLLGSVPrlDAAQG 266
Cdd:PRK14271 201 KIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAetarYVAGLSGDVK--DAKRG 275
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-232 |
4.90e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.82 E-value: 4.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 28 SYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarvSGSIRLHGKELLGLSDHAMSQIRGrMIGTvfQDPMSALTPVYt 107
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG----QGEILLNGRPLSDWSAAELARHRA-YLSQ--QQSPPFAMPVF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 108 igdqiaEAIEIHSREISRADARRRAV-ELLELVGIAqpERRARAFpHELSGGERQRVVIAIAI-----ANDPD--LLICD 179
Cdd:COG4138 88 ------QYLALHQPAGASSEAVEQLLaQLAEALGLE--DKLSRPL-TQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 180 EPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:COG4138 159 EPMNSLDVAQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-248 |
5.03e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 87.76 E-value: 5.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 20 EVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLpeyarvsgsIRLHGKELLGlsDHA----MSQIRG-----RM 90
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI---------ISETGQTIVG--DYAipanLKKIKEvkrlrKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 91 IGTVFQDPMSALTPvYTIGDQIAEAiEIHSREiSRADARRRAVELLELVGIaqPERRARAFPHELSGGERQRVVIAIAIA 170
Cdd:PRK13645 92 IGLVFQFPEYQLFQ-ETIEKDIAFG-PVNLGE-NKQEAYKKVPELLKLVQL--PEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 171 NDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDRRM 248
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQEL 244
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
30-278 |
5.11e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.04 E-value: 5.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 30 HIDPGEVLAIVGESGCGKTTaalaVIGLLPEYARVSGSIRLHGKELLglsDHAMSQIRgrmigTVFQDpmSALTPVYTIG 109
Cdd:PRK11247 34 HIPAGQFVAVVGRSGCGKST----LLRLLAGLETPSAGELLAGTAPL---AEAREDTR-----LMFQD--ARLLPWKKVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 110 DQIAEAIeihsreisRADARRRAVELLELVGIAQperRARAFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTV 189
Cdd:PRK11247 100 DNVGLGL--------KGQWRDAALQALAAVGLAD---RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 190 QAQILDVLRTARDVTGAAVLIITHDlgvVSE---FADRALVMYAGRPVEIAAVDeLYRDRRmpytvglLGSV--PRLDAA 264
Cdd:PRK11247 169 RIEMQDLIESLWQQHGFTVLLVTHD---VSEavaMADRVLLIEEGKIGLDLTVD-LPRPRR-------RGSArlAELEAE 237
|
250
....*....|....
gi 1424538268 265 QGTRLIPIPGAPPT 278
Cdd:PRK11247 238 VLQRVMSRGESEPT 251
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-234 |
5.46e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.49 E-value: 5.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 20 EVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlpeYARVSGSIRLHGKELLGLSDHA-MSQIRgRMIGTVFQDP 98
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGL---HVPTQGSVRVDDTLITSTSKNKdIKQIR-KKVGLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 99 MSALTPVYTIGDQiaeAIEIHSREISRADARRRAVELLELVGIAQpERRARAfPHELSGGERQRVVIAIAIANDPDLLIC 178
Cdd:PRK13649 95 ESQLFEETVLKDV---AFGPQNFGVSQEEAEALAREKLALVGISE-SLFEKN-PFELSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 179 DEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPV 234
Cdd:PRK13649 170 DEPTAGLDPKGRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
352-601 |
6.42e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.99 E-value: 6.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 352 VLRVSDLTKTYRLTKGVvvrrrvgevravDGISFTLEQGRTLGIVGESGSGKSTTLNQILELT---KPEAGSIEILGTDV 428
Cdd:PRK09984 4 IIRVEKLAKTFNQHQAL------------HAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 429 AVLDAAAR--RRLRTELQVVFQDpvASLDPRLPVYD-VIAEPLRANGFHR-------HECEERVAELLAVVGLDHSDASR 498
Cdd:PRK09984 72 QREGRLARdiRKSRANTGYIFQQ--FNLVNRLSVLEnVLIGALGSTPFWRtcfswftREQKQRALQALTRVGMVHFAHQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 499 YpAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYR 578
Cdd:PRK09984 150 V-STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQ 228
|
250 260
....*....|....*....|...
gi 1424538268 579 GMIVEQGESdQVFTNPQHEYTRR 601
Cdd:PRK09984 229 GHVFYDGSS-QQFDNERFDHLYR 250
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
383-605 |
7.00e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 90.29 E-value: 7.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTkPEAGSIEILGTDVAVLDAAARRRlrtELQVVFQDPvasldpRLPvyd 462
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRK---HLSWVGQNP------QLP--- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 463 viAEPLRAN---GFHrHECEERVAELLA-----------VVGLDH--SDASrypAEFSGGQKQRIGIARALALQPKILAL 526
Cdd:PRK11174 436 --HGTLRDNvllGNP-DASDEQLQQALEnawvseflpllPQGLDTpiGDQA---AGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 527 DEPVSALDVSIQAGIVNLLLDLQRrfGLSYLFVSHDLSVVKHLaHRVAVMYRGMIVEQGESDQVFTnpQHEYTRRLLAA 605
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQ--AGGLFATLLAH 583
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
31-245 |
7.12e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.48 E-value: 7.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 31 IDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELLGLSDHAMSQIRGRMIGTVFQDPMSALTPVYTIGD 110
Cdd:PRK13643 29 VKKGSYTALIGHTGSGKSTLLQHLNGLLQP---TEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEETVLKD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 111 QiaeAIEIHSREISRADARRRAVELLELVGIAQpERRARAfPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQ 190
Cdd:PRK13643 106 V---AFGPQNFGIPKEKAEKIAAEKLEMVGLAD-EFWEKS-PFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 191 AQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRD 245
Cdd:PRK13643 181 IEMMQLFESIHQ-SGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-242 |
9.12e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 89.90 E-value: 9.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 12 VTFETEDIEVPAVRGT------SYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeYarvSGSIRLHGKELlglSDHAMSQ 85
Cdd:PRK11174 348 VTIEAEDLEILSPDGKtlagplNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-Y---QGSLKINGIEL---RELDPES 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 86 IRgRMIGTVFQDPmsaLTPVYTIGDQIAEA-IEIHSREISRADARRRAVELLELV--GIAQP--ERRARafpheLSGGER 160
Cdd:PRK11174 421 WR-KHLSWVGQNP---QLPHGTLRDNVLLGnPDASDEQLQQALENAWVSEFLPLLpqGLDTPigDQAAG-----LSVGQA 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 161 QRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARdvTGAAVLIITHDLGVVSEFaDRALVMYAGRPVEIAAVD 240
Cdd:PRK11174 492 QRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS--RRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYA 568
|
..
gi 1424538268 241 EL 242
Cdd:PRK11174 569 EL 570
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
383-598 |
1.14e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 88.16 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARrrlrtELQVVFQDpvASLDPRLPVYD 462
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER-----GVGMVFQS--YALYPHLSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 463 VIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIV 542
Cdd:PRK11000 95 NMSFGLKLAGAKKEEINQRVNQVAEVLQLAHL-LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 543 NLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQHEY 598
Cdd:PRK11000 174 IEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRF 229
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-575 |
1.31e-18 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 89.46 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 33 PGEVLAIVGESGCGKTTAalavIGLLpeyarvSGSIrlhgKELLGLSDHAMS--QIRGRMIGTVFQDPMSAL-----TPV 105
Cdd:COG1245 98 KGKVTGILGPNGIGKSTA----LKIL------SGEL----KPNLGDYDEEPSwdEVLKRFRGTELQDYFKKLangeiKVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 106 YTIG--DQIAEAIEIHSREI-SRADARRRAVELLELVGIAQP-ERRARafphELSGGERQRVVIAIAIANDPDLLICDEP 181
Cdd:COG1245 164 HKPQyvDLIPKVFKGTVRELlEKVDERGKLDELAEKLGLENIlDRDIS----ELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 182 TTALDVTvqaQILDVLRTARDVT--GAAVLIITHDLGVVSEFADRALVMYaGRPveiaavdelyrdrrmpytvGLLGSVP 259
Cdd:COG1245 240 SSYLDIY---QRLNVARLIRELAeeGKYVLVVEHDLAILDYLADYVHILY-GEP-------------------GVYGVVS 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 260 RldaAQGTRlipipgapptmtslspgactfaprcpLAIDECLsaepdlvrvaDGHwaacIRTDDVAGRSAADVFGVSTQP 339
Cdd:COG1245 297 K---PKSVR--------------------------VGINQYL----------DGY----LPEENVRIRDEPIEFEVHAPR 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 340 PPNNAaggqpPVVLRVSDLTKTYRltkgvvvrrrvgevravdgiSFTLE-------QGRTLGIVGESGSGKsTTLNQIL- 411
Cdd:COG1245 334 REKEE-----ETLVEYPDLTKSYG--------------------GFSLEveggeirEGEVLGIVGPNGIGK-TTFAKILa 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 412 -ELtKPEAGSIEilgTDVAV------LDAAARRRLRTELQVVFQDPVASldprLPVYDVIAEPLRANGFHrhecEERVAE 484
Cdd:COG1245 388 gVL-KPDEGEVD---EDLKIsykpqyISPDYDGTVEEFLRSANTDDFGS----SYYKTEIIKPLGLEKLL----DKNVKD 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 485 LlavvgldhsdasrypaefSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLS 564
Cdd:COG1245 456 L------------------SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIY 517
|
570
....*....|.
gi 1424538268 565 VVKHLAHRVAV 575
Cdd:COG1245 518 LIDYISDRLMV 528
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-231 |
1.41e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.09 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETEDIevpAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlpeyarvsgsIRLHGKELLGLSD 80
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHT---ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGF----------VRLASGKISILGQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 HAMSQIRGRMIGTVFQDPMSALTPVYTIGDQIAEAIEIHSREISRADARRRAVELLELVGIAQPERRARAFpHELSGGER 160
Cdd:PRK15056 70 PTRQALQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQI-GELSGGQK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 161 QRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRAlVMYAG 231
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRD-EGKTMLVSTHNLGSVTEFCDYT-VMVKG 217
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-245 |
2.53e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 84.83 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETEDievpAVRGTSYHIDPGEVLAIVGESGCGKTT--AALAVIG-LLPEYArVSGSIRLHGKELLG 77
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTllRSINRMNdLNPEVT-ITGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 78 LSDHAMsQIRgRMIGTVFQDPmsalTPV-YTIGDQIAEAIEIHS-REISRADArrrAVELlELVGIA---QPERRARAFP 152
Cdd:PRK14239 77 PRTDTV-DLR-KEIGMVFQQP----NPFpMSIYENVVYGLRLKGiKDKQVLDE---AVEK-SLKGASiwdEVKDRLHDSA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 153 HELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvtGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:PRK14239 147 LGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFFLDGD 224
|
250
....*....|...
gi 1424538268 233 PVEIAAVDELYRD 245
Cdd:PRK14239 225 LIEYNDTKQMFMN 237
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-242 |
3.32e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.57 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 26 GTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYARVSGSIRLHGKELlglsdhAMSQIRgRMIGTVFQDPMsaLTPV 105
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPI------DAKEMR-AISAYVQQDDL--FIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 106 YTIGDQIAEAIEIHSREISRADARRRAV-ELLELVG--------IAQPERRarafpHELSGGERQRVVIAIAIANDPDLL 176
Cdd:TIGR00955 114 LTVREHLMFQAHLRMPRRVTKKEKRERVdEVLQALGlrkcantrIGVPGRV-----KGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 177 ICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDEL 242
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
381-585 |
3.69e-18 |
|
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: 83.23 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAaarRRLRTELQVVFQDPV---ASLDPR 457
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPL---EDLRSSLTIIPQDPTlfsGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 458 LPVYDviaeplrangfhrHECEERVAELLAVvgldhsdaSRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSI 537
Cdd:cd03369 102 LDPFD-------------EYSDEEIYGALRV--------SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1424538268 538 QAGIVNLLLDLQRrfGLSYLFVSHDLSVVKHLAhRVAVMYRGMIVEQG 585
Cdd:cd03369 161 DALIQKTIREEFT--NSTILTIAHRLRTIIDYD-KILVMDAGEVKEYD 205
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
5-235 |
3.91e-18 |
|
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: 87.95 E-value: 3.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFE----TEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAA-LavigLLPEYARVSGSIRLHGKELLGLS 79
Cdd:COG5265 351 LVVGGGEVRFEnvsfGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLArL----LFRFYDVTSGRILIDGQDIRDVT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 80 DHAmsqIRgRMIGTVFQDPmsaltpVY---TIGDQIAEAieihsreisRADARRRAVEllELVGIAQPERRARAFPH--- 153
Cdd:COG5265 427 QAS---LR-AAIGIVPQDT------VLfndTIAYNIAYG---------RPDASEEEVE--AAARAAQIHDFIESLPDgyd 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 154 --------ELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRT-ARDVTgaaVLIITHDLGVVSEfADR 224
Cdd:COG5265 486 trvgerglKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREvARGRT---TLVIAHRLSTIVD-ADE 561
|
250
....*....|.
gi 1424538268 225 ALVMYAGRPVE 235
Cdd:COG5265 562 ILVLEAGRIVE 572
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-261 |
4.18e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.85 E-value: 4.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEdieVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKEllgLSDHAM 83
Cdd:PRK13652 3 LIETRDLCYSYSGS---KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKP---TSGSVLIRGEP---ITKENI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 SQIRgRMIGTVFQDPmsaltpvytiGDQIAE-------AIEIHSREISRADARRRAVELLELVGIAQPERRArafPHELS 156
Cdd:PRK13652 74 REVR-KFVGLVFQNP----------DDQIFSptveqdiAFGPINLGLDEETVAHRVSSALHMLGLEELRDRV---PHHLS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 157 GGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEI 236
Cdd:PRK13652 140 GGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
250 260
....*....|....*....|....*.
gi 1424538268 237 AAVDELYRDRRMPYTVGL-LGSVPRL 261
Cdd:PRK13652 220 GTVEEIFLQPDLLARVHLdLPSLPKL 245
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-579 |
4.44e-18 |
|
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: 87.57 E-value: 4.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 21 VPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeYARVSGSIRLHGKELLGLSdhaMSQIRGRMIGTVFQDPMs 100
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYP-HGTWDGEIYWSGSPLKASN---IRDTERAGIVIIHQELT- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 101 aLTPVYTIGDQIAEAIEI-HSREISRADAR-RRAVELLELVGI-AQPERRARAfphELSGGERQRVVIAIAIANDPDLLI 177
Cdd:TIGR02633 89 -LVPELSVAENIFLGNEItLPGGRMAYNAMyLRAKNLLRELQLdADNVTRPVG---DYGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 178 CDEPTTALDVTVQAQILDVLRTARdVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDRRMPYTVGllgs 257
Cdd:TIGR02633 165 LDEPSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG---- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 258 vprldaaqgtrlipipgapPTMTSLSpgactfaPRCPLAI-DECLSAEpdlvrvadghwaacirtddvagrsaadvfGVS 336
Cdd:TIGR02633 240 -------------------REITSLY-------PHEPHEIgDVILEAR-----------------------------NLT 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 337 TQPPPNnaaggqpPVVLRVSDltktyrltkgvvvrrrvgevravdgISFTLEQGRTLGIVGESGSGKsTTLNQILELTKP 416
Cdd:TIGR02633 265 CWDVIN-------PHRKRVDD-------------------------VSFSLRRGEILGVAGLVGAGR-TELVQALFGAYP 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 417 --EAGSIEILGTDVAVLDAAarRRLRTELQVVFQD-------PVASL--DPRLPVYDVIAEPLRANGFHRHECEERVAEL 485
Cdd:TIGR02633 312 gkFEGNVFINGKPVDIRNPA--QAIRAGIAMVPEDrkrhgivPILGVgkNITLSVLKSFCFKMRIDAAAELQIIGSAIQR 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 486 LAVvgldHSDASRYP-AEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLS 564
Cdd:TIGR02633 390 LKV----KTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELA 464
|
570
....*....|....*
gi 1424538268 565 VVKHLAHRVAVMYRG 579
Cdd:TIGR02633 465 EVLGLSDRVLVIGEG 479
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
11-242 |
8.16e-18 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 87.25 E-value: 8.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDiEVPAVRGTSYHIDPGEVLAIVGESGCGKTTaalaVIGLLPE-YARVSGSIRLHGKELLGLSDHAMSqirgR 89
Cdd:TIGR01192 339 HITFEFAN-SSQGVFDVSFEAKAGQTVAIVGPTGAGKTT----LINLLQRvYDPTVGQILIDGIDINTVTRESLR----K 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 90 MIGTVFQDpmsALTPVYTIGDQIAEAIEIHS-REISRADARRRAVELLE--------LVGiaqpERRARafpheLSGGER 160
Cdd:TIGR01192 410 SIATVFQD---AGLFNRSIRENIRLGREGATdEEVYEAAKAAAAHDFILkrsngydtLVG----ERGNR-----LSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 161 QRVVIAIAIANDPDLLICDEPTTALDVTVQAQI---LDVLRTARdvtgaAVLIITHDLGVVSEfADRALVMYAGRPVEIA 237
Cdd:TIGR01192 478 QRLAIARAILKNAPILVLDEATSALDVETEARVknaIDALRKNR-----TTFIIAHRLSTVRN-ADLVLFLDQGRLIEKG 551
|
....*
gi 1424538268 238 AVDEL 242
Cdd:TIGR01192 552 SFQEL 556
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
383-595 |
1.01e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.02 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRlrteLQVVFQDPVASLDPRLPVYD 462
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR----RGIGYLPQEASIFRRLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 463 VIAEPLRA-NGFHRHECEERVAELLAVVGLDHSDASRYPAeFSGGQKQRIGIARALALQPKILALDEPVSALDvSIQAGI 541
Cdd:PRK10895 98 NLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQS-LSGGERRRVEIARALAANPKFILLDEPFAGVD-PISVID 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 542 VNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQ 595
Cdd:PRK10895 176 IKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
382-591 |
1.02e-17 |
|
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: 86.73 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRL------RTELqvvFQDPVA--- 452
Cdd:COG4618 350 GVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHigylpqDVEL---FDGTIAeni 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 453 ----SLDPRlpvyDVIAEPLRAnGFHrheceervaELLA--------VVGldhSDASRypaeFSGGQKQRIGIARALALQ 520
Cdd:COG4618 427 arfgDADPE----KVVAAAKLA-GVH---------EMILrlpdgydtRIG---EGGAR----LSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 521 PKILALDEPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQGESDQVF 591
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVL 554
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
383-585 |
1.04e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 86.61 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDvavLDAAARRRLRTELQVV------FQDPVAsldp 456
Cdd:PRK11176 362 INFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTLASLRNQVALVsqnvhlFNDTIA---- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 457 rlpvyDVIAEPlRANGFHRHECEE--RVAELLAVV-----GLDhSDASRYPAEFSGGQKQRIGIARALALQPKILALDEP 529
Cdd:PRK11176 435 -----NNIAYA-RTEQYSREQIEEaaRMAYAMDFInkmdnGLD-TVIGENGVLLSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 530 VSALDVSIQAGIVNLLLDLQRrfGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQG 585
Cdd:PRK11176 508 TSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-242 |
1.30e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.42 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTaalaVIGLLP-EYARVSGSIRLHGKELlglSDHAMSQIRgR 89
Cdd:PRK11160 343 NVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKST----LLQLLTrAWDPQQGEILLNGQPI---ADYSEAALR-Q 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 90 MIGTVFQDpmsaltpVYTIGDQIAEAIEIHSREISraDARRRAVelLELVGIA---QPERRARAFPHE----LSGGERQR 162
Cdd:PRK11160 415 AISVVSQR-------VHLFSATLRDNLLLAAPNAS--DEALIEV--LQQVGLEkllEDDKGLNAWLGEggrqLSGGEQRR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 163 VVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRT-ARDVTgaaVLIITHDLGVVSEFaDRALVMYAGRPVEIAAVDE 241
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEhAQNKT---VLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQE 559
|
.
gi 1424538268 242 L 242
Cdd:PRK11160 560 L 560
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-241 |
1.51e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.44 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTF------------------ETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIG--LLPE 60
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTL-LKLIAgiLEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 61 yarvSGSIRLHGK--ELLGLsdhamsqirgrmiGTVFQDPMSALTPVYTIGdqiaeaiEIHSreISRADARRRAVELLEL 138
Cdd:COG1134 80 ----SGRVEVNGRvsALLEL-------------GAGFHPELTGRENIYLNG-------RLLG--LSRKEIDEKFDEIVEF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 139 VGIA----QPERRarafpheLSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHD 214
Cdd:COG1134 134 AELGdfidQPVKT-------YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRE-SGRTVIFVSHS 205
|
250 260
....*....|....*....|....*..
gi 1424538268 215 LGVVSEFADRALVMYAGRPVEIAAVDE 241
Cdd:COG1134 206 MGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-223 |
1.60e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 82.91 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 7 VTDLNVTFETEDIEV-----PAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGL--LPEYARVSGSIRLHGKELLGlS 79
Cdd:PRK14243 4 LNGTETVLRTENLNVyygsfLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFRVEGKVTFHGKNLYA-P 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 80 DHAMSQIRgRMIGTVFQDPMSALTPVYtigDQIAEAIEIHSREISRADARRRAVELLELVGIAQPERRARAFphELSGGE 159
Cdd:PRK14243 83 DVDPVEVR-RRIGMVFQKPNPFPKSIY---DNIAYGARINGYKGDMDELVERSLRQAALWDEVKDKLKQSGL--SLSGGQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 160 RQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRT-ARDVTgaaVLIITHDLGVVSEFAD 223
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHElKEQYT---IIIVTHNMQQAARVSD 218
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
31-261 |
1.67e-17 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 81.82 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 31 IDPGEVLAIVGESGCGKTTAALAVIGLLPeyaRVSGSIRLHGKEllglsdhamSQIRGRMIGTVFQD-------PMSALT 103
Cdd:TIGR03771 3 ADKGELLGLLGPNGAGKTTLLRAILGLIP---PAKGTVKVAGAS---------PGKGWRHIGYVPQRhefawdfPISVAH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 104 PVYTigdqiAEAIEIHSREISRADARRRAVELLELVGIAQPERRARAfphELSGGERQRVVIAIAIANDPDLLICDEPTT 183
Cdd:TIGR03771 71 TVMS-----GRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVG---ELSGGQRQRVLVARALATRPSVLLLDEPFT 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 184 ALDVTVQAQILDVLrTARDVTGAAVLIITHDLGVVSEFADRaLVMYAGRPVEIAAVDELYRDRRMPYTVGLLGSVPRL 261
Cdd:TIGR03771 143 GLDMPTQELLTELF-IELAGAGTAILMTTHDLAQAMATCDR-VVLLNGRVIADGTPQQLQDPAPWMTTFGVSDSSPLL 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-232 |
1.81e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 82.29 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 27 TSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarvSGSIRLHGKELLGLSDHAMSQIRGRMIGtvfQDPMSALTPVY 106
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG----SGSIQFAGQPLEAWSAAELARHRAYLSQ---QQTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 107 tigdqiaEAIEIHSREISRADARRRAV-ELLELVGIAQPERRArafPHELSGGERQRVVIAIAI-----ANDPD--LLIC 178
Cdd:PRK03695 88 -------QYLTLHQPDKTRTEAVASALnEVAEALGLDDKLGRS---VNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 179 DEPTTALDVTVQAqILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:PRK03695 158 DEPMNSLDVAQQA-ALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-232 |
1.85e-17 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 80.43 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTT-AALAVIGLLPEyarvSGSIRLHGkellglsdhamsqirgr 89
Cdd:cd03247 5 NVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTlLQLLTGDLKPQ----QGEITLDG----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 90 migtvfqdpmsalTPVYTIGDQIAEAIEIHSREISRADArrravELLELVGIaqperrarafphELSGGERQRVVIAIAI 169
Cdd:cd03247 64 -------------VPVSDLEKALSSLISVLNQRPYLFDT-----TLRNNLGR------------RFSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 170 ANDPDLLICDEPTTALDVTVQAQILD-VLRTARDVTgaaVLIITHDLGVVsEFADRALVMYAGR 232
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSlIFEVLKDKT---LIWITHHLTGI-EHMDKILFLENGK 173
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
381-585 |
2.87e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 83.21 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDvavlDAAARRRLRTELQVVF----QdpvasLDP 456
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV----PFKRRKEFARRIGVVFgqrsQ-----LWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 457 RLPVYDviaeplranGF--HRH-------ECEERVAELLAVVGLDhsdasrypaEF--------SGGQKQRIGIARALAL 519
Cdd:COG4586 110 DLPAID---------SFrlLKAiyripdaEYKKRLDELVELLDLG---------ELldtpvrqlSLGQRMRCELAAALLH 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 520 QPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQG 585
Cdd:COG4586 172 RPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDG 237
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-575 |
2.92e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 85.25 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 33 PGEVLAIVGESGCGKTTAalavIGLLpeyarvSGSIRLHgkelLGLSDHAMS--QIRGRMIGTVFQDPMSAL-----TPV 105
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTA----VKIL------SGELIPN----LGDYEEEPSwdEVLKRFRGTELQNYFKKLyngeiKVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 106 YTIG--DQIAEAIEIHSREI-SRADARRRAVELLELVGIAQP-ERRARafphELSGGERQRVVIAIAIANDPDLLICDEP 181
Cdd:PRK13409 164 HKPQyvDLIPKVFKGKVRELlKKVDERGKLDEVVERLGLENIlDRDIS----ELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 182 TTALDVTvqaQILDVLRTARDVT-GAAVLIITHDLGVVSEFADRALVMYaGRPveiaavdelyrdrrmpytvGLLGSV-- 258
Cdd:PRK13409 240 TSYLDIR---QRLNVARLIRELAeGKYVLVVEHDLAVLDYLADNVHIAY-GEP-------------------GAYGVVsk 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 259 PRldaaqGTRlipipgapptmtslspgactfaprcpLAIDECLsaepdlvrvaDGHwaacIRTDDVAGRSAADVFgvSTQ 338
Cdd:PRK13409 297 PK-----GVR--------------------------VGINEYL----------KGY----LPEENMRIRPEPIEF--EER 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 339 PPPNNAAGgqpPVVLRVSDLTKTYRltkgvvvrrrvgevravdgiSFTLE-------QGRTLGIVGESGSGKsTTLNQIL 411
Cdd:PRK13409 330 PPRDESER---ETLVEYPDLTKKLG--------------------DFSLEveggeiyEGEVIGIVGPNGIGK-TTFAKLL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 412 --ELtKPEAGSIEilgtdvavldaaarrrlrTELQVVFQDPVASLDPRLPVYDV---IAEPLRANgFHRHECEER--VAE 484
Cdd:PRK13409 386 agVL-KPDEGEVD------------------PELKISYKPQYIKPDYDGTVEDLlrsITDDLGSS-YYKSEIIKPlqLER 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 485 LLavvgldhsdaSRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLS 564
Cdd:PRK13409 446 LL----------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIY 515
|
570
....*....|.
gi 1424538268 565 VVKHLAHRVAV 575
Cdd:PRK13409 516 MIDYISDRLMV 526
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
383-590 |
3.78e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.76 E-value: 3.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAArrrlrtelqvvFQDPVASLDPRLP--- 459
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA-----------FARKVAYLPQQLPaae 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 460 ---VYDVIA---EPLR-ANGFHRHECEERVAELLAVVGLDhSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSA 532
Cdd:PRK10575 99 gmtVRELVAigrYPWHgALGRFGAADREKVEEAISLVGLK-PLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 533 LDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQV 590
Cdd:PRK10575 178 LDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-242 |
4.04e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 81.28 E-value: 4.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 6 EVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIG-LLPeyaRVSGSIRLHGKELlglsDHAMS 84
Cdd:COG4604 3 EIKNVSKRYGGKVV----LDDVSLTIPKGGITALIGPNGAGKSTL-LSMISrLLP---PDSGEVLVDGLDV----ATTPS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 QIRGRMIGTVFQDPmsALTPVYTIGDQIAEAIEIHSR-EISRADAR--RRAVELLELVGIAQperrarAFPHELSGGERQ 161
Cdd:COG4604 71 RELAKRLAILRQEN--HINSRLTVRELVAFGRFPYSKgRLTAEDREiiDEAIAYLDLEDLAD------RYLDELSGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 162 RVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDE 241
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEE 222
|
.
gi 1424538268 242 L 242
Cdd:COG4604 223 I 223
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
382-600 |
4.25e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 81.75 E-value: 4.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTL------NQILELTKPEaGSIEILGTDVAVLD---AAARRRLrtelQVVFQDPva 452
Cdd:PRK14243 28 NVWLDIPKNQITAFIGPSGCGKSTILrcfnrlNDLIPGFRVE-GKVTFHGKNLYAPDvdpVEVRRRI----GMVFQKP-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 453 slDPrLP--VYDVIAEPLRANGFhRHECEERVAELL--AVVGLDHSDASRYPA-EFSGGQKQRIGIARALALQPKILALD 527
Cdd:PRK14243 101 --NP-FPksIYDNIAYGARINGY-KGDMDELVERSLrqAALWDEVKDKLKQSGlSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 528 EPVSALDVSIQAGIVNLLLDLQRRFglSYLFVSHDLsvvkHLAHRVAVMY-------------RGMIVEQGESDQVFTNP 594
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQY--TIIIVTHNM----QQAARVSDMTaffnveltegggrYGYLVEFDRTEKIFNSP 250
|
....*.
gi 1424538268 595 QHEYTR 600
Cdd:PRK14243 251 QQQATR 256
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
383-595 |
4.33e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.13 E-value: 4.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTkPEAGSIEILGTDVAVLDAA--ARRRLRTELQvvfQDPVASLdprlPV 460
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAelARHRAYLSQQ---QTPPFAM----PV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGfHRHECEERVAELLAVVGLDhSDASRYPAEFSGGQKQRIGIA-------RALALQPKILALDEPVSAL 533
Cdd:PRK03695 87 FQYLTLHQPDKT-RTEAVASALNEVAEALGLD-DKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 534 DVSiQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNPQ 595
Cdd:PRK03695 165 DVA-QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
11-232 |
4.45e-17 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 84.71 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELlglsDHAMSQIRGRM 90
Cdd:TIGR01842 321 NVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPP---TSGSVRLDGADL----KQWDRETFGKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 91 IGTVFQDpmsaltpVYTIGDQIAEaieihsrEISRADARRRAVELLELVGIAQPERRARAFPH-----------ELSGGE 159
Cdd:TIGR01842 394 IGYLPQD-------VELFPGTVAE-------NIARFGENADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQ 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 160 RQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARdVTGAAVLIITHDLGVVsEFADRALVMYAGR 232
Cdd:TIGR01842 460 RQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALK-ARGITVVVITHRPSLL-GCVDKILVLQDGR 530
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
11-235 |
5.32e-17 |
|
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: 80.23 E-value: 5.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeyaRVSGSIRLHGKEL--LGLSDhamsqIRG 88
Cdd:cd03244 7 NVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE---LSSGSILIDGVDIskIGLHD-----LRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 89 RmIGTVFQDPM-------SALTP--VYTiGDQIAEAIE-IHSREISRADArrravELLELVGIAQPErrarafphELSGG 158
Cdd:cd03244 79 R-ISIIPQDPVlfsgtirSNLDPfgEYS-DEELWQALErVGLKEFVESLP-----GGLDTVVEEGGE--------NLSVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 159 ERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTA-RDVTgaaVLIITHDLGVVSEFaDRALVMYAGRPVE 235
Cdd:cd03244 144 QRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAfKDCT---VLTIAHRLDTIIDS-DRILVLDKGRVVE 217
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
384-592 |
6.10e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.47 E-value: 6.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 384 SFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVavldaaaRRRLRTELqVVFQDPVASLDPRLPVY-- 461
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-------RQALQKNL-VAYVPQSEEVDWSFPVLve 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 DVIAEP-------LRANGFHRHECeerVAELLAVVG-LDHSdaSRYPAEFSGGQKQRIGIARALALQPKILALDEPVSAL 533
Cdd:PRK15056 99 DVVMMGryghmgwLRRAKKRDRQI---VTAALARVDmVEFR--HRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 534 DVSIQAGIVNLLLDLqRRFGLSYLFVSHDLSVVKHLAHrVAVMYRGMIVEQGESDQVFT 592
Cdd:PRK15056 174 DVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFT 230
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-248 |
6.76e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 84.39 E-value: 6.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETEDiEVPAVRGTSYHIDPGEVLAIVGESGCGKTT-AALavigLLPEYARVSGSIRLHGKELLGLS 79
Cdd:TIGR00958 475 LEGLIEFQDVSFSYPNRP-DVPVLKGLTFTLHPGEVVALVGPSGSGKSTvAAL----LQNLYQPTGGQVLLDGVPLVQYD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 80 DHAMSqirgRMIGTVFQDP--MSAltpvyTIGDQIAEAIEIHSREISRADARRRAVEllELVGIAQPERRARAFPH--EL 155
Cdd:TIGR00958 550 HHYLH----RQVALVGQEPvlFSG-----SVRENIAYGLTDTPDEEIMAAAKAANAH--DFIMEFPNGYDTEVGEKgsQL 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 156 SGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQaQILDVLRTARDVTgaaVLIITHDLGVVsEFADRALVMYAGRPVE 235
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALDAECE-QLLQESRSRASRT---VLLIAHRLSTV-ERADQILVLKKGSVVE 693
|
250
....*....|...
gi 1424538268 236 IAAVDELYRDRRM 248
Cdd:TIGR00958 694 MGTHKQLMEDQGC 706
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-232 |
9.09e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.01 E-value: 9.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 28 SYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKellglsDHAMSQIRGRMIGTVFQDpmSALTPVYT 107
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTP---ASGSLTLNGQ------DHTTTPPSRRPVSMLFQE--NNLFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 108 IGDQIAeaIEIHSREISRADARRRAVELLELVGIAQPERRaraFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDV 187
Cdd:PRK10771 88 VAQNIG--LGLNPGLKLNAAQREKLHAIARQMGIEDLLAR---LPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1424538268 188 TVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:PRK10771 163 ALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-243 |
9.31e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 79.89 E-value: 9.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEdievPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHGKELlglSDHAM 83
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkPD----SGKILLDGQDI---TKLPM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 SQIRGRMIG------TVFQDpmsaltpvYTIGDQIAEAIEIHsrEISRADARRRAVELLELVGIaQPERRARAFphELSG 157
Cdd:cd03218 70 HKRARLGIGylpqeaSIFRK--------LTVEENILAVLEIR--GLSKKEREEKLEELLEEFHI-THLRKSKAS--SLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 158 GERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGR----- 232
Cdd:cd03218 137 GERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETLSITDRAYIIYEGKvlaeg 215
|
250
....*....|....*
gi 1424538268 233 -PVEIAA---VDELY 243
Cdd:cd03218 216 tPEEIAAnelVRKVY 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
22-234 |
9.46e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.80 E-value: 9.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 22 PAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYArvsGSIrlhgkELLGLSDHAMSQIRGRMIGTVFQdpMSA 101
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA---GKI-----TVLGVPVPARARLARARIGVVPQ--FDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 102 LTPVYTIgdqiAEAIEIHSREIsRADARRRAVELLELVGIAQPERRARAFPHELSGGERQRVVIAIAIANDPDLLICDEP 181
Cdd:PRK13536 125 LDLEFTV----RENLLVFGRYF-GMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 182 TTALDVTVQAQILDVLRT--ARdvtGAAVLIITHDLGVVSEFADRALVMYAGRPV 234
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSllAR---GKTILLTTHFMEEAERLCDRLCVLEAGRKI 251
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
234-300 |
1.64e-16 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 73.97 E-value: 1.64e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 234 VEIAAVDELYRDRRMPYTVGLLGSVPRLDAAQgTRLIPIPGAPPTMTSLSPGaCTFAPRCPLAIDEC 300
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPK-RPLYTIPGNVPSLLELPEG-CPFAPRCPFATEEC 65
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
21-244 |
1.65e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 81.43 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 21 VPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlpeyARV-SGSIRLHGKELLGLSDhamsqiRGRMIGTVFQDpm 99
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL----ERItSGEIWIGGRVVNELEP------ADRDIAMVFQN-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 100 SALTPVYTIGDQIAEAIEIhsREISRADARRR---AVELLELvgiaQP--ERRarafPHELSGGERQRVVIAIAIANDPD 174
Cdd:PRK11650 85 YALYPHMSVRENMAYGLKI--RGMPKAEIEERvaeAARILEL----EPllDRK----PRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 175 LLICDEPTTALDVTVQAQI-LDVLRTARDVtGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYR 244
Cdd:PRK11650 155 VFLFDEPLSNLDAKLRVQMrLEIQRLHRRL-KTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYE 224
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
382-594 |
1.80e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 82.84 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAArrrLRTELQVVFQDPVASLDprlPVY 461
Cdd:PRK10789 333 NVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS---WRSRLAVVSQTPFLFSD---TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 DVIAepLRANGFHRHECEErVAELLAVvgldHSDASRYPAEF-----------SGGQKQRIGIARALALQPKILALDEPV 530
Cdd:PRK10789 407 NNIA--LGRPDATQQEIEH-VARLASV----HDDILRLPQGYdtevgergvmlSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 531 SALDVSIQAGIVNLLldLQRRFGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQGESDQVFTNP 594
Cdd:PRK10789 480 SAVDGRTEHQILHNL--RQWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
381-588 |
1.95e-16 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 79.23 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQIL--ELTKPEAGSIEILGTDVAVLDAAARRRLrtELQVVFQDPVASldPRL 458
Cdd:TIGR01978 17 KGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghPSYEVTSGTILFKGQDLLELEPDERARA--GLFLAFQYPEEI--PGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 459 PVYDVIAEPLRANGFHRHECE-------ERVAELLAVVGLDHSDASRYPAE-FSGGQKQRIGIARALALQPKILALDEPV 530
Cdd:TIGR01978 93 SNLEFLRSALNARRSARGEEPldlldfeKLLKEKLALLDMDEEFLNRSVNEgFSGGEKKRNEILQMALLEPKLAILDEID 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 531 SALDVSIQAGIVNLLLDLqRRFGLSYLFVSHDLSVVKHLA-HRVAVMYRGMIVEQGESD 588
Cdd:TIGR01978 173 SGLDIDALKIVAEGINRL-REPDRSFLIITHYQRLLNYIKpDYVHVLLDGRIVKSGDVE 230
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-223 |
2.14e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 79.31 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTaalaVIGLLPEYARVSGSIRLHGK-ELLGLSDHA- 82
Cdd:PRK14258 8 IKVNNLSFYYDTQKI----LEGVSMEIYQSKVTAIIGPSGCGKST----FLKCLNRMNELESEVRVEGRvEFFNQNIYEr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 83 ---MSQIRgRMIGTVFQDPMSALTPVYtigDQIAEAIEI---HSReISRADARRRAVELLELVGIAQPERRARAFphELS 156
Cdd:PRK14258 80 rvnLNRLR-RQVSMVHPKPNLFPMSVY---DNVAYGVKIvgwRPK-LEIDDIVESALKDADLWDEIKHKIHKSAL--DLS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 157 GGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFAD 223
Cdd:PRK14258 153 GGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-237 |
2.47e-16 |
|
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: 77.84 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFeTEDIEvPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHGKELLGLSDHAM 83
Cdd:cd03369 7 IEVENLSVRY-APDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAE----EGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 SqirgRMIGTVFQDPM-------SALTPV--YTiGDQIAEAIEIHSREISradarrravellelvgiaqperrarafphe 154
Cdd:cd03369 81 R----SSLTIIPQDPTlfsgtirSNLDPFdeYS-DEEIYGALRVSEGGLN------------------------------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 155 LSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTarDVTGAAVLIITHDLGVVSEFaDRALVMYAGRPV 234
Cdd:cd03369 126 LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
...
gi 1424538268 235 EIA 237
Cdd:cd03369 203 EYD 205
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
11-234 |
2.80e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.26 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDiEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEYARVSGSirlhgkellGLSDHAMSQIRG- 88
Cdd:PRK13644 6 NVSYSYPD-GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQKGKVLVS---------GIDTGDFSKLQGi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 89 -RMIGTVFQDPMSALtpvytIGDQIAEAIEIHSRE--ISRADARRRAVELLELVGIAQPERRArafPHELSGGERQRVVI 165
Cdd:PRK13644 76 rKLVGIVFQNPETQF-----VGRTVEEDLAFGPENlcLPPIEIRKRVDRALAEIGLEKYRHRS---PKTLSGGQGQCVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 166 AIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEfADRALVMYAGRPV 234
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEELHD-ADRIIVMDRGKIV 214
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-614 |
3.07e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.88 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFetedievPAVR---GTSYHIDPGEVLAIVGESGCGKTTAaLAVIGllPEYARVSGSIRLHGKELlg 77
Cdd:PRK11288 1 SSPYLSFDGIGKTF-------PGVKaldDISFDCRAGQVHALMGENGAGKSTL-LKILS--GNYQPDAGSILIDGQEM-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 78 lsdhamsqirgrmigtVFQDPMSALTPVYTIGDQ---------IAEAI---EIHSRE--ISRADARRRAVELLELVGIA- 142
Cdd:PRK11288 69 ----------------RFASTTAALAAGVAIIYQelhlvpemtVAENLylgQLPHKGgiVNRRLLNYEAREQLEHLGVDi 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 143 QPERRARafphELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFA 222
Cdd:PRK11288 133 DPDTPLK----YLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRA-EGRVILYVSHRMEEIFALC 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 223 DRALVMYAGRPVE-IAAVDELYRDRrmpytvgllgsvprldaaqgtrlipipgapptmtslspgactfaprcplaidecl 301
Cdd:PRK11288 208 DAITVFKDGRYVAtFDDMAQVDRDQ------------------------------------------------------- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 302 saepdLVRvadghwaacirtdDVAGRSAADVFGVSTQPppnnaaggQPPVVLRVSDLtktyrltKGVVVRRrvgevravd 381
Cdd:PRK11288 233 -----LVQ-------------AMVGREIGDIYGYRPRP--------LGEVRLRLDGL-------KGPGLRE--------- 270
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRL--------RTELQVVfqdPVAS 453
Cdd:PRK11288 271 PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgimlcpedRKAEGII---PVHS 347
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 454 ldprlpVYDVIA-----EPLRANGFHRHECEERVAEL----LAVVGLDHSDASRYpaeFSGGQKQRIGIARALALQPKIL 524
Cdd:PRK11288 348 ------VADNINisarrHHLRAGCLINNRWEAENADRfirsLNIKTPSREQLIMN---LSGGNQQKAILGRWLSEDMKVI 418
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 525 ALDEPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVeqGESDQVFTNPQheytRRLLA 604
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA--GELAREQATER----QALSL 491
|
650
....*....|
gi 1424538268 605 AVPRAHSDVA 614
Cdd:PRK11288 492 ALPRTSAAVA 501
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
382-585 |
3.18e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 77.57 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRTELQVVFQDPvasldPRLPvy 461
Cdd:cd03217 18 GVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGEDITDLPPEERARLGIFLAFQYP-----PEIP-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 dviaeplrangfhrhecEERVAELLavvgldhsdasRYPAE-FSGGQKQRIGIARALALQPKILALDEPVSALDV---SI 537
Cdd:cd03217 91 -----------------GVKNADFL-----------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIdalRL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1424538268 538 QAGIVNLLLDLqrrfGLSYLFVSHDLSVVKHL-AHRVAVMYRGMIVEQG 585
Cdd:cd03217 143 VAEVINKLREE----GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
383-566 |
4.10e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.23 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEilgtdvavldaaarRRLRTELQVVFQDpvASLDPRLPvyd 462
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------------RNGKLRIGYVPQK--LYLDTTLP--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 463 viaepLRANGFHRHECEERVAELLAVvgLDHSDASR---YPAE-FSGGQKQRIGIARALALQPKILALDEPVSALDVSIQ 538
Cdd:PRK09544 84 -----LTVNRFLRLRPGTKKEDILPA--LKRVQAGHlidAPMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180
....*....|....*....|....*...
gi 1424538268 539 AGIVNLLLDLQRRFGLSYLFVSHDLSVV 566
Cdd:PRK09544 157 VALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
22-215 |
4.14e-16 |
|
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: 81.64 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 22 PAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELLGLSDHAMSqirgRMIGTVFQDPMSA 101
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP---LQGEVTLDGVPVSSLDQDEVR----RRVSVCAQDAHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 102 LTpvyTIGDQIAeaieihsreISRADARRRAV-ELLELVGIAQPerrARAFPH-----------ELSGGERQRVVIAIAI 169
Cdd:TIGR02868 422 DT---TVRENLR---------LARPDATDEELwAALERVGLADW---LRALPDgldtvlgeggaRLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1424538268 170 ANDPDLLICDEPTTALDVTVQAQILDVLRTARDvtGAAVLIITHDL 215
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
293-563 |
7.14e-16 |
|
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: 80.87 E-value: 7.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 293 CPLAIDECLSAEPDLVRVADGHWAACIRTDDVAGrsAADVFGVSTQPPPNNAAGGQPPVVLRvsDLTKTYrltkgvvvrr 372
Cdd:TIGR02868 279 LPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLD--AAGPVAEGSAPAAGAVGLGKPTLELR--DLSAGY---------- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 373 rVGEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLrteLQVVFQDPva 452
Cdd:TIGR02868 345 -PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR---VSVCAQDA-- 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 453 sldprlpvyDVIAEPLRAN-GFHRHEC-EERVAELLAVVGLdHSDASRYP-----------AEFSGGQKQRIGIARALAL 519
Cdd:TIGR02868 419 ---------HLFDTTVRENlRLARPDAtDEELWAALERVGL-ADWLRALPdgldtvlgeggARLSGGERQRLALARALLA 488
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1424538268 520 QPKILALDEPVSALDVSIQAGIVNLLLDLQRrfGLSYLFVSHDL 563
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
383-592 |
8.25e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 77.72 E-value: 8.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVavlDAAARRRLRTELQVVFQDPVASLDprLPVYD 462
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI---QHYASKEVARRIGLLAQNATTPGD--ITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 463 VIA------EPLRANgfHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVS 536
Cdd:PRK10253 101 LVArgryphQPLFTR--WRKEDEEAVTKAMQATGITHL-ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 537 IQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFT 592
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
31-232 |
8.48e-16 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 76.44 E-value: 8.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 31 IDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELLGLSDHAmsqirgRMIGTVFQDpmSALTPVYTIGD 110
Cdd:TIGR01277 21 VADGEIVAIMGPSGAGKSTLLNLIAGFIEP---ASGSIKVNDQSHTGLAPYQ------RPVSMLFQE--NNLFAHLTVRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 111 QIAeaIEIHSREISRADARRRAVELLELVGIAQPERRaraFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQ 190
Cdd:TIGR01277 90 NIG--LGLHPGLKLNAEQQEKVVDAAQQVGIADYLDR---LPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1424538268 191 AQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:TIGR01277 165 EEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
381-569 |
1.37e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.15 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTK--PEAGSIEI----LGTDVAVLDAaarrrlrtelqvvfqdpvasL 454
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVpdnqFGREASLIDA--------------------I 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 455 DPRLPVYDVIaeplrangfhrheceervaELLAVVGLdhSDAS---RYPAEFSGGQKQRIGIARALALQPKILALDEPVS 531
Cdd:COG2401 107 GRKGDFKDAV-------------------ELLNAVGL--SDAVlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 1424538268 532 ALDVSiQAGIVNL-LLDLQRRFGLSYLFVSHDLSVVKHL 569
Cdd:COG2401 166 HLDRQ-TAKRVARnLQKLARRAGITLVVATHHYDVIDDL 203
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
24-248 |
1.38e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.47 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 24 VRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeyaRVSGSIRLHGKELLGLSDHAMSQirgRMIGTVFQDPmsALT 103
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP---RDAGNIIIDDEDISLLPLHARAR---RGIGYLPQEA--SIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 104 PVYTIGDQIAEAIEIHsREISRADARRRAVELLELVGIAQPERrarAFPHELSGGERQRVVIAIAIANDPDLLICDEPTT 183
Cdd:PRK10895 91 RRLSVYDNLMAVLQIR-DDLSAEQREDRANELMEEFHIEHLRD---SMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 184 ALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDRRM 248
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
381-589 |
1.42e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.87 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAArrrLRTELQVVFQDP---VASLDPR 457
Cdd:PRK11160 357 KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA---LRQAISVVSQRVhlfSATLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 458 LpvydVIAEPlRANgfhrhecEERVAELLAVVGLDH------------SDASRypaEFSGGQKQRIGIARALALQPKILA 525
Cdd:PRK11160 434 L----LLAAP-NAS-------DEALIEVLQQVGLEKlleddkglnawlGEGGR---QLSGGEQRRLGIARALLHDAPLLL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 526 LDEPVSALDVSIQAGIVNLLLDLQRrfGLSYLFVSHDLSVVKHLaHRVAVMYRGMIVEQGESDQ 589
Cdd:PRK11160 499 LDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQE 559
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-243 |
2.13e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 76.62 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 24 VRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEY---ARVSGSIRLHGKELLGLSDHAMSqirgRMIGTVFQDPMS 100
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYdskIKVDGKVLYFGKDIFQIDAIKLR----KEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 101 alTPVYTIGDQIAEAIEIHSREISRaDARRRAVELLELVGI-AQPERRARAFPHELSGGERQRVVIAIAIANDPDLLICD 179
Cdd:PRK14246 102 --FPHLSIYDNIAYPLKSHGIKEKR-EIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 180 EPTTALDVtVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELY 243
Cdd:PRK14246 179 EPTSMIDI-VNSQAIEKLITELK-NEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
382-573 |
2.24e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.58 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIeilgtdvavldaaaRRRLRTELQVVFQDpvASLDPRLP-- 459
Cdd:NF040873 10 GVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV--------------RRAGGARVAYVPQR--SEVPDSLPlt 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 460 VYDVIA----EPLRANGFHRHECEERVAELLAVVGLdHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDV 535
Cdd:NF040873 74 VRDLVAmgrwARRGLWRRLTRDDRAAVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 1424538268 536 SIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRV 573
Cdd:NF040873 153 ESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
381-594 |
3.41e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.96 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLrteLQVVFQDPVASLDPRL-P 459
Cdd:PRK09536 20 DGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR---VASVPQDTSLSFEFDVrQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 460 VYDVIAEPLRANgFHRHECEER--VAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSI 537
Cdd:PRK09536 97 VVEMGRTPHRSR-FDTWTETDRaaVERAMERTGVAQF-ADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINH 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 538 QAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTNP 594
Cdd:PRK09536 175 QVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
382-541 |
4.02e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 79.40 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLdaaARRRLRTELQVVFQDPVA-------SL 454
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GLMDLRKVLGIIPQAPVLfsgtvrfNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 455 DPrlpvydviaeplrangFHRH------ECEERvAELLAVV-----GLDhSDASRYPAEFSGGQKQRIGIARALALQPKI 523
Cdd:PLN03130 1334 DP----------------FNEHndadlwESLER-AHLKDVIrrnslGLD-AEVSEAGENFSVGQRQLLSLARALLRRSKI 1395
|
170
....*....|....*...
gi 1424538268 524 LALDEPVSALDVSIQAGI 541
Cdd:PLN03130 1396 LVLDEATAAVDVRTDALI 1413
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
24-240 |
4.71e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.31 E-value: 4.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 24 VRGTSYHIDPGEVLAIVGESGCGKTT--AALAviGLLPEYarvSGSIRL-HGKELLGLSdhamsqirgrmigtvfQDPms 100
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTllRAIA--GLWPYG---SGRIARpAGARVLFLP----------------QRP-- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 101 altpvYTIGDQIAEAI--EIHSREISRADARrravELLELVGIAQ-PER--RARAFPHELSGGERQRVVIAIAIANDPDL 175
Cdd:COG4178 436 -----YLPLGTLREALlyPATAEAFSDAELR----EALEAVGLGHlAERldEEADWDQVLSLGEQQRLAFARLLLHKPDW 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 176 LICDEPTTALDVTVQAQILDVLRTArdVTGAAVLIITHDlGVVSEFADRALVMYAGRPVEIAAVD 240
Cdd:COG4178 507 LFLDEATSALDEENEAALYQLLREE--LPGTTVISVGHR-STLAAFHDRVLELTGDGSWQLLPAE 568
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
382-585 |
4.90e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 74.61 E-value: 4.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQIleltkpeAGSIEILGT---DVAVLDAAARRRLrtelqvvFQDPVASLD--- 455
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAI-------SGRVEGGGTtsgQILFNGQPRKPDQ-------FQKCVAYVRqdd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 456 ---PRLPVYDVI--AEPLRangFHRHECEERVAELLAVVGLDH----SDASRYPAEFSGGQKQRIGIARALALQPKILAL 526
Cdd:cd03234 91 illPGLTVRETLtyTAILR---LPRKSSDAIRKKRVEDVLLRDlaltRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 527 DEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQG 585
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-232 |
4.96e-15 |
|
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: 74.04 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDIE-VPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGllpEYARVSGSIRLHGKellglsdham 83
Cdd:cd03250 1 ISVEDASFTWDSGEQEtSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG---ELEKLSGSVSVPGS---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 sqirgrmIGTVFQDP--MSAltpvyTIGDQIaeaieIHSREIsraDARR--RAVELLELvgiaqpERRARAFPH------ 153
Cdd:cd03250 68 -------IAYVSQEPwiQNG-----TIRENI-----LFGKPF---DEERyeKVIKACAL------EPDLEILPDgdltei 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 154 -E----LSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEfADRALVM 228
Cdd:cd03250 122 gEkginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVL 200
|
....
gi 1424538268 229 YAGR 232
Cdd:cd03250 201 DNGR 204
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-232 |
1.36e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.68 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 36 VLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHGKELlglSDHAmSQI----RGRMIGTVFQDpmSALTPVYTI-- 108
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTrPQ----KGRIVLNGRVL---FDAE-KGIclppEKRRIGYVFQD--ARLFPHYKVrg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 109 ----GdqiaeaieihsreISRADARR--RAVELLelvGIAQPERRaraFPHELSGGERQRVVIAIAIANDPDLLICDEPT 182
Cdd:PRK11144 96 nlryG-------------MAKSMVAQfdKIVALL---GIEPLLDR---YPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 183 TALDVTVQAQILDVL-RTARDVTgAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:PRK11144 157 ASLDLPRKRELLPYLeRLAREIN-IPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-235 |
1.40e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 76.37 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 21 VPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeYARVSGSIRLHGkELLGLSDHAMSQIRGrmIGTVFQDpmS 100
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP-HGSYEGEILFDG-EVCRFKDIRDSEALG--IVIIHQE--L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 101 ALTPVYTIGDQIAEAIEIHSRE-ISRADARRRAVELLELVGIAQPerrarafPHELSG----GERQRVVIAIAIANDPDL 175
Cdd:NF040905 88 ALIPYLSIAENIFLGNERAKRGvIDWNETNRRARELLAKVGLDES-------PDTLVTdigvGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 176 LICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVE 235
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
395-591 |
1.55e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.68 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 395 IVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAArrrLRTELQVVFQDPVasldprlpvydVIAEPLRAN-GF 473
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV---LRQGVAMVQQDPV-----------VLADTFLANvTL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 474 HRHECEERVAELLAVVGLD----------HSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVN 543
Cdd:PRK10790 438 GRDISEEQVWQALETVQLAelarslpdglYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQ 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1424538268 544 LLLDLQRRFGLsyLFVSHDLSVVKHlAHRVAVMYRGMIVEQGESDQVF 591
Cdd:PRK10790 518 ALAAVREHTTL--VVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-228 |
1.55e-14 |
|
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: 70.94 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTaalavigllpeyarvsgsirlhgkeLLGLsdhams 84
Cdd:cd03221 1 IELENLSKTYGGKLL----LKDISLTINPGDRIGLVGRNGAGKST-------------------------LLKL------ 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 qirgrmigtvfqdpmsaltpvytigdqIAEAIEIHSREISRADArrravellelVGIAQperraraFPHeLSGGERQRVV 164
Cdd:cd03221 46 ---------------------------IAGELEPDEGIVTWGST----------VKIGY-------FEQ-LSGGEKMRLA 80
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 165 IAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvtgaAVLIITHDLGVVSEFADRALVM 228
Cdd:cd03221 81 LAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIEL 140
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-250 |
1.59e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.36 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETEDI---EVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeyaRVSGSIRLHGKELLG 77
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVtsrDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK---RAGGEIRLNGKDISP 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 78 LSDhaMSQIRGRMIGTVFQDPMSALTPVYTIGDQIAEAIEI-------------HSREISRADARRravELLEL--VGIA 142
Cdd:PRK09700 330 RSP--LDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLkdggykgamglfhEVDEQRTAENQR---ELLALkcHSVN 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 143 QPerrarafPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFA 222
Cdd:PRK09700 405 QN-------ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVC 476
|
250 260
....*....|....*....|....*....
gi 1424538268 223 DRALVMYAGRPVEI-AAVDELYRDRRMPY 250
Cdd:PRK09700 477 DRIAVFCEGRLTQIlTNRDDMSEEEIMAW 505
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
34-228 |
1.86e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 74.03 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 34 GEVLAIVGESGCGKTTAaLAVIG--LLPEyarvSGSIRLHGKELLGLSDHAMSQIRGRMiGTVFQDpmSALTPVYTIGDQ 111
Cdd:PRK11831 33 GKITAIMGPSGIGKTTL-LRLIGgqIAPD----HGEILFDGENIPAMSRSRLYTVRKRM-SMLFQS--GALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 112 IAEAIEIHSReISRADARRRAVELLELVGIaqpERRARAFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALD---VT 188
Cdd:PRK11831 105 VAYPLREHTQ-LPAPLLHSTVMMKLEAVGL---RGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDpitMG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1424538268 189 VQAQILDVLRTARDVTgaaVLIITHDLGVVSEFADRALVM 228
Cdd:PRK11831 181 VLVKLISELNSALGVT---CVVVSHDVPEVLSIADHAYIV 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
382-607 |
1.95e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.94 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLrteLQVVFQDPVA-------SL 454
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV---LSIIPQSPVLfsgtvrfNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 455 DPRLPVYDviAEPLRAngFHRHECEERVAEllAVVGLDhSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALD 534
Cdd:PLN03232 1331 DPFSEHND--ADLWEA--LERAHIKDVIDR--NPFGLD-AEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 535 VSIQAGIVNLLLDLQRrfGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVEQGESDQVFTNPQHEYTRRLLAAVP 607
Cdd:PLN03232 1404 VRTDSLIQRTIREEFK--SCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGP 1473
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-226 |
2.53e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.22 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLpeyARVSGSIRLHGkellglsd 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRV----LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLV---APDEGVIKRNG-------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 hamsQIRgrmIGTVFQDPMSALTPVYTIGDQIAEAIEIHSREISRADARRRAVELLElvgiaQPERRarafpheLSGGER 160
Cdd:PRK09544 66 ----KLR---IGYVPQKLYLDTTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLID-----APMQK-------LSGGET 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 161 QRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRAL 226
Cdd:PRK09544 127 QRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
11-232 |
2.65e-14 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 72.50 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETED-IEVPAVRGTSYHIDPGEVLAIVGESGCGKTTaalaVIGLLPE-YARVSGSIRLHGKELlGLSDHAMSQirg 88
Cdd:cd03248 16 NVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKST----VVALLENfYQPQGGQVLLDGKPI-SQYEHKYLH--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 89 RMIGTVFQDP-MSAltpvYTIGDQIAEAIEIHSREI-----SRADARRRAVELLELVGIAQPERRArafphELSGGERQR 162
Cdd:cd03248 88 SKVSLVGQEPvLFA----RSLQDNIAYGLQSCSFECvkeaaQKAHAHSFISELASGYDTEVGEKGS-----QLSGGQKQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 163 VVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRtaRDVTGAAVLIITHDLGVVsEFADRALVMYAGR 232
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQVQQALY--DWPERRTVLVIAHRLSTV-ERADQILVLDGGR 225
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
20-242 |
4.27e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 74.00 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 20 EVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYARvsgsiRLHGKELLGLSDHAMSQIRG--RMIGTVFQD 97
Cdd:NF000106 25 EVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGR-----RPWRF*TWCANRRALRRTIG*hRPVR*GRRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 98 PMSALTPVYTIGDQIaeaieihsrEISRADARRRAVELLELVGIAQPERRARAfphELSGGERQRVVIAIAIANDPDLLI 177
Cdd:NF000106 100 SFSGRENLYMIGR*L---------DLSRKDARARADELLERFSLTEAAGRAAA---KYSGGMRRRLDLAASMIGRPAVLY 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 178 CDEPTTALDVTVQAQILDVLRT-ARDvtGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDEL 242
Cdd:NF000106 168 LDEPTTGLDPRTRNEVWDEVRSmVRD--GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
382-545 |
4.93e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.44 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAArrrlrtelQVVFQDPVASLDPRLPVy 461
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE--------ACHYLGHRNAMKPALTV- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 dviAEPLR--ANGFHRHECeeRVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQA 539
Cdd:PRK13539 91 ---AENLEfwAAFLGGEEL--DIAAALEAVGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
....*.
gi 1424538268 540 GIVNLL 545
Cdd:PRK13539 165 LFAELI 170
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
381-576 |
6.48e-14 |
|
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: 69.01 E-value: 6.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEilgtdvavldaaarrrlrtelqvvfqdpvasLDPRLPV 460
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-------------------------------WGSTVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YdviaeplrangfhrheceervaellavvgldhsdasrYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDV-SIQA 539
Cdd:cd03221 66 G-------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLeSIEA 108
|
170 180 190
....*....|....*....|....*....|....*..
gi 1424538268 540 gIVNLLLDLQRrfglSYLFVSHDLSVVKHLAHRVAVM 576
Cdd:cd03221 109 -LEEALKEYPG----TVILVSHDRYFLDQVATKIIEL 140
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-232 |
9.07e-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: 71.02 E-value: 9.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 13 TFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIG--LLPEyarvSGSIRLHGK--ELLGLsdhamsqirg 88
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTL-LRLLAgiYPPD----SGTVTVRGRvsSLLGL---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 89 rmiGTVFQDPMSALTPVYTIGdqiaeaiEIHSreISRADARRRAVELLELVGIAQ----PERrarafphELSGGERQRVV 164
Cdd:cd03220 92 ---GGGFNPELTGRENIYLNG-------RLLG--LSRKEIDEKIDEIIEFSELGDfidlPVK-------TYSSGMKARLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 165 IAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:cd03220 153 FAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLK-QGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
383-568 |
9.55e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.07 E-value: 9.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEIlgTDVAVLDAAARRRLRTELQVVFQDPVASLDP------ 456
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDINLKWWRSKIGVVSQDPLLFSNSiknnik 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 457 ----RLPVYDVIAEPLRANGF-------HRHECEERVA-------------ELLAVVG-----------------LDHSD 495
Cdd:PTZ00265 482 yslySLKDLEALSNYYNEDGNdsqenknKRNSCRAKCAgdlndmsnttdsnELIEMRKnyqtikdsevvdvskkvLIHDF 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 496 ASRYP-----------AEFSGGQKQRIGIARALALQPKILALDEPVSALDVS----IQAGIVNLLLDLQRrfglSYLFVS 560
Cdd:PTZ00265 562 VSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseylVQKTINNLKGNENR----ITIIIA 637
|
....*...
gi 1424538268 561 HDLSVVKH 568
Cdd:PTZ00265 638 HRLSTIRY 645
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
31-257 |
9.55e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.14 E-value: 9.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 31 IDPGEVLAIVGESGCGKTTAaLAVIGLLPEYArvSGsirlhgkELLgLSDHAMSQI--RGRMIGTVFQDpmSALTPVYTI 108
Cdd:PRK11000 26 IHEGEFVVFVGPSGCGKSTL-LRMIAGLEDIT--SG-------DLF-IGEKRMNDVppAERGVGMVFQS--YALYPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 109 GDQIAEAIEIHSreISRADARRR---AVELLELVGIAqpERRarafPHELSGGERQRVVIAIAIANDPDLLICDEPTTAL 185
Cdd:PRK11000 93 AENMSFGLKLAG--AKKEEINQRvnqVAEVLQLAHLL--DRK----PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 186 DVTVQAQI-LDVLRTARDVtGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYRDRRMPYTVGLLGS 257
Cdd:PRK11000 165 DAALRVQMrIEISRLHKRL-GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGS 236
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
382-566 |
1.34e-13 |
|
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: 69.69 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLdaaarRRLRTElQVVFQDPVASLDPRLPVy 461
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-----RDEPHE-NILYLGHLPGLKPELSA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 dviAEPLR-ANGFHRHEcEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:TIGR01189 91 ---LENLHfWAAIHGGA-QRTIEDALAAVGLTGF-EDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|....*.
gi 1424538268 541 IVNLLLDLQRRFGLSYLFVSHDLSVV 566
Cdd:TIGR01189 166 LAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-233 |
1.89e-13 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 70.47 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 33 PGEVLAIVGESGCGKTTAALAVIG-LLPEYARvsgsirlHGKEllGLSDHAMSQIRGRMIGTVFQDPMS-----ALTPVY 106
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGkLKPNLGK-------FDDP--PDWDEILDEFRGSELQNYFTKLLEgdvkvIVKPQY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 107 TigDQIAEAIEIHSREI-SRADARRRAVELLELVGIAQPERRARAfphELSGGERQRVVIAIAIANDPDLLICDEPTTAL 185
Cdd:cd03236 96 V--DLIPKAVKGKVGELlKKKDERGKLDELVDQLELRHVLDRNID---QLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1424538268 186 DVtvqAQILDVLRTARDVT--GAAVLIITHDLGVVSEFADRALVMYaGRP 233
Cdd:cd03236 171 DI---KQRLNAARLIRELAedDNYVLVVEHDLAVLDYLSDYIHCLY-GEP 216
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-234 |
2.13e-13 |
|
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: 69.21 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 20 EVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYARVSGSIRLHGKEllglSDHAMSQIRGRMIGTVFQDpm 99
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIP----YKEFAEKYPGEIIYVSEED-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 100 sALTPVYTIGDQIAEAIEIHSREISRadarrravellelvGIaqperrarafphelSGGERQRVVIAIAIANDPDLLICD 179
Cdd:cd03233 93 -VHFPTLTVRETLDFALRCKGNEFVR--------------GI--------------SGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 180 EPTTALDVTVQAQILDVLRTARDVTGAAVLIITH--DLGVVSEFaDRALVMYAGRPV 234
Cdd:cd03233 144 NSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYqaSDEIYDLF-DKVLVLYEGRQI 199
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-218 |
2.41e-13 |
|
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: 68.92 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 20 EVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELLGLSDHAMSQIrgrmigtVFQDPM 99
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP---DSGEVRWNGTPLAEQRDEPHENI-------LYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 100 SALTPVYTIGDQIAEAIEIHSreisraDARRRAVELLELVGIAQPERRARAFpheLSGGERQRVVIAIAIANDPDLLICD 179
Cdd:TIGR01189 82 PGLKPELSALENLHFWAAIHG------GAQRTIEDALAAVGLTGFEDLPAAQ---LSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1424538268 180 EPTTALDVTVQAQILDVLRtARDVTGAAVLIITH-DLGVV 218
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLR-AHLARGGIVLLTTHqDLGLV 191
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
385-582 |
2.81e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.68 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 385 FTLEQGRTLGIVGESGSGKStTLNQILELTKP-EAGSIeILGTDVAVldaaARrrlrteLQvvfQDPvasldPRL---PV 460
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKS-TLMKILNGEVLlDDGRI-IYEQDLIV----AR------LQ---QDP-----PRNvegTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANG-----FHR------HECEERVAELLAVVG--LDHSDASRYP------------------AEFSGGQKQ 509
Cdd:PRK11147 84 YDFVAEGIEEQAeylkrYHDishlveTDPSEKNLNELAKLQeqLDHHNLWQLEnrinevlaqlgldpdaalSSLSGGWLR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 510 RIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDlqrrFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIV 582
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT----FQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4-227 |
3.25e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.53 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEDIEVPAvrGTSYHidpGEVLAIVGESGCGKTTAALAVIGLL-PEYARVSGSIRLHGKellglsdha 82
Cdd:PRK13409 340 LVEYPDLTKKLGDFSLEVEG--GEIYE---GEVIGIVGPNGIGKTTFAKLLAGVLkPDEGEVDPELKISYK--------- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 83 mSQ-IRGRMIGTVfQDPMSALTPVYT---IGDQIAEAIEIHsreisradarrravELLElvgiaqpeRRARafphELSGG 158
Cdd:PRK13409 406 -PQyIKPDYDGTV-EDLLRSITDDLGssyYKSEIIKPLQLE--------------RLLD--------KNVK----DLSGG 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 159 ERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALV 227
Cdd:PRK13409 458 ELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-217 |
3.91e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.75 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 25 RGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELlGLSDHAmSQIRgrMIGtvfqdPMSALTP 104
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP---AAGTIKLDGGDI-DDPDVA-EACH--YLG-----HRNAMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 105 VYTIGDQIAEAIEIHSREISRADArrrAVELLELVGIAqpERRARafphELSGGERQRVVIA-IAIANDPdLLICDEPTT 183
Cdd:PRK13539 87 ALTVAENLEFWAAFLGGEELDIAA---ALEAVGLAPLA--HLPFG----YLSAGQKRRVALArLLVSNRP-IWILDEPTA 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1424538268 184 ALDVTVQAQILDVLRTARDvTGAAVLIITH-DLGV 217
Cdd:PRK13539 157 ALDAAAVALFAELIRAHLA-QGGIVIAATHiPLGL 190
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
4-227 |
4.23e-13 |
|
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: 72.12 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEDIEVPAvrGTsyhIDPGEVLAIVGESGCGKTTAALAVIGLL-PEYARVSGSIRLHGKellglsdha 82
Cdd:COG1245 341 LVEYPDLTKSYGGFSLEVEG--GE---IREGEVLGIVGPNGIGKTTFAKILAGVLkPDEGEVDEDLKISYK--------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 83 mSQ-IRGRMIGTVFQDPMSALTPVYT---IGDQIAEAIEIHsreisradarrravELLElvgiaqpeRRARafphELSGG 158
Cdd:COG1245 407 -PQyISPDYDGTVEEFLRSANTDDFGssyYKTEIIKPLGLE--------------KLLD--------KNVK----DLSGG 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 159 ERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALV 227
Cdd:COG1245 460 ELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
381-573 |
4.58e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.15 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEIL-GTDVAVLdaaARRrlrtelqvvfqdpvasldPRLP 459
Cdd:COG4178 380 EDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPaGARVLFL---PQR------------------PYLP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 460 V---YDVIAEPLRANGFHrhecEERVAELLAVVGLDH-----SDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVS 531
Cdd:COG4178 439 LgtlREALLYPATAEAFS----DAELREALEAVGLGHlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1424538268 532 ALDVSIQAGIVNLLldLQRRFGLSYLFVSHDLSVVKHLAHRV 573
Cdd:COG4178 515 ALDEENEAALYQLL--REELPGTTVISVGHRSTLAAFHDRVL 554
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
31-242 |
5.22e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.63 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 31 IDPGEVLAIVGESGCGKTTAALAVIGLLpeyARVSGSIRLHGKELlglsDHAMSQIRGRMIGTVFQDpmsALTPV-YTIG 109
Cdd:PRK10253 30 IPDGHFTAIIGPNGCGKSTLLRTLSRLM---TPAHGHVWLDGEHI----QHYASKEVARRIGLLAQN---ATTPGdITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 110 DQIAEAIEIHSREISR-----ADARRRAvelLELVGIAQperRARAFPHELSGGERQRVVIAIAIANDPDLLICDEPTTA 184
Cdd:PRK10253 100 ELVARGRYPHQPLFTRwrkedEEAVTKA---MQATGITH---LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 185 LDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDEL 242
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-236 |
6.05e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.45 E-value: 6.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 15 ETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyARVSGSIRLhgkellglsdhamsqirgrmigtv 94
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKG-TPVAGCVDV------------------------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 95 fqdPMSALTPVYTIGDQIAEAIEIHSreisradarrrAVELLELVGIAQPER-RARafPHELSGGERQRVVIAIAIANDP 173
Cdd:COG2401 92 ---PDNQFGREASLIDAIGRKGDFKD-----------AVELLNAVGLSDAVLwLRR--FKELSTGQKFRFRLALLLAERP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 174 DLLICDEPTTALDVTVqAQIL--DVLRTARDvTGAAVLIITHDLGVVSEFADRALVM--YAGRPVEI 236
Cdd:COG2401 156 KLLVIDEFCSHLDRQT-AKRVarNLQKLARR-AGITLVVATHHYDVIDDLQPDLLIFvgYGGVPEEK 220
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
24-273 |
1.21e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.70 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 24 VRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEY-----ARVSGSIRLHGKELLGLSDHAMSQIRGRMigtvfqdP 98
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgARVTGDVTLNGEPLAAIDAPRLARLRAVL-------P 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 99 MSALTPVYTIGDQI-----------AEAIEIHSREIsradarrrAVELLELVGIAQPERRARAfphELSGGERQRVVIAI 167
Cdd:PRK13547 90 QAAQPAFAFSAREIvllgrypharrAGALTHRDGEI--------AWQALALAGATALVGRDVT---TLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 168 AIAN---------DPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAA 238
Cdd:PRK13547 159 VLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1424538268 239 VDELYRDRRMPYTVGLlgSVPRLDAAQGTRLIPIP 273
Cdd:PRK13547 239 PADVLTPAHIARCYGF--AVRLVDAGDGVPPVIVP 271
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
383-593 |
1.65e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 70.30 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTdvAVLDAAArrrlrtelqvvfqdpvASLDPRLPVYd 462
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS--AALIAIS----------------SGLNGQLTGI- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 463 viaEPLRANGFHRHECEERVAELLAVVgLDHSDASRY---PAE-FSGGQKQRIGIARALALQPKILALDEpvsALDVSIQ 538
Cdd:PRK13545 104 ---ENIELKGLMMGLTKEKIKEIIPEI-IEFADIGKFiyqPVKtYSSGMKSRLGFAISVHINPDILVIDE---ALSVGDQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 539 AgIVNLLLDLQRRF---GLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTN 593
Cdd:PRK13545 177 T-FTKKCLDKMNEFkeqGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
7-232 |
3.11e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.52 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 7 VTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGllpeyarvsgsiRLHGKELLG---LSDHAM 83
Cdd:PLN03211 71 ISDETRQIQERTI----LNGVTGMASPGEILAVLGPSGSGKSTLLNALAG------------RIQGNNFTGtilANNRKP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 SQIRGRMIGTVFQDPMsaLTPVYTIGDQIAEAIEIH-SREISRADARRRAVELLELVGIAQPERR--ARAFPHELSGGER 160
Cdd:PLN03211 135 TKQILKRTGFVTQDDI--LYPHLTVRETLVFCSLLRlPKSLTKQEKILVAESVISELGLTKCENTiiGNSFIRGISGGER 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 161 QRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:PLN03211 213 KRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-235 |
3.43e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.94 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFEtediEVPAVRGTSYHIDPGEVLAIVGESGCGKTTaaLAVIgLLPEYARVSGSIRLhGKEL-LGLSDHA 82
Cdd:COG0488 315 VLELEGLSKSYG----DKTLLDDLSLRIDRGDRIGLIGPNGAGKST--LLKL-LAGELEPDSGTVKL-GETVkIGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 83 MSQIRGRMigTVFQdpmsaltpvyTIGDQIAEAIEIHSREI------SRADARRRAvellelvgiaqperrarafpHELS 156
Cdd:COG0488 387 QEELDPDK--TVLD----------ELRDGAPGGTEQEVRGYlgrflfSGDDAFKPV--------------------GVLS 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 157 GGERQRVVIAIAIANDPDLLICDEPTTALDV-TVQAqILDVLrtaRDVTGaAVLIITHDLGVVSEFADRALVMYAGRPVE 235
Cdd:COG0488 435 GGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA-LEEAL---DDFPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
382-573 |
4.61e-12 |
|
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: 65.59 E-value: 4.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLrteLQVVFQDPV-ASLDPRlpv 460
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGL---LYLGHAPGIkTTLSVL--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 ydviaEPLRAngFHRHECEERVAELLAVVGLDHSDaSRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAG 540
Cdd:cd03231 92 -----ENLRF--WHADHSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|...
gi 1424538268 541 IVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRV 573
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-245 |
4.87e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.59 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 13 TFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTaalaVIGLLPEYARVS-GSIRLHGkelLGLSDHAMSQIRGRMi 91
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKST----LLSLIQRHFDVSeGDIRFHD---IPLTKLQLDSWRSRL- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 92 GTVFQDPmsaltpvYTIGDQIAEAI-----EIHSREISRAdARRRAV--ELLELVGIAQPERRARAFphELSGGERQRVV 164
Cdd:PRK10789 392 AVVSQTP-------FLFSDTVANNIalgrpDATQQEIEHV-ARLASVhdDILRLPQGYDTEVGERGV--MLSGGQKQRIS 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 165 IAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvtGAAVLIITHDLGVVSEfADRALVMYAGRPVEIAAVDEL-- 242
Cdd:PRK10789 462 IARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLaq 538
|
....*..
gi 1424538268 243 ----YRD 245
Cdd:PRK10789 539 qsgwYRD 545
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-235 |
5.05e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.35 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGlLPEYARVSGSIRLHGKELLGLSDHAM 83
Cdd:PRK09580 1 MLSIKDLHVSVEDKAI----LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG-REDYEVTGGTVEFKGKDLLELSPEDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 SqirGRMIGTVFQDPM------------SALTPVYTIGDQiaEAIEihsrEISRADARRRAVELLELvgiaQPERRARAF 151
Cdd:PRK09580 76 A---GEGIFMAFQYPVeipgvsnqfflqTALNAVRSYRGQ--EPLD----RFDFQDLMEEKIALLKM----PEDLLTRSV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 152 PHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFA-DRALVMYA 230
Cdd:PRK09580 143 NVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRD-GKRSFIIVTHYQRILDYIKpDYVHVLYQ 221
|
....*
gi 1424538268 231 GRPVE 235
Cdd:PRK09580 222 GRIVK 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
381-529 |
5.23e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.00 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAvlDAAARRRLRTElqvvfqdpVA-------- 452
Cdd:NF033858 18 DDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRAVCPR--------IAympqglgk 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 453 SLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDhSDASRyPA-EFSGGQKQRIGIARALALQPKILALDEP 529
Cdd:NF033858 88 NLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLA-PFADR-PAgKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
382-579 |
6.64e-12 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 64.80 E-value: 6.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQIL-ELTKPEaGSIEILGTdVAVldaaarrrlrtelqvvfqdpvASLDPRLP- 459
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLgELEKLS-GSVSVPGS-IAY---------------------VSQEPWIQn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 460 --VYDVIAeplrangFHRHECEERVAELLAVVGLDhSDASRYPA-------E----FSGGQKQRIGIARALALQPKILAL 526
Cdd:cd03250 80 gtIRENIL-------FGKPFDEERYEKVIKACALE-PDLEILPDgdlteigEkginLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 527 DEPVSALDVS-----IQAGIVNLLLDLQRRfglsyLFVSHDLSVVKHlAHRVAVMYRG 579
Cdd:cd03250 152 DDPLSAVDAHvgrhiFENCILGLLLNNKTR-----ILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-233 |
7.18e-12 |
|
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: 65.89 E-value: 7.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 31 IDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvsgsirlHGKELLGLSDHAM--SQIRGRMIGTVFQDPMSALTPVYT 107
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLkPD----------EGDIEIELDTVSYkpQYIKADYEGTVRDLLSSITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 108 IGDQIAEAIEIhsreisradarrravelLELVGIAqpERRARafphELSGGERQRVVIAIAIANDPDLLICDEPTTALDV 187
Cdd:cd03237 92 HPYFKTEIAKP-----------------LQIEQIL--DREVP----ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1424538268 188 TVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVmYAGRP 233
Cdd:cd03237 149 EQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV-FEGEP 193
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
383-585 |
7.50e-12 |
|
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: 68.82 E-value: 7.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLdaaARRRLRTELQVVFQDPVasldprlpvyd 462
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI---GLHDLRFKITIIPQDPV----------- 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 463 VIAEPLRAN--GFHRHECEE-----RVAELLAVV-----GLDHsDASRYPAEFSGGQKQRIGIARALALQPKILALDEPV 530
Cdd:TIGR00957 1371 LFSGSLRMNldPFSQYSDEEvwwalELAHLKTFVsalpdKLDH-ECAEGGENLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 531 SALDVS----IQAGIVNLLLDlqrrfgLSYLFVSHDLSVVKHLAhRVAVMYRGMIVEQG 585
Cdd:TIGR00957 1450 AAVDLEtdnlIQSTIRTQFED------CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
383-594 |
8.12e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.52 E-value: 8.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQIL-----------------------------------------ELTKPEAG-- 419
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnEFSLTKEGgs 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 420 ---------SIEILGTDVAVLDAAARRrLRTELQVVFQDPVASldpRLPVYDVIAeplrangFHRHECE----ERVAELL 486
Cdd:PTZ00265 1267 gedstvfknSGKILLDGVDICDYNLKD-LRNLFSIVSQEPMLF---NMSIYENIK-------FGKEDATredvKRACKFA 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 487 AVVGLDHSDASRYPA-------EFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRfglsylfv 559
Cdd:PTZ00265 1336 AIDEFIESLPNKYDTnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK-------- 1407
|
250 260 270
....*....|....*....|....*....|....*..
gi 1424538268 560 sHDLSVVKhLAHRVAVMYRgmiveqgeSDQ--VFTNP 594
Cdd:PTZ00265 1408 -ADKTIIT-IAHRIASIKR--------SDKivVFNNP 1434
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-213 |
9.10e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.43 E-value: 9.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTAAlAVIGLLPEYARVSGSIRLHGKELLGLSDHAM 83
Cdd:CHL00131 7 ILEIKNLHASVNENEI----LKGLNLSINKGEIHAIMGPNGSGKSTLS-KVIAGHPAYKILEGDILFKGESILDLEPEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 SQiRGRMIGtvFQDPmsaltpvytigdqiaeaIEIHSreISRAD-------ARRRAVEL---------------LELVGI 141
Cdd:CHL00131 82 AH-LGIFLA--FQYP-----------------IEIPG--VSNADflrlaynSKRKFQGLpeldplefleiinekLKLVGM 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 142 aQPERRARAFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITH 213
Cdd:CHL00131 140 -DPSFLSRNVNEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMT-SENSIILITH 209
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
381-596 |
1.00e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.62 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQIL-ELTKPEA-------GSIEILGTDVAVLDAAARRRLRTELQVVFQdPVA 452
Cdd:PRK13547 18 RDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQ-PAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 453 SLDPRLPVYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSDAsRYPAEFSGGQKQRIGIARALA---------LQPKI 523
Cdd:PRK13547 97 AFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVG-RDVTTLSGGELARVQFARVLAqlwpphdaaQPPRY 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 524 LALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTnPQH 596
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT-PAH 247
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
382-593 |
1.49e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.52 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAarRRLRTELQVVFQDPvasldpRLPVY 461
Cdd:PRK11614 23 EVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA--KIMREAVAIVPEGR------RVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 DVIAEPLRANGF--HRHECEERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQA 539
Cdd:PRK11614 95 MTVEENLAMGGFfaERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 540 GIVNLLLDLqRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTN 593
Cdd:PRK11614 175 QIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
112-560 |
1.53e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.46 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 112 IAEAIEIHSR--EISRADARRRAVELLELVGIAQ-PERRARafphELSGGERQRVVIAIAIANDPDLLICDEPTTALDVT 188
Cdd:NF033858 95 VFENLDFFGRlfGQDAAERRRRIDELLRATGLAPfADRPAG----KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 189 VQAQ---ILDVLRTARDvtGAAVLIITHDLGVVSEFaDRALVMYAGR------PVEIAA------VDELYrdrrmpytVG 253
Cdd:NF033858 171 SRRQfweLIDRIRAERP--GMSVLVATAYMEEAERF-DWLVAMDAGRvlatgtPAELLArtgadtLEAAF--------IA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 254 LLGSVPRldaaQGTRLIPIPgapptmtslspgactfaPRCPLAIDEclsaepdlvrVAdghwaacIRTDDVAGRsaadvF 333
Cdd:NF033858 240 LLPEEKR----RGHQPVVIP-----------------PRPADDDDE----------PA-------IEARGLTMR-----F 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 334 GvstqpppnnaaggqppvvlrvsDLTktyrltkgvvvrrrvgevrAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILEL 413
Cdd:NF033858 277 G----------------------DFT-------------------AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 414 TKPEAGSIEILGTDVAVLDAAARRR---------LRTELqVVFQDPVasLDPRLpvydviaeplrangFH--RHECEERV 482
Cdd:NF033858 316 LPASEGEAWLFGQPVDAGDIATRRRvgymsqafsLYGEL-TVRQNLE--LHARL--------------FHlpAAEIAARV 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 483 AELLAVVGL-DHSDAsrYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSyLFVS 560
Cdd:NF033858 379 AEMLERFDLaDVADA--LPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFIS 454
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
28-214 |
1.78e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.35 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 28 SYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHGKELLGLSDHAMSQirgrmigtvfQDPMSALTPVY 106
Cdd:PRK10247 27 SFSLRAGEFKLITGPSGCGKSTLLKIVASLIsPT----SGTLLFEGEDISTLKPEIYRQ----------QVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 107 ---TIGDQIAEAIEIhsreisRADARRRAVELLELVGIAQPERRARAFPHELSGGERQRVVIAIAIANDPDLLICDEPTT 183
Cdd:PRK10247 93 fgdTVYDNLIFPWQI------RNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190
....*....|....*....|....*....|..
gi 1424538268 184 ALDVTVQAQILDVL-RTARDvTGAAVLIITHD 214
Cdd:PRK10247 167 ALDESNKHNVNEIIhRYVRE-QNIAVLWVTHD 197
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-235 |
1.98e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 66.67 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETEDiEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLlpeYARVSGSIRLHGKELLGLSDHAMSQirgrM 90
Cdd:PRK10790 345 NVSFAYRD-DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGY---YPLTEGEIRLDGRPLSSLSHSVLRQ----G 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 91 IGTVFQDPMSALTPVY---TIGDQIAEAIEIHSREisradarrrAVELLELVgiaqperraRAFP-----------HELS 156
Cdd:PRK10790 417 VAMVQQDPVVLADTFLanvTLGRDISEEQVWQALE---------TVQLAELA---------RSLPdglytplgeqgNNLS 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 157 GGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTgaAVLIITHDLGVVSEfADRALVMYAGRPVE 235
Cdd:PRK10790 479 VGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRLSTIVE-ADTILVLHRGQAVE 554
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
125-244 |
3.50e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.04 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 125 RADARRRAVELLELVGIAQPERRaraFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVT 204
Cdd:PRK10575 121 GAADREKVEEAISLVGLKPLAHR---LVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQER 197
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1424538268 205 GAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDELYR 244
Cdd:PRK10575 198 GLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
28-213 |
4.19e-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: 61.79 E-value: 4.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 28 SYHIDPGEVLAIVGESGCGKTT--AALAviGLLPEYarvSGSIRLHGKEllglsdhamsqirgrmiGTVF--QDPmsaLT 103
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSlfRALA--GLWPWG---SGRIGMPEGE-----------------DLLFlpQRP---YL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 104 PVYTIGDQIAeaieihsreisradarrravellelvgiaqperraraFP--HELSGGERQRVVIAIAIANDPDLLICDEP 181
Cdd:cd03223 76 PLGTLREQLI-------------------------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEA 118
|
170 180 190
....*....|....*....|....*....|..
gi 1424538268 182 TTALDVTVQAQILDVLRTArdvtGAAVLIITH 213
Cdd:cd03223 119 TSALDEESEDRLYQLLKEL----GITVISVGH 146
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
381-583 |
4.89e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.20 E-value: 4.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTtLNQILELTKPeAGSIE--IlgtdvaVLDAAARRrlrtelqvvFQDPVAS----- 453
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKST-LMKVLSGVYP-HGSYEgeI------LFDGEVCR---------FKDIRDSealgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 454 --------LDPRLPVYDVI---AEPLRANGFHRHECEERVAELLAVVGLDHSDASRYpAEFSGGQKQRIGIARALALQPK 522
Cdd:NF040905 81 viihqelaLIPYLSIAENIflgNERAKRGVIDWNETNRRARELLAKVGLDESPDTLV-TDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 523 ILALDEPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVE 583
Cdd:NF040905 160 LLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
382-588 |
5.39e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.12 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTtlnqileLTKPEAG--SIEILGTDV-----AVLDAAARRRLRTELQVVFQDPV--- 451
Cdd:CHL00131 25 GLNLSINKGEIHAIMGPNGSGKST-------LSKVIAGhpAYKILEGDIlfkgeSILDLEPEERAHLGIFLAFQYPIeip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 452 ---------ASLDPRLPVY-DVIAEPLrangfhrhECEERVAELLAVVGLDHSDASRYPAE-FSGGQKQRIGIARALALQ 520
Cdd:CHL00131 98 gvsnadflrLAYNSKRKFQgLPELDPL--------EFLEIINEKLKLVGMDPSFLSRNVNEgFSGGEKKRNEILQMALLD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 521 PKILALDEPVSALDV----SIQAGIvNLLLDLQRrfglSYLFVSHD---LSVVKhlAHRVAVMYRGMIVEQGESD 588
Cdd:CHL00131 170 SELAILDETDSGLDIdalkIIAEGI-NKLMTSEN----SIILITHYqrlLDYIK--PDYVHVMQNGKIIKTGDAE 237
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
155-562 |
7.80e-11 |
|
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: 64.96 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 155 LSGGERQRVVIAIAIANDPDLLICDEPTTALDvtvqAQILDVL-RTARDVTGAaVLIITHD---LGVVSEFA---DRA-L 226
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLeRHLQEYPGT-VVAVTHDryfLDNVAGWIlelDRGrG 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 227 VMYAG----------RPVEIAAVDELYRDRRMPYTVGLLGSVPRLDAAQG-TRLIpipgapptmtslspgactfaprcpl 295
Cdd:TIGR03719 237 IPWEGnysswleqkqKRLEQEEKEESARQKTLKRELEWVRQSPKGRQAKSkARLA------------------------- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 296 AIDECLSAEPDlvrvadghwaaciRTDDVAgrsaadvfgvSTQPPPNNAAGGqppVVLRVSDLTKTY--RLtkgvvvrrr 373
Cdd:TIGR03719 292 RYEELLSQEFQ-------------KRNETA----------EIYIPPGPRLGD---KVIEAENLTKAFgdKL--------- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 374 vgevrAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGT-DVAVLDAaarrrlrtelqvvFQDpva 452
Cdd:TIGR03719 337 -----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvKLAYVDQ-------------SRD--- 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 453 SLDPRLPVYDVIAEPLRANGFHRHECEERvaellAVVG---LDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEP 529
Cdd:TIGR03719 396 ALDPNKTVWEEISGGLDIIKLGKREIPSR-----AYVGrfnFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
410 420 430
....*....|....*....|....*....|...
gi 1424538268 530 VSALDVSIQAGIVNLLLDlqrrFGLSYLFVSHD 562
Cdd:TIGR03719 471 TNDLDVETLRALEEALLN----FAGCAVVISHD 499
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
383-561 |
1.01e-10 |
|
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: 60.63 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEIL-GTDVAVLdaaarrrlrtelqvvfqdpvasldPRLPvY 461
Cdd:cd03223 20 LSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPeGEDLLFL------------------------PQRP-Y 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 dVIAEPLRangfhrheceervaellavvgldhsDASRYP--AEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQA 539
Cdd:cd03223 75 -LPLGTLR-------------------------EQLIYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|..
gi 1424538268 540 givnLLLDLQRRFGLSYLFVSH 561
Cdd:cd03223 129 ----RLYQLLKELGITVISVGH 146
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
381-585 |
1.03e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 65.03 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAV-LDAaarrrLRTELQVVFQDPVasLDPRLP 459
Cdd:TIGR01257 947 DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETnLDA-----VRQSLGMCPQHNI--LFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 460 VYDVIAEPLRANGFHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQA 539
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1424538268 540 GIVNLLldLQRRFGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQG 585
Cdd:TIGR01257 1099 SIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
20-234 |
1.04e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.20 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 20 EVPAVRGTSYHIDPGEVLAIVGESGCGKTTaalaVIGLLPEYARVS-GSIRLHGKELlglSDHAMSQIRGRMIGTVFQDP 98
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTT----LLGTLCGDPRATsGRIVFDGKDI---TDWQTAKIMREAVAIVPEGR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 99 --MSALTpvytigdqIAEAIEIHSREISRADARRRAVELLELVGIAQPERRARAfpHELSGGERQRVVIAIAIANDPDLL 176
Cdd:PRK11614 90 rvFSRMT--------VEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRA--GTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 177 ICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPV 234
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
381-597 |
1.05e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 62.53 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGtDVAVLDAAarrrlrtelqvvfqdpvASLDPRLPV 460
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAIS-----------------AGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEPLRANGFHRHECEERVAELLAVVGLD---HSDASRYpaefSGGQKQRIGIARALALQPKILALDEPVSALDVSI 537
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGefiYQPVKKY----SSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 538 QAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFtnPQHE 597
Cdd:PRK13546 179 AQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL--PKYE 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-232 |
1.71e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 64.65 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 22 PAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELlglsDHAMSQIRgRMIGTVFQDpmSA 101
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP---TSGTVLVGGKDI----ETNLDAVR-QSLGMCPQH--NI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 102 LTPVYTIGDQIAEAIEIHSReiSRADARRRAVELLELVGIAQpERRARAfpHELSGGERQRVVIAIAIANDPDLLICDEP 181
Cdd:TIGR01257 1014 LFHHLTVAEHILFYAQLKGR--SWEEAQLEMEAMLEDTGLHH-KRNEEA--QDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 182 TTALDVTVQAQILDVLRTARdvTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYR--SGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-232 |
1.73e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 63.69 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 24 VRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeyARVSGSIRLHGKELlgLSDHAMSQIRGRmIGTVFQD-PMSAL 102
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYP--GKFEGNVFINGKPV--DIRNPAQAIRAG-IAMVPEDrKRHGI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 103 TPVYTIGDQIAEAIEIHSREISRADArrrAVElLELVGIAQPERRARAFPHE-----LSGGERQRVVIAIAIANDPDLLI 177
Cdd:TIGR02633 351 VPILGVGKNITLSVLKSFCFKMRIDA---AAE-LQIIGSAIQRLKVKTASPFlpigrLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 178 CDEPTTALDVTVQAQILDVL-RTARDvtGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLInQLAQE--GVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-231 |
2.15e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.57 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 1 MTAVLEVTDLNVTFETEDievpAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYARVSGSIRLHGKELLGLSD 80
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 81 HAMSQIRGRM-IGTVFQ-----DPMSALTPVYTIGDQIAEAIEIHSREISRADaRRRAVELLELVGIAQperraraFPHE 154
Cdd:PRK09984 77 LARDIRKSRAnTGYIFQqfnlvNRLSVLENVLIGALGSTPFWRTCFSWFTREQ-KQRALQALTRVGMVH-------FAHQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 155 ----LSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYA 230
Cdd:PRK09984 149 rvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQ 228
|
.
gi 1424538268 231 G 231
Cdd:PRK09984 229 G 229
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
384-575 |
3.07e-10 |
|
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: 60.88 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 384 SFTLE-------QGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVldaaARRRLRTELQVVFQDPVASLDP 456
Cdd:cd03237 12 EFTLEveggsisESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY----KPQYIKADYEGTVRDLLSSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 457 RL---PVYDV-IAEPLRANGFHrhecEERVAELlavvgldhsdasrypaefSGGQKQRIGIARALALQPKILALDEPVSA 532
Cdd:cd03237 88 DFythPYFKTeIAKPLQIEQIL----DREVPEL------------------SGGELQRVAIAACLSKDADIYLLDEPSAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1424538268 533 LDVSiQAGIVNLLLdlqRRFGL----SYLFVSHDLSVVKHLAHRVAV 575
Cdd:cd03237 146 LDVE-QRLMASKVI---RRFAEnnekTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
383-567 |
4.53e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.58 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVavldaaARRRLRTELQVVFQDPVASLDPRLpvyd 462
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI------KKDLCTYQKQLCFVGHRSGINPYL---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 463 viaePLRANGF---HRHECEERVAELLAVVGLDHsdASRYPAE-FSGGQKQRIGIARALALQPKILALDEPVSALDvsiQ 538
Cdd:PRK13540 90 ----TLRENCLydiHFSPGAVGITELCRLFSLEH--LIDYPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---E 160
|
170 180 190
....*....|....*....|....*....|..
gi 1424538268 539 AGIVNLLLDLQ--RRFGLSYLFVSH-DLSVVK 567
Cdd:PRK13540 161 LSLLTIITKIQehRAKGGAVLLTSHqDLPLNK 192
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-232 |
4.65e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.11 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVtFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGllPEYAR-VSGSIRLHGKEL------- 75
Cdd:NF040905 257 VFEVKNWTV-YHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG--RSYGRnISGTVFKDGKEVdvstvsd 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 76 ---------------LGLsdHAMSQIRgRMIgtvfqdPMSALTPVYTIGdQIAEAIEIHSREISRADARRRAVELLELVG 140
Cdd:NF040905 334 aidaglayvtedrkgYGL--NLIDDIK-RNI------TLANLGKVSRRG-VIDENEEIKVAEEYRKKMNIKTPSVFQKVG 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 141 iaqperrarafphELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSE 220
Cdd:NF040905 404 -------------NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAA-EGKGVIVISSELPELLG 469
|
250
....*....|..
gi 1424538268 221 FADRALVMYAGR 232
Cdd:NF040905 470 MCDRIYVMNEGR 481
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
345-579 |
6.26e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.72 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 345 AGGQPPVVLRVSDLTKTYRLTKGVVVrrrvgevravDGISFTLEQGRTLGIVGESGSGKSTTLNQIleltkpeAGSIEIL 424
Cdd:TIGR01257 1930 SGGNKTDILRLNELTKVYSGTSSPAV----------DRLCVGVRPGECFGLLGVNGAGKTTTFKML-------TGDTTVT 1992
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 425 GTDVAVldaaARRRLRTELQVVFQDPvasldPRLPVYDVIAEPL----------RANGFHRHECEERVAELLAVVGLDHS 494
Cdd:TIGR01257 1993 SGDATV----AGKSILTNISDVHQNM-----GYCPQFDAIDDLLtgrehlylyaRLRGVPAEEIEKVANWSIQSLGLSLY 2063
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 495 dASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVA 574
Cdd:TIGR01257 2064 -ADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLA 2141
|
....*
gi 1424538268 575 VMYRG 579
Cdd:TIGR01257 2142 IMVKG 2146
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-242 |
1.16e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.50 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 7 VTDLNVTFETEDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAvigLLPEYARVSGSIRLHGkellglsdhamsqi 86
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSA---LLAEMDKVEGHVHMKG-------------- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 87 rgrmigTVFQDPMSAltpvYTIGDQIAEAIEI-HSREISRADARRRAVELLE----LVGIAQPERRARAFphELSGGERQ 161
Cdd:TIGR00957 700 ------SVAYVPQQA----WIQNDSLRENILFgKALNEKYYQQVLEACALLPdleiLPSGDRTEIGEKGV--NLSGGQKQ 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 162 RVVIAIAIANDPDLLICDEPTTALDVTVQAQILD-VLRTARDVTGAAVLIITHDLGVVSEfADRALVMYAGRPVEIAAVD 240
Cdd:TIGR00957 768 RVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQ 846
|
..
gi 1424538268 241 EL 242
Cdd:TIGR00957 847 EL 848
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
475-616 |
1.45e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.13 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 475 RHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRfGL 554
Cdd:NF000106 118 RKDARARADELLERFSLTEA-AGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GA 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 555 SYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQVFTN---------PQHEYT-RRLLAAVPRAHSDVASG 616
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKvggrtlqirPAHAAElDRMVGAIAQAGLDGIAG 267
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
384-535 |
1.75e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.64 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 384 SFTLEQGRTLGIVGESGSGKSTTLN--------------QILELTKpeagsiEILGTDVAVL------DAAARRRLRTEL 443
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTFLRymamhaidgipkncQILHVEQ------EVVGDDTTALqcvlntDIERTQLLEEEA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 444 QVVFQD-----PVASLDPRLPVY-----DVIAEPL-----RANGFHRHECEERVAELLAVVGLDHSDASRYPAEFSGGQK 508
Cdd:PLN03073 271 QLVAQQrelefETETGKGKGANKdgvdkDAVSQRLeeiykRLELIDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWR 350
|
170 180
....*....|....*....|....*..
gi 1424538268 509 QRIGIARALALQPKILALDEPVSALDV 535
Cdd:PLN03073 351 MRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
386-577 |
2.53e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.18 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 386 TLEQGRTLGIVGESGSGKSTTLNqIL--ELtKPEAGSIEILGTDVAVLDaaarrRLR-TELQVVFQDpVASLDPRL---P 459
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALK-ILsgEL-KPNLGDYDEEPSWDEVLK-----RFRgTELQDYFKK-LANGEIKVahkP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 460 VY-DVIaePLRANGfhrheceeRVAELLAVV-------------GLDHSdASRYPAEFSGGQKQRIGIARALALQPKILA 525
Cdd:COG1245 167 QYvDLI--PKVFKG--------TVRELLEKVdergkldelaeklGLENI-LDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 526 LDEPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMY 577
Cdd:COG1245 236 FDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
381-535 |
3.57e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.12 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKsTTLNQILE-LTKPEAGSIEILGTDVavldaaarRRLRTELQvvfQDP-----VASL 454
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGK-TSLLRILAgLARPDAGEVLWQGEPI--------RRQRDEYH---QDLlylghQPGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 455 DPRLPVYdviaEPLRAN-GFHRHECEERVAELLAVVGL-DHSDAsryPAE-FSGGQKQRIGIARALALQPKILALDEPVS 531
Cdd:PRK13538 86 KTELTAL----ENLRFYqRLHGPGDDEALWEALAQVGLaGFEDV---PVRqLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
....
gi 1424538268 532 ALDV 535
Cdd:PRK13538 159 AIDK 162
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
28-228 |
4.22e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.26 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 28 SYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSDHAMSQIrgrmIGTVFQDPMSALTPVYT 107
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLL---SGERQSQFSHITRLSFEQLQKL----VSDEWQRNNTDMLSPGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 108 --IGDQIAEAIEIHSREISRADarrravELLELVGIAQP-ERRaraFPHeLSGGERQRVVIAIAIANDPDLLICDEPTTA 184
Cdd:PRK10938 96 ddTGRTTAEIIQDEVKDPARCE------QLAQQFGITALlDRR---FKY-LSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1424538268 185 LDVTVQAQILDVLRTARDVTGAAVLIIT--HDlgvVSEFADRALVM 228
Cdd:PRK10938 166 LDVASRQQLAELLASLHQSGITLVLVLNrfDE---IPDFVQFAGVL 208
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
383-538 |
4.73e-09 |
|
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: 57.94 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEaGSIEILGTDvavLDAAARRRLRTELQVVFQDpvasldprlpVYd 462
Cdd:cd03289 23 ISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVS---WNSVPLQKWRKAFGVIPQK----------VF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 463 VIAEPLRAN----GFHRHECEERVAEllaVVGLdHSDASRYPAE-----------FSGGQKQRIGIARALALQPKILALD 527
Cdd:cd03289 88 IFSGTFRKNldpyGKWSDEEIWKVAE---EVGL-KSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLD 163
|
170
....*....|..
gi 1424538268 528 EPVSALD-VSIQ 538
Cdd:cd03289 164 EPSAHLDpITYQ 175
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
383-580 |
5.72e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 56.57 E-value: 5.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEiLGTDVAVLDAAARRRLRTELQVVFqdpvASLDPRLPVYD 462
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH-WSNKNESEPSFEATRSRNRYSVAY----AAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 463 VIAEPLRANGFH--RHECEERVAELLAVVGL----DHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVS 536
Cdd:cd03290 95 VEENITFGSPFNkqRYKAVTDACSLQPDIDLlpfgDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1424538268 537 I-----QAGIVNLLLDLQRrfglSYLFVSHDLSVVKHlAHRVAVMYRGM 580
Cdd:cd03290 175 LsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAMKDGS 218
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
383-568 |
5.78e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.99 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTtLNQIL---------ELTKPEAGSIEILGTDVAVldaaARRRLRTelQVVFQDPVas 453
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSS-LFRILgelwpvyggRLTKPAKGKLFYVPQRPYM----TLGTLRD--QIIYPDSS-- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 454 ldprlpvydviaEPLRANGFHRHECEErvaeLLAVVGLDH--------SDASRYPAEFSGGQKQRIGIARALALQPKILA 525
Cdd:TIGR00954 542 ------------EDMKRRGLSDKDLEQ----ILDNVQLTHilereggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1424538268 526 LDEPVSALDVSIQAGIVNLLldlqRRFGLSYLFVSHDLSVVKH 568
Cdd:TIGR00954 606 LDECTSAVSVDVEGYMYRLC----REFGITLFSVSHRKSLWKY 644
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
350-585 |
5.96e-09 |
|
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: 56.02 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 350 PVVLRVSDLTKTyrltkgVVVRRRVGEVRAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEA--GSIEILGTD 427
Cdd:cd03213 1 GVTLSFRNLTVT------VKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 428 VAvldaaaRRRLRTELQVVFQDPVasLDPRLPVY---DVIAEpLRangfhrheceervaellavvGLdhsdasrypaefS 504
Cdd:cd03213 75 LD------KRSFRKIIGYVPQDDI--LHPTLTVRetlMFAAK-LR--------------------GL------------S 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 505 GGQKQRIGIARALALQPKILALDEPVSALDvsiqAGIVNLLLDLQRRF---GLSYLFVSHDLS-VVKHLAHRVAVMYRGM 580
Cdd:cd03213 114 GGERKRVSIALELVSNPSLLFLDEPTSGLD----SSSALQVMSLLRRLadtGRTIICSIHQPSsEIFELFDKLLLLSQGR 189
|
....*
gi 1424538268 581 IVEQG 585
Cdd:cd03213 190 VIYFG 194
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-213 |
6.30e-09 |
|
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: 56.10 E-value: 6.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 18 DIEVPAVR-----GTSYHIDPGEVLAIVGESGCGKTTaALAVIGLLPEYARVSGSIRLHGKELlglsDHAMSqirgRMIG 92
Cdd:cd03232 12 TVPVKGGKrqllnNISGYVKPGTLTALMGESGAGKTT-LLDVLAGRKTAGVITGEILINGRPL----DKNFQ----RSTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 93 TVFQdpMSALTPVYTigdqIAEAIEIHsreisrADARrravellelvgiaqperrarafphELSGGERQRVVIAIAIAND 172
Cdd:cd03232 83 YVEQ--QDVHSPNLT----VREALRFS------ALLR------------------------GLSVEQRKRLTIGVELAAK 126
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1424538268 173 PDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITH 213
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFLKKLAD-SGQAILCTIH 166
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-252 |
1.08e-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: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 17 EDIEVpAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLpEYARvsGSIRLHGkelLGLSDHAMSQIRGRmIGTVFQ 96
Cdd:TIGR00957 1296 EDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRIN-ESAE--GEIIIDG---LNIAKIGLHDLRFK-ITIIPQ 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 97 DPM-------SALTPVYTIGDQiaeaiEIHSreisradarrrAVELLELVGI--AQPERraraFPHE-------LSGGER 160
Cdd:TIGR00957 1368 DPVlfsgslrMNLDPFSQYSDE-----EVWW-----------ALELAHLKTFvsALPDK----LDHEcaeggenLSVGQR 1427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 161 QRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvtGAAVLIITHDLGVVSEFAdRALVMYAGRPVEIAAVD 240
Cdd:TIGR00957 1428 QLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFE--DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPS 1504
|
250
....*....|..
gi 1424538268 241 ELYRDRRMPYTV 252
Cdd:TIGR00957 1505 NLLQQRGIFYSM 1516
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-214 |
1.09e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEDIevpaVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIG-LLPEyarvSGSIRLHGKELLGLSDha 82
Cdd:PRK11147 319 VFEMENVNYQIDGKQL----VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGqLQAD----SGRIHCGTKLEVAYFD-- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 83 msQIRgrmigtvfqdpmSALTPVYTIGDQIAEA---IEIHSREisradarrRAVellelVGIAQ----PERRARAFPHEL 155
Cdd:PRK11147 389 --QHR------------AELDPEKTVMDNLAEGkqeVMVNGRP--------RHV-----LGYLQdflfHPKRAMTPVKAL 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 156 SGGERQRVVIAIAIANDPDLLICDEPTTALDVtvqaQILDVLRTARDVTGAAVLIITHD 214
Cdd:PRK11147 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
383-593 |
2.29e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQIL-ELTKPEAGSIEILGTDVAVldaaarrrlrtelqvvfqdpvasldPRLPVy 461
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLgELSHAETSSVVIRGSVAYV-------------------------PQVSW- 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 dVIAEPLRANGFHRHECE-ERVAELLAVVGLDHsDASRYPAE-----------FSGGQKQRIGIARALALQPKILALDEP 529
Cdd:PLN03232 690 -IFNATVRENILFGSDFEsERYWRAIDVTALQH-DLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 530 VSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKhLAHRVAVMYRGMIVEQGESDQVFTN 593
Cdd:PLN03232 768 LSALDAHVAHQVFDSCMKDELK-GKTRVLVTNQLHFLP-LMDRIILVSEGMIKEEGTFAELSKS 829
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-231 |
2.53e-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: 54.64 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 21 VPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGllpEYARVSGSIRLHGKELLGLSDHAMSQIRGRMIGTVFQDPms 100
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILG---EMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKP-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 101 altpvYTIGDQIAEAIEIHS-------REISRADARRRAVELLELVGiaQPERRARAFphELSGGERQRVVIAIAIANDP 173
Cdd:cd03290 89 -----WLLNATVEENITFGSpfnkqryKAVTDACSLQPDIDLLPFGD--QTEIGERGI--NLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 174 DLLICDEPTTALDV-----TVQAQILDVLRTARdvtgAAVLIITHDLGVVSEfADRALVMYAG 231
Cdd:cd03290 160 NIVFLDDPFSALDIhlsdhLMQEGILKFLQDDK----RTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
386-577 |
2.66e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 386 TLEQGRTLGIVGESGSGKSTTLNqIL--ELtKPEAGSIEILGTDVAVLDAAARrrlrTELQVVFQDpVASLDPRL---PV 460
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVK-ILsgEL-IPNLGDYEEEPSWDEVLKRFRG----TELQNYFKK-LYNGEIKVvhkPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 Y-DVIAEPLRANgfhrheceerVAELLAVV-------------GLDHSdASRYPAEFSGGQKQRIGIARALALQPKILAL 526
Cdd:PRK13409 168 YvDLIPKVFKGK----------VRELLKKVdergkldevverlGLENI-LDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 527 DEPVSALDVSIQAGIVNLLLDLQRrfGLSYLFVSHDLSVVKHLAHRVAVMY 577
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-218 |
3.49e-08 |
|
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: 54.04 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 26 GTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYArvsGSIRLHGKELlglsDHAMSQIRGRMIGTVFQDPM-SALTP 104
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLA---GRVLLNGGPL----DFQRDSIARGLLYLGHAPGIkTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 105 VYTIgdqiaeaieihsREISRADARRRAVELLELVGIAQPERRArafPHELSGGERQRVVIAIAIANDPDLLICDEPTTA 184
Cdd:cd03231 91 LENL------------RFWHADHSDEQVEEALARVGLNGFEDRP---VAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190
....*....|....*....|....*....|....
gi 1424538268 185 LDVTVQAQILDVLRTARDVTGAAVLIITHDLGVV 218
Cdd:cd03231 156 LDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-236 |
4.17e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNvtfeteDIEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPeyaRVSGSIRLHGKELlglSDHAM 83
Cdd:PRK10982 250 ILEVRNLT------SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE---KSAGTITLHGKKI---NNHNA 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 84 SQIRGRMIGTVFQDPMSalTPVYTIGDqiaeaIEIHSReISRADARRRAVELLELVGIAQPER------RARAFPHE--- 154
Cdd:PRK10982 318 NEAINHGFALVTEERRS--TGIYAYLD-----IGFNSL-ISNIRNYKNKVGLLDNSRMKSDTQwvidsmRVKTPGHRtqi 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 155 --LSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILD-VLRTARDVTGaaVLIITHDLGVVSEFADRALVMYAG 231
Cdd:PRK10982 390 gsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQlIAELAKKDKG--IIIISSEMPELLGITDRILVMSNG 467
|
....*
gi 1424538268 232 RPVEI 236
Cdd:PRK10982 468 LVAGI 472
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-186 |
4.34e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.29 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 23 AVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELlGLSDHA-------MSQ---IRGRMig 92
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPA---SEGEAWLFGQPV-DAGDIAtrrrvgyMSQafsLYGEL-- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 93 TVFQDpmsaltpvytigdqiaeaIEIHSR--EISRADARRRAVELLELVGIAQperRARAFPHELSGGERQRVVIAIAIA 170
Cdd:NF033858 355 TVRQN------------------LELHARlfHLPAAEIAARVAEMLERFDLAD---VADALPDSLPLGIRQRLSLAVAVI 413
|
170
....*....|....*.
gi 1424538268 171 NDPDLLICDEPTTALD 186
Cdd:NF033858 414 HKPELLILDEPTSGVD 429
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
154-233 |
4.72e-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: 53.34 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 154 ELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDVTGAAVLIITHDLGVVSEFADRALVMYaGRP 233
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE-GEP 149
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
390-577 |
5.27e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.29 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 390 GRTLGIVGESGSGKSTTLnQIL--ELtKPEAGSIEILGTDVAVLDAAARrrlrTELQVVFQDPV-ASLDP-RLPVY-DVI 464
Cdd:cd03236 26 GQVLGLVGPNGIGKSTAL-KILagKL-KPNLGKFDDPPDWDEILDEFRG----SELQNYFTKLLeGDVKViVKPQYvDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 465 aePLRANG-----FHRHECEERVAELLAVVGLDHSdASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQA 539
Cdd:cd03236 100 --PKAVKGkvgelLKKKDERGKLDELVDQLELRHV-LDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1424538268 540 GIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMY 577
Cdd:cd03236 177 NAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
382-615 |
6.17e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.94 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAvldAAARRRLRTELQVVFQDPV-------ASL 454
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG---AYGLRELRRQFSMIPQDPVlfdgtvrQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 455 DPRLPvydviAEPlrangfhrheceERVAELLAVVGLDHSDASRYP----------AEFSGGQKQRIGIARALALQPK-- 522
Cdd:PTZ00243 1405 DPFLE-----ASS------------AEVWAALELVGLRERVASESEgidsrvleggSNYSVGQRQLMCMARALLKKGSgf 1467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 523 ILaLDEPVS----ALDVSIQAGIVNllldlqrrfglsyLFVSHDLSVVKHLAHRVA------VMYRGMIVEQGESDQVFT 592
Cdd:PTZ00243 1468 IL-MDEATAnidpALDRQIQATVMS-------------AFSAYTVITIAHRLHTVAqydkiiVMDHGAVAEMGSPRELVM 1533
|
250 260
....*....|....*....|...
gi 1424538268 593 NPQHEYTRRLLAAVPRAHSDVAS 615
Cdd:PTZ00243 1534 NRQSIFHSMVEALGRSEAKRFLQ 1556
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-195 |
6.60e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 54.48 E-value: 6.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 22 PAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGllpEYARVSGSIRLHGKelLGLSdhamSQIRGRMIGTVFQDPMSA 101
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILG---ELEPSEGKIKHSGR--ISFS----SQFSWIMPGTIKENIIFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 102 LtpvytigdqiaeaieihsreiSRADARRRAVellelVGIAQPERRARAFPHE-----------LSGGERQRVVIAIAIA 170
Cdd:cd03291 122 V---------------------SYDEYRYKSV-----VKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVY 175
|
170 180
....*....|....*....|....*
gi 1424538268 171 NDPDLLICDEPTTALDVTVQAQILD 195
Cdd:cd03291 176 KDADLYLLDSPFGYLDVFTEKEIFE 200
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
384-562 |
7.52e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 384 SFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEIlGT--DVAVLDaaaRRRlrtelqvvfqdpvASLDPRLPVY 461
Cdd:PRK11147 339 SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTklEVAYFD---QHR-------------AELDPEKTVM 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 DVIAE---PLRANGFHRHeceervaellaVVG-----LDHSDASRYPAE-FSGGQKQRIGIARaLALQP-KILALDEPVS 531
Cdd:PRK11147 402 DNLAEgkqEVMVNGRPRH-----------VLGylqdfLFHPKRAMTPVKaLSGGERNRLLLAR-LFLKPsNLLILDEPTN 469
|
170 180 190
....*....|....*....|....*....|.
gi 1424538268 532 ALDVSiqagIVNLLLDLQRRFGLSYLFVSHD 562
Cdd:PRK11147 470 DLDVE----TLELLEELLDSYQGTVLLVSHD 496
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-242 |
8.39e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.51 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 20 EVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYARVSGSIRlhgkellglsdhamsqirgrmiGTVFQDPM 99
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIR----------------------GTVAYVPQ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 100 SALTPVYTIGDQIAEAIEIHSREISRA---DARRRAVELLElvGIAQPERRARAFphELSGGERQRVVIAIAIANDPDLL 176
Cdd:PLN03130 687 VSWIFNATVRDNILFGSPFDPERYERAidvTALQHDLDLLP--GGDLTEIGERGV--NISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 177 ICDEPTTALDVTVQAQILD-VLRtaRDVTGAAVLIITHDLGVVSEfADRALVMYAGRPVEIAAVDEL 242
Cdd:PLN03130 763 IFDDPLSALDAHVGRQVFDkCIK--DELRGKTRVLVTNQLHFLSQ-VDRIILVHEGMIKEEGTYEEL 826
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
381-585 |
9.06e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.72 E-value: 9.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQIL-ELTKPEaGSIEILGTDVAVLDAAARRRLRTELQVVFQDPvasLDPrlP 459
Cdd:TIGR00957 655 NGITFSIPEGALVAVVGQVGCGKSSLLSALLaEMDKVE-GHVHMKGSVAYVPQQAWIQNDSLRENILFGKA---LNE--K 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 460 VYDVIAEPlrangfhrheCEeRVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQA 539
Cdd:TIGR00957 729 YYQQVLEA----------CA-LLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1424538268 540 GIVNLLLDLQRRF-GLSYLFVSHDLSVVKHLaHRVAVMYRGMIVEQG 585
Cdd:TIGR00957 798 HIFEHVIGPEGVLkNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
390-583 |
9.95e-08 |
|
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: 53.37 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 390 GRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAaarRRLRTELQVVFQDPVA-------SLDPRLPVYD 462
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPL---HTLRSRLSIILQDPILfsgsirfNLDPECKCTD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 463 -VIAEPLRangfhrheceerVAELLAVV-----GLDhSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVS 536
Cdd:cd03288 124 dRLWEALE------------IAQLKNMVkslpgGLD-AVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 537 IQagivNLlldLQRRFGLSYLfvshDLSVVKhLAHRVA---------VMYRGMIVE 583
Cdd:cd03288 191 TE----NI---LQKVVMTAFA----DRTVVT-IAHRVStildadlvlVLSRGILVE 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
383-538 |
1.03e-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: 55.30 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEaGSIEILGTDvavLDAAARRRLRTELQVVFQDpvasldprlpVYd 462
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVS---WNSVTLQTWRKAFGVIPQK----------VF- 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 463 VIAEPLRAN--GFHRHECEE--RVAEllaVVGLdHSDASRYPAE-----------FSGGQKQRIGIARALALQPKILALD 527
Cdd:TIGR01271 1303 IFSGTFRKNldPYEQWSDEEiwKVAE---EVGL-KSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLD 1378
|
170
....*....|..
gi 1424538268 528 EPVSALD-VSIQ 538
Cdd:TIGR01271 1379 EPSAHLDpVTLQ 1390
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-236 |
1.46e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.22 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 33 PGEVLAIVGESGCGKTTAALAVIGLLPEYARVSgsirlhgkellglsdhamsqirgrmigtvfqdpmsaltpVYTIGDQI 112
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV---------------------------------------IYIDGEDI 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 113 AEAIEIHSREISRADarrravellelvgiaqperraraFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQ 192
Cdd:smart00382 42 LEEVLDQLLLIIVGG-----------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAL 98
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1424538268 193 ILDVLRTARDV-----TGAAVLIITHDlgvVSEFADRALVMYAGRPVEI 236
Cdd:smart00382 99 LLLLEELRLLLllkseKNLTVILTTND---EKDLGPALLRRRFDRRIVL 144
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
382-589 |
1.71e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 54.28 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNqilELTKPEAGSIEILGTDVAVLDAAARRRLRTELQVVFQDPVasLDPRLPVY 461
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMN---ALAFRSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDL--FIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 D--VIAEPLRangFHRH----ECEERVAELLAVVGLDHSDASRYPAE-----FSGGQKQRIGIARALALQPKILALDEPV 530
Cdd:TIGR00955 118 EhlMFQAHLR---MPRRvtkkEKRERVDEVLQALGLRKCANTRIGVPgrvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 531 SALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSV-VKHLAHRVAVMYRGMIVEQGESDQ 589
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQPSSeLFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
381-551 |
1.99e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.12 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQIleltkpeAGSIEILGTDVAVL--DAAARRRLRTELQVVFQDPVasLDPRL 458
Cdd:PLN03211 85 NGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQGNNFTGTILanNRKPTKQILKRTGFVTQDDI--LYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 459 PVYD--VIAEPLRANGFHRHECEERVAE-LLAVVGLDHSDASRYPAEF----SGGQKQRIGIARALALQPKILALDEPVS 531
Cdd:PLN03211 156 TVREtlVFCSLLRLPKSLTKQEKILVAEsVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180
....*....|....*....|
gi 1424538268 532 ALDVSIQAGIVNLLLDLQRR 551
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQK 255
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
383-589 |
3.59e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDA-----------AARRR---LRTELQVVFQ 448
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAneainhgfalvTEERRstgIYAYLDIGFN 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 449 DPVASLDPRLPVYDVIAEplrangfHRHECEER-VAELLAVVGLDHSDASrypAEFSGGQKQRIGIARALALQPKILALD 527
Cdd:PRK10982 347 SLISNIRNYKNKVGLLDN-------SRMKSDTQwVIDSMRVKTPGHRTQI---GSLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 528 EPVSALDVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGM---IVEQGESDQ 589
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLvagIVDTKTTTQ 480
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-195 |
3.63e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 53.76 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 22 PAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGllpEYARVSGSIRLHGKelLGLSdhamSQIRGRMIGTvfqdpmsa 101
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMG---ELEPSEGKIKHSGR--ISFS----PQTSWIMPGT-------- 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 102 ltpvytIGDQIAEAIeihsreiSRADARRRAVellelVGIAQPERRARAFPHE-----------LSGGERQRVVIAIAIA 170
Cdd:TIGR01271 503 ------IKDNIIFGL-------SYDEYRYTSV-----IKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVY 564
|
170 180
....*....|....*....|....*
gi 1424538268 171 NDPDLLICDEPTTALDVTVQAQILD 195
Cdd:TIGR01271 565 KDADLYLLDSPFTHLDVVTEKEIFE 589
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-220 |
3.98e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.96 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 25 RGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYArvsGSIRLHGKELLGLSDHamsqirgrmigtvFQDPM----- 99
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDA---GEVLWQGEPIRRQRDE-------------YHQDLlylgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 100 -----SALTPVYTIgdQIAEAIeihSREISRADARrravELLELVGIAqpeRRARAFPHELSGGERQRVVIAIAIANDPD 174
Cdd:PRK13538 82 qpgikTELTALENL--RFYQRL---HGPGDDEALW----EALAQVGLA---GFEDVPVRQLSAGQQRRVALARLWLTRAP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1424538268 175 LLICDEPTTALDVTVQAQILDVLR--TARdvtGAAVLIITH-DLGVVSE 220
Cdd:PRK13538 150 LWILDEPFTAIDKQGVARLEALLAqhAEQ---GGMVILTTHqDLPVASD 195
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-245 |
4.56e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 19 IEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYARVSGSIRlhgkellglsdhamsqirgrmiGTVFQDP 98
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIR----------------------GSVAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 99 MSALTPVYTIGDQIAEAIEIHSREISRA-DARRRAVELLELVGIAQPERRARAFphELSGGERQRVVIAIAIANDPDLLI 177
Cdd:PLN03232 686 QVSWIFNATVRENILFGSDFESERYWRAiDVTALQHDLDLLPGRDLTEIGERGV--NISGGQKQRVSMARAVYSNSDIYI 763
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 178 CDEPTTALDVTVQAQILDVLrTARDVTGAAVLIITHDLGVVSEFaDRALVMYAGRPVEIAAVDELYRD 245
Cdd:PLN03232 764 FDDPLSALDAHVAHQVFDSC-MKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
28-214 |
4.62e-07 |
|
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: 52.63 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 28 SYHIDPGEVLAIVGESGCGKTTAALAVIGL-LPEyarvSGSIRLHGKELLGLSDhamsQIRgrmigtvfqdpmSALTPVY 106
Cdd:TIGR03719 342 SFKLPPGGIVGVIGPNGAGKSTLFRMITGQeQPD----SGTIEIGETVKLAYVD----QSR------------DALDPNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 107 TIGDQIAEA---IEIHSREI-SRADARR---RAVELLELVGiaqperrarafphELSGGERQRVVIAIAIANDPDLLICD 179
Cdd:TIGR03719 402 TVWEEISGGldiIKLGKREIpSRAYVGRfnfKGSDQQKKVG-------------QLSGGERNRVHLAKTLKSGGNVLLLD 468
|
170 180 190
....*....|....*....|....*....|....*.
gi 1424538268 180 EPTTALDV-TVQAqildvLRTARDVTGAAVLIITHD 214
Cdd:TIGR03719 469 EPTNDLDVeTLRA-----LEEALLNFAGCAVVISHD 499
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
31-234 |
5.69e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 31 IDPGEVLAIVGESGCGKTTAALAVIGLLPEYAR-VSGSIRLHGkelLGLSDhAMSQIRGRMIgtvfqdpMSALT----PV 105
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIgVEGVITYDG---ITPEE-IKKHYRGDVV-------YNAETdvhfPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 106 YTIGDQIAEAIEIHSRE-----ISRADARRRAVEL-LELVG--IAQPERRARAFPHELSGGERQRVVIAIAIANDPDLLI 177
Cdd:TIGR00956 153 LTVGETLDFAARCKTPQnrpdgVSREEYAKHIADVyMATYGlsHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1424538268 178 CDEPTTALDVTVQAQILDVLRTARDVTGAAVLII-------THDLgvvseFaDRALVMYAGRPV 234
Cdd:TIGR00956 233 WDNATRGLDSATALEFIRALKTSANILDTTPLVAiyqcsqdAYEL-----F-DKVIVLYEGYQI 290
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
155-228 |
6.02e-07 |
|
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: 50.01 E-value: 6.02e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 155 LSGGERQRVVIA--IAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEfADRALVM 228
Cdd:cd03238 88 LSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLID-LGNTVILIEHNLDVLSS-ADWIIDF 161
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
382-586 |
7.32e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.95 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTtLNQIL---ELTKPEAGSIEILGTDVavLDAAARRRLRTELQVVFQDPVASldprl 458
Cdd:PRK09580 19 GLNLEVRPGEVHAIMGPNGSGKST-LSATLagrEDYEVTGGTVEFKGKDL--LELSPEDRAGEGIFMAFQYPVEI----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 459 pvydviaePLRANGFHRHECEERVAELLAVVGLDHSDASRYPAE-------------------FSGGQKQRIGIARALAL 519
Cdd:PRK09580 91 --------PGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEkiallkmpedlltrsvnvgFSGGEKKRNDILQMAVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 520 QPKILALDEPVSALDV---SIQAGIVNLLLDLQRrfglSYLFVSHDLSVVKHLA-HRVAVMYRGMIVEQGE 586
Cdd:PRK09580 163 EPELCILDESDSGLDIdalKIVADGVNSLRDGKR----SFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGD 229
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-231 |
8.29e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 8.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 33 PGEVLAIVGESGCGKTTaalaVIGLLPEyaRVSGSIRLHGKELLGlsDHAMSQIRGRMIGTVFQ-DPMSALTPVytigdq 111
Cdd:TIGR00956 788 PGTLTALMGASGAGKTT----LLNVLAE--RVTTGVITGGDRLVN--GRPLDSSFQRSIGYVQQqDLHLPTSTV------ 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 112 iAEAIEIHSR-----EISRADARRRAVELLELVGIaqpERRARAF---PHE-LSGGERQRVVIAIAIANDPDLLI-CDEP 181
Cdd:TIGR00956 854 -RESLRFSAYlrqpkSVSKSEKMEYVEEVIKLLEM---ESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 182 TTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVV--SEFaDRALVMYAG 231
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKLAD-HGQAILCTIHQPSAIlfEEF-DRLLLLQKG 979
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
383-593 |
1.01e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.05 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQIL-ELTKPEAGSIEILGTdVA-------VLDAAARRrlrtelQVVFQDPVasl 454
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLgELPPRSDASVVIRGT-VAyvpqvswIFNATVRD------NILFGSPF--- 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 455 dprlpvydviaEPLRANGFHRHECEERVAELLAvvGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALD 534
Cdd:PLN03130 706 -----------DPERYERAIDVTALQHDLDLLP--GGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 535 VSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLaHRVAVMYRGMIVEQGESDQVFTN 593
Cdd:PLN03130 773 AHVGRQVFDKCIKDELR-GKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
381-573 |
1.15e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEilGTDVAVLDAAArrrlrtelqvvfQDPVASLDPRLPV 460
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK--WSENANIGYYA------------QDHAYDFENDLTL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDVIAEplrangfHRHEC--EERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDV-SI 537
Cdd:PRK15064 402 FDWMSQ-------WRQEGddEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMeSI 474
|
170 180 190
....*....|....*....|....*....|....*.
gi 1424538268 538 QAgiVNLLLDLqrrFGLSYLFVSHDLSVVKHLAHRV 573
Cdd:PRK15064 475 ES--LNMALEK---YEGTLIFVSHDREFVSSLATRI 505
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
11-228 |
1.30e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 11 NVTFETE---DIEVpaVRGTSYHIDPGEVLAIVGESGCGKTTAaLAVIGLLpeYARVSGSIRLHGKEllGLSDHAMSQIR 87
Cdd:PTZ00265 387 NVRFHYDtrkDVEI--YKDLNFTLTEGKTYAFVGESGCGKSTI-LKLIERL--YDPTEGDIIINDSH--NLKDINLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 88 GRmIGTVFQDPM--------SALTPVYTIGDqiAEAIEIHSRE---ISRADARRR-------------------AVELL- 136
Cdd:PTZ00265 460 SK-IGVVSQDPLlfsnsiknNIKYSLYSLKD--LEALSNYYNEdgnDSQENKNKRnscrakcagdlndmsnttdSNELIe 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 137 -----------ELVGIAQP---ERRARAFP-----------HELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQA 191
Cdd:PTZ00265 537 mrknyqtikdsEVVDVSKKvliHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
|
250 260 270
....*....|....*....|....*....|....*..
gi 1424538268 192 QILDVLRTARDVTGAAVLIITHDLGVVsEFADRALVM 228
Cdd:PTZ00265 617 LVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVL 652
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
382-567 |
1.39e-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: 48.86 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 382 GISFTLEQGRTLGIVGESGSGKSTTLNQILEltkpeagsieilgtdvavldAAARRRLRTELQVVFQDPVASLDprlpvy 461
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY--------------------ASGKARLISFLPKFSRNKLIFID------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 dviaePLRAngfhrheceervaelLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPK--ILALDEPVSALDVSIQA 539
Cdd:cd03238 67 -----QLQF---------------LIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180
....*....|....*....|....*...
gi 1424538268 540 GIVNLLLDLqRRFGLSYLFVSHDLSVVK 567
Cdd:cd03238 127 QLLEVIKGL-IDLGNTVILIEHNLDVLS 153
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-242 |
1.43e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 22 PAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLpEYARvsGSIRLHGKEL--LGLSDhamsqIRgRMIGTVFQDPM 99
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIV-ELEK--GRIMIDDCDVakFGLTD-----LR-RVLSIIPQSPV 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 100 SALTPVYTIGDQIAEAIEIHSRE-ISRA---DARRRAVELLElvgiAQPERRARAFphelSGGERQRVVIAIAIANDPDL 175
Cdd:PLN03232 1321 LFSGTVRFNIDPFSEHNDADLWEaLERAhikDVIDRNPFGLD----AEVSEGGENF----SVGQRQLLSLARALLRRSKI 1392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 176 LICDEPTTALDVTVQAQILDVLRtaRDVTGAAVLIITHDLGVVSEfADRALVMYAGRPVEIAAVDEL 242
Cdd:PLN03232 1393 LVLDEATASVDVRTDSLIQRTIR--EEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQEL 1456
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-227 |
1.52e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEDiEVPAVRGTSYHIDPGEVLAIVGESGCGKTTaalaVIGLLPEY----------------------- 61
Cdd:PTZ00265 1166 IEIMDVNFRYISRP-NVPIYKDLTFSCDSKKTTAIVGETGSGKST----VMSLLMRFydlkndhhivfknehtndmtneq 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 62 --------------------------ARVSGSIRLHGKELL---GLSDHAMSQIRGrMIGTVFQDPMSALTPVYtigdqi 112
Cdd:PTZ00265 1241 dyqgdeeqnvgmknvnefsltkeggsGEDSTVFKNSGKILLdgvDICDYNLKDLRN-LFSIVSQEPMLFNMSIY------ 1313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 113 aEAIEIHSREISRADARRRAV-----ELLELVGiAQPERRARAFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDV 187
Cdd:PTZ00265 1314 -ENIKFGKEDATREDVKRACKfaaidEFIESLP-NKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1391
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1424538268 188 TVQAQILDVLRTARDVTGAAVLIITHDLGVVSEfADRALV 227
Cdd:PTZ00265 1392 NSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1430
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-242 |
1.62e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 22 PAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHGKEL--LGLSDhamsqIRgRMIGTVFQDP 98
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVeLE----RGRILIDGCDIskFGLMD-----LR-KVLGIIPQAP 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 99 M-------SALTPVYTIGD-QIAEAIE-IHSREISRADARRRAVELLELvgiaqperrarafPHELSGGERQRVVIAIAI 169
Cdd:PLN03130 1323 VlfsgtvrFNLDPFNEHNDaDLWESLErAHLKDVIRRNSLGLDAEVSEA-------------GENFSVGQRQLLSLARAL 1389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1424538268 170 ANDPDLLICDEPTTALDVTVQAQILDVLRtaRDVTGAAVLIITHDLGVVSEfADRALVMYAGRPVEIAAVDEL 242
Cdd:PLN03130 1390 LRRSKILVLDEATAAVDVRTDALIQKTIR--EEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENL 1459
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
389-570 |
1.68e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.14 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 389 QGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRTELqvvfqdpvasldprlpvydviaepl 468
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 469 rangfhrheceervaellavvgldhsdasRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGI-----VN 543
Cdd:smart00382 56 -----------------------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLR 106
|
170 180
....*....|....*....|....*..
gi 1424538268 544 LLLDLQRRFGLSYLFVSHDLSVVKHLA 570
Cdd:smart00382 107 LLLLLKSEKNLTVILTTNDEKDLGPAL 133
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-231 |
1.71e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.55 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 22 PAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGllpEYARVSGSIRLHGKELLGlsdhAMSQIRGRMigtvfqdpmsA 101
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG---DTTVTSGDATVAGKSILT----NISDVHQNM----------G 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 102 LTPVYTIGDQIaeaieIHSREISRADARRRAVELLELVGIAQ-----------PERRARAFphelSGGERQRVVIAIAIA 170
Cdd:TIGR01257 2016 YCPQFDAIDDL-----LTGREHLYLYARLRGVPAEEIEKVANwsiqslglslyADRLAGTY----SGGNKRKLSTAIALI 2086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 171 NDPDLLICDEPTTALDVTVQAQ----ILDVLRTARdvtgaAVLIITHDLGVVSEFADRALVMYAG 231
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMlwntIVSIIREGR-----AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
381-606 |
1.96e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGIsftLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTDVAVLDAAARRRLRTElqVVFqdpVASLDPRLPV 460
Cdd:TIGR00956 81 DGL---IKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGITPEEIKKHYRGD--VVY---NAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDViAEPL-----------RANGFHRHECEERVAEL-LAVVGLDHSDASRYPAEF----SGGQKQRIGIARALALQPKIL 524
Cdd:TIGR00956 153 LTV-GETLdfaarcktpqnRPDGVSREEYAKHIADVyMATYGLSHTRNTKVGNDFvrgvSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 525 ALDEPVSALDVSIQAGIVNlLLDLQRRFGLSYLFV-----SHDlsvVKHLAHRVAVMYRGMIVEQGESDQV--------F 591
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIR-ALKTSANILDTTPLVaiyqcSQD---AYELFDKVIVLYEGYQIYFGPADKAkqyfekmgF 307
|
250
....*....|....*
gi 1424538268 592 TNPQHEYTRRLLAAV 606
Cdd:TIGR00956 308 KCPDRQTTADFLTSL 322
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-246 |
2.28e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 24 VRGTSYHIDPGEVLAIVGESGCGKTTaalavigLLPEYARV----SGSIRLHGKEllgLSDHAMSQIRgRMIGTVFQDPM 99
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKST-------LLLTFMRMvevcGGEIRVNGRE---IGAYGLRELR-RQFSMIPQDPV 1394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 100 SALTPVYTIGDQIAEAieiHSREISRAdarrravelLELVGIAQP--------ERRARAFPHELSGGERQRVVIAIA-IA 170
Cdd:PTZ00243 1395 LFDGTVRQNVDPFLEA---SSAEVWAA---------LELVGLRERvasesegiDSRVLEGGSNYSVGQRQLMCMARAlLK 1462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 171 NDPDLLICDEPTTALDVTVQAQILDVLRTArdVTGAAVLIITHDLGVVSEFaDRALVMYAGRPVEIAAVDELYRDR 246
Cdd:PTZ00243 1463 KGSGFILMDEATANIDPALDRQIQATVMSA--FSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
381-535 |
2.35e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.55 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGT--------DVAVLDAAA----------RRRLRTE 442
Cdd:PRK10636 18 DNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnqETPALPQPAleyvidgdreYRQLEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 443 LQVVFQ----DPVASLDPRLPVYDviAEPLRAngfhrheceeRVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALA 518
Cdd:PRK10636 98 LHDANErndgHAIATIHGKLDAID--AWTIRS----------RAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALI 165
|
170
....*....|....*..
gi 1424538268 519 LQPKILALDEPVSALDV 535
Cdd:PRK10636 166 CRSDLLLLDEPTNHLDL 182
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
5-251 |
2.56e-06 |
|
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: 49.14 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 5 LEVTDLNVTFETEdiEVPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPEYarvSGSIRLHGKELLGLSDHAMs 84
Cdd:cd03288 20 IKIHDLCVRYENN--LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF---DGKIVIDGIDISKLPLHTL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 85 qiRGRMiGTVFQDPMsaltpvytigdQIAEAIEIH-SREISRADARrraveLLELVGIAQPERRARAFPHEL-------- 155
Cdd:cd03288 94 --RSRL-SIILQDPI-----------LFSGSIRFNlDPECKCTDDR-----LWEALEIAQLKNMVKSLPGGLdavvtegg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 156 ---SGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTArdVTGAAVLIITHDLGVVSEfADRALVMYAGR 232
Cdd:cd03288 155 enfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTA--FADRTVVTIAHRVSTILD-ADLVLVLSRGI 231
|
250
....*....|....*....
gi 1424538268 233 PVEIAAVDELYRDRRMPYT 251
Cdd:cd03288 232 LVECDTPENLLAQEDGVFA 250
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
383-528 |
2.64e-06 |
|
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: 50.18 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEIlgtDVAVLDAAARRRLRTELQVVFQDPVasLDPRLPVYD 462
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL---DGQPVTADNREAYRQLFSAVFSDFH--LFDRLLGLD 425
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1424538268 463 VIAEPlrangfhrheceERVAELLAVVGLDH---------SDasrypAEFSGGQKQRIGIARALALQPKILALDE 528
Cdd:COG4615 426 GEADP------------ARARELLERLELDHkvsvedgrfST-----TDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
29-213 |
3.69e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.31 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 29 YHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHGKellglsdHAMSQIRGRMIGTVFQDPmsALTPVYT 107
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLhVE----SGQIQIDGK-------TATRGDRSRFMAYLGHLP--GLKADLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 108 IGDQIAEAIEIHSREisradARRRAVELLELVGIAQPErraRAFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDV 187
Cdd:PRK13543 99 TLENLHFLCGLHGRR-----AKQMPGSALAIVGLAGYE---DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
170 180
....*....|....*....|....*.
gi 1424538268 188 TvQAQILDVLRTARDVTGAAVLIITH 213
Cdd:PRK13543 171 E-GITLVNRMISAHLRGGGAALVTTH 195
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
153-229 |
3.84e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.35 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 153 HELSGGERQRVVIAIAIA----NDPDLLICDEPTTALDVTVQAQILDVLRtARDVTGAAVLIITHDLGVVsEFADRALVM 228
Cdd:cd03227 76 LQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAIL-EHLVKGAQVIVITHLPELA-ELADKLIHI 153
|
.
gi 1424538268 229 Y 229
Cdd:cd03227 154 K 154
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
31-569 |
4.41e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 31 IDPGEVLAIVGESGCGKTTaalaVIGLLP-EYARVSGSIRLHGKELLGLSDHAMSQIRGRMIGTV------FQDPMSALT 103
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKST----LLALLKnEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVidgdreYRQLEAQLH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 104 PVYTIGDQIAEAIeIHSR--EISRADARRRAVELLELVGIAQP--ERRARAFphelSGGERQRVVIAIAIANDPDLLICD 179
Cdd:PRK10636 100 DANERNDGHAIAT-IHGKldAIDAWTIRSRAASLLHGLGFSNEqlERPVSDF----SGGWRMRLNLAQALICRSDLLLLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 180 EPTTALDvtvqaqiLDVL----RTARDVTGAAVLiITHDLGVVSEFADRALvmyagrPVEIAAVDElyrdrrmpYTvgll 255
Cdd:PRK10636 175 EPTNHLD-------LDAViwleKWLKSYQGTLIL-ISHDRDFLDPIVDKII------HIEQQSLFE--------YT---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 256 GSVPRLDAAQGTRLipipgapPTMTSLSPGACTFAPRCPLAIDEcLSAEPDLVRVADGHWAACIRTDDVAGRSAADVFGV 335
Cdd:PRK10636 229 GNYSSFEVQRATRL-------AQQQAMYESQQERVAHLQSYIDR-FRAKATKAKQAQSRIKMLERMELIAPAHVDNPFHF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 336 STQPPPNnaaggQPPVVLRVSDLTKTYrltkgvvvrrrvGEVRAVDGISFTLEQGRTLGIVGESGSGKSTtlnqileLTK 415
Cdd:PRK10636 301 SFRAPES-----LPNPLLKMEKVSAGY------------GDRIILDSIKLNLVPGSRIGLLGRNGAGKST-------LIK 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 416 PEAGSIEILGTDVAV-----LDAAARRRLrtELQVVFQDPVASLDPRLPvydviaeplrangfhrHECEERVAELLAVVG 490
Cdd:PRK10636 357 LLAGELAPVSGEIGLakgikLGYFAQHQL--EFLRADESPLQHLARLAP----------------QELEQKLRDYLGGFG 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 491 LDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDlqrrFGLSYLFVSHDlsvvKHL 569
Cdd:PRK10636 419 FQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALID----FEGALVVVSHD----RHL 489
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
582-608 |
5.33e-06 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 44.31 E-value: 5.33e-06
10 20
....*....|....*....|....*..
gi 1424538268 582 VEQGESDQVFTNPQHEYTRRLLAAVPR 608
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPR 27
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
154-218 |
7.25e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.99 E-value: 7.25e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 154 ELSGGERQRVVIAIAI---ANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVV 218
Cdd:cd03271 169 TLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVD-KGNTVVVIEHNLDVI 235
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
383-583 |
7.57e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.81 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKStTLNQILE-LTKPEAGSIEIlgtDVAVLDAAARRRLRTELQVVFQDpvasldprlpvY 461
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKS-TLAMLLTgLYQPQSGEILL---DGKPVTAEQPEDYRKLFSAVFTD-----------F 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 DVIAEPLRANGFHRHecEERVAELLAVVGLDH----SDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSI 537
Cdd:PRK10522 407 HLFDQLLGPEGKPAN--PALVEKWLERLKMAHklelEDGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1424538268 538 QAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHlAHRVAVMYRGMIVE 583
Cdd:PRK10522 485 RREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
351-562 |
8.41e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 8.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 351 VVLRVSDLTKTY--RLtkgvvvrrrvgevrAVDGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEIlGTDV 428
Cdd:PRK11819 323 KVIEAENLSKSFgdRL--------------LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 429 avldaaarrrlrtELQVVFQDPvASLDPRLPVYDVIAE------------PLRAN----GFHRHECEERVAELlavvgld 492
Cdd:PRK11819 388 -------------KLAYVDQSR-DALDPNKTVWEEISGgldiikvgnreiPSRAYvgrfNFKGGDQQKKVGVL------- 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 493 hsdasrypaefSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDlqrrFGLSYLFVSHD 562
Cdd:PRK11819 447 -----------SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLE----FPGCAVVISHD 501
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
383-561 |
9.33e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.15 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGTdvavldaAARRRLRTELqVVFQDPVASLDPRLpvyD 462
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK-------TATRGDRSRF-MAYLGHLPGLKADL---S 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 463 VIAEPLRANGFHRHECEERVAELLAVVGL-DHSDAsrYPAEFSGGQKQRIGIARaLALQPKIL-ALDEPVSALDVSiqaG 540
Cdd:PRK13543 99 TLENLHFLCGLHGRRAKQMPGSALAIVGLaGYEDT--LVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLDLE---G 172
|
170 180
....*....|....*....|...
gi 1424538268 541 I--VNLLLDLQRRFGLSYLFVSH 561
Cdd:PRK13543 173 ItlVNRMISAHLRGGGAALVTTH 195
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
155-218 |
9.54e-06 |
|
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: 48.86 E-value: 9.54e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 155 LSGGERQRVVIAIAI---ANDPDLLICDEPTTAL---DVtvqAQILDVLRTARDvTGAAVLIITHDLGVV 218
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLhfdDI---KKLLEVLQRLVD-KGNTVVVIEHNLDVI 895
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
383-541 |
1.27e-05 |
|
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: 48.37 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIEILGtdvavldaaarrRLRTELQVVFQDPVASLDPRL--PV 460
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------RISFSPQTSWIMPGTIKDNIIfgLS 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 461 YDviaeplrangfhrhecEERVAELLAVVGLDHsDASRYPAE-----------FSGGQKQRIGIARALALQPKILALDEP 529
Cdd:TIGR01271 513 YD----------------EYRYTSVIKACQLEE-DIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 575
|
170
....*....|..
gi 1424538268 530 VSALDVSIQAGI 541
Cdd:TIGR01271 576 FTHLDVVTEKEI 587
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
38-225 |
1.55e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.06 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 38 AIVGESGCGKTTAALAVigllpEYArVSGSIRLHGKELLGLSDHAMSQIRGRMIGTVFQDPMSALTPVYTIGDQIAEAIE 117
Cdd:cd03240 26 LIVGQNGAGKTTIIEAL-----KYA-LTGELPPNSKGGAHDPKLIREGEVRAQVKLAFENANGKKYTITRSLAILENVIF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 118 IHSREIsradarrrAVELLELVGiaqperrarafphELSGGERQRVVIAIAIA------NDPDLLICDEPTTALDV-TVQ 190
Cdd:cd03240 100 CHQGES--------NWPLLDMRG-------------RCSGGEKVLASLIIRLAlaetfgSNCGILALDEPTTNLDEeNIE 158
|
170 180 190
....*....|....*....|....*....|....*
gi 1424538268 191 AQILDVLRTARDVTGAAVLIITHDlgvvSEFADRA 225
Cdd:cd03240 159 ESLAEIIEERKSQKNFQLIVITHD----EELVDAA 189
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
383-562 |
2.24e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIeilgtdvavldaaaRRRLRTELQVVFQDPVASLDprlpvyd 462
Cdd:PLN03073 528 LNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV--------------FRSAKVRMAVFSQHHVDGLD------- 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 463 VIAEPLrangFHRHEC-----EERVAELLAVVGLDHSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDV-S 536
Cdd:PLN03073 587 LSSNPL----LYMMRCfpgvpEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLdA 662
|
170 180
....*....|....*....|....*.
gi 1424538268 537 IQAGIVNLLLdlqrrFGLSYLFVSHD 562
Cdd:PLN03073 663 VEALIQGLVL-----FQGGVLMVSHD 683
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-234 |
2.83e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.53 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 33 PGEVLAIVGESGCGKTTAaLAVIGLLPEYARVSGSIRLHGKEllglsdhAMSQIRGRMIGTVFQDPMSalTPVYTIGDQ- 111
Cdd:PLN03140 905 PGVLTALMGVSGAGKTTL-MDVLAGRKTGGYIEGDIRISGFP-------KKQETFARISGYCEQNDIH--SPQVTVRESl 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 112 IAEAIEIHSREISRADARRRAVELLELVGIAQPERRARAFP--HELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTV 189
Cdd:PLN03140 975 IYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1424538268 190 QAQILDVLRTARDvTGAAVLIITHDLGV-VSEFADRALVMYAGRPV 234
Cdd:PLN03140 1055 AAIVMRTVRNTVD-TGRTVVCTIHQPSIdIFEAFDELLLMKRGGQV 1099
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
155-214 |
4.22e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 4.22e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 155 LSGGERQRVVIAIAIANDPDLLICDEPTTALDvtvqAQILDVL-RTARDVTGaAVLIITHD 214
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLeQFLHDYPG-TVVAVTHD 219
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
155-243 |
4.29e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.56 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 155 LSGGERQRVVIA---IAIANDPDLLICDEPTTAL---DVtvqAQILDVLRTARDvTGAAVLIITHDLGVVSEfAD----- 223
Cdd:COG0178 827 LSGGEAQRVKLAselSKRSTGKTLYILDEPTTGLhfhDI---RKLLEVLHRLVD-KGNTVVVIEHNLDVIKT-ADwiidl 901
|
90 100
....*....|....*....|....*....
gi 1424538268 224 ---------RalVMYAGRPVEIAAVDELY 243
Cdd:COG0178 902 gpeggdgggE--IVAEGTPEEVAKVKASY 928
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
581-608 |
6.29e-05 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 41.96 E-value: 6.29e-05
10 20
....*....|....*....|....*...
gi 1424538268 581 IVEQGESDQVFTNPQHEYTRRLLAAVPR 608
Cdd:TIGR01727 2 IVETGPAEEIFKNPLHPYTKALLSAIPT 29
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
31-238 |
6.66e-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: 45.94 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 31 IDPGEVLAIVGESGCGKTTAALAVIGLlpeYARVSGSIRLHGKEllgLSDHAMSQIRgRMIGTVFQDpmsaltpvYTIGD 110
Cdd:COG4615 355 IRRGELVFIVGGNGSGKSTLAKLLTGL---YRPESGEILLDGQP---VTADNREAYR-QLFSAVFSD--------FHLFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 111 QIAeaieihsrEISRADARRRAVELLELVGIA-QPERRARAF-PHELSGGERQRVVIAIAIANDPDLLICDEptTALDvt 188
Cdd:COG4615 420 RLL--------GLDGEADPARARELLERLELDhKVSVEDGRFsTTDLSQGQRKRLALLVALLEDRPILVFDE--WAAD-- 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 189 vQ---------AQILDVLRtARdvtGAAVLIITHD---LGVvsefADRALVMYAGRPVEIAA 238
Cdd:COG4615 488 -QdpefrrvfyTELLPELK-AR---GKTVIAISHDdryFDL----ADRVLKMDYGKLVELTG 540
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-213 |
7.44e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.17 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 4 VLEVTDLNVTFETEdievPAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLL-PEyarvSGSIRLHGKELlgLSDHA 82
Cdd:PRK13540 1 MLDVIELDFDYHDQ----PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLnPE----KGEILFERQSI--KKDLC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 83 MSQIRGRMIGTvfqdpMSALTPVYTIGDQIAEAIEIHSreisradarrRAVELLELVGIAQPERRARAFPHELSGGERQR 162
Cdd:PRK13540 71 TYQKQLCFVGH-----RSGINPYLTLRENCLYDIHFSP----------GAVGITELCRLFSLEHLIDYPCGLLSSGQKRQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 163 VVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLRTARdVTGAAVLIITH 213
Cdd:PRK13540 136 VALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHR-AKGGAVLLTSH 185
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
34-242 |
8.74e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 34 GEVLAIVGESGCGKTTAALAVIGLLPEyarVSGSIRLHGKELL-----GLSDH--AMSQIRGRMIGTVF-QDPMSALTPv 105
Cdd:PRK13546 50 GDVIGLVGINGSGKSTLSNIIGGSLSP---TVGKVDRNGEVSViaisaGLSGQltGIENIEFKMLCMGFkRKEIKAMTP- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 106 ytigdqiaEAIEIHsreisradarrravELLELvgIAQPERRarafpheLSGGERQRVVIAIAIANDPDLLICDEPTTAL 185
Cdd:PRK13546 126 --------KIIEFS--------------ELGEF--IYQPVKK-------YSSGMRAKLGFSINITVNPDILVIDEALSVG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 186 DVTVQAQILDVLRTARDvTGAAVLIITHDLGVVSEFADRALVMYAGRPVEIAAVDEL 242
Cdd:PRK13546 175 DQTFAQKCLDKIYEFKE-QNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
502-577 |
9.30e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.33 E-value: 9.30e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424538268 502 EFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAHRVAVMY 577
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
383-587 |
1.08e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKSTTLNQIL---ELTKPE---AGSIEILGTDVAVLDAAARRrlrtelQVVFQDPVASLDp 456
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLsqfEISEGRvwaERSIAYVPQQAWIMNATVRG------NILFFDEEDAAR- 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 457 rlpvydvIAEPLRANgfhrhECEERVAELLAvvGLDhSDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVS 536
Cdd:PTZ00243 752 -------LADAVRVS-----QLEADLAQLGG--GLE-TEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 537 IQAGIVNLLLdLQRRFGLSYLFVSHDLSVVKHLAHRVAvMYRGMIVEQGES 587
Cdd:PTZ00243 817 VGERVVEECF-LGALAGKTRVLATHQVHVVPRADYVVA-LGDGRVEFSGSS 865
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
395-571 |
2.52e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.96 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 395 IVGESGSGKSTTLNQILeltkpeagsieilgtdVAVLDAAARRRLRTELQvvfqdpvasldPRLPVYDVIAEPLrangfh 474
Cdd:cd03227 26 ITGPNGSGKSTILDAIG----------------LALGGAQSATRRRSGVK-----------AGCIVAAVSAELI------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 475 rheceervaelLAVVGLdhsdasrypaefSGGQKQRIGIARALALQPK----ILALDEPVSALD---VSIQAGIVNLLLD 547
Cdd:cd03227 73 -----------FTRLQL------------SGGEKELSALALILALASLkprpLYILDEIDRGLDprdGQALAEAILEHLV 129
|
170 180
....*....|....*....|....
gi 1424538268 548 LQRRFglsyLFVSHDLSVVKHLAH 571
Cdd:cd03227 130 KGAQV----IVITHLPELAELADK 149
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
155-218 |
3.30e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 3.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 155 LSGGERQRVVIA---IAIANDPDLLICDEPTTALDVTVQAQILDVLRTARDvTGAAVLIITHDLGVV 218
Cdd:PRK00635 810 LSGGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTH-QGHTVVIIEHNMHVV 875
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
381-534 |
5.98e-04 |
|
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: 42.61 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 381 DGISFTLEQGRTLGIVGESGSGKSTTLNQILELTKPEAGSIeILGTDVAV--------LDAAARRRLRTELQVvfQDPVA 452
Cdd:TIGR03719 22 KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA-RPQPGIKVgylpqepqLDPTKTVRENVEEGV--AEIKD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 453 SLDPRLPVYDVIAEP-----------------LRANGFHRHECEERVAellavvgldhSDASRYP------AEFSGGQKQ 509
Cdd:TIGR03719 99 ALDRFNEISAKYAEPdadfdklaaeqaelqeiIDAADAWDLDSQLEIA----------MDALRCPpwdadvTKLSGGERR 168
|
170 180
....*....|....*....|....*
gi 1424538268 510 RIGIARALALQPKILALDEPVSALD 534
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
383-585 |
6.26e-04 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.47 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 383 ISFTLEQGRTLGIVGESGSGKST----TL-----------------NQILELTKPEAGSIEILGTDVAVLDAAARRRLRT 441
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSlafdTIyaegqrryveslsayarQFLGQMDKPDVDSIEGLSPAIAIDQKTTSRNPRS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 442 ELQVVFQdpvasldprlpVYDViaepLRANgFHRHECEERVAELLAVvGLDHSDASRYPAEFSGGQKQRIGIARAL--AL 519
Cdd:cd03270 94 TVGTVTE-----------IYDY----LRLL-FARVGIRERLGFLVDV-GLGYLTLSRSAPTLSGGEAQRIRLATQIgsGL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1424538268 520 QPKILALDEPVSALDVSIQAGIVNLLLDLqRRFGLSYLFVSHDLSVVKHLAHRV-----AVMYRGMIVEQG 585
Cdd:cd03270 157 TGVLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRAADHVIdigpgAGVHGGEIVAQG 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
384-590 |
7.92e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 384 SFTLEQGRTLGIVGESGSGKSTtLNQIL--ELTkPEAGSIEILGTDVAVLD--------AAARRRLRTELQVVFQDpvas 453
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSA-LARALagELP-LLSGERQSQFSHITRLSfeqlqklvSDEWQRNNTDMLSPGED---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 454 lDPRLPVYDVIAEPLRANgfhrheceERVAELLAVVGLDHSDASRYpAEFSGGQKQRIGIARALALQPKILALDEPVSAL 533
Cdd:PRK10938 97 -DTGRTTAEIIQDEVKDP--------ARCEQLAQQFGITALLDRRF-KYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1424538268 534 DVSIQAGIVNLLLDLQRRfGLSYLFVSHDLSVVKHLAHRVAVMYRGMIVEQGESDQV 590
Cdd:PRK10938 167 DVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
384-571 |
8.14e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.05 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 384 SFTLEQGRTLgIVGESGSGKSTTLNQILELTKPEAgsieILGTDVAVLDA--AARRRLRTELQVVFQDpvasldprlpvy 461
Cdd:cd03240 17 EIEFFSPLTL-IVGQNGAGKTTIIEALKYALTGEL----PPNSKGGAHDPklIREGEVRAQVKLAFEN------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 462 dviaeplrANGfHRHECEERVAELLAVVGLdHSDASRYPAE-----FSGGQKQ------RIGIARALALQPKILALDEPV 530
Cdd:cd03240 80 --------ANG-KKYTITRSLAILENVIFC-HQGESNWPLLdmrgrCSGGEKVlasliiRLALAETFGSNCGILALDEPT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1424538268 531 SALDV-SIQAGIVNLLLDLQRRFGLSYLFVSHDLSVVKHLAH 571
Cdd:cd03240 150 TNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADH 191
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
155-222 |
9.84e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 9.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424538268 155 LSGGERQRVVIAIAIA------NDPDLLICDEPTTALDVTVQAQILDVLR-TARDVTG-AAVLIITH--DLGVVSEFA 222
Cdd:PRK01156 802 LSGGEKTAVAFALRVAvaqflnNDKSLLIMDEPTAFLDEDRRTNLKDIIEySLKDSSDiPQVIMISHhrELLSVADVA 879
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
155-218 |
1.73e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 1.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 155 LSGGERQRVVIAIAI---ANDPDLLICDEPTTAL---DVtvqAQILDVLRTARDvTGAAVLIITHDLGVV 218
Cdd:PRK00349 831 LSGGEAQRVKLAKELskrSTGKTLYILDEPTTGLhfeDI---RKLLEVLHRLVD-KGNTVVVIEHNLDVI 896
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
154-214 |
2.38e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.87 E-value: 2.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1424538268 154 ELSGGERQRVVIAIAIANDPDLLICDEPTTALDV-TVQAqildvLRTARDVTGAAVLIITHD 214
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVeTLRA-----LEEALLEFPGCAVVISHD 501
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-186 |
3.53e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.38 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 22 PAVRGTSYHIDPGEVLAIVGESGCGKTTAALAVIGLLPE-YarvSGSIRLHGKELlGlSDHAMSQIRgRMIGTVfqdpMS 100
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQgY---SNDLTLFGRRR-G-SGETIWDIK-KHIGYV----SS 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 101 ALTPVYTIGDQIAEAI---EIHSREISRA--DARRR-AVELLELVGIAqpERRARAFPHELSGGERQRVVIAIAIANDPD 174
Cdd:PRK10938 344 SLHLDYRVSTSVRNVIlsgFFDSIGIYQAvsDRQQKlAQQWLDILGID--KRTADAPFHSLSWGQQRLALIVRALVKHPT 421
|
170
....*....|..
gi 1424538268 175 LLICDEPTTALD 186
Cdd:PRK10938 422 LLILDEPLQGLD 433
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
155-232 |
6.11e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.84 E-value: 6.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1424538268 155 LSGGERQRVVIAIAIANDPDLLICDEPTTALDV-TVQAQILDVLrtardVTGAAVLIITHDLGVVSEFADRALVMYAGR 232
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLdAVEALIQGLV-----LFQGGVLMVSHDEHLISGSVDELWVVSEGK 701
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
124-224 |
7.53e-03 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.39 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 124 SRADARRRAVELLEL-VGIAQPERRARAfpheLSGGERQRVVIAIAIANDPD--LLICDEPTTALDVTVQAQILDVLRTA 200
Cdd:cd03270 110 ARVGIRERLGFLVDVgLGYLTLSRSAPT----LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRL 185
|
90 100
....*....|....*....|....
gi 1424538268 201 RDVtGAAVLIITHDLGVVSEfADR 224
Cdd:cd03270 186 RDL-GNTVLVVEHDEDTIRA-ADH 207
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
155-237 |
8.33e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.38 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424538268 155 LSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQIL-DVLRTArdVTGAAVLIITHDLGVVSEfADRALVMYAGRp 233
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVeECFLGA--LAGKTRVLATHQVHVVPR-ADYVVALGDGR- 858
|
....
gi 1424538268 234 VEIA 237
Cdd:PTZ00243 859 VEFS 862
|
|
|