|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-623 |
0e+00 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 1217.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 1 MPHSDELDASDVLAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLL 80
Cdd:PRK10261 1 MPHSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 81 RRRNRQVIELGEQSASQMRHVRGADIAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEAKA 160
Cdd:PRK10261 81 RRRSRQVIELSEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 161 ILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVL 240
Cdd:PRK10261 161 ILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 241 VMYQGEAVETGSVEQIFHAPQHPYTKALLAAVPQLGAMNGHELPRRFPLISLHDPSHVEPQTEQDTVVEGEPILRVRNLV 320
Cdd:PRK10261 241 VMYQGEAVETGSVEQIFHAPQHPYTRALLAAVPQLGAMKGLDYPRRFPLISLEHPAKQEPPIEQDTVVDGEPILQVRNLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 321 TRFPLRSGILNRVTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQPLR 400
Cdd:PRK10261 321 TRFPLRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 401 RDIQFIFQDPYASLDPRQTVGYSILEPLRVHGLLQGDAGSKRVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALAL 480
Cdd:PRK10261 401 RDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALAL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 481 NPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQHPYT 560
Cdd:PRK10261 481 NPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYT 560
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 561 RKLMAAVPVADPSHHRPQRVLLSDDIPSNIRKRGEEISPVSLQLVGPGHYVARPLPENALSRL 623
Cdd:PRK10261 561 RKLMAAVPVADPSRQRPQRVLLSDDLPSNIHLRGEEVAAVSLQCVGPGHYVAQPQSEYAFMRR 623
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-571 |
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: 823.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVScDEMLLRRRnrqviELG 91
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPS-GSILFDGQ-----DLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 EQSASQMRHVRGADIAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEAKAILSRYPHQLSG 171
Cdd:COG4172 80 GLSERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 252 SVEQIFHAPQHPYTKALLAAVPQLgamnghelprrfplislhDPSHVEPqteqdtvvEGEPILRVRNLVTRFPLRSGILN 331
Cdd:COG4172 240 PTAELFAAPQHPYTRKLLAAEPRG------------------DPRPVPP--------DAPPLLEARDLKVWFPIKRGLFR 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 332 RVTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQrGEIIFNGQRIDTLAASKLQPLRRDIQFIFQDPY 411
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 412 ASLDPRQTVGYSILEPLRVHGL-LQGDAGSKRVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADES 490
Cdd:COG4172 373 GSLSPRMTVGQIIAEGLRVHGPgLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEP 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 491 VSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQHPYTRKLMAAVPVA 570
Cdd:COG4172 453 TSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPLL 532
|
.
gi 949724212 571 D 571
Cdd:COG4172 533 E 533
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-573 |
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: 706.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 10 SDVLAVSNLNIAFEQeqQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGgevscdemllrRRNRQVIE 89
Cdd:COG1123 2 TPLLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGG-----------RISGEVLL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 90 LGEQSASQMRHVRGADIAMIFQEPMTSLNPVfTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIPeakAILSRYPHQL 169
Cdd:COG1123 69 DGRDLLELSEALRGRRIGMVFQDPMTQLNPV-TVGDQIAEALEN-LGLSRAEARARVLELLEAVGLE---RRLDRYPHQL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVE 249
Cdd:COG1123 144 SGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 250 TGSVEQIFHAPQhpytkaLLAAVPQLGAMNGHELPRRfplislhdpshvepqteqdtvVEGEPILRVRNLVTRFPLRSGi 329
Cdd:COG1123 224 DGPPEEILAAPQ------ALAAVPRLGAARGRAAPAA---------------------AAAEPLLEVRNLSKRYPVRGK- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 330 lnrvtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQPLRRDIQFIFQD 409
Cdd:COG1123 276 -----GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQD 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 410 PYASLDPRQTVGYSILEPLRVHGLLQGDAGSKRVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
Cdd:COG1123 351 PYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDE 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 490 SVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQHPYTRKLMAAVPV 569
Cdd:COG1123 431 PTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAAVPS 510
|
....
gi 949724212 570 ADPS 573
Cdd:COG1123 511 LDPA 514
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-565 |
0e+00 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 550.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 9 ASDVLAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNrqvi 88
Cdd:PRK15134 2 TQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGES---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 89 eLGEQSASQMRHVRGADIAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEAKAILSRYPHQ 168
Cdd:PRK15134 78 -LLHASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAV 248
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 249 ETGSVEQIFHAPQHPYTKALLAAVPQlgamnGHELPrrfplislhdpshvepqTEQDTvvegEPILRVRNLVTRFPLRSG 328
Cdd:PRK15134 237 EQNRAATLFSAPTHPYTQKLLNSEPS-----GDPVP-----------------LPEPA----SPLLDVEQLQVAFPIRKG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 329 ILNRVTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQrGEIIFNGQRIDTLAASKLQPLRRDIQFIFQ 408
Cdd:PRK15134 291 ILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQLLPVRHRIQVVFQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 409 DPYASLDPRQTVGYSILEPLRVH-GLLQGDAGSKRVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIA 487
Cdd:PRK15134 370 DPNSSLNPRLNVLQIIEEGLRVHqPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIIL 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 488 DESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQHPYTRKLMA 565
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
309-619 |
1.54e-170 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 488.09 E-value: 1.54e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 309 EGEPILRVRNLVTRFPLRSGILNRVTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRI 388
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 389 DTLAASKLQPLRRDIQFIFQDPYASLDPRQTVGYSILEPLRVHGLLQGDAGSKRVAWLLERVGLLPEHAWRYPHEFSGGQ 468
Cdd:COG4608 83 TGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 469 RQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTR 548
Cdd:COG4608 163 RQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 549 RAVFENPQHPYTRKLMAAVPVADPSHHRpQRVLLSDDIPSNI-----------------RKRGEEisPVsLQLVGPGHYV 611
Cdd:COG4608 243 DELYARPLHPYTQALLSAVPVPDPERRR-ERIVLEGDVPSPLnppsgcrfhtrcpyaqdRCATEE--PP-LREVGPGHQV 318
|
....*...
gi 949724212 612 ARPLPENA 619
Cdd:COG4608 319 ACHLAEEG 326
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-277 |
3.62e-144 |
|
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: 420.61 E-value: 3.62e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIE---QAGGEVscdemLLRRRNrqvi 88
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEI-----LFDGED---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 89 eLGEQSASQMRHVRGADIAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEAKAILSRYPHQ 168
Cdd:COG0444 72 -LLKLSEKELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAV 248
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
250 260
....*....|....*....|....*....
gi 949724212 249 ETGSVEQIFHAPQHPYTKALLAAVPQLGA 277
Cdd:COG0444 231 EEGPVEELFENPRHPYTRALLSSIPRLDP 259
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
313-612 |
5.75e-141 |
|
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: 412.52 E-value: 5.75e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 313 ILRVRNLVTRFPLRSGilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQR---GEIIFNGQRID 389
Cdd:COG0444 1 LLEVRNLKVYFPTRRG-------VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 390 TLAASKLQPLR-RDIQFIFQDPYASLDPRQTVGYSILEPLRVHGLLQGDAGSKRVAWLLERVGLLP--EHAWRYPHEFSG 466
Cdd:COG0444 74 KLSEKELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 467 GQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 547 TRRAVFENPQHPYTRKLMAAVPVADPSHHRpqRVLLSDDIPSNI---------------RKRGEEISPVsLQLVGPGHYV 611
Cdd:COG0444 234 PVEELFENPRHPYTRALLSSIPRLDPDGRR--LIPIPGEPPSLLnppsgcrfhprcpyaMDRCREEEPP-LREVGPGHRV 310
|
.
gi 949724212 612 A 612
Cdd:COG0444 311 A 311
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
310-588 |
1.64e-113 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 342.71 E-value: 1.64e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 310 GEPILRVRNLVTRFPLRSGILnRVTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQriD 389
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVKRGLF-KPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQ--D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 390 TLAASK--LQPLRRDIQFIFQDPYASLDPRQTVGYSILEPLRVHGLLQGDAGSKRVAWLLERVGLLPEHAWRYPHEFSGG 467
Cdd:PRK11308 79 LLKADPeaQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 468 QRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGT 547
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 949724212 548 RRAVFENPQHPYTRKLMAAVPVADPSHHRPqRVLLSDDIPS 588
Cdd:PRK11308 239 KEQIFNNPRHPYTQALLSATPRLNPDDRRE-RIKLTGELPS 278
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
306-590 |
2.93e-112 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 339.37 E-value: 2.93e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 306 TVVEGEPILRVRNLVTRFPLRSG--ILNRVTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIF 383
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDIKDGkqWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 384 NGQRIDTLAASKLQPLRRDIQFIFQDPYASLDPRQTVGYSILEPLRV-HGLLQGDAGSKRVAWLLERVGLLPEHAWRYPH 462
Cdd:PRK15079 81 LGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 463 EFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 949724212 543 VEIGTRRAVFENPQHPYTRKLMAAVPVADPSHHRPQRV-LLSDDIPSNI 590
Cdd:PRK15079 241 VELGTYDEVYHNPLHPYTKALMSAVPIPDPDLERNKTIqLLEGELPSPI 289
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
313-546 |
2.12e-111 |
|
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: 333.32 E-value: 2.12e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 313 ILRVRNLVTRFPLRSGilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLA 392
Cdd:cd03257 1 LLEVKNLSVSFPTGGG-------SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 393 ASKLQPLRRDIQFIFQDPYASLDPRQTVGYSILEPLRVHGLLQGDAGSKRVAWL-LERVGLLPEHAWRYPHEFSGGQRQR 471
Cdd:cd03257 74 RRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLlLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 472 ICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
9-284 |
5.13e-111 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 336.31 E-value: 5.13e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 9 ASDVLAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAG---GEVscdemllRRRNR 85
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSA-------TFNGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 86 QVIELGEQsasQMRHVRGADIAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEAKAILSRY 165
Cdd:PRK09473 82 EILNLPEK---ELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQG 245
Cdd:PRK09473 159 PHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 949724212 246 EAVETGSVEQIFHAPQHPYTKALLAAVPQLGAmNGHELP 284
Cdd:PRK09473 239 RTMEYGNARDVFYQPSHPYSIGLLNAVPRLDA-EGESLL 276
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-251 |
2.26e-106 |
|
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: 320.22 E-value: 2.26e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDemllrrrNRQVIELG 91
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFD-------GKDLLKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 EQsasqMRHVRGADIAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASHEEAMvEAKRMLDQVRIPEAKAILSRYPHQLSG 171
Cdd:cd03257 74 RR----LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEAR-KEAVLLLLVGVGLPEEVLNRYPHELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
314-568 |
8.56e-103 |
|
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: 312.12 E-value: 8.56e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFPLRSgilnrvtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdTLAA 393
Cdd:COG1124 2 LEVRNLSVSYGQGG-------RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV-TRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 SKlqPLRRDIQFIFQDPYASLDPRQTVGYSILEPLRVHGLLQGDAgskRVAWLLERVGLLPEHAWRYPHEFSGGQRQRIC 473
Cdd:COG1124 74 RK--AFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREE---RIAELLEQVGLPPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 474 IARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFE 553
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
250
....*....|....*
gi 949724212 554 NPQHPYTRKLMAAVP 568
Cdd:COG1124 229 GPKHPYTRELLAASL 243
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
311-583 |
2.33e-99 |
|
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: 313.16 E-value: 2.33e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFplRSGilnrvTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQ----RGEIIFNGQ 386
Cdd:COG4172 4 MPLLSVEDLSVAF--GQG-----GGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 387 RIDTLAASKLQPLR-RDIQFIFQDPYASLDPRQTVGYSILEPLRVHGLLQGDAGSKRVAWLLERVGLlPEHAWR---YPH 462
Cdd:COG4172 77 DLLGLSERELRRIRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGI-PDPERRldaYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 463 EFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 949724212 543 VEIGTRRAVFENPQHPYTRKLMAAVPVADPSHHRP-QRVLLS 583
Cdd:COG4172 236 VEQGPTAELFAAPQHPYTRKLLAAEPRGDPRPVPPdAPPLLE 277
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
12-277 |
2.86e-97 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 300.51 E-value: 2.86e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGgEVSCDEMLLRRRNRQVIelg 91
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPG-RVMAEKLEFNGQDLQRI--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 eqSASQMRHVRGADIAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEAKAILSRYPHQLSG 171
Cdd:PRK11022 79 --SEKERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
250 260
....*....|....*....|....*.
gi 949724212 252 SVEQIFHAPQHPYTKALLAAVPQLGA 277
Cdd:PRK11022 237 KAHDIFRAPRHPYTQALLRALPEFAQ 262
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
311-566 |
3.27e-94 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 290.59 E-value: 3.27e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPLRSGILNRvtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDT 390
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGLFRR--QQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 391 laaSKLQPLRRDIQFIFQDPYASLDPRQTVGySILE-PLRVHGLLQGDAGSKRVAWLLERVGLLPEHAWRYPHEFSGGQR 469
Cdd:COG4167 80 ---GDYKYRCKHIRMIFQDPNTSLNPRLNIG-QILEePLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 470 QRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRR 549
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTA 235
|
250
....*....|....*..
gi 949724212 550 AVFENPQHPYTRKLMAA 566
Cdd:COG4167 236 EVFANPQHEVTKRLIES 252
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-273 |
8.22e-89 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 278.92 E-value: 8.22e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 22 FEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEmllrrrnrqvIELGEQSASQMRHV 101
Cdd:COG4608 24 FGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG----------QDITGLSGRELRPL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 102 RgADIAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEAKAilSRYPHQLSGGMRQRVMIAM 181
Cdd:COG4608 94 R-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHA--DRYPHEFSGGQRQRIGIAR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQ 261
Cdd:COG4608 171 ALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPL 250
|
250
....*....|..
gi 949724212 262 HPYTKALLAAVP 273
Cdd:COG4608 251 HPYTQALLSAVP 262
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-277 |
1.11e-82 |
|
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: 260.12 E-value: 1.11e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRqvielge 92
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRR------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 93 qsasqmRHVRGaDIAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASHEEamvEAKRMLDQVRIPEAkaILSRYPHQLSGG 172
Cdd:COG1124 75 ------KAFRR-RVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREE---RIAELLEQVGLPPS--FLDRYPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGS 252
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELT 222
|
250 260
....*....|....*....|....*
gi 949724212 253 VEQIFHAPQHPYTKALLAAVPQLGA 277
Cdd:COG1124 223 VADLLAGPKHPYTRELLAASLAFER 247
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
12-273 |
3.12e-81 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 259.25 E-value: 3.12e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFE---------QEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVscdeMLLRR 82
Cdd:PRK15079 8 LLEVADLKVHFDikdgkqwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEV----AWLGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 83 rnrqviELGEQSASQMRHVRgADIAMIFQEPMTSLNPVFTVGEQIAESIRLHQ-GASHEEAMVEAKRMLDQVRI-PEaka 160
Cdd:PRK15079 84 ------DLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHpKLSRQEVKDRVKAMMLKVGLlPN--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 161 ILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVL 240
Cdd:PRK15079 154 LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 233
|
250 260 270
....*....|....*....|....*....|...
gi 949724212 241 VMYQGEAVETGSVEQIFHAPQHPYTKALLAAVP 273
Cdd:PRK15079 234 VMYLGHAVELGTYDEVYHNPLHPYTKALMSAVP 266
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
31-271 |
1.24e-76 |
|
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: 243.43 E-value: 1.24e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLlrrRNRQVIELGeqsasqmrhVRGADIAMIF 110
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILL---DGRPLLPLS---------IRGRHIATIM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEPMTSLNPVFTVGEQIAESIRLHqGASHEEAMVEAKRMLDQVRIPEAKAILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:TIGR02770 69 QNPRTAFNPLFTMGNHAIETLRSL-GKLSKQARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 191 IADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQHPYTKALLA 270
Cdd:TIGR02770 148 IADEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227
|
.
gi 949724212 271 A 271
Cdd:TIGR02770 228 A 228
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
13-293 |
1.43e-74 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 241.73 E-value: 1.43e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGgEVSCDEMLLRRrnrqvIELGE 92
Cdd:COG4170 4 LDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNW-HVTADRFRWNG-----IDLLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 93 QSASQMRHVRGADIAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASH-----EEAMVEAKRMLDQVRIPEAKAILSRYPH 167
Cdd:COG4170 78 LSPRERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrfKWRKKRAIELLHRVGIKDHKDIMNSYPH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEA 247
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQT 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 949724212 248 VETGSVEQIFHAPQHPYTKALLAAVPQLgamnGHELPRRFPLISLH 293
Cdd:COG4170 238 VESGPTEQILKSPHHPYTKALLRSMPDF----RQPLPHKSRLNTLP 279
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
311-580 |
2.44e-73 |
|
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: 244.43 E-value: 2.44e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPlrsgilnrvTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQ---RGEIIFNGQr 387
Cdd:COG1123 2 TPLLEVRDLSVRYP---------GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGR- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 388 iDTLAASkLQPLRRDIQFIFQDPYASLDPrQTVGYSILEPLRVHGLLQGDAGsKRVAWLLERVGLlPEHAWRYPHEFSGG 467
Cdd:COG1123 72 -DLLELS-EALRGRRIGMVFQDPMTQLNP-VTVGDQIAEALENLGLSRAEAR-ARVLELLEAVGL-ERRLDRYPHQLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 468 QRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGT 547
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
250 260 270
....*....|....*....|....*....|...
gi 949724212 548 RRAVFENPQhpytrkLMAAVPVADPSHHRPQRV 580
Cdd:COG1123 227 PEEILAAPQ------ALAAVPRLGAARGRAAPA 253
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
26-286 |
2.81e-70 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 230.24 E-value: 2.81e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 26 QQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTAlSLMHLIEQ-AGGEvscdemlLRRRNRQVIELGEQSASQMRHvrga 104
Cdd:PRK11308 25 ERLVKALDGVSFTLERGKTLAVVGESGCGKSTLA-RLLTMIETpTGGE-------LYYQGQDLLKADPEAQKLLRQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 105 DIAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRI-PEAkaiLSRYPHQLSGGMRQRVMIAMAL 183
Cdd:PRK11308 93 KIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEH---YDRYPHMFSGGQRQRIAIARAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQHP 263
Cdd:PRK11308 170 MLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHP 249
|
250 260
....*....|....*....|...
gi 949724212 264 YTKALLAAVPQLgamngHELPRR 286
Cdd:PRK11308 250 YTQALLSATPRL-----NPDDRR 267
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
313-576 |
2.63e-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: 225.84 E-value: 2.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 313 ILRVRNLVTRFplRSGILNRVTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLA 392
Cdd:TIGR02769 2 LLEVRDVTHTY--RTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 393 ASKLQPLRRDIQFIFQDPYASLDPRQTVGYSILEPLRVHGLLQGDAGSKRVAWLLERVGLLPEHAWRYPHEFSGGQRQRI 472
Cdd:TIGR02769 80 RKQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 473 CIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEiGTRRAVF 552
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE-ECDVAQL 238
|
250 260
....*....|....*....|....
gi 949724212 553 ENPQHPYTRKLMAAVPVADPSHHR 576
Cdd:TIGR02769 239 LSFKHPAGRNLQSAVLPEHPVRRS 262
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
311-571 |
8.16e-67 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 221.52 E-value: 8.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPLRSGIlnrvtreVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQ---RGEIIFNGQR 387
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGD-------VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 388 IDTLAASKLQPLR-RDIQFIFQDPYASLDPRQTVGYSILEPLRVH-GLLQGDAGSKRVAwLLERVGLlPEHAWR---YPH 462
Cdd:PRK09473 83 ILNLPEKELNKLRaEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHkGMSKAEAFEESVR-MLDAVKM-PEARKRmkmYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 463 EFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 240
|
250 260
....*....|....*....|....*....
gi 949724212 543 VEIGTRRAVFENPQHPYTRKLMAAVPVAD 571
Cdd:PRK09473 241 MEYGNARDVFYQPSHPYSIGLLNAVPRLD 269
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
311-566 |
1.28e-66 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 218.89 E-value: 1.28e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPLRSGILNRvtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRidt 390
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGWFRR--QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 391 LAASKLQPLRRDIQFIFQDPYASLDPRQTVGYSILEPLRVHGLLQGDAGSKRVAWLLERVGLLPEHAWRYPHEFSGGQRQ 470
Cdd:PRK15112 77 LHFGDYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 471 RICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRA 550
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTAD 236
|
250
....*....|....*.
gi 949724212 551 VFENPQHPYTRKLMAA 566
Cdd:PRK15112 237 VLASPLHELTKRLIAG 252
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
312-572 |
3.33e-65 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 214.94 E-value: 3.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 312 PILRVRNLVTRFPLRSGILNRVTREVhaVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTL 391
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGLSGKHQHQTV--LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 392 AASKLQPLRRDIQFIFQDPYASLDPRQTVGYSILEPLRvHGLLQGDAG-SKRVAWLLERVGLLPEHAWRYPHEFSGGQRQ 470
Cdd:PRK10419 80 NRAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLR-HLLSLDKAErLARASEMLRAVDLDDSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 471 RICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEigtRRA 550
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE---TQP 235
|
250 260
....*....|....*....|....
gi 949724212 551 VFENP--QHPYTRKLMAAVPVADP 572
Cdd:PRK10419 236 VGDKLtfSSPAGRVLQNAVLPAFP 259
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
12-272 |
5.48e-65 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 214.29 E-value: 5.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEqaggEVSCDEMLLRRRNRQVIELG 91
Cdd:COG4107 8 LLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKS-TLLKCLYFDL----APTSGSVYYRDRDGGPRDLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 EQSASQMRHVRGADIAMIFQEPMTSLNPVFTVGEQIAESIrLHQGASHEEAM-VEAKRMLDQVRIPeakaiLSR---YPH 167
Cdd:COG4107 83 ALSEAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAERL-MAAGERHYGDIrARALEWLERVEIP-----LERiddLPR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEA 247
Cdd:COG4107 157 TFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRV 236
|
250 260
....*....|....*....|....*
gi 949724212 248 VETGSVEQIFHAPQHPYTKALLAAV 272
Cdd:COG4107 237 VESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
313-580 |
1.34e-63 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 213.02 E-value: 1.34e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 313 ILRVRNLVTRFPLRSGilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTtgraLLRLV----ESQRGEIIFNGQRI 388
Cdd:COG1135 1 MIELENLSKTFPTKGG-------PVTALDDVSLTIEKGEIFGIIGYSGAGKST----LIRCInlleRPTSGSVLVDGVDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 389 DTLAASKLQPLRRDIQFIFQDpyASLDPRQTVGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLlPEHAWRYPHEFSGGQ 468
Cdd:COG1135 70 TALSERELRAARRKIGMIFQH--FNLLSSRTVAENVALPLEIAGVPKAEI-RKRVAELLELVGL-SDKADAYPSQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 469 RQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTR 548
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPV 225
|
250 260 270
....*....|....*....|....*....|..
gi 949724212 549 RAVFENPQHPYTRKLMAAVPVADPSHHRPQRV 580
Cdd:COG1135 226 LDVFANPQSELTRRFLPTVLNDELPEELLARL 257
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
32-271 |
9.87e-62 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 205.32 E-value: 9.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 32 VRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEqAGgevscdemlLRRRNRQVIELGEQSASQmrHVRGADIAMIFQ 111
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILP-AG---------VRQTAGRVLLDGKPVAPC--ALRGRKIATIMQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 112 EPMTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAkrmLDQVRIPEAKAILSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
Cdd:PRK10418 87 NPRSAFNPLHTMHTHARETCLALGKPADDATLTAA---LEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 192 ADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQHPYTKALLAA 271
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
10-286 |
1.61e-61 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 205.07 E-value: 1.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 10 SDVLAVSNLNIAFE-----QEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRN 84
Cdd:COG4167 2 SALLEVRNLSKTFKyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 85 RQVielgeqsasQMRHVRgadiaMIFQEPMTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRI-PEAKAIls 163
Cdd:COG4167 82 YKY---------RCKHIR-----MIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLlPEHANF-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 164 rYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMY 243
Cdd:COG4167 146 -YPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMH 224
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 949724212 244 QGEAVETGSVEQIFHAPQHPYTKALLAAvpQLGAMNGHELPRR 286
Cdd:COG4167 225 QGEVVEYGKTAEVFANPQHEVTKRLIES--HFGEALTADAWRR 265
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-270 |
2.50e-60 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 209.95 E-value: 2.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 8 DASDVLAVSNLNIAFEQEQ---QRV----SAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIeQAGGEVSCDEMLL 80
Cdd:PRK15134 271 PASPLLDVEQLQVAFPIRKgilKRTvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 81 RRRNRQvielgeqsasQMRHVRgADIAMIFQEPMTSLNPVFTVGEQIAESIRLHQ---GASHEEAMVeaKRMLDQVRI-P 156
Cdd:PRK15134 350 HNLNRR----------QLLPVR-HRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQptlSAAQREQQV--IAVMEEVGLdP 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 157 EAKailSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIA 236
Cdd:PRK15134 417 ETR---HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALC 493
|
250 260 270
....*....|....*....|....*....|....
gi 949724212 237 DRVLVMYQGEAVETGSVEQIFHAPQHPYTKALLA 270
Cdd:PRK15134 494 HQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
312-572 |
1.66e-58 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 204.94 E-value: 1.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 312 PILRVRNLVTRFplRSGilnRVTREVhaVENVSFDLWPGETLSLVGESGCGKSTTGRALLRL-----VESQRGEIIFNGQ 386
Cdd:PRK15134 4 PLLAIENLSVAF--RQQ---QTVRTV--VNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 387 RIDTLAASKLQPLRRD-IQFIFQDPYASLDPRQTVGYSILEPLRVHGLLQGDAGSKRVAWLLERVGLlpEHAWR----YP 461
Cdd:PRK15134 77 SLLHASEQTLRGVRGNkIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGI--RQAAKrltdYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 462 HEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQ 541
Cdd:PRK15134 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
250 260 270
....*....|....*....|....*....|.
gi 949724212 542 IVEIGTRRAVFENPQHPYTRKLMAAVPVADP 572
Cdd:PRK15134 235 CVEQNRAATLFSAPTHPYTQKLLNSEPSGDP 265
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
339-568 |
3.76e-58 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 198.43 E-value: 3.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVE----SQRGEIIFNGQRIDTLAASKLQPL-RRDIQFIFQDPYAS 413
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERRNLvGAEVAMIFQDPMTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 414 LDPRQTVGYSILEPLRVHgllQGdaGSK-----RVAWLLERVGLlPEHAWR---YPHEFSGGQRQRICIARALALNPKVI 485
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVH---QG--GNKktrrqRAIDLLNQVGI-PDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 486 IADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQHPYTRKLMA 565
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLR 255
|
...
gi 949724212 566 AVP 568
Cdd:PRK11022 256 ALP 258
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
310-561 |
1.61e-57 |
|
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: 193.66 E-value: 1.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 310 GEPILRVRNLVTRFplrsGilnrvTREVHavENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRID 389
Cdd:COG1127 2 SEPMIEVRNLTKSF----G-----DRVVL--DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 390 TLAASKLQPLRRDIQFIFQDP--YASLdprqTVGYSILEPLRVHGLLQGDAGSKRVAWLLERVGlLPEHAWRYPHEFSGG 467
Cdd:COG1127 71 GLSEKELYELRRRIGMLFQGGalFDSL----TVFENVAFPLREHTDLSEAEIRELVLEKLELVG-LPGAADKMPSELSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 468 QRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGT 547
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
250
....*....|....
gi 949724212 548 RRAVFENPqHPYTR 561
Cdd:COG1127 226 PEELLASD-DPWVR 238
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
312-559 |
1.96e-57 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 197.24 E-value: 1.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 312 PILRVRNLVTRFPlrsgilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTL 391
Cdd:COG3842 4 PALELENVSKRYG-----------DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 392 AASKlqplrRDIQFIFQDpYAsLDP----RQTVGYsilePLRVHGLLQGDAgSKRVAWLLERVGLlPEHAWRYPHEFSGG 467
Cdd:COG3842 73 PPEK-----RNVGMVFQD-YA-LFPhltvAENVAF----GLRMRGVPKAEI-RARVAELLELVGL-EGLADRYPHQLSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 468 QRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHD----MAvverISHRVAVMYLGQIV 543
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRIAVMNDGRIE 215
|
250
....*....|....*.
gi 949724212 544 EIGTRRAVFENPQHPY 559
Cdd:COG3842 216 QVGTPEEIYERPATRF 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
335-556 |
8.25e-57 |
|
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: 191.64 E-value: 8.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 335 REVHAVENVSFDLWPGETLSLVGESGCGKSTtgraLLRLVE----SQRGEIIFNGQRIDTLAASKLQPLRRDIQFIFQDp 410
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKST----LIRCINglerPTSGSVLVDGTDLTLLSGKELRKARRRIGMIFQH- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 411 YASLDPRqTVGYSILEPLRVHGLLQGDAGsKRVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADES 490
Cdd:cd03258 91 FNLLSSR-TVFENVALPLEIAGVPKAEIE-ERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 491 VSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQ 556
Cdd:cd03258 168 TSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
334-567 |
2.06e-55 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 191.55 E-value: 2.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 334 TREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQPLRRDIQFIFQdpYAS 413
Cdd:PRK11153 15 GRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQ--HFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 414 LDPRQTVGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSA 493
Cdd:PRK11153 93 LLSSRTVFDNVALPLELAGTPKAEI-KARVTELLELVGL-SDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 949724212 494 LDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQHPYTRKLMAAV 567
Cdd:PRK11153 171 LDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQST 244
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
314-561 |
4.08e-53 |
|
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: 181.55 E-value: 4.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFplrsGilnrvTREVHavENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAA 393
Cdd:cd03261 1 IELRGLTKSF----G-----GRTVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 SKLQPLRRDIQFIFQDP--YASLDPRQTVGYsilePLRVHGLLQGDAGSKRVAWLLERVGLLPEHAwRYPHEFSGGQRQR 471
Cdd:cd03261 70 AELYRLRRRMGMLFQSGalFDSLTVFENVAF----PLREHTRLSEEEIREIVLEKLEAVGLRGAED-LYPAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 472 ICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAV 551
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
250
....*....|
gi 949724212 552 FeNPQHPYTR 561
Cdd:cd03261 225 R-ASDDPLVR 233
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
12-325 |
8.41e-53 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 184.24 E-value: 8.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHlIEQAGGEVSCDEMllrRRNRqvIELG 91
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRM---RFDD--IDLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 EQSASQMRHVRGADIAMIFQEPMTSLNPVFTVGEQIAESIR--LHQGASHEEAMVEAKR---MLDQVRIPEAKAILSRYP 166
Cdd:PRK15093 77 RLSPRERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPgwTYKGRWWQRFGWRKRRaieLLHRVGIKDHKDAMRSFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGE 246
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 247 AVETGSVEQIFHAPQHPYTKALLAAVPQLGAMNGHE-----LPRRFPLISlHDP--SHVEPQT--EQDTVVEGEPILRVR 317
Cdd:PRK15093 237 TVETAPSKELVTTPHHPYTQALIRAIPDFGSAMPHKsrlntLPGAIPLLE-HLPigCRLGPRCpyAQRECIETPRLTGAK 315
|
330
....*....|
gi 949724212 318 N--LVTRFPL 325
Cdd:PRK15093 316 NhlYACHFPL 325
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
29-545 |
1.21e-52 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 188.30 E-value: 1.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSvTalsLMHLI---EQA-GGEVSCDEMLLRRRN-RQVIELGeqsasqmrhvrg 103
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKS-T---LMKILsgvYQPdSGEILLDGEPVRFRSpRDAQAAG------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 104 adIAMIFQEPmtSLNPVFTVgeqiAESIRLHQ-----GASHEEAMV-EAKRMLDQVRIPE-AKAILSRyphqLSGGMRQR 176
Cdd:COG1129 81 --IAIIHQEL--NLVPNLSV----AENIFLGReprrgGLIDWRAMRrRARELLARLGLDIdPDTPVGD----LSVAQQQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQI 256
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 257 fhapqhpyTKALLAAvpqlgAMNGHELPRRFPlislhdPSHVEPqteqdtvveGEPILRVRNLVTRfplrsgilnrvtre 336
Cdd:COG1129 228 --------TEDELVR-----LMVGRELEDLFP------KRAAAP---------GEVVLEVEGLSVG-------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 337 vHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTlaASKLQPLRRDIQF---------IF 407
Cdd:COG1129 266 -GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRI--RSPRDAIRAGIAYvpedrkgegLV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 408 QDpyasLDPRQTVGYSILEPLRVHGLLQGDAGSKRVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIA 487
Cdd:COG1129 343 LD----LSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLIL 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 488 DESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIVEI 545
Cdd:COG1129 419 DEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGE 475
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
314-542 |
1.46e-52 |
|
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: 179.61 E-value: 1.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFPLRSgilnrvtREVHAVENVSFDLWPGETLSLVGESGCGKSTtgraLLRLV----ESQRGEIIFNGQRID 389
Cdd:cd03255 1 IELKNLSKTYGGGG-------EKVQALKGVSLSIEKGEFVAIVGPSGSGKST----LLNILggldRPTSGEVRVDGTDIS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 390 TLAASKLQPLRRD-IQFIFQDPYasLDPRQTVGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLlPEHAWRYPHEFSGGQ 468
Cdd:cd03255 70 KLSEKELAAFRRRhIGFVFQSFN--LLPDLTALENVELPLLLAGVPKKER-RERAEELLERVGL-GDRLNHYPSELSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 949724212 469 RQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERiSHRVAVMYLGQI 542
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
311-544 |
2.49e-52 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 179.47 E-value: 2.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPLRSGilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTtgraLLRLV----ESQRGEIIFNGQ 386
Cdd:COG1136 2 SPLLELRNLTKSYGTGEG-------EVTALRGVSLSIEAGEFVAIVGPSGSGKST----LLNILggldRPTSGEVLIDGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 387 RIDTLAASKLQPLRRD-IQFIFQDPYasLDPRQTVGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLlPEHAWRYPHEFS 465
Cdd:COG1136 71 DISSLSERELARLRRRhIGFVFQFFN--LLPELTALENVALPLLLAGVSRKER-RERARELLERVGL-GDRLDHRPSQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 466 GGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERiSHRVAVMYLGQIVE 544
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-546 |
2.57e-52 |
|
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: 188.09 E-value: 2.57e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQeqqrVSAVRNLSFRLKRGETLAIVGESGSGKSVtalsLMHLI------EQAGGEV-----SCDEMLLR 81
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSV----LMHVLrgmdqyEPTSGRIiyhvaLCEKCGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 82 RR---------------NRQVIELGEQSASQMRHVRgADIAMIFQEPMtSLNPVFTVGEQIAESirLHQ-GASHEEAMVE 145
Cdd:TIGR03269 73 ERpskvgepcpvcggtlEPEEVDFWNLSDKLRRRIR-KRIAIMLQRTF-ALYGDDTVLDNVLEA--LEEiGYEGKEAVGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 146 AKRMLDQVRIPEAKAILSRyphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFI 225
Cdd:TIGR03269 149 AVDLIEMVQLSHRITHIAR---DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 226 THDMGVVADIADRVLVMYQGEAVETGSVEQIfhapqhpyTKALLAAVPQLgamnghelprrfplislhdpshvepqtEQD 305
Cdd:TIGR03269 226 SHWPEVIEDLSDKAIWLENGEIKEEGTPDEV--------VAVFMEGVSEV---------------------------EKE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 306 TVVE-GEPILRVRNLVTRF-PLRSGIlnrvtreVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIF 383
Cdd:TIGR03269 271 CEVEvGEPIIKVRNVSKRYiSVDRGV-------VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 384 ngqRI--DTLAASKLQPLRRD-----IQFIFQDpyASLDPRQTVGYSILEPLRVHglLQGDAGSKRVAWLLERVGLLPEH 456
Cdd:TIGR03269 344 ---RVgdEWVDMTKPGPDGRGrakryIGILHQE--YDLYPHRTVLDNLTEAIGLE--LPDELARMKAVITLKMVGFDEEK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 457 AW----RYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISH 532
Cdd:TIGR03269 417 AEeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCD 496
|
570
....*....|....
gi 949724212 533 RVAVMYLGQIVEIG 546
Cdd:TIGR03269 497 RAALMRDGKIVKIG 510
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
29-551 |
7.40e-52 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 186.00 E-value: 7.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLI---EQA-GGEVSCDEMLLRRRN-RQVIELGeqsasqmrhvrg 103
Cdd:COG3845 18 VVANDDVSLTVRPGEIHALLGENGAGKS----TLMKILyglYQPdSGEILIDGKPVRIRSpRDAIALG------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 104 adIAMIFQEPMtsLNPVFTVgeqiAESIRLhqGASHEEAMVEAKRMLDQvripEAKAILSRYP---------HQLSGGMR 174
Cdd:COG3845 82 --IGMVHQHFM--LVPNLTV----AENIVL--GLEPTKGGRLDRKAARA----RIRELSERYGldvdpdakvEDLSVGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 175 QRVMIAMALSCRPAVLIADEPTTALdvTIQaQILQLIKVLQQ--DMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGS 252
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVL--TPQ-EADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 253 VEQIfhapqhpyTKALLAAvpqlgAMNGHElprrfplislhdpshVEPQTEQDTVVEGEPILRVRNLVTRFPlrsgilnr 332
Cdd:COG3845 225 TAET--------SEEELAE-----LMVGRE---------------VLLRVEKAPAEPGEVVLEVENLSVRDD-------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 333 vtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLqpLRRDIQFIFQDpya 412
Cdd:COG3845 269 --RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER--RRLGVAYIPED--- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 413 sldpRQTVG----YSILE----------PLRVHGLLQGDAGSKRVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARAL 478
Cdd:COG3845 342 ----RLGRGlvpdMSVAEnlilgryrrpPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPARSLSGGNQQKVILAREL 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 479 ALNPKVIIADESVSALDVS----IRGQIINLmldlqRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAV 551
Cdd:COG3845 418 SRDPKLLIAAQPTRGLDVGaiefIHQRLLEL-----RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
15-274 |
7.47e-52 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 181.81 E-value: 7.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 15 VSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQA-GGEVSCDEmllrrrnrqvIELGEQ 93
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS-TLIRCINLLERPtSGSVLVDG----------VDLTAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 94 SASQMRHVRgADIAMIFQEP--MTSLnpvfTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIpEAKAilSRYPHQLSG 171
Cdd:COG1135 73 SERELRAAR-RKIGMIFQHFnlLSSR----TVAENVALPLEI-AGVPKAEIRKRVAELLELVGL-SDKA--DAYPSQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQG 223
|
250 260
....*....|....*....|...
gi 949724212 252 SVEQIFHAPQHPYTKALLAAVPQ 274
Cdd:COG1135 224 PVLDVFANPQSELTRRFLPTVLN 246
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
313-567 |
1.01e-51 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 177.88 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 313 ILRVRNLVTRFplrsGilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdTLA 392
Cdd:COG1126 1 MIEIENLHKSF----G-------DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 393 ASKLQPLRRDIQFIFQDpyASLDPRQTVgysiLE-----PLRVHGLLQGDAgSKRVAWLLERVGLLpEHAWRYPHEFSGG 467
Cdd:COG1126 69 KKDINKLRRKVGMVFQQ--FNLFPHLTV----LEnvtlaPIKVKKMSKAEA-EERAMELLERVGLA-DKADAYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 468 QRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGT 547
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGP 219
|
250 260
....*....|....*....|
gi 949724212 548 RRAVFENPQHPYTRKLMAAV 567
Cdd:COG1126 220 PEEFFENPQHERTRAFLSKV 239
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
330-546 |
1.45e-51 |
|
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: 176.94 E-value: 1.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 330 LNRVTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdtlaaSKLQPLRRDIQFIFQD 409
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-----TGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 410 PyaSLDPRQTVGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
Cdd:cd03259 81 Y--ALFPHLTVAENIAFGLKLRGVPKAEI-RARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 490 SVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
12-272 |
2.01e-50 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 174.41 E-value: 2.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSvTAL-SLMHLIEQAGGEVSCDEMLLRRRNRQViel 90
Cdd:COG1126 1 MIEIENLHKSFGDLE----VLKGISLDVEKGEVVVIIGPSGSGKS-TLLrCINLLEEPDSGTITVDGEDLTDSKKDI--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 91 geqsasqmRHVRgADIAMIFQepmtSLN--PVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEaKAilSRYPHQ 168
Cdd:COG1126 73 --------NKLR-RKVGMVFQ----QFNlfPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLAD-KA--DAYPAQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVL-QQDMSMgvIFITHDMGVVADIADRVLVMYQGEA 247
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLaKEGMTM--VVVTHEMGFAREVADRVVFMDGGRI 214
|
250 260
....*....|....*....|....*
gi 949724212 248 VETGSVEQIFHAPQHPYTKALLAAV 272
Cdd:COG1126 215 VEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
339-572 |
6.80e-50 |
|
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: 174.37 E-value: 6.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQPLRR-DIQFIFQDpyASLDPR 417
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQS--FALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 418 QTVGYSILEPLRVHGllQGDAGSKRVAW-LLERVGLlpeHAW--RYPHEFSGGQRQRICIARALALNPKVIIADESVSAL 494
Cdd:cd03294 117 RTVLENVAFGLEVQG--VPRAEREERAAeALELVGL---EGWehKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 495 DVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQHPYTRKLMAAVPVADP 572
Cdd:cd03294 192 DPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVDRAKV 269
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
314-537 |
2.49e-49 |
|
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: 171.12 E-value: 2.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFPLRSGilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdtlaa 393
Cdd:cd03293 1 LEVRNVSKTYGGGGG-------AVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 sklQPLRRDIQFIFQDPyaSLDPRQTVGYSILEPLRVHGLLQGDAGsKRVAWLLERVGLLpEHAWRYPHEFSGGQRQRIC 473
Cdd:cd03293 69 ---TGPGPDRGYVFQQD--ALLPWLTVLDNVALGLELQGVPKAEAR-ERAEELLELVGLS-GFENAYPHQLSGGMRQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 474 IARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDM--AVveRISHRVAVM 537
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIdeAV--FLADRVVVL 205
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
339-561 |
8.28e-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: 170.56 E-value: 8.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLqplRRDIQFIFQDpyASLDPRQ 418
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---RRKIGYVIQQ--IGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 419 TVGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLLPEH-AWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVS 497
Cdd:cd03295 91 TVEENIALVPKLLKWPKEKI-RERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPI 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 949724212 498 IRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQHPYTR 561
Cdd:cd03295 170 TRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVA 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
13-246 |
1.14e-48 |
|
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: 169.21 E-value: 1.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQA-GGEVSCDEmllrrrnrqvIELG 91
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGLDRPtSGEVRVDG----------TDIS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 EQSASQMRHVRGADIAMIFQEPmtSLNPVFTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIPEakaILSRYPHQLSG 171
Cdd:cd03255 70 KLSEKELAAFRRRHIGFVFQSF--NLLPDLTALENVELPLLL-AGVPKKERRERAEELLERVGLGD---RLNHYPSELSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMgVVADIADRVLVMYQGE 246
Cdd:cd03255 144 GQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
311-545 |
4.41e-48 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 169.11 E-value: 4.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPLRSGilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTtgraLLRLV----ESQRGEIIFNGQ 386
Cdd:COG1116 5 APALELRGVSKRFPTGGG-------GVTALDDVSLTVAAGEFVALVGPSGCGKST----LLRLIagleKPTSGEVLVDGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 387 RIDtlaasklqPLRRDIQFIFQDPyaSLDPRQTVGYSILEPLRVHGLLQGDAGsKRVAWLLERVGLLpEHAWRYPHEFSG 466
Cdd:COG1116 74 PVT--------GPGPDRGVVFQEP--ALLPWLTVLDNVALGLELRGVPKAERR-ERARELLELVGLA-GFEDAYPHQLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 467 GQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDM--AVveRISHRVAVM--YLGQI 542
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVdeAV--FLADRVVVLsaRPGRI 219
|
...
gi 949724212 543 VEI 545
Cdd:COG1116 220 VEE 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
338-556 |
5.86e-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: 167.80 E-value: 5.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 338 HAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdtlaaSKLQPLRRDIQFIFQDpYAsLDPR 417
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-----TNLPPHKRPVNTVFQN-YA-LFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 418 QTVGYSILEPLRVHGLLQGDAGsKRVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVS 497
Cdd:cd03300 87 LTVFENIAFGLRLKKLPKAEIK-ERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 498 IRGQI-INLMlDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQ 556
Cdd:cd03300 165 LRKDMqLELK-RLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
15-261 |
7.70e-48 |
|
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: 167.37 E-value: 7.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 15 VSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQ-AGGEVSCDEMllrrrnrqviELGEQ 93
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGLERpTSGSVLVDGT----------DLTLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 94 SASQMRHVRgADIAMIFQE--PMTSLnpvfTVGEQIAESIRLHqGASHEEAMVEAKRMLDQVRIpEAKAilSRYPHQLSG 171
Cdd:cd03258 73 SGKELRKAR-RRIGMIFQHfnLLSSR----TVFENVALPLEIA-GVPKAEIEERVLELLELVGL-EDKA--DAYPAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:cd03258 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEG 223
|
250
....*....|
gi 949724212 252 SVEQIFHAPQ 261
Cdd:cd03258 224 TVEEVFANPQ 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-249 |
1.40e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 166.37 E-value: 1.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 10 SDVLAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQA-GGEVSCDEmllrrrnrqvI 88
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGLDRPtSGEVLIDG----------Q 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 89 ELGEQSASQMRHVRGADIAMIFQEPmtSLNPVFTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIPEakaILSRYPHQ 168
Cdd:COG1136 71 DISSLSERELARLRRRHIGFVFQFF--NLLPELTALENVALPLLL-AGVSRKERRERARELLERVGLGD---RLDHRPSQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMgVVADIADRVLVMYQGEAV 248
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
.
gi 949724212 249 E 249
Cdd:COG1136 224 S 224
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
312-543 |
2.26e-47 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 166.77 E-value: 2.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 312 PILRVRNLVTRFPlrsgilnrvtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTL 391
Cdd:COG3638 1 PMLELRNLSKRYP----------GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 392 AASKLQPLRRDIQFIFQDPYasLDPRQTV---------GYsileplrvHGLLQGDAGS------KRVAWLLERVGLLpEH 456
Cdd:COG3638 71 RGRALRRLRRRIGMIFQQFN--LVPRLSVltnvlagrlGR--------TSTWRSLLGLfppedrERALEALERVGLA-DK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 457 AWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAV 536
Cdd:COG3638 140 AYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIG 219
|
....*..
gi 949724212 537 MYLGQIV 543
Cdd:COG3638 220 LRDGRVV 226
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
31-274 |
3.47e-47 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 166.64 E-value: 3.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSvTALSLM--HLIEQAGgevscdEMLLRRRNRQVIELGEQSASQMRHVRGADIAM 108
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKT-TLLNALsaRLAPDAG------EVHYRMRDGQLRDLYALSEAERRRLLRTEWGF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 109 IFQEPMTSLNPVFTVGEQIAEsiRLH-QGASH-EEAMVEAKRMLDQVRIPEAKaiLSRYPHQLSGGMRQRVMIAMALSCR 186
Cdd:PRK11701 94 VHQHPRDGLRMQVSAGGNIGE--RLMaVGARHyGDIRATAGDWLERVEIDAAR--IDDLPTTFSGGMQQRLQIARNLVTH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 187 PAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQHPYTK 266
Cdd:PRK11701 170 PRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQ 249
|
....*...
gi 949724212 267 ALLAAVPQ 274
Cdd:PRK11701 250 LLVSSVLQ 257
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
330-551 |
4.81e-47 |
|
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: 165.05 E-value: 4.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 330 LNRVTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQR-----GEIIFNGQRIDTLAASKLQpLRRDIQ 404
Cdd:cd03260 6 LNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDVLE-LRRRVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 405 FIFQDPYasldP-RQTVGYSILEPLRVHGLLQGDAGSKRVAWLLERVGLLPEHAWR-YPHEFSGGQRQRICIARALALNP 482
Cdd:cd03260 85 MVFQKPN----PfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 483 KVIIADESVSALDVSIRGQIINLMLDLQRELGIayLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAV 551
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAELKKEYTI--VIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
314-556 |
9.99e-47 |
|
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: 164.43 E-value: 9.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFPlrsgilnrvtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQridTLAA 393
Cdd:COG1122 1 IELENLSFSYP----------GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGK---DITK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 SKLQPLRRDIQFIFQDPyaslDpRQTVGYSILE----PLRVHGLLQGDAgSKRVAWLLERVGLLpEHAWRYPHEFSGGQR 469
Cdd:COG1122 68 KNLRELRRKVGLVFQNP----D-DQLFAPTVEEdvafGPENLGLPREEI-RERVEEALELVGLE-HLADRPPHELSGGQK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 470 QRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRR 549
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
....*..
gi 949724212 550 AVFENPQ 556
Cdd:COG1122 220 EVFSDYE 226
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
312-568 |
7.58e-46 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 165.08 E-value: 7.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 312 PILRVRNLVTRFPLRSGIlnrvtreVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRL------VESQRgeIIFNG 385
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGR-------VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGItkdnwhVTADR--FRWNG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 386 qrIDTLAAS---KLQPLRRDIQFIFQDPYASLDPRQTVGYSILE-----PLRVHGLLQGDAGSKRVAWLLERVGLL-PEH 456
Cdd:COG4170 73 --IDLLKLSpreRRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEaipswTFKGKWWQRFKWRKKRAIELLHRVGIKdHKD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 457 AWR-YPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVA 535
Cdd:COG4170 151 IMNsYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTIT 230
|
250 260 270
....*....|....*....|....*....|...
gi 949724212 536 VMYLGQIVEIGTRRAVFENPQHPYTRKLMAAVP 568
Cdd:COG4170 231 VLYCGQTVESGPTEQILKSPHHPYTKALLRSMP 263
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
311-567 |
1.41e-45 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 162.02 E-value: 1.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPLRsgilnrvtrevHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIF---NGQR 387
Cdd:PRK11701 4 QPLLSVRGLTKLYGPR-----------KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 388 IDTLAASKLQP---LRRDIQFIFQDPYASLDPRQTVGYSILEPL-----RVHGLLQGDAGSkrvaWLlERVGLLPEHAWR 459
Cdd:PRK11701 73 RDLYALSEAERrrlLRTEWGFVHQHPRDGLRMQVSAGGNIGERLmavgaRHYGDIRATAGD----WL-ERVEIDAARIDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 460 YPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYL 539
Cdd:PRK11701 148 LPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
250 260
....*....|....*....|....*...
gi 949724212 540 GQIVEIGTRRAVFENPQHPYTRKLMAAV 567
Cdd:PRK11701 228 GRVVESGLTDQVLDDPQHPYTQLLVSSV 255
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
314-560 |
1.54e-45 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 164.93 E-value: 1.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFPlrsgilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTtgraLLR----LVESQRGEIIFNGQRID 389
Cdd:COG1118 3 IEVRNISKRFG-----------SFTLLDDVSLEIASGELVALLGPSGSGKTT----LLRiiagLETPDSGRIVLNGRDLF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 390 TlaasKLQPLRRDIQFIFQDpYAsLDPRQTVGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLlPEHAWRYPHEFSGGQR 469
Cdd:COG1118 68 T----NLPPRERRVGFVFQH-YA-LFPHMTVAENIAFGLRVRPPSKAEI-RARVEELLELVQL-EGLADRYPSQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 470 QRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRR 549
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPD 219
|
250
....*....|.
gi 949724212 550 AVFENPQHPYT 560
Cdd:COG1118 220 EVYDRPATPFV 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
337-548 |
1.55e-45 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 160.99 E-value: 1.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 337 VHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQPLRRDIQFIFQDpyASLDP 416
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQD--FRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 417 RQTVGYSILEPLRVHGLLQGDAGsKRVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDV 496
Cdd:COG2884 93 DRTVYENVALPLRVTGKSRKEIR-RRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 949724212 497 SIRGQIINLMLDLQReLGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTR 548
Cdd:COG2884 171 ETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
12-271 |
2.24e-45 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 161.88 E-value: 2.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQE-----QQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLrrrnrq 86
Cdd:PRK15112 4 LLEVRNLSKTFRYRtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 87 viELGEQSASQMRhvrgadIAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEAKAilSRYP 166
Cdd:PRK15112 78 --HFGDYSYRSQR------IRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHA--SYYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGE 246
Cdd:PRK15112 148 HMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGE 227
|
250 260
....*....|....*....|....*
gi 949724212 247 AVETGSVEQIFHAPQHPYTKALLAA 271
Cdd:PRK15112 228 VVERGSTADVLASPLHELTKRLIAG 252
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
314-541 |
2.64e-45 |
|
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: 158.50 E-value: 2.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFPlrsgilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAA 393
Cdd:cd03229 1 LELKNVSKRYG-----------QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 sKLQPLRRDIQFIFQDPyaSLDPRQTVGYSILEPLrvhgllqgdagskrvawllervgllpehawryphefSGGQRQRIC 473
Cdd:cd03229 70 -ELPPLRRRIGMVFQDF--ALFPHLTVLENIALGL------------------------------------SGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 474 IARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQ 541
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
16-316 |
3.81e-45 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 163.43 E-value: 3.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 16 SNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQ-AGGEVSCDEmllrrrnrqvIELGEQS 94
Cdd:PRK11153 5 KNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLLERpTSGRVLVDG----------QDLTALS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 95 ASQMRHVRgADIAMIFQEpmtslnpvF------TVGEQIAESIRLhQGASHEEamVEAK--RMLDQVRIpEAKAilSRYP 166
Cdd:PRK11153 74 EKELRKAR-RQIGMIFQH--------FnllssrTVFDNVALPLEL-AGTPKAE--IKARvtELLELVGL-SDKA--DRYP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGE 246
Cdd:PRK11153 139 AQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGR 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 247 AVETGSVEQIFHAPQHPYTKALLAAVpqlgamnghelprrfplISLHDPSHVEPQTEQDTVVEGEPILRV 316
Cdd:PRK11153 219 LVEQGTVSEVFSHPKHPLTREFIQST-----------------LHLDLPEDYLARLQAEPTTGSGPLLRL 271
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-261 |
7.13e-45 |
|
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: 159.42 E-value: 7.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQQrvsAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRqvielge 92
Cdd:COG1122 1 IELENLSFSYPGGTP---ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNL------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 93 qsasqmRHVRgADIAMIFQEPMTSL-NPvfTVGEQIAESIRlHQGASHEEAMVEAKRMLDQVRIPEakaILSRYPHQLSG 171
Cdd:COG1122 71 ------RELR-RKVGLVFQNPDDQLfAP--TVEEDVAFGPE-NLGLPREEIRERVEEALELVGLEH---LADRPPHELSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:COG1122 138 GQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADG 216
|
250
....*....|
gi 949724212 252 SVEQIFHAPQ 261
Cdd:COG1122 217 TPREVFSDYE 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
314-551 |
1.52e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 158.69 E-value: 1.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFplrsgilnrvtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAA 393
Cdd:COG1131 1 IEVRGLTKRY-----------GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 SklqpLRRDIQFIFQDPyaSLDPRQTVGysilEPLRVHGLLQGDAGS---KRVAWLLERVGLlPEHAWRYPHEFSGGQRQ 470
Cdd:COG1131 70 E----VRRRIGYVPQEP--ALYPDLTVR----ENLRFFARLYGLPRKearERIDELLELFGL-TDAADRKVGTLSGGMKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 471 RICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRA 550
Cdd:COG1131 139 RLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE 217
|
.
gi 949724212 551 V 551
Cdd:COG1131 218 L 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
27-272 |
2.92e-44 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 159.08 E-value: 2.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 27 QRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRqvielgeqsaSQMRHVRGaDI 106
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR----------AQRKAFRR-DI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 107 AMIFQEPMTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEAkaILSRYPHQLSGGMRQRVMIAMALSCR 186
Cdd:PRK10419 92 QMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDS--VLDKRPPQLSGGQLQRVCLARALAVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 187 PAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHApQHPYTK 266
Cdd:PRK10419 170 PKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTF-SSPAGR 248
|
....*.
gi 949724212 267 ALLAAV 272
Cdd:PRK10419 249 VLQNAV 254
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
314-543 |
3.94e-43 |
|
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: 155.03 E-value: 3.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFPlrsgilnrvtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAA 393
Cdd:cd03256 1 IEVENLSKTYP----------NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 SKLQPLRRDIQFIFQDPyaSLDPRQTVGYSILEP-LRVHGLLQGDAGS-----KRVAW-LLERVGLLpEHAWRYPHEFSG 466
Cdd:cd03256 71 KALRQLRRQIGMIFQQF--NLIERLSVLENVLSGrLGRRSTWRSLFGLfpkeeKQRALaALERVGLL-DKAYQRADQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 467 GQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
306-561 |
6.74e-43 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 154.81 E-value: 6.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 306 TVVEGEPILRVRNLVTRFplrsgilnrvtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLR---LVESQR--GE 380
Cdd:COG1117 4 PASTLEPKIEVRNLNVYY-----------GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPGARveGE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 381 IIFNGQRIdtlAASKLQP--LRRDIQFIFQ--DPYASldprqtvgySILE----PLRVHGLLQGDAGSKRVAWLLERVGL 452
Cdd:COG1117 73 ILLDGEDI---YDPDVDVveLRRRVGMVFQkpNPFPK---------SIYDnvayGLRLHGIKSKSELDEIVEESLRKAAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 453 LPE-----HawRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIayLFISHDMAVV 527
Cdd:COG1117 141 WDEvkdrlK--KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTI--VIVTHNMQQA 216
|
250 260 270
....*....|....*....|....*....|....
gi 949724212 528 ERISHRVAVMYLGQIVEIGTRRAVFENPQHPYTR 561
Cdd:COG1117 217 ARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTE 250
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
13-242 |
3.30e-42 |
|
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: 151.86 E-value: 3.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMH-LIEQAGGEVSCDEMLLRRRNRqvielg 91
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS-TLLRIIAgLERPTSGEVLVDGEPVTGPGP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 eqsasqmrhvrgaDIAMIFQEPmtSLNPVFTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIPEAkaiLSRYPHQLSG 171
Cdd:cd03293 74 -------------DRGYVFQQD--ALLPWLTVLDNVALGLEL-QGVPKAEARERAEELLELVGLSGF---ENAYPHQLSG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVM 242
Cdd:cd03293 135 GMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
12-272 |
3.39e-42 |
|
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: 152.68 E-value: 3.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSvTALSLM--HLIEQAGgevscdEMLLRRRNRQVIE 89
Cdd:TIGR02323 3 LLQVSGLSKSYGGGK----GCRDVSFDLYPGEVLGIVGESGSGKS-TLLGCLagRLAPDHG------TATYIMRSGAELE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 90 LGEQSASQMRHVRGADIAMIFQEPMTSLNPVFTVGEQIAESIrLHQGASHEEAM-VEAKRMLDQVRIPEAKaiLSRYPHQ 168
Cdd:TIGR02323 72 LYQLSEAERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERL-MAIGARHYGNIrATAQDWLEEVEIDPTR--IDDLPRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAV 248
Cdd:TIGR02323 149 FSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVV 228
|
250 260
....*....|....*....|....
gi 949724212 249 ETGSVEQIFHAPQHPYTKALLAAV 272
Cdd:TIGR02323 229 ESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
12-269 |
5.02e-42 |
|
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: 151.67 E-value: 5.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQeqQRVsaVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEmllrrrnrqvIELG 91
Cdd:COG1127 5 MIEVRNLTKSFGD--RVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDG----------QDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 EQSASQMRHVRgADIAMIFQEP--MTSLnpvfTVGEQIAESIRLHQGASHEEA--MVEAKrmLDQVRIPEAKailSRYPH 167
Cdd:COG1127 71 GLSEKELYELR-RRIGMLFQGGalFDSL----TVFENVAFPLREHTDLSEAEIreLVLEK--LELVGLPGAA---DKMPS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEA 247
Cdd:COG1127 141 ELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
250 260
....*....|....*....|..
gi 949724212 248 VETGSVEQIFHAPqHPYTKALL 269
Cdd:COG1127 221 IAEGTPEELLASD-DPWVRQFL 241
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
338-542 |
1.46e-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: 149.60 E-value: 1.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 338 HAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdTLAASKLQPLRRDIQFIFQDpyASLDPR 417
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQKVGMVFQQ--FNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 418 QTVGYSILE-PLRVHGLLQGDAGsKRVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDV 496
Cdd:cd03262 91 LTVLENITLaPIKVKGMSKAEAE-ERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 949724212 497 SIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:cd03262 169 ELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
19-246 |
1.56e-41 |
|
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: 149.54 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 19 NIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRrrnrqvielgeqsASQM 98
Cdd:cd03225 4 NLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT-------------KLSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 99 RHVRGaDIAMIFQEPMTSL-NPvfTVGEQIAESIRlHQGASHEEAMVEAKRMLDQVRIpeaKAILSRYPHQLSGGMRQRV 177
Cdd:cd03225 71 KELRR-KVGLVFQNPDDQFfGP--TVEEEVAFGLE-NLGLPEEEIEERVEEALELVGL---EGLRDRSPFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 178 MIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMsMGVIFITHDMGVVADIADRVLVMYQGE 246
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
31-257 |
1.64e-41 |
|
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: 151.45 E-value: 1.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSvTALSLMH-LIEQAGGEVSCDEMLLRRRNRQvielgeqsasQMRHVRgADIAMI 109
Cdd:TIGR04521 20 ALDDVSLTIEDGEFVAIIGHTGSGKS-TLIQHLNgLLKPTSGTVTIDGRDITAKKKK----------KLKDLR-KKVGLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 110 FQEPMTSLnpvF--TVGEQIAESIRlHQGASHEEAMVEAKRMLDQVRIPEAkaILSRYPHQLSGGMRQRVMIAMALSCRP 187
Cdd:TIGR04521 88 FQFPEHQL---FeeTVYKDIAFGPK-NLGLSEEEAEERVKEALELVGLDEE--YLERSPFELSGGQMRRVAIAGVLAMEP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 188 AVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIF 257
Cdd:TIGR04521 162 EVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
28-256 |
3.47e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 149.44 E-value: 3.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 28 RVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCdemllrrrnrqvieLGEQSASQMRHVRgADIA 107
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRV--------------LGEDVARDPAEVR-RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 108 MIFQEPmtSLNPVFTVGEQIAESIRLHqGASHEEAMVEAKRMLDQVRIPEAKailSRYPHQLSGGMRQRVMIAMALSCRP 187
Cdd:COG1131 77 YVPQEP--ALYPDLTVRENLRFFARLY-GLPRKEARERIDELLELFGLTDAA---DRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 188 AVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQI 256
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
330-557 |
3.67e-41 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 152.92 E-value: 3.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 330 LNRVTR---EVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAasklqPLRRDIQFI 406
Cdd:COG3839 6 LENVSKsygGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP-----PKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 407 FQDpYAsLDPRQTVGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVII 486
Cdd:COG3839 81 FQS-YA-LYPHMTVYENIAFPLKLRKVPKAEI-DRRVREAAELLGLED-LLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 487 ADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHD----MAvverISHRVAVMYLGQIVEIGTRRAVFENPQH 557
Cdd:COG3839 157 LDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMT----LADRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
314-559 |
1.05e-40 |
|
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: 148.26 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFPlrsgilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRidtlaA 393
Cdd:cd03296 3 IEVRNVSKRFG-----------DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGED-----A 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 SKLQPLRRDIQFIFQDpYAsLDPRQTVGYSILEPLRVHGLLQG---DAGSKRVAWLLERVGLlPEHAWRYPHEFSGGQRQ 470
Cdd:cd03296 67 TDVPVQERNVGFVFQH-YA-LFRHMTVFDNVAFGLRVKPRSERppeAEIRAKVHELLKLVQL-DWLADRYPAQLSGGQRQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 471 RICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRA 550
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
....*....
gi 949724212 551 VFENPQHPY 559
Cdd:cd03296 224 VYDHPASPF 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
315-541 |
1.17e-40 |
|
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: 147.23 E-value: 1.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 315 RVRNLVTRFPlrsgilnrvTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDtlaAS 394
Cdd:cd03225 1 ELKNLSFSYP---------DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT---KL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 395 KLQPLRRDIQFIFQDPyaslDpRQTVGYSILE----PLRVHGLLQGDAgSKRVAWLLERVGLLpEHAWRYPHEFSGGQRQ 470
Cdd:cd03225 69 SLKELRRKVGLVFQNP----D-DQFFGPTVEEevafGLENLGLPEEEI-EERVEEALELVGLE-GLRDRSPFTLSGGQKQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 471 RICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQ 541
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
15-266 |
1.59e-40 |
|
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: 147.65 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 15 VSNLNIAFEQeqQRVsaVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEmllrrrnrqvIELGEQS 94
Cdd:cd03261 3 LRGLTKSFGG--RTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDG----------EDISGLS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 95 ASQMRHVRgADIAMIFQEP--MTSLnpvfTVGEQIAESIRLHQGASHEE--AMVEAKrmLDQVRIPEAKailSRYPHQLS 170
Cdd:cd03261 69 EAELYRLR-RRMGMLFQSGalFDSL----TVFENVAFPLREHTRLSEEEirEIVLEK--LEAVGLRGAE---DLYPAELS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVET 250
Cdd:cd03261 139 GGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
250
....*....|....*.
gi 949724212 251 GSVEQIFHApQHPYTK 266
Cdd:cd03261 219 GTPEELRAS-DDPLVR 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-542 |
3.50e-40 |
|
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: 153.44 E-value: 3.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKS--VTALSLMHLIEQAGGEVSCDEMLLRrrnrqvielgeqsASQMRHVRGADI 106
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKStlMKILSGVYPHGTWDGEIYWSGSPLK-------------ASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 107 AMIFQEPMtsLNPVFTVGEQI--AESIRLHQGASHEEAMV-EAKRMLDQVRIPEAKaiLSRYPHQLSGGMRQRVMIAMAL 183
Cdd:TIGR02633 81 VIIHQELT--LVPELSVAENIflGNEITLPGGRMAYNAMYlRAKNLLRELQLDADN--VTRPVGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIfhapqhp 263
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 264 ytkallaAVPQLGA-MNGHELPRRFPlislHDPSHVepqteqdtvveGEPILRVRNLVTRFPlrsgilnrVTREVHAVEN 342
Cdd:TIGR02633 229 -------SEDDIITmMVGREITSLYP----HEPHEI-----------GDVILEARNLTCWDV--------INPHRKRVDD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 343 VSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQ-RGEIIFNGQRIDTlaASKLQPLRRDIQFIFQD-PYASLDPRQTV 420
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDI--RNPAQAIRAGIAMVPEDrKRHGIVPILGV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 421 GYSI----LEPLRVHGLLQGDAGSKRVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDV 496
Cdd:TIGR02633 357 GKNItlsvLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 949724212 497 SIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:TIGR02633 437 GAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
314-546 |
3.79e-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: 145.86 E-value: 3.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFPlrsgilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdtlaa 393
Cdd:cd03301 1 VELENVTKRFG-----------NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 SKLQPLRRDIQFIFQDpYAsLDPRQTVGYSILEPLRVHGLLQG--DAGSKRVAWLLERVGLLPehawRYPHEFSGGQRQR 471
Cdd:cd03301 65 TDLPPKDRDIAMVFQN-YA-LYPHMTVYDNIAFGLKLRKVPKDeiDERVREVAELLQIEHLLD----RKPKQLSGGQRQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 472 ICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03301 139 VALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
9-242 |
5.60e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 146.77 E-value: 5.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 9 ASDVLAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMH-LIEQAGGEVSCDemllrrrNRQV 87
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS-TLLRLIAgLEKPTSGEVLVD-------GKPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 88 IELGeqsasqmrhvrgADIAMIFQEPmtSLNPVFTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIPEAkaiLSRYPH 167
Cdd:COG1116 76 TGPG------------PDRGVVFQEP--ALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLAGF---EDAYPH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDV----TIQAQILQlikvLQQDMSMGVIFITHDmgvVAD---IADRVL 240
Cdd:COG1116 138 QLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQDELLR----LWQETGKTVLFVTHD---VDEavfLADRVV 210
|
..
gi 949724212 241 VM 242
Cdd:COG1116 211 VL 212
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
314-542 |
9.06e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 144.57 E-value: 9.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFPLRSgILNrvtrevhaveNVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAA 393
Cdd:COG4619 1 LELEGLSFRVGGKP-ILS----------PVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 SKLqplRRDIQFIFQDPYAsldPRQTVGYSILEPLRVHGLlqgDAGSKRVAWLLERVGLlPEHAWRYP-HEFSGGQRQRI 472
Cdd:COG4619 70 PEW---RRQVAYVPQEPAL---WGGTVRDNLPFPFQLRER---KFDRERALELLERLGL-PPDILDKPvERLSGGERQRL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 473 CIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
311-567 |
1.25e-39 |
|
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: 145.74 E-value: 1.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPLRSGilnrvtrevhaVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIF---NGQR 387
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKG-----------CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 388 IDTLA---ASKLQPLRRDIQFIFQDPYASLDPRQTVGYSILEPLRVHGLLQ-GDAGSKRVAWLlERVGLLPEHAWRYPHE 463
Cdd:TIGR02323 70 LELYQlseAERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHyGNIRATAQDWL-EEVEIDPTRIDDLPRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 464 FSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
Cdd:TIGR02323 149 FSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVV 228
|
250 260
....*....|....*....|....
gi 949724212 544 EIGTRRAVFENPQHPYTRKLMAAV 567
Cdd:TIGR02323 229 ESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
31-251 |
3.73e-39 |
|
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: 143.04 E-value: 3.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDemllrrrnrqvielGEQSASQMRHVRgaDIAMIF 110
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID--------------GRDVTGVPPERR--NIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEPmtSLNPVFTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIPEakaILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:cd03259 79 QDY--ALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEG---LLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 191 IADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
340-489 |
6.38e-39 |
|
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: 140.09 E-value: 6.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDtlaASKLQPLRRDIQFIFQDPyaSLDPRQT 419
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT---DDERKSLRKEIGYVFQDP--QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 420 VGYSILEPLRVHGLLQGDAGSkRVAWLLERVGL---LPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREKDA-RAEEALEKLGLgdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
314-547 |
6.94e-39 |
|
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: 143.46 E-value: 6.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFplrsgilnrvtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGqrIDtlAA 393
Cdd:COG4555 2 IEVENLSKKY-----------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG--ED--VR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 SKLQPLRRDIQFIFQDPYasLDPRQTVgysiLEPLRVHGLLQGDAGS---KRVAWLLERVGLlPEHAWRYPHEFSGGQRQ 470
Cdd:COG4555 67 KEPREARRQIGVLPDERG--LYDRLTV----RENIRYFAELYGLFDEelkKRIEELIELLGL-EEFLDRRVGELSTGMKK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 471 RICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLqRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGT 547
Cdd:COG4555 140 KVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
340-566 |
1.70e-38 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 142.53 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRL----VESQRGEIIFNGQRIdtlAASKLQPlrRDIQFIFQDPYASLD 415
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPV---APCALRG--RKIATIMQNPRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 416 PRQTVGYSILEPLRVHGLLQGDAgskRVAWLLERVGLlpEHAWR----YPHEFSGGQRQRICIARALALNPKVIIADESV 491
Cdd:PRK10418 94 PLHTMHTHARETCLALGKPADDA---TLTAALEAVGL--ENAARvlklYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 492 SALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQHPYTRKLMAA 566
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
29-273 |
2.66e-38 |
|
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: 142.40 E-value: 2.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMH-LIEQAGGEVSCDemllrrrNRQVIELgeqSASQMRHVRGADIA 107
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKS-TLLRCINrLIEPTSGKVLID-------GQDIAAM---SRKELRELRRKKIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 108 MIFQEpmTSLNPVFTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIpeaKAILSRYPHQLSGGMRQRVMIAMALSCRP 187
Cdd:cd03294 106 MVFQS--FALLPHRTVLENVAFGLEV-QGVPRAEREERAAEALELVGL---EGWEHKYPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 188 AVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQHPYTKA 267
Cdd:cd03294 180 DILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVRE 259
|
....*.
gi 949724212 268 LLAAVP 273
Cdd:cd03294 260 FFRGVD 265
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
29-542 |
1.31e-37 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 146.23 E-value: 1.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIEQA------GGEVscdemllrrrnrqVIELGEQSASQMRHVR 102
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKS----TLMKVLSGVyphgtyEGEI-------------IFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 103 GADIAMIFQEPMtsLNPVFTVGEQI--AESIrLHQGASHEEAMV-EAKRMLDQVRI---PEAKAilsrypHQLSGGMRQR 176
Cdd:PRK13549 81 RAGIAIIHQELA--LVKELSVLENIflGNEI-TPGGIMDYDAMYlRAQKLLAQLKLdinPATPV------GNLGLGQQQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQqdmSMGV--IFITHDMGVVADIADRVLVMYQGEAVETGSVE 254
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK---AHGIacIYISHKLNEVKAISDTICVIRDGRHIGTRPAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 255 QIfhapqhpytkallaAVPQLGA-MNGHELPRRFPlislHDPSHVepqteqdtvveGEPILRVRNLVTRFPlrsgilnrV 333
Cdd:PRK13549 229 GM--------------TEDDIITmMVGRELTALYP----REPHTI-----------GEVILEVRNLTAWDP--------V 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 334 TREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQ-RGEIIFNGQRIDTlaASKLQPLRRDIQFIFQDPYA 412
Cdd:PRK13549 272 NPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKI--RNPQQAIAQGIAMVPEDRKR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 413 -SLDPRQTVGYSI----LEPLRVHGLLQGDAGSKRVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIA 487
Cdd:PRK13549 350 dGIVPVMGVGKNItlaaLDRFTGGSRIDDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILIL 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 488 DESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:PRK13549 430 DEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-276 |
2.47e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 140.15 E-value: 2.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 8 DASDVLAVSNLNiaFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMllrrrnrqv 87
Cdd:PRK13635 1 MKEEIIRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 88 iELGEQSASQMRhvrgADIAMIFQEPmtslNPVF---TVGEQIAESIRlHQGASHEEaMVE-AKRMLDQVRIPEakaILS 163
Cdd:PRK13635 70 -VLSEETVWDVR----RQVGMVFQNP----DNQFvgaTVQDDVAFGLE-NIGVPREE-MVErVDQALRQVGMED---FLN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADiADRVLVMY 243
Cdd:PRK13635 136 REPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMN 214
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 949724212 244 QGEAVETGSVEQIFHAPQH--------PYTKALLAAVPQLG 276
Cdd:PRK13635 215 KGEILEEGTPEEIFKSGHMlqeigldvPFSVKLKELLKRNG 255
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-256 |
6.39e-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: 137.31 E-value: 6.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQ------AGGEVSCDEMLLRRRNRQ 86
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKS-TLLRLLNRLNDlipgapDEGEVLLDGKDIYDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 87 VIELGEQsasqmrhvrgadIAMIFQEPmtslNPV-FTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIP-EAKAILSr 164
Cdd:cd03260 76 VLELRRR------------VGMVFQKP----NPFpGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWdEVKDRLH- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 165 yPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADIADRVLVMYQ 244
Cdd:cd03260 139 -ALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYT--IVIVTHNMQQAARVADRTAFLLN 215
|
250
....*....|..
gi 949724212 245 GEAVETGSVEQI 256
Cdd:cd03260 216 GRLVEFGPTEQI 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
308-555 |
8.28e-37 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 141.24 E-value: 8.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 308 VEGEPILRVRNLVTRFPlrsgilnrvTREVhaVENVSFDLWPGETLSLVGESGCGKSTtgraLLRLV----ESQRGEIIF 383
Cdd:PRK09452 9 SSLSPLVELRGISKSFD---------GKEV--ISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIagfeTPDSGRIML 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 384 NGQRIDTLAASKlqplrRDIQFIFQDpYAsLDPRQTVGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLlPEHAWRYPHE 463
Cdd:PRK09452 74 DGQDITHVPAEN-----RHVNTVFQS-YA-LFPHMTVFENVAFGLRMQKTPAAEI-TPRVMEALRMVQL-EEFAQRKPHQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 464 FSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
Cdd:PRK09452 145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIE 224
|
250
....*....|..
gi 949724212 544 EIGTRRAVFENP 555
Cdd:PRK09452 225 QDGTPREIYEEP 236
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
312-571 |
9.20e-37 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 141.13 E-value: 9.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 312 PILRVRNLVTRFplrSGIlnrvtrevHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdtl 391
Cdd:PRK11607 18 PLLEIRNLTKSF---DGQ--------HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 392 aaSKLQPLRRDIQFIFQDpYAsLDPRQTVGYSILEPLRVHGLLQGDAGSkRVAWLLERVGLLpEHAWRYPHEFSGGQRQR 471
Cdd:PRK11607 84 --SHVPPYQRPINMMFQS-YA-LFPHMTVEQNIAFGLKQDKLPKAEIAS-RVNEMLGLVHMQ-EFAKRKPHQLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 472 ICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAV 551
Cdd:PRK11607 158 VALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
250 260
....*....|....*....|
gi 949724212 552 FENPQHPYTRKLMAAVPVAD 571
Cdd:PRK11607 238 YEHPTTRYSAEFIGSVNVFE 257
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
339-556 |
1.80e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 136.68 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRID---TLAASKLQPLRRDIQFIFQDpYaSLD 415
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfskTPSDKAIRELRRNVGMVFQQ-Y-NLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 416 PRQTVGYSILE-PLRVHGLLQGDAgSKRVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSAL 494
Cdd:PRK11124 95 PHLTVQQNLIEaPCRVLGLSKDQA-LARAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 495 DVSIRGQIINLMLDLQrELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAvFENPQ 556
Cdd:PRK11124 173 DPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQ 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
31-271 |
3.18e-36 |
|
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: 135.89 E-value: 3.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEmllrrrnrqvIELGEQSASQMRHvrgaDIAMIF 110
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDG----------EDIREQDPVELRR----KIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEpmTSLNPVFTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIPEAKaILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:cd03295 82 QQ--IGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGLDPAE-FADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 191 IADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQHPYTKALLA 270
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
|
.
gi 949724212 271 A 271
Cdd:cd03295 238 A 238
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-272 |
4.82e-36 |
|
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: 135.56 E-value: 4.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFeqeqQRVSAVRNLSFRLKRGETLAIVGESGSGKSvTAL-SLMHLIEQAGGEVSCDEMLLRRRNRQviEL 90
Cdd:COG1120 1 MLEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKS-TLLrALAGLLKPSSGEVLLDGRDLASLSRR--EL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 91 GEQsasqmrhvrgadIAMIFQEPMTSLNpvFTVgeqiAESIRL----HQGA-----SHEEAMVEakRMLDQVRIpEAKAi 161
Cdd:COG1120 74 ARR------------IAYVPQEPPAPFG--LTV----RELVALgrypHLGLfgrpsAEDREAVE--EALERTGL-EHLA- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 162 lSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLV 241
Cdd:COG1120 132 -DRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVL 210
|
250 260 270
....*....|....*....|....*....|.
gi 949724212 242 MYQGEAVETGSVEQIFhapqhpyTKALLAAV 272
Cdd:COG1120 211 LKDGRIVAQGPPEEVL-------TPELLEEV 234
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
15-246 |
6.13e-36 |
|
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: 134.19 E-value: 6.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 15 VSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEmllrrrnrQVIELGEQS 94
Cdd:cd03262 3 IKNLHKSFGDFH----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDG--------LKLTDDKKN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 95 ASQMRhvrgADIAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEaKAilSRYPHQLSGGMR 174
Cdd:cd03262 71 INELR----QKVGMVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLAD-KA--DAYPAQLSGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQD-MSMgvIFITHDMGVVADIADRVLVMYQGE 246
Cdd:cd03262 142 QRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTM--VVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-257 |
9.13e-36 |
|
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: 135.25 E-value: 9.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 19 NIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRrrnrqvielgeqSASQM 98
Cdd:TIGR04520 5 NVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL------------DEENL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 99 RHVRGAdIAMIFQepmtslNP--VF---TVGEQIA---ESirlhQGASHEEaMVEakrmldqvRIPEA------KAILSR 164
Cdd:TIGR04520 73 WEIRKK-VGMVFQ------NPdnQFvgaTVEDDVAfglEN----LGVPREE-MRK--------RVDEAlklvgmEDFRDR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADiADRVLVMYQ 244
Cdd:TIGR04520 133 EPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNK 211
|
250
....*....|...
gi 949724212 245 GEAVETGSVEQIF 257
Cdd:TIGR04520 212 GKIVAEGTPREIF 224
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
355-569 |
9.76e-36 |
|
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: 136.85 E-value: 9.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 355 LVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdtlaaSKLQPLRRDIQFIFQDpYAsLDPRQTVGYSILEPLRVHGLL 434
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV-----TNVPPHLRHINMVFQS-YA-LFPHMTVEENVAFGLKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 435 QGDAGSkRVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELG 514
Cdd:TIGR01187 74 RAEIKP-RVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 515 IAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQHPYTRKLMAAVPV 569
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINV 206
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
29-551 |
1.12e-35 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 140.96 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqaGGEVSCDEMLLRRRNRQVIELGEQSASQMrhvrgaDIAM 108
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKS----TLMKII---AGIVPPDSGTLEIGGNPCARLTPAKAHQL------GIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 109 IFQEPMtsLNPVFTVGEQIAesIRLHQGASHEEAMVEAKRMLDQVRIPEAKAILsryphqLSGGMRQRVMIAMALSCRPA 188
Cdd:PRK15439 91 VPQEPL--LFPNLSVKENIL--FGLPKRQASMQKMKQLLAALGCQLDLDSSAGS------LEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 189 VLIADEPTTALDVTIQAQILQLIKVLQQdMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHApqhpytkAL 268
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD-------DI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 269 LAAV-PQLGAMNGHELPRrfplISLHDPSHvEPQTEQDTvvegePILRVRNLvtrfplrSGilnrvtrevHAVENVSFDL 347
Cdd:PRK15439 233 IQAItPAAREKSLSASQK----LWLELPGN-RRQQAAGA-----PVLTVEDL-------TG---------EGFRNISLEV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 348 WPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLaaSKLQPLRRDIQFIFQDpyasldpRQTVGYSILEP 427
Cdd:PRK15439 287 RAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAL--STAQRLARGLVYLPED-------RQSSGLYLDAP 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 428 LR--VHGLLQGDAG----SKRVAWLLER----VGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVS 497
Cdd:PRK15439 358 LAwnVCALTHNRRGfwikPARENAVLERyrraLNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 949724212 498 IRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAV 551
Cdd:PRK15439 438 ARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
29-264 |
1.30e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 137.15 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLI----EQAGGEvscdemllrrrnrqvIELGEQSASQMR-HVRg 103
Cdd:COG3842 18 VTALDDVSLSIEPGEFVALLGPSGCGKT----TLLRMIagfeTPDSGR---------------ILLDGRDVTGLPpEKR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 104 aDIAMIFQEPmtSLNPVFTVGEQIAESIRlHQGASHEEAMVEAKRMLDQVRIPE-AKailsRYPHQLSGGMRQRVMIAMA 182
Cdd:COG3842 78 -NVGMVFQDY--ALFPHLTVAENVAFGLR-MRGVPKAEIRARVAELLELVGLEGlAD----RYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQH 262
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPAT 229
|
..
gi 949724212 263 PY 264
Cdd:COG3842 230 RF 231
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
312-588 |
1.52e-35 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 136.47 E-value: 1.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 312 PILRVRNLVTRFPLRSGilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRlVESQRGEIIFNGQRIDTL 391
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDG-------WVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRMRFDDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 392 AASKLQPLRR------DIQFIFQDPYASLDPRQTVGYSILEPlrVHGLLQGDAGSKRVAW-------LLERVGLL-PEHA 457
Cdd:PRK15093 74 DLLRLSPRERrklvghNVSMIFQEPQSCLDPSERVGRQLMQN--IPGWTYKGRWWQRFGWrkrraieLLHRVGIKdHKDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 458 WR-YPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAV 536
Cdd:PRK15093 152 MRsFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINV 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 949724212 537 MYLGQIVEIGTRRAVFENPQHPYTRKLMAAVP-VADPSHHRPQRVLLSDDIPS 588
Cdd:PRK15093 232 LYCGQTVETAPSKELVTTPHHPYTQALIRAIPdFGSAMPHKSRLNTLPGAIPL 284
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
32-197 |
1.59e-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: 130.85 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 32 VRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDemllrrrnrqvielGEQSASQMRHVRGADIAMIFQ 111
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLD--------------GQDLTDDERKSLRKEIGYVFQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 112 EPmtSLNPVFTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIPE-AKAILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:pfam00005 67 DP--QLFPRLTVRENLRLGLLL-KGLSKREKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLL 143
|
....*..
gi 949724212 191 IADEPTT 197
Cdd:pfam00005 144 LLDEPTA 150
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
311-566 |
2.02e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 134.76 E-value: 2.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPlrsgilnrvTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQridT 390
Cdd:PRK13635 3 EEIIRVEHISFRYP---------DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 391 LAASKLQPLRRDIQFIFQDPyasldPRQTVGYSILEP----LRVHGLLQgDAGSKRVAWLLERVGLLpEHAWRYPHEFSG 466
Cdd:PRK13635 71 LSEETVWDVRRQVGMVFQNP-----DNQFVGATVQDDvafgLENIGVPR-EEMVERVDQALRQVGME-DFLNREPHRLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 467 GQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
250 260
....*....|....*....|....*...
gi 949724212 547 TRRAVFENPQH--------PYTRKLMAA 566
Cdd:PRK13635 223 TPEEIFKSGHMlqeigldvPFSVKLKEL 250
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
314-556 |
2.73e-35 |
|
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: 132.95 E-value: 2.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFplrsgilnrvtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAA 393
Cdd:cd03219 1 LEVRGLTKRF-----------GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 SKLqpLRRDIQFIFQDPyaSLDPRQTVgysiLEPLRVHGLLQGDAGS-------------KRVAWLLERVGLlPEHAWRY 460
Cdd:cd03219 70 HEI--ARLGIGRTFQIP--RLFPELTV----LENVMVAAQARTGSGLllararreerearERAEELLERVGL-ADLADRP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 461 PHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLqRELGIAYLFISHDMAVVERISHRVAVMYLG 540
Cdd:cd03219 141 AGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
250
....*....|....*.
gi 949724212 541 QIVEIGTRRAVFENPQ 556
Cdd:cd03219 220 RVIAEGTPDEVRNNPR 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
15-261 |
3.20e-35 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 133.22 E-value: 3.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 15 VSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQA-GGEVSCdemllrrRNRQVIELGEQ 93
Cdd:PRK11124 5 LNGINCFYGAHQ----ALFDITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLEMPrSGTLNI-------AGNHFDFSKTP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 94 SASQMRHVRgADIAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIpEAKAilSRYPHQLSGGM 173
Cdd:PRK11124 73 SDKAIRELR-RNVGMVFQQ--YNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRL-KPYA--DRFPLHLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIfITHDMGVVADIADRVLVMYQGEAVETGSV 253
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVI-VTHEVEVARKTASRVVYMENGHIVEQGDA 225
|
....*...
gi 949724212 254 EQiFHAPQ 261
Cdd:PRK11124 226 SC-FTQPQ 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
339-556 |
3.82e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 132.83 E-value: 3.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRID---TLAASKLQPLRRDIQFIFQDpYaSLD 415
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIRLLRQKVGMVFQQ-Y-NLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 416 PRQTVGYSILE-PLRVHGLLQGDAgSKRVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSAL 494
Cdd:COG4161 95 PHLTVMENLIEaPCKVLGLSKEQA-REKAMKLLARLRL-TDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 495 DVSIRGQIINLMLDLQrELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTrRAVFENPQ 556
Cdd:COG4161 173 DPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQ 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
314-547 |
4.06e-35 |
|
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: 132.24 E-value: 4.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFPlrsgilnrvTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAA 393
Cdd:cd03263 1 LQIRNLTKTYK---------KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 SklqpLRRDIQFIFQDpyASLDPRQTVgysiLEPLRVHGLLQG---DAGSKRVAWLLERVGLLPeHAWRYPHEFSGGQRQ 470
Cdd:cd03263 72 A----ARQSLGYCPQF--DALFDELTV----REHLRFYARLKGlpkSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 471 RICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIayLFISHDMAVVERISHRVAVMYLGQIVEIGT 547
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKLRCIGS 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
342-546 |
4.72e-35 |
|
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: 131.65 E-value: 4.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 342 NVSFDLwPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRI-DTLAASKLQPLRRDIQFIFQDpyASLDPRQTV 420
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfDSRKKINLPPQQRKIGLVFQQ--YALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 421 GYSILEPLRVHGLLQGdagSKRVAWLLERVGLlpEH-AWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIR 499
Cdd:cd03297 93 RENLAFGLKRKRNRED---RISVDELLDLLGL--DHlLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 949724212 500 GQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
330-541 |
7.44e-35 |
|
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: 129.29 E-value: 7.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 330 LNRVTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdtlAASKLQPLRRDIQFIFQd 409
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI---AKLPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 410 pyasldprqtvgysileplrvhgllqgdagskrvawllervgllpehawrypheFSGGQRQRICIARALALNPKVIIADE 489
Cdd:cd00267 81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 949724212 490 SVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQ 541
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
336-562 |
9.59e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 131.96 E-value: 9.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 EVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVE-----SQRGEIIFNGQRIDTLAASKLqplRRDIQFIFQDP 410
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIEL---RRRVQMVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 411 yaslDPRQTVgySILEPLRVHGLLQGDAGSK-----RVAWLLERVGLLPEHAWRY---PHEFSGGQRQRICIARALALNP 482
Cdd:PRK14247 92 ----NPIPNL--SIFENVALGLKLNRLVKSKkelqeRVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 483 KVIIADESVSALDVSIRGQIINLMLDLQRELGIayLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQHPYTRK 562
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKIESLFLELKKDMTI--VLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEK 243
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
340-556 |
1.24e-34 |
|
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: 131.30 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLaasklQPLRRDIQFIFQDpYAsLDPRQT 419
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL-----PPEKRDISYVPQN-YA-LFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 420 VGYSILEPLRvHGLLQGDAGSKRVAWLLERVGLlpEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSI 498
Cdd:cd03299 88 VYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGI--DHLLnRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 499 RGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQ 556
Cdd:cd03299 165 KEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
13-246 |
2.19e-34 |
|
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: 128.46 E-value: 2.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRQVIELGE 92
Cdd:cd03229 1 LELKNVSKRYGQKT----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 93 qsasqmrhvrgaDIAMIFQEPmtSLNPVFTVGEQIAESirlhqgasheeamveakrmldqvripeakailsryphqLSGG 172
Cdd:cd03229 77 ------------RIGMVFQDF--ALFPHLTVLENIALG--------------------------------------LSGG 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 949724212 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGE 246
Cdd:cd03229 105 QQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
338-562 |
2.28e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 131.12 E-value: 2.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 338 HAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQ-----RGEIIFNGQRIDTLAASKLQpLRRDIQFIFQdpYA 412
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIE-VRREVGMVFQ--YP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 413 SLDPRQTVGYSILEPLRVHGLLQG-DAGSKRVAWLLERVGLLPEHAWR---YPHEFSGGQRQRICIARALALNPKVIIAD 488
Cdd:PRK14267 95 NPFPHLTIYDNVAIGVKLNGLVKSkKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 949724212 489 ESVSALDVSIRGQIINLMLDLQRELGIayLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQHPYTRK 562
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKEYTI--VLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEK 246
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
314-542 |
5.03e-34 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 127.51 E-value: 5.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFplrsgilnrvtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAA 393
Cdd:cd03230 1 IEVRNLSKRY-----------GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 SklqpLRRDIQFIFQDP--YASLDPRQTVgysileplrvhgllqgdagskrvawllervgllpehawryphEFSGGQRQR 471
Cdd:cd03230 70 E----VKRRIGYLPEEPslYENLTVRENL------------------------------------------KLSGGMKQR 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 472 ICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:cd03230 104 LALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
313-567 |
1.23e-33 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 129.01 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 313 ILRVRNLVTRFPlrsgilnrvTREVhaVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLA 392
Cdd:COG1120 1 MLEAENLSVGYG---------GRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 393 ASKLqplRRDIQFIFQDPYASldprqtvgysilEPLRV-----------HGLLQ--GDAGSKRVAWLLERVGLLpEHAWR 459
Cdd:COG1120 70 RREL---ARRIAYVPQEPPAP------------FGLTVrelvalgryphLGLFGrpSAEDREAVEEALERTGLE-HLADR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 460 YPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYL 539
Cdd:COG1120 134 PVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKD 213
|
250 260
....*....|....*....|....*...
gi 949724212 540 GQIVEIGTRRAVFenpqhpyTRKLMAAV 567
Cdd:COG1120 214 GRIVAQGPPEEVL-------TPELLEEV 234
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
35-269 |
1.70e-33 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 128.71 E-value: 1.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 35 LSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQ-AGGEVSCDEMLLRrrnrQVIELGEQSaSQMRHVRgADIAMIFQEp 113
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLEQpEAGTIRVGDITID----TARSLSQQK-GLIRQLR-QHVGFVFQN- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 114 mTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEAKailSRYPHQLSGGMRQRVMIAMALSCRPAVLIAD 193
Cdd:PRK11264 94 -FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKE---TSYPRRLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 194 EPTTALDVTIQAQILQLIKVLQQDMSMGVIfITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQHPYTKALL 269
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFL 244
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
12-256 |
1.89e-33 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 128.05 E-value: 1.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqAGgevscdemLLRRRNRQVIELG 91
Cdd:COG4555 1 MIEVENLSKKYGKVP----ALKDVSFTAKDGEITGLLGPNGAGKT----TLLRML--AG--------LLKPDSGSILIDG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 EQSASQMRHVRgADIAMIFQEPMtsLNPVFTVGEQIAESIRLHqGASHEEAMVEAKRMLDQVRIPEakaILSRYPHQLSG 171
Cdd:COG4555 63 EDVRKEPREAR-RQIGVLPDERG--LYDRLTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEE---FLDRRVGELST 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMgVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:COG4555 136 GMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKT-VLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
|
....*
gi 949724212 252 SVEQI 256
Cdd:COG4555 215 SLDEL 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-267 |
1.90e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 128.62 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 4 SDELDASDVLAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSvTAL-SL--MH-LIEQA--GGEV---- 73
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQ----ALKDINLDIPENKVTALIGPSGCGKS-TLLrCLnrMNdLIPGArvEGEIlldg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 74 ------SCDEMLLRRRnrqvielgeqsasqmrhvrgadIAMIFQEPmtslNPvF--TVGEQIAESIRLHQGASHEE--AM 143
Cdd:COG1117 78 ediydpDVDVVELRRR----------------------VGMVFQKP----NP-FpkSIYDNVAYGLRLHGIKSKSEldEI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 144 VEakRMLDQVRI-PEAKAILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgV 222
Cdd:COG1117 131 VE--ESLRKAALwDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYT--I 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 949724212 223 IFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQHPYTKA 267
Cdd:COG1117 207 VIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTED 251
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
314-541 |
2.04e-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: 2.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFPlrsgilnrvTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLaa 393
Cdd:cd03228 1 IEFKNVSFSYP---------GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 sKLQPLRRDIQFIFQDPYasLDPRqTVGYSILeplrvhgllqgdagskrvawllervgllpehawryphefSGGQRQRIC 473
Cdd:cd03228 70 -DLESLRKNIAYVPQDPF--LFSG-TIRENIL---------------------------------------SGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 474 IARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIayLFISHDMAVVERiSHRVAVMYLGQ 541
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEALRALAKGKTV--IVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
12-250 |
2.69e-33 |
|
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: 127.55 E-value: 2.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQA-GGEVscdeMLLRRrnrqviEL 90
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS-TLLGLLAGLDRPtSGTV----RLAGQ------DL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 91 GEQSASQMRHVRGADIAMIFQEPMtsLNPVFTVGEQIAESIRLhqgASHEEAMVEAKRMLDQV----RipeakaiLSRYP 166
Cdd:COG4181 77 FALDEDARARLRARHVGFVFQSFQ--LLPTLTALENVMLPLEL---AGRRDARARARALLERVglghR-------LDHYP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGvVADIADRVLVMYQGE 246
Cdd:COG4181 145 AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA-LAARCDRVLRLRAGR 223
|
....
gi 949724212 247 AVET 250
Cdd:COG4181 224 LVED 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
10-287 |
4.42e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 128.31 E-value: 4.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 10 SDVLAVSNLNIAFEQEQQRVSaVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRrrnrqvie 89
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 90 lgEQSASQMRHvrgaDIAMIFQEPMTSLNPVfTVGEQIAESIRlHQGASHEEAMVEAKRMLDQVRIPEAKailSRYPHQL 169
Cdd:PRK13650 73 --EENVWDIRH----KIGMVFQNPDNQFVGA-TVEDDVAFGLE-NKGIPHEEMKERVNEALELVGMQDFK---EREPARL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVAdIADRVLVMYQGEAVE 249
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVES 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 949724212 250 TGSVEQIFHAPQH--------PYTKALLAAVPQlgamNGHELPRRF 287
Cdd:PRK13650 221 TSTPRELFSRGNDllqlgldiPFTTSLVQSLRQ----NGYDLPEGY 262
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
13-265 |
7.90e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 129.50 E-value: 7.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqAGgevscdemlLRRRNRQVIELGE 92
Cdd:COG1118 3 IEVRNISKRFGSFT----LLDDVSLEIASGELVALLGPSGSGKT----TLLRII--AG---------LETPDSGRIVLNG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 93 QSASQMRHVRGADIAMIFQEPMtsLNPVFTVGEQIAESIRlHQGASHEEAMVEAKRMLDQVRIPE-AKailsRYPHQLSG 171
Cdd:COG1118 64 RDLFTNLPPRERRVGFVFQHYA--LFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGlAD----RYPSQLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:COG1118 137 GQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVG 216
|
250
....*....|....
gi 949724212 252 SVEQIFHAPQHPYT 265
Cdd:COG1118 217 TPDEVYDRPATPFV 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
19-246 |
8.21e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 125.31 E-value: 8.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 19 NIAFEQEQQRVsaVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVscdemLLRRRNRQvielgEQSASQM 98
Cdd:COG4619 5 GLSFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEI-----YLDGKPLS-----AMPPPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 99 RHvrgaDIAMIFQEPmtslnPVF--TVGEQIAESIRLHQGASHEEamvEAKRMLDQVRIPEAkaILSRYPHQLSGGMRQR 176
Cdd:COG4619 73 RR----QVAYVPQEP-----ALWggTVRDNLPFPFQLRERKFDRE---RALELLERLGLPPD--ILDKPVERLSGGERQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGE 246
Cdd:COG4619 139 LALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
15-261 |
8.63e-33 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 126.28 E-value: 8.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 15 VSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQAggevscdemllrrRNRQVIELGEQ- 93
Cdd:COG4161 5 LKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLETP-------------DSGQLNIAGHQf 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 94 ------SASQMRHVRGaDIAMIFQEpmTSLNPVFTVGEQIAES-IRLhQGASHEEAMVEAKRMLDQVRIPEaKAilSRYP 166
Cdd:COG4161 67 dfsqkpSEKAIRLLRQ-KVGMVFQQ--YNLWPHLTVMENLIEApCKV-LGLSKEQAREKAMKLLARLRLTD-KA--DRFP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQdmsMGV--IFITHDMGVVADIADRVLVMYQ 244
Cdd:COG4161 140 LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQ---TGItqVIVTHEVEFARKVASQVVYMEK 216
|
250
....*....|....*..
gi 949724212 245 GEAVETGSVEqIFHAPQ 261
Cdd:COG4161 217 GRIIEQGDAS-HFTQPQ 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
31-261 |
1.47e-32 |
|
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: 125.43 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSvTALSLMhlieqAGGE-VSCDEMLLRrrNRQVIELGEqsasqmrHVRGadIAMI 109
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKT-TLLRLI-----AGFEtPTSGEILLD--GKDITNLPP-------HKRP--VNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 110 FQEpmTSLNPVFTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIpeaKAILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
Cdd:cd03300 78 FQN--YALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQL---EGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 190 LIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQ 261
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
311-560 |
2.03e-32 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 125.66 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPLRSgilnrvtrevhAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVE-----SQRGEIIFNG 385
Cdd:PRK14239 3 EPILQVSDLSVYYNKKK-----------ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 386 QRIDTLAASKLQpLRRDIQFIFQDPyaslDPrqtVGYSILEPLrVHGL-LQGDAGSKRVAWLLERvGLLPEHAWR----Y 460
Cdd:PRK14239 72 HNIYSPRTDTVD-LRKEIGMVFQQP----NP---FPMSIYENV-VYGLrLKGIKDKQVLDEAVEK-SLKGASIWDevkdR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 461 PHE----FSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIayLFISHDMAVVERISHRVAV 536
Cdd:PRK14239 142 LHDsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGF 219
|
250 260
....*....|....*....|....
gi 949724212 537 MYLGQIVEIGTRRAVFENPQHPYT 560
Cdd:PRK14239 220 FLDGDLIEYNDTKQMFMNPKHKET 243
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
342-567 |
8.60e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 123.28 E-value: 8.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 342 NVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQpLRRDIQFIFQDPYasLDPRQTVg 421
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERL-IRQEAGMVFQQFY--LFPHLTA- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 422 ysiLE-----PLRVHGLLQGDAgSKRVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDV 496
Cdd:PRK09493 95 ---LEnvmfgPLRVRGASKEEA-EKQARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 497 SIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQHPYTRKLMAAV 567
Cdd:PRK09493 170 ELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
339-570 |
1.22e-31 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 127.07 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQPLRRD-IQFIFQDpyASLDPR 417
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQS--FALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 418 QTVGYSILEPLRVHGLLQGDAGSKRVAwLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVS 497
Cdd:PRK10070 121 MTVLDNTAFGMELAGINAEERREKALD-ALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 498 IRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQHPYTRKLMAAVPVA 570
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDIS 271
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
340-543 |
1.35e-31 |
|
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: 121.60 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdtlaasKLQPLRRDIQFIFQDPYasldpRQT 419
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI------KAKERRKSIGYVMQDVD-----YQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 420 VGYSILEPLRVhGLLQGDAGSKRVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIR 499
Cdd:cd03226 85 FTDSVREELLL-GLKELDAGNEQAETVLKDLDLYALKE-RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 949724212 500 GQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
Cdd:cd03226 163 ERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
316-564 |
1.45e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 122.94 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 316 VRNLVTRFPLRSgILNRVTREVHavenvsfdlwPGETLSLVGESGCGKSTTGRA--LLRLVESQR---GEIIFNGQRIDT 390
Cdd:PRK11264 6 VKNLVKKFHGQT-VLHGIDLEVK----------PGEVVAIIGPSGSGKTTLLRCinLLEQPEAGTirvGDITIDTARSLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 391 LAASKLQPLRRDIQFIFQDpyASLDPRQTVGYSILE-PLRVHGLLQGDAgSKRVAWLLERVGLLPEHAwRYPHEFSGGQR 469
Cdd:PRK11264 75 QQKGLIRQLRQHVGFVFQN--FNLFPHRTVLENIIEgPVIVKGEPKEEA-TARARELLAKVGLAGKET-SYPRRLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 470 QRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRR 549
Cdd:PRK11264 151 QRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
|
250
....*....|....*
gi 949724212 550 AVFENPQHPYTRKLM 564
Cdd:PRK11264 230 ALFADPQQPRTRQFL 244
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
12-245 |
1.56e-31 |
|
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: 122.05 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMhlieqaGGEVSCDEMLLRRRNRQVIELG 91
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKT-TLLTLI------GGLRSVQEGSLKVLGQELHGAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 EQSASQMRHvrgaDIAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEAkaiLSRYPHQLSG 171
Cdd:TIGR02982 74 KKQLVQLRR----RIGYIFQA--HNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGLGDH---LNYYPHNLSG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 949724212 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVaDIADRVLVMYQG 245
Cdd:TIGR02982 145 GQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRIL-DVADRILQMEDG 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
15-264 |
1.94e-31 |
|
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: 122.45 E-value: 1.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 15 VSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqAGgevscdemlLRRRNRQVIELGEQS 94
Cdd:cd03296 5 VRNVSKRFGDFV----ALDDVSLDIPSGELVALLGPSGSGKT----TLLRLI--AG---------LERPDSGTILFGGED 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 95 ASQMrHVRGADIAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEAKAILSRYPHQLSGGMR 174
Cdd:cd03296 66 ATDV-PVQERNVGFVFQH--YALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVE 254
Cdd:cd03296 143 QRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPD 222
|
250
....*....|
gi 949724212 255 QIFHAPQHPY 264
Cdd:cd03296 223 EVYDHPASPF 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
31-246 |
2.90e-31 |
|
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: 119.81 E-value: 2.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDemllrrrnrqvielGEQSASQMRHVRGaDIAMIF 110
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL--------------GKDIKKEPEEVKR-RIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEPmtSLNPVFTVGEQIaesirlhqgasheeamveakrmldqvripeakailsryphQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:cd03230 80 EEP--SLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 191 IADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRVLVMYQGE 246
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
336-554 |
3.82e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 122.85 E-value: 3.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 EVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdTLAASKLQPLRRDIQFIFQDPYASLD 415
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVKLSDIRKKVGLVFQYPEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 416 pRQTVGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLLPE-HAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSAL 494
Cdd:PRK13637 98 -EETIEKDIAFGPINLGLSEEEI-ENRVKRAMNIVGLDYEdYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 495 DVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFEN 554
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
311-559 |
4.83e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 121.35 E-value: 4.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFplrsgilnrvtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQridt 390
Cdd:COG1121 4 MPAIELENLTVSY-----------GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 391 laasKLQPLRRDIQFIFQdpYASLDP------RQTVGYSILEPLRVHGLLqGDAGSKRVAWLLERVGLLpEHAWRYPHEF 464
Cdd:COG1121 69 ----PPRRARRRIGYVPQ--RAEVDWdfpitvRDVVLMGRYGRRGLFRRP-SRADREAVDEALERVGLE-DLADRPIGEL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 465 SGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMyLGQIVE 544
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVA 218
|
250
....*....|....*..
gi 949724212 545 IGTRRAVF--ENPQHPY 559
Cdd:COG1121 219 HGPPEEVLtpENLSRAY 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
311-550 |
6.03e-31 |
|
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: 120.62 E-value: 6.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPLRSGilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTtgraLLRLV----ESQRGEIIFNGQ 386
Cdd:COG4181 6 APIIELRGLTKTVGTGAG-------ELTILKGISLEVEAGESVAIVGASGSGKST----LLGLLagldRPTSGTVRLAGQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 387 RIDTLAASKLQPLRRD-IQFIFQdpyaS--LDPRQTVgysiLE----PLrvhgLLQGDAGS-KRVAWLLERVGL--LPEH 456
Cdd:COG4181 75 DLFALDEDARARLRARhVGFVFQ----SfqLLPTLTA----LEnvmlPL----ELAGRRDArARARALLERVGLghRLDH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 457 awrYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERiSHRVAV 536
Cdd:COG4181 143 ---YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLR 218
|
250
....*....|....
gi 949724212 537 MYLGQIVEIGTRRA 550
Cdd:COG4181 219 LRAGRLVEDTAATA 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
287-547 |
1.06e-30 |
|
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: 126.80 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 287 FPLISLHDPSHvePQTEQDTVVEGEPILRVRNLVTRFPLRSGILNrvtrevhaveNVSFDLWPGETLSLVGESGCGKSTT 366
Cdd:COG4988 312 FALLDAPEPAA--PAGTAPLPAAGPPSIELEDVSFSYPGGRPALD----------GLSLTIPPGERVALVGPSGAGKSTL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 367 GRALLRLVESQRGEIIFNGQRIDTLAaskLQPLRRDIQFIFQDPYasldprqTVGYSILEPLRvhgLLQGDAGSKRVAWL 446
Cdd:COG4988 380 LNLLLGFLPPYSGSILINGVDLSDLD---PASWRRQIAWVPQNPY-------LFAGTIRENLR---LGRPDASDEELEAA 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 447 LERVGL------LP--------EHAWRypheFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRE 512
Cdd:COG4988 447 LEAAGLdefvaaLPdgldtplgEGGRG----LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG 522
|
250 260 270
....*....|....*....|....*....|....*
gi 949724212 513 LGIayLFISHDMAVVERISHRVaVMYLGQIVEIGT 547
Cdd:COG4988 523 RTV--ILITHRLALLAQADRIL-VLDDGRIVEQGT 554
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
12-245 |
1.42e-30 |
|
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: 119.38 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqaGG--EVSCDEMLLRRRNrqvie 89
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKS----TLLHLL---GGldNPTSGEVLFNGQS----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 90 LGEQSASQMRHVRGADIAMIFQepMTSLNPVFTVGEQIAESIrLHQGASHEEAMVEAKRMLDQVripEAKAILSRYPHQL 169
Cdd:TIGR02211 69 LSKLSSNERAKLRNKKLGFIYQ--FHHLLPDFTALENVAMPL-LIGKKSVKEAKERAYEMLEKV---GLEHRINHRPSEL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGvVADIADRVLVMYQG 245
Cdd:TIGR02211 143 SGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLE-LAKKLDRVLEMKDG 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
314-543 |
1.53e-30 |
|
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: 117.14 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFPlrsgilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTlaA 393
Cdd:cd03216 1 LELRGITKRFG-----------GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF--A 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 SKLQPLRRDIQFIFQdpyasldprqtvgysileplrvhgllqgdagskrvawllervgllpehawrypheFSGGQRQRIC 473
Cdd:cd03216 68 SPRDARRAGIAMVYQ-------------------------------------------------------LSVGERQMVE 92
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 474 IARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
Cdd:cd03216 93 IARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-257 |
1.76e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.48 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 19 NIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNrqvielgeqsasqM 98
Cdd:PRK13632 12 NVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN-------------L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 99 RHVRGaDIAMIFQEPmtslNPVF---TVGEQIAESIrlhqgashEEAMVEAKRMLD-------QVRIpeaKAILSRYPHQ 168
Cdd:PRK13632 79 KEIRK-KIGIIFQNP----DNQFigaTVEDDIAFGL--------ENKKVPPKKMKDiiddlakKVGM---EDYLDKEPQN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVAdIADRVLVMYQGEAV 248
Cdd:PRK13632 143 LSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLI 221
|
....*....
gi 949724212 249 ETGSVEQIF 257
Cdd:PRK13632 222 AQGKPKEIL 230
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
337-542 |
2.06e-30 |
|
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: 118.66 E-value: 2.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 337 VHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQPLRRDIQFIFQDpyASLDP 416
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 417 RQTVGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLlpEHAWR-YPHEFSGGQRQRICIARALALNPKVIIADESVSALD 495
Cdd:cd03292 92 DRNVYENVAFALEVTGVPPREI-RKRVPAALELVGL--SHKHRaLPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 949724212 496 VSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:cd03292 169 PDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
32-261 |
2.25e-30 |
|
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: 119.36 E-value: 2.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 32 VRNLSFRLKRGETLAIVGESGSGKSVtalslmhLIEQAGGEVSCDEMLLRRRNRQVIELgeqsASQMRhvrgaDIAMIFQ 111
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSV-------LLETIAGFIKPDSGKILLNGKDITNL----PPEKR-----DISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 112 EpmTSLNPVFTVGEQIAESIRlHQGASHEEAMVEAKRMLDQVRIPEakaILSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
Cdd:cd03299 79 N--YALFPHMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGIDH---LLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 192 ADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQ 261
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
311-537 |
2.82e-30 |
|
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: 118.69 E-value: 2.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPLRsgilNRVTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFN--GQRI 388
Cdd:COG4778 2 TTLLEVENLSKTFTLH----LQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 389 DTLAASKLQPL---RRDI----QFifqdpyasLD--PRQTVGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLlPEHAWR 459
Cdd:COG4778 78 DLAQASPREILalrRRTIgyvsQF--------LRviPRVSALDVVAEPLLERGVDREEA-RARARELLARLNL-PERLWD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 460 -YPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVM 537
Cdd:COG4778 148 lPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDV 225
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
298-559 |
3.11e-30 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 126.49 E-value: 3.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 298 VEPQTEQDTVVEGEPI--LRVRNLVTRFPlrsgilnrvTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVE 375
Cdd:COG2274 456 PEREEGRSKLSLPRLKgdIELENVSFRYP---------GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 376 SQRGEIIFNGQRIDTLAaskLQPLRRDIQFIFQDPYasLDPRqtvgySILEPLRVHgllQGDAGSKRVAWLLERVGLlpe 455
Cdd:COG2274 527 PTSGRILIDGIDLRQID---PASLRRQIGVVLQDVF--LFSG-----TIRENITLG---DPDATDEEIIEAARLAGL--- 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 456 hawrypHEF-------------------SGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRelGIA 516
Cdd:COG2274 591 ------HDFiealpmgydtvvgeggsnlSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRT 662
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 949724212 517 YLFISHDMAVVeRISHRVAVMYLGQIVEIGTRRAVFENPQHPY 559
Cdd:COG2274 663 VIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLARKGLYA 704
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
28-275 |
3.20e-30 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 118.75 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 28 RVSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqAGgevscdemlLRRRNRQVIELGEQSASQMrHVRGADIA 107
Cdd:TIGR00968 12 SFQALDDVNLEVPTGSLVALLGPSGSGKS----TLLRII--AG---------LEQPDSGRIRLNGQDATRV-HARDRKIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 108 MIFQEpmTSLNPVFTVGEQIAESIRLHQgasHEEAMVEAK--RMLDQVRIpeaKAILSRYPHQLSGGMRQRVMIAMALSC 185
Cdd:TIGR00968 76 FVFQH--YALFKHLTVRDNIAFGLEIRK---HPKAKIKARveELLELVQL---EGLGDRYPNQLSGGQRQRVALARALAV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQHPYT 265
Cdd:TIGR00968 148 EPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFV 227
|
250
....*....|
gi 949724212 266 KALLAAVPQL 275
Cdd:TIGR00968 228 MSFLGEVNVL 237
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
316-547 |
3.45e-30 |
|
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: 118.24 E-value: 3.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 316 VRNLVTRFplrsgilnrvtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASk 395
Cdd:cd03265 3 VENLVKKY-----------GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 396 lqpLRRDIQFIFQDPyaSLDPRQTvGYsilEPLRVHGLLQGDAGSK---RVAWLLERVGLLpEHAWRYPHEFSGGQRQRI 472
Cdd:cd03265 71 ---VRRRIGIVFQDL--SVDDELT-GW---ENLYIHARLYGVPGAErreRIDELLDFVGLL-EAADRLVKTYSGGMRRRL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 473 CIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGT 547
Cdd:cd03265 141 EIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGT 215
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
29-251 |
3.90e-30 |
|
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: 117.74 E-value: 3.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEmllrrrnRQVIELGEQSAsqmrhvrgaDIAM 108
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG-------RDVTDLPPKDR---------DIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 109 IFQEpmTSLNPVFTVGEQIAESIRLHqGASHEEAmveAKRMLDQVRIPEAKAILSRYPHQLSGGMRQRVMIAMALSCRPA 188
Cdd:cd03301 77 VFQN--YALYPHMTVYDNIAFGLKLR-KVPKDEI---DERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 189 VLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
31-249 |
4.15e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 118.23 E-value: 4.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQA-GGEVSCDEMLLRR-RNRQVielgeqsaSQMRhvRgaDIAM 108
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKS-TLLKLLYGEERPtSGQVLVNGQDLSRlKRREI--------PYLR--R--RIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 109 IFQEpmtslnpvF------TVGEQIAESIRLHqGASHEEAMVEAKRMLDQVRIpEAKAilSRYPHQLSGGMRQRVMIAMA 182
Cdd:COG2884 84 VFQD--------FrllpdrTVYENVALPLRVT-GKSRKEIRRRVREVLDLVGL-SDKA--KALPHELSGGEQQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQdmsMG--VIFITHDMGVVADIADRVLVMYQGEAVE 249
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINR---RGttVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
340-546 |
4.22e-30 |
|
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: 116.77 E-value: 4.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLqplrrdiqfifqdpyasldpRQT 419
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------------------ARK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 420 VGYsileplrvhgLLQgdagskrvawLLERVGLLPEhAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIR 499
Cdd:cd03214 75 IAY----------VPQ----------ALELLGLAHL-ADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 949724212 500 GQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
12-256 |
7.02e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 118.24 E-value: 7.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQQrvsAVRNLSFRLKRGETLAIVGESGSGKSvTAL-SLMHLIEQAGGEVSCDEmllrrrnrqvIEL 90
Cdd:COG3638 2 MLELRNLSKRYPGGTP---ALDDVSLEIERGEFVALIGPSGAGKS-TLLrCLNGLVEPTSGEILVDG----------QDV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 91 GEQSASQMRHVRgADIAMIFQEP-----MTSLNPVFTvGeqiaesiRLHQ--------GASHEEAMVEAKRMLDQVRIPE 157
Cdd:COG3638 68 TALRGRALRRLR-RRIGMIFQQFnlvprLSVLTNVLA-G-------RLGRtstwrsllGLFPPEDRERALEALERVGLAD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 158 aKAiLSRyPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIAD 237
Cdd:COG3638 139 -KA-YQR-ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYAD 215
|
250
....*....|....*....
gi 949724212 238 RVLVMYQGEAVETGSVEQI 256
Cdd:COG3638 216 RIIGLRDGRVVFDGPPAEL 234
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
289-565 |
1.04e-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: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 289 LISLHDPSHVEPQTEQDTVVEGEPILRVRNLVTRFPlrsgilnrvTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGR 368
Cdd:COG4987 309 LNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYP---------GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLA 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 369 ALLRLVESQRGEIIFNGQRIDTLAASKlqpLRRDIQFIFQDPY--ASldprqtvgySILEPLRvhgLLQGDAGSKRVAWL 446
Cdd:COG4987 380 LLLRFLDPQSGSITLGGVDLRDLDEDD---LRRRIAVVPQRPHlfDT---------TLRENLR---LARPDATDEELWAA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 447 LERVGL------LPE--HAWRYPH--EFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIa 516
Cdd:COG4987 445 LERVGLgdwlaaLPDglDTWLGEGgrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV- 523
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 949724212 517 yLFISHDMAVVERIsHRVAVMYLGQIVEIGTRRAVFEnpQHPYTRKLMA 565
Cdd:COG4987 524 -LLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLA--QNGRYRQLYQ 568
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-257 |
1.50e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.11 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 8 DASDVLAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSvTAL-SLMHLIEQAGGEVSCDEMLLRRRNRQ 86
Cdd:COG1121 2 MMMPAIELENLTVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKS-TLLkAILGLLPPTSGTVRLFGKPPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 87 vielgeqsasqmrhvrgadIAMIFQepMTSLNPVF--TVGEQIAESIRLHQG------ASHEEAMVEAkrmLDQVripEA 158
Cdd:COG1121 77 -------------------IGYVPQ--RAEVDWDFpiTVRDVVLMGRYGRRGlfrrpsRADREAVDEA---LERV---GL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 159 KAILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADR 238
Cdd:COG1121 130 EDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDR 208
|
250
....*....|....*....
gi 949724212 239 VLVMyQGEAVETGSVEQIF 257
Cdd:COG1121 209 VLLL-NRGLVAHGPPEEVL 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
338-543 |
1.60e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 116.51 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 338 HAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQPLRRDIQFIFQDPYASLDpr 417
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 418 QTVGYSILEPLRVHGlLQGDAGSKRVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVS 497
Cdd:PRK10908 94 RTVYDNVAIPLIIAG-ASGDDIRRRVSAALDKVGLL-DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 949724212 498 IRGQIINLMLDLQReLGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
Cdd:PRK10908 172 LSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
339-556 |
1.62e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 117.93 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDtlaASKLQPLRRDIQFIFQDPyasldPRQ 418
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT---DDNFEKLRKHIGIVFQNP-----DNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 419 TVG----YSILEPLRVHgLLQGDAGSKRVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSAL 494
Cdd:PRK13648 96 FVGsivkYDVAFGLENH-AVPYDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 495 DVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHrVAVMYLGQIVEIGTRRAVFENPQ 556
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADH-VIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-251 |
1.63e-29 |
|
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: 114.84 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 14 AVSNLNIAFeqeQQRVsAVRNLSFRLKRGETLAIVGESGSGKSvTAL-SLMHLIEQAGGEvscdemllrrrnrqvIELGE 92
Cdd:cd03214 1 EVENLSVGY---GGRT-VLDDLSLSIEAGEIVGILGPNGAGKS-TLLkTLAGLLKPSSGE---------------ILLDG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 93 QSASQMRHVRGA-DIAMIFQepmtslnpvftvgeqiaesirlhqgasheeamveakrMLDQVRIpeaKAILSRYPHQLSG 171
Cdd:cd03214 61 KDLASLSPKELArKIAYVPQ-------------------------------------ALELLGL---AHLADRPFNELSG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:cd03214 101 GERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
13-261 |
3.22e-29 |
|
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: 116.00 E-value: 3.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQeqqrVSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLI----EQAGGEVS-CDEMLLRRRNRQV 87
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKT----TLFNLIsgflRPTSGSVLfDGEDITGLPPHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 88 IELGeqsasqmrhvrgadIAMIFQEP-----MTSLNPVfTVGEQIA--ESIRLHQGASHEEAMVE-AKRMLDQVRIPEak 159
Cdd:cd03219 73 ARLG--------------IGRTFQIPrlfpeLTVLENV-MVAAQARtgSGLLLARARREEREARErAEELLERVGLAD-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 160 aILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRV 239
Cdd:cd03219 136 -LADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRV 213
|
250 260
....*....|....*....|..
gi 949724212 240 LVMYQGEAVETGSVEQIFHAPQ 261
Cdd:cd03219 214 TVLDQGRVIAEGTPDEVRNNPR 235
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
336-565 |
3.66e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 116.61 E-value: 3.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 EVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAAS----------KLQPLRRDIQF 405
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 406 IFQdpYASLDPRQTVGYSILE-PLRVHGLLQGDAGSKRVAWLlERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKV 484
Cdd:PRK10619 97 VFQ--HFNLWSHMTVLENVMEaPIQVLGLSKQEARERAVKYL-AKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 485 IIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQHPYTRKLM 564
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFL 252
|
.
gi 949724212 565 A 565
Cdd:PRK10619 253 K 253
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
336-552 |
6.56e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 116.37 E-value: 6.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 EVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRidtLAASKLQPLRRDIQFIFQDPyasld 415
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL---LTEENVWDIRHKIGMVFQNP----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 416 PRQTVGYSIlEPLRVHGL----LQGDAGSKRVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESV 491
Cdd:PRK13650 91 DNQFVGATV-EDDVAFGLenkgIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 492 SALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVErISHRVAVMYLGQIVEIGTRRAVF 552
Cdd:PRK13650 169 SMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELF 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-261 |
6.88e-29 |
|
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: 115.52 E-value: 6.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 9 ASDVLAVSNLNIAFeqeqQRVSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLI----EQAGGEVSCD-EMLLRRR 83
Cdd:COG0411 1 SDPLLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKT----TLFNLItgfyRPTSGRILFDgRDITGLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 84 NRQVIELGeqsasqmrhvrgadIAMIFQepMTSLNPVFTVGEQIAESIRLHQGAS--------------HEEAMVEAKRM 149
Cdd:COG0411 73 PHRIARLG--------------IARTFQ--NPRLFPELTVLENVLVAAHARLGRGllaallrlprarreEREARERAEEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 150 LDQVRIpEAKAilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDM 229
Cdd:COG0411 137 LERVGL-ADRA--DEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDM 213
|
250 260 270
....*....|....*....|....*....|..
gi 949724212 230 GVVADIADRVLVMYQGEAVETGSVEQIFHAPQ 261
Cdd:COG0411 214 DLVMGLADRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
343-575 |
7.05e-29 |
|
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: 118.29 E-value: 7.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 343 VSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQridTLAASK----LQPLRRDIQFIFQDpyASLDPRq 418
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR---TLFDSRkgifLPPEKRRIGYVFQE--ARLFPH- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 419 tvgYSILEPLRvHGLLQGDAGSKRVAW--LLERVGLlpEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADESVSALD 495
Cdd:TIGR02142 90 ---LSVRGNLR-YGMKRARPSERRISFerVIELLGI--GHLLgRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 496 VSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQHPYTRK------LMAAVPV 569
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLARedqgslIEGVVAE 243
|
....*.
gi 949724212 570 ADPSHH 575
Cdd:TIGR02142 244 HDQHYG 249
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
31-288 |
7.18e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 118.98 E-value: 7.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEmllrrrnrqvIELGEQSASQMRHVRGADIAMIF 110
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG----------VDIAKISDAELREVRRKKIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEpmTSLNPVFTVGEQIAESIRLHQGASHEEAmveaKRMLDQVRIPEAKAILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:PRK10070 113 QS--FALMPHMTVLDNTAFGMELAGINAEERR----EKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 191 IADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQHPYTKALLA 270
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
|
250
....*....|....*...
gi 949724212 271 AVPQLGAMNGHELPRRFP 288
Cdd:PRK10070 267 GVDISQVFSAKDIARRTP 284
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
31-257 |
7.22e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 116.30 E-value: 7.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEmllrrrnrqvIELGEQSASqMRHVRgADIAMIF 110
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG----------VDITDKKVK-LSDIR-KKVGLVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEPMTSLnpvF--TVGEQIAESIRlHQGASHEEAMVEAKRMLDQVRIPEAKaILSRYPHQLSGGMRQRVMIAMALSCRPA 188
Cdd:PRK13637 90 QYPEYQL---FeeTIEKDIAFGPI-NLGLSEEEIENRVKRAMNIVGLDYED-YKDKSPFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 189 VLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIF 257
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
7-257 |
7.70e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 117.26 E-value: 7.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 7 LDASDVLAVSNLNIAFEQEQ-QRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRR-- 83
Cdd:PRK13631 16 LSDDIILRVKNLYCVFDEKQeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKkn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 84 -NRQVIELGEQSASQMRHVRGAdIAMIFQEPMTSLnpvF--TVGEQIA-ESIRLhqGASHEEAMVEAKRMLDQVRIPEAk 159
Cdd:PRK13631 96 nHELITNPYSKKIKNFKELRRR-VSMVFQFPEYQL---FkdTIEKDIMfGPVAL--GVKKSEAKKLAKFYLNKMGLDDS- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 160 aILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRV 239
Cdd:PRK13631 169 -YLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEV 246
|
250
....*....|....*...
gi 949724212 240 LVMYQGEAVETGSVEQIF 257
Cdd:PRK13631 247 IVMDKGKILKTGTPYEIF 264
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
34-261 |
8.56e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 116.27 E-value: 8.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 34 NLSFRlkRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEmllrrrnrQVIElGEQSASQMRHVRgADIAMIFQEP 113
Cdd:PRK13634 27 NVSIP--SGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGE--------RVIT-AGKKNKKLKPLR-KKVGIVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 114 MTSLnpvF--TVGEQIAESiRLHQGASHEEAMVEAKRMLDQVRIPEAkaILSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
Cdd:PRK13634 95 EHQL---FeeTVEKDICFG-PMNFGVSEEDAKQKAREMIELVGLPEE--LLARSPFELSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 192 ADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQ 261
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
31-256 |
1.09e-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: 114.00 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGE-------VSCDEMLLRRRnrqvielgeqsasqmrhvrg 103
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdVVREPREVRRR-------------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 104 adIAMIFQEPmtSLNPVFTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIPEAKailSRYPHQLSGGMRQRVMIAMAL 183
Cdd:cd03265 75 --IGIVFQDL--SVDDELTGWENLYIHARL-YGVPGAERRERIDELLDFVGLLEAA---DRLVKTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQI 256
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
29-550 |
1.17e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 120.27 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDemllrrrNRQVIELGEQSASQMrhvrgaDIAM 108
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN-------NINYNKLDHKLAAQL------GIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 109 IFQE-----PMTSLNPVFtVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIpeaKAILSRYPHQLSGGMRQRVMIAMAL 183
Cdd:PRK09700 85 IYQElsvidELTVLENLY-IGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGL---KVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 184 SCRPAVLIADEPTTALdvtIQAQILQLIKVLQQDMSMG--VIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIfhapq 261
Cdd:PRK09700 161 MLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQLRKEGtaIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 262 hpYTKALLAAvpqlgaMNGHELPRRFPlislhdpshvePQTEQDTVVEGEPILRVRNLVTRfplrsgilnrvtrEVHAVE 341
Cdd:PRK09700 233 --SNDDIVRL------MVGRELQNRFN-----------AMKENVSNLAHETVFEVRNVTSR-------------DRKKVR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 342 NVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDtlAASKLQPLRRDIQFIFQDP-----YASLDP 416
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAVKKGMAYITESRrdngfFPNFSI 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 417 RQTVgySILEPLRVHGL-----LQGDAGSKRVAWLLERVGLLPEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADES 490
Cdd:PRK09700 359 AQNM--AISRSLKDGGYkgamgLFHEVDEQRTAENQRELLALKCHSVnQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 491 VSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRA 550
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
312-534 |
1.38e-28 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 114.14 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 312 PILRVRNLVTRFplRSGilnRVTREVhaVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTL 391
Cdd:PRK11629 4 ILLQCDNLCKRY--QEG---SVQTDV--LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 392 AASKLQPLR-RDIQFIFQdpYASLDPRQTVGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLlPEHAWRYPHEFSGGQRQ 470
Cdd:PRK11629 77 SSAAKAELRnQKLGFIYQ--FHHLLPDFTALENVAMPLLIGKKKPAEI-NSRALEMLAAVGL-EHRANHRPSELSGGERQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 949724212 471 RICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRV 534
Cdd:PRK11629 153 RVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
17-245 |
1.44e-28 |
|
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: 113.54 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 17 NLNIAFEQEQQRVSAvrNLSFRLKrGETLAIVGESGSGKSvTALSLMHLIEQA-GGEVSCDEMLLRRRNRQVIelgeqSA 95
Cdd:cd03297 1 MLCVDIEKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKS-TLLRCIAGLEKPdGGTIVLNGTVLFDSRKKIN-----LP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 96 SQMRHvrgadIAMIFQEpmTSLNPVFTVGEQIAESIRLHqgaSHEEAMVEAKRMLDQVRIPEakaILSRYPHQLSGGMRQ 175
Cdd:cd03297 72 PQQRK-----IGLVFQQ--YALFPHLNVRENLAFGLKRK---RNREDRISVDELLDLLGLDH---LLNRYPAQLSGGEKQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQG 245
Cdd:cd03297 139 RVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
313-546 |
1.53e-28 |
|
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: 113.62 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 313 ILRVRNLVTRFPLrsgilnrVTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGqrIDTLA 392
Cdd:cd03266 1 MITADALTKRFRD-------VKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 393 ASklQPLRRDIQFIFQDP--YASLDPRQTVGYSIleplRVHGLlQGDAGSKRVAWLLERVGLlPEHAWRYPHEFSGGQRQ 470
Cdd:cd03266 72 EP--AEARRRLGFVSDSTglYDRLTARENLEYFA----GLYGL-KGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 471 RICIARALALNPKVIIADESVSALDVSIRgQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMAT-RALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
311-544 |
1.72e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 119.35 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPlrsGilnrvtreVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDt 390
Cdd:COG1129 2 EPLLEMRGISKSFG---G--------VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 391 lAASKLQPLRRDIQFIFQDPyaSLDPRQTVGYSIL---EPLRvHGLLQGDAGSKRVAWLLERVGlLPEHAWRYPHEFSGG 467
Cdd:COG1129 70 -FRSPRDAQAAGIAIIHQEL--NLVPNLSVAENIFlgrEPRR-GGLIDWRAMRRRARELLARLG-LDIDPDTPVGDLSVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 468 QRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLqRELGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
Cdd:COG1129 145 QQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVG 220
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-242 |
1.84e-28 |
|
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: 113.01 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 15 VSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSvTAL-SLMHLIEQAGGEvscdemllrrrnrqvIELGEQ 93
Cdd:cd03235 2 VEDLTVSYGGHP----VLEDVSFEVKPGEFLAIVGPNGAGKS-TLLkAILGLLKPTSGS---------------IRVFGK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 94 SASQMRHvrgaDIAMIFQEpmTSLNPVF--TVGEQIA----ESIRLHQGASHEEaMVEAKRMLDQVRIpeaKAILSRYPH 167
Cdd:cd03235 62 PLEKERK----RIGYVPQR--RSIDRDFpiSVRDVVLmglyGHKGLFRRLSKAD-KAKVDEALERVGL---SELADRQIG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRVLVM 242
Cdd:cd03235 132 ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
29-262 |
1.94e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 116.71 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqAG------GEVSCDemllrrrNRQVIELgeqsasqmrHVR 102
Cdd:COG3839 16 VEALKDIDLDIEDGEFLVLLGPSGCGKS----TLLRMI--AGledptsGEILIG-------GRDVTDL---------PPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 103 GADIAMIFQEPmtSLNPVFTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIPEakaILSRYPHQLSGGMRQRVMIAMA 182
Cdd:COG3839 74 DRNIAMVFQSY--ALYPHMTVYENIAFPLKL-RKVPKAEIDRRVREAAELLGLED---LLDRKPKQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHD----MGvvadIADRVLVMYQGEAVETGSVEQIFH 258
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMT----LADRIAVMNDGRIQQVGTPEELYD 223
|
....
gi 949724212 259 APQH 262
Cdd:COG3839 224 RPAN 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
344-564 |
2.21e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 113.31 E-value: 2.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 344 SFDLW--PGETLSLVGESGCGKSTtgraLLRLV----ESQRGEIIFNGQRIDTLAasklqPLRRDIQFIFQDP--YASLD 415
Cdd:COG3840 17 RFDLTiaAGERVAILGPSGAGKST----LLNLIagflPPDSGRILWNGQDLTALP-----PAERPVSMLFQENnlFPHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 416 PRQTVGYSILEPLRVhgllqGDAGSKRVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALD 495
Cdd:COG3840 88 VAQNIGLGLRPGLKL-----TAEQRAQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 496 VSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQHPYTRKLM 564
Cdd:COG3840 162 PALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
342-555 |
3.74e-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: 115.97 E-value: 3.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 342 NVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRI-DTLAASKLQPLRRDIQFIFQDpyASLDPRQTV 420
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqDSARGIFLPPHRRRIGYVFQE--ARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 421 gysiLEPLRvHGLLQGDAGSKRVAW--LLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSI 498
Cdd:COG4148 95 ----RGNLL-YGRKRAPRAERRISFdeVVELLGIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 499 RGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENP 555
Cdd:COG4148 169 KAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
339-556 |
4.56e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.55 E-value: 4.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQridTLAASKLQPLRRDIQFIFQDPyasldPRQ 418
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI---TISKENLKEIRKKIGIIFQNP-----DNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 419 TVGYSI-------LEPLRVhgllQGDAGSKRVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESV 491
Cdd:PRK13632 96 FIGATVeddiafgLENKKV----PPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDEST 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 492 SALDVSIRGQIINLMLDLQRELGIAYLFISHDMAvvERI-SHRVAVMYLGQIVEIGTRRAVFENPQ 556
Cdd:PRK13632 171 SMLDPKGKREIKKIMVDLRKTRKKTLISITHDMD--EAIlADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-255 |
4.67e-28 |
|
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: 118.71 E-value: 4.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 4 SDELDASDVLAVSNLNIAFEQEQQrvsAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEmllrrr 83
Cdd:COG4988 328 PLPAAGPPSIELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING------ 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 84 nrqvIELGEQSASQMRhvrgADIAMIFQEPmtslnpvFTVGEQIAESIRLHQGASHEEAMVEAkrmLDQVRIPEakaILS 163
Cdd:COG4988 399 ----VDLSDLDPASWR----RQIAWVPQNP-------YLFAGTIRENLRLGRPDASDEELEAA---LEAAGLDE---FVA 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 164 RYPH-----------QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVV 232
Cdd:COG4988 458 ALPDgldtplgeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRT--VILITHRLALL 535
|
250 260
....*....|....*....|...
gi 949724212 233 ADiADRVLVMYQGEAVETGSVEQ 255
Cdd:COG4988 536 AQ-ADRILVLDDGRIVEQGTHEE 557
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
318-555 |
4.93e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 115.57 E-value: 4.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 318 NLVTRFPLRSGILNrvtrevhaveNVSFDLWPGETLSLVGESGCGKSTtgraLLRLV---ESQR-GEIIFNGQRIdtlaa 393
Cdd:PRK10851 6 ANIKKSFGRTQVLN----------DISLDIPSGQMVALLGPSGSGKTT----LLRIIaglEHQTsGHIRFHGTDV----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 SKLQPLRRDIQFIFQDpYAsLDPRQTVGYSILEPLRV---HGLLQGDAGSKRVAWLLERVGLlpEH-AWRYPHEFSGGQR 469
Cdd:PRK10851 67 SRLHARDRKVGFVFQH-YA-LFRHMTVFDNIAFGLTVlprRERPNAAAIKAKVTQLLEMVQL--AHlADRYPAQLSGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 470 QRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRR 549
Cdd:PRK10851 143 QRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
....*.
gi 949724212 550 AVFENP 555
Cdd:PRK10851 223 QVWREP 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
338-537 |
5.15e-28 |
|
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: 111.86 E-value: 5.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 338 HAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQridtlaasKLQPLRRDIQFIFQ----DPYAS 413
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK--------PLEKERKRIGYVPQrrsiDRDFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 414 LDPRQTVGYSILEPLRVHGLLqGDAGSKRVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSA 493
Cdd:cd03235 85 ISVRDVVLMGLYGHKGLFRRL-SKADKAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 949724212 494 LDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVM 537
Cdd:cd03235 163 VDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
13-264 |
1.00e-27 |
|
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: 114.75 E-value: 1.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQeqqrVSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqAGgevscdemlLRRRNRQVIELGE 92
Cdd:TIGR03265 5 LSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKT----TLLRII--AG---------LERQTAGTIYQGG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 93 QSAS----QMRhvrgaDIAMIFQEpmTSLNPVFTVGEQIAESIRlHQGASHEEAMVEAKRMLDQVRIPEAKailSRYPHQ 168
Cdd:TIGR03265 66 RDITrlppQKR-----DYGIVFQS--YALFPNLTVADNIAYGLK-NRGMGRAEVAERVAELLDLVGLPGSE---RKYPGQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAV 248
Cdd:TIGR03265 135 LSGGQQQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIE 214
|
250
....*....|....*.
gi 949724212 249 ETGSVEQIFHAPQHPY 264
Cdd:TIGR03265 215 QVGTPQEIYRHPATPF 230
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
340-525 |
1.04e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 111.03 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRAL---LRLVESQRGEIIFNGQRIDTlaaskLQPLRRDIQFIFQDPYasLDP 416
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtLSPAFSASGEVLLNGRRLTA-----LPAEQRRIGILFQDDL--LFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 417 RQTVGYSILEPLRVHglLQGDAGSKRVAWLLERVGlLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDV 496
Cdd:COG4136 90 HLSVGENLAFALPPT--IGRAQRRARVEQALEEAG-LAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
170 180
....*....|....*....|....*....
gi 949724212 497 SIRGQIINLMLDLQRELGIAYLFISHDMA 525
Cdd:COG4136 167 ALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
12-242 |
1.20e-27 |
|
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: 111.37 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAF---EQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLI-----EQAGgevscdEMLLRRR 83
Cdd:COG4778 4 LLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKS----TLLKCIygnylPDSG------SILVRHD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 84 NrQVIELGEQSASQMRHVRGADIAMIFQepmtSLNPVFTVG--EQIAESIrLHQGASHEEAMVEAKRMLDQVRIPEAKAI 161
Cdd:COG4778 74 G-GWVDLAQASPREILALRRRTIGYVSQ----FLRVIPRVSalDVVAEPL-LERGVDREEARARARELLARLNLPERLWD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 162 LsrYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRVLV 241
Cdd:COG4778 148 L--PPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVD 224
|
.
gi 949724212 242 M 242
Cdd:COG4778 225 V 225
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
34-272 |
1.43e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 111.34 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 34 NLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQ-AGGEVSCDEMLLRRRNRQVielgeqsasqmRHVRgADIAMIFQE 112
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKS-TLLRCINKLEEiTSGDLIVDGLKVNDPKVDE-----------RLIR-QEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 113 pmTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEAKailSRYPHQLSGGMRQRVMIAMALSCRPAVLIA 192
Cdd:PRK09493 86 --FYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERA---HHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 193 DEPTTALDVTIQAQILQLIKVLQQD-MSMgvIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQHPYTKALLAA 271
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEgMTM--VIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQH 238
|
.
gi 949724212 272 V 272
Cdd:PRK09493 239 V 239
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
314-551 |
1.55e-27 |
|
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: 110.60 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFplrsgilnrvtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAA 393
Cdd:cd03224 1 LEVENLNAGY-----------GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 SKLqpLRRDIQFIFQDPyaSLDPRQTVgysiLEPLRVHGLLQGDAGSK-RVAWLLERVGLLPEHAWRYPHEFSGGQRQRI 472
Cdd:cd03224 70 HER--ARAGIGYVPEGR--RIFPELTV----EENLLLGAYARRRAKRKaRLERVYELFPRLKERRKQLAGTLSGGEQQML 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 473 CIARALALNPKVIIADESVSALDVSIRGQIINLMLDLqRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAV 551
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
313-556 |
1.72e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.09 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 313 ILRVRNLVTRFPLRSGILNrvtrevhaveNVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLA 392
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALK----------GINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 393 ASKLQpLRRDIQFIFQDPYASL-DPR--QTVGYSilePLRVHglLQGDAGSKRVAWLLERVGLLpEHAWRYPHEFSGGQR 469
Cdd:PRK13639 71 KSLLE-VRKTVGIVFQNPDDQLfAPTveEDVAFG---PLNLG--LSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 470 QRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRR 549
Cdd:PRK13639 144 KRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222
|
....*..
gi 949724212 550 AVFENPQ 556
Cdd:PRK13639 223 EVFSDIE 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-275 |
3.52e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 111.33 E-value: 3.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 23 EQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMllrrrnrqvielgeqSASQMRHVr 102
Cdd:PRK13633 17 NEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGL---------------DTSDEENL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 103 gADI----AMIFQEPMTSLnpVFT-VGEQIA---ESIrlhqGASHEEAMVEAKRMLDQVRIPEAKailsRY-PHQLSGGM 173
Cdd:PRK13633 81 -WDIrnkaGMVFQNPDNQI--VATiVEEDVAfgpENL----GIPPEEIRERVDESLKKVGMYEYR----RHaPHLLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADiADRVLVMYQGEAVETGSV 253
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTP 228
|
250 260
....*....|....*....|..
gi 949724212 254 EQIFhaPQHPYTKALLAAVPQL 275
Cdd:PRK13633 229 KEIF--KEVEMMKKIGLDVPQV 248
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
12-287 |
3.56e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 111.34 E-value: 3.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQQrVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDemllrrrnrqvielG 91
Cdd:PRK13642 4 ILEVENLVFKYEKESD-VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKID--------------G 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 EQ-SASQMRHVRgADIAMIFQEPMTSLnpvftVGEQIAESIRL---HQGASHEEAMVEAKRMLDQVRIPEAKailSRYPH 167
Cdd:PRK13642 69 ELlTAENVWNLR-RKIGMVFQNPDNQF-----VGATVEDDVAFgmeNQGIPREEMIKRVDEALLAVNMLDFK---TREPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADiADRVLVMYQGEA 247
Cdd:PRK13642 140 RLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 949724212 248 VETGSVEQIFHAPQH--------PYTKALLAAVpqlgAMNGHELPRRF 287
Cdd:PRK13642 219 IKEAAPSELFATSEDmveigldvPFSSNLMKDL----RKNGFDLPEKY 262
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-562 |
4.19e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 110.52 E-value: 4.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVE------SQRGEIIFNGQRIDTLAASKLqplRRDIQFIFQDPYAS 413
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKL---RKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 414 ldPRQTVGYSILEPLRVHGLLQGDAGSKRVAWLLERVGLLPEHAWRY---PHEFSGGQRQRICIARALALNPKVIIADES 490
Cdd:PRK14246 103 --PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 491 VSALDVSIRGQIINLMLDLQRELGIayLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQHPYTRK 562
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAI--VIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
31-253 |
5.30e-27 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 109.13 E-value: 5.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDemllrrrnrqvielGEQSASQMRHVRGaDIAMIF 110
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN--------------GYSIRTDRKAARQ-SLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEPMtsLNPVFTVGEQIAESIRLHqGASHEEAMVEAKRMLDQVRIPEAKailSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:cd03263 82 QFDA--LFDELTVREHLRFYARLK-GLPKSEIKEEVELLLRVLGLTDKA---NKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 191 IADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADIADRVLVMYQGEAVETGSV 253
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRKGRS--IILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
19-269 |
5.36e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 109.46 E-value: 5.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 19 NIAFEQEQQRVSAvrnlSFRLKRGETLAIVGESGSGKSvtalSLMHLI----EQAGGEVSCDemllrrrnrqvielGEQS 94
Cdd:COG3840 6 DLTYRYGDFPLRF----DLTIAAGERVAILGPSGAGKS----TLLNLIagflPPDSGRILWN--------------GQDL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 95 ASQMRHVRGadIAMIFQEpmTSLNPVFTVGEQIAESIR--LHQGASHEEAMVEAkrmLDQVRIpeaKAILSRYPHQLSGG 172
Cdd:COG3840 64 TALPPAERP--VSMLFQE--NNLFPHLTVAQNIGLGLRpgLKLTAEQRAQVEQA---LERVGL---AGLLDRLPGQLSGG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGS 252
Cdd:COG3840 134 QRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGP 213
|
250
....*....|....*..
gi 949724212 253 VEQIFHAPQHPYTKALL 269
Cdd:COG3840 214 TAALLDGEPPPALAAYL 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
340-555 |
5.54e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 112.51 E-value: 5.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdtlAASKLQplRRDIQFIFQDpYAsLDPRQT 419
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIQ--QRDICMVFQS-YA-LFPHMS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 420 VGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIR 499
Cdd:PRK11432 95 LGENVGYGLKMLGVPKEER-KQRVKEALELVDL-AGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 500 GQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENP 555
Cdd:PRK11432 173 RSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
29-566 |
6.33e-27 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 114.72 E-value: 6.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIEqagGEVSCDEMLLRRRNRQVIELGEQSASQmrhvrgADIAM 108
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKS----TMMKVLT---GIYTRDAGSILYLGKEVTFNGPKSSQE------AGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 109 IFQEpmtsLN--PVFTvgeqIAESIRLHQGASHEEAMVEAKRMLDqvripEAKAILSRY-----PHQLSG----GMRQRV 177
Cdd:PRK10762 84 IHQE----LNliPQLT----IAENIFLGREFVNRFGRIDWKKMYA-----EADKLLARLnlrfsSDKLVGelsiGEQQMV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 178 MIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIf 257
Cdd:PRK10762 151 EIAKVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 258 hapqhpyTKALLaavpqLGAMNGHELPRRFPLISlhdpshvepqteqdtVVEGEPILRVRNLvtrfplrSGilnrvtrev 337
Cdd:PRK10762 229 -------TEDSL-----IEMMVGRKLEDQYPRLD---------------KAPGEVRLKVDNL-------SG--------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 338 HAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTlaASKLQPLRRDIQFIFQDpyasldpR 417
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT--RSPQDGLANGIVYISED-------R 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 418 Q----TVGYSILEPL---------RVHGLLQGDAGSKRVAWLLE-----------RVGLLpehawryphefSGGQRQRIC 473
Cdd:PRK10762 337 KrdglVLGMSVKENMsltalryfsRAGGSLKHADEQQAVSDFIRlfniktpsmeqAIGLL-----------SGGNQQKVA 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 474 IARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIV-EIGTRRAVF 552
Cdd:PRK10762 406 IARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRISgEFTREQATQ 484
|
570
....*....|....
gi 949724212 553 EnpqhpytrKLMAA 566
Cdd:PRK10762 485 E--------KLMAA 490
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
19-256 |
8.29e-27 |
|
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: 115.70 E-value: 8.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 19 NIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqAGgevscdemlLRRRNRQVIELGEQSASQM 98
Cdd:COG2274 478 NVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKS----TLLKLL--LG---------LYEPTSGRILIDGIDLRQI 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 99 --RHVRgADIAMIFQEPMtslnpVF--TvgeqIAESIRLHQGASHEEAMVEAKRMLdqvripEAKAILSRYPH------- 167
Cdd:COG2274 543 dpASLR-RQIGVVLQDVF-----LFsgT----IRENITLGDPDATDEEIIEAARLA------GLHDFIEALPMgydtvvg 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 168 ----QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADiADRVLVMY 243
Cdd:COG2274 607 eggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRT--VIIIAHRLSTIRL-ADRIIVLD 683
|
250
....*....|...
gi 949724212 244 QGEAVETGSVEQI 256
Cdd:COG2274 684 KGRIVEDGTHEEL 696
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
334-547 |
1.07e-26 |
|
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: 108.78 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 334 TR-EVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAaskLQPLRRDIQFIFQDP-- 410
Cdd:cd03249 12 SRpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---LRWLRSQIGLVSQEPvl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 411 -YASLdpRQTVGYSILEPLRVHgllqgDAGSKRVAWLLERVGLLPEhawRY-----PH--EFSGGQRQRICIARALALNP 482
Cdd:cd03249 89 fDGTI--AENIRYGKPDATDEE-----VEEAAKKANIHDFIMSLPD---GYdtlvgERgsQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 483 KVIIADESVSALDvSIRGQIINLMLDLQRElGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGT 547
Cdd:cd03249 159 KILLLDEATSALD-AESEKLVQEALDRAMK-GRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQGT 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
31-257 |
1.20e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.87 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRQvielgeqsaSQMRHVRgADIAMIF 110
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKD---------KYIRPVR-KRIGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEPMTSLnpvF--TVGEQIAESIRlHQGASHEEAMVEAKRMLDQVRIPeaKAILSRYPHQLSGGMRQRVMIAMALSCRPA 188
Cdd:PRK13646 92 QFPESQL---FedTVEREIIFGPK-NFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSPFQMSGGQMRKIAIVSILAMNPD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 189 VLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIF 257
Cdd:PRK13646 166 IIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-242 |
1.30e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 109.18 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMH-LIEQAGGEVSCDemllrrrnrqvielG 91
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT-TLLNLIAgFLAPSSGEITLD--------------G 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 EQSASQmrhvrGADIAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIPEAKailSRYPHQLSG 171
Cdd:COG4525 69 VPVTGP-----GADRGVVFQK--DALLPWLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGLADFA---RRRIWQLSG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVM 242
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-270 |
1.46e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 108.90 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 9 ASDVLAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIE---QAGGEVSCDEMLLRRRNR 85
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLEkpsEGSIVVNGQTINLVRDKD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 86 QVIELGEQSASQMRHVRgadIAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEAKAIlsRY 165
Cdd:PRK10619 77 GQLKVADKNQLRLLRTR---LTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQG--KY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIfITHDMGVVADIADRVLVMYQG 245
Cdd:PRK10619 150 PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLHQG 228
|
250 260
....*....|....*....|....*
gi 949724212 246 EAVETGSVEQIFHAPQHPYTKALLA 270
Cdd:PRK10619 229 KIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
30-257 |
1.51e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.40 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 30 SAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRQVIElgeqsasqmrhVRgADIAMI 109
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLE-----------VR-KTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 110 FQEPMTSL-NPvfTVGEQIAESiRLHQGASHEEamVEaKRMLDQVRIPEAKAILSRYPHQLSGGMRQRVMIAMALSCRPA 188
Cdd:PRK13639 84 FQNPDDQLfAP--TVEEDVAFG-PLNLGLSKEE--VE-KRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 189 VLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIF 257
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
12-256 |
1.97e-26 |
|
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: 108.15 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQQrvsAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMllrrrnrqviELG 91
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQ---ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGT----------DIT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 EQSASQMRHVRgADIAMIFQE-----PMTSLNPVFT--VGEQiaESIRLHQGASHEEAMVEAKRMLDQVRIpeAKAILSR 164
Cdd:TIGR02315 68 KLRGKKLRKLR-RRIGMIFQHynlieRLTVLENVLHgrLGYK--PTWRSLLGRFSEEDKERALSALERVGL--ADKAYQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 165 yPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQ 244
Cdd:TIGR02315 143 -ADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKA 221
|
250
....*....|..
gi 949724212 245 GEAVETGSVEQI 256
Cdd:TIGR02315 222 GEIVFDGAPSEL 233
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
334-554 |
2.12e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.02 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 334 TREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGqrIDTLAASKLQPLRRDIQFIFQDPyas 413
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDIRNKAGMVFQNP--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 414 ldPRQTVGySILEPLRVHGL----LQGDAGSKRVAWLLERVGLlpehaWRY----PHEFSGGQRQRICIARALALNPKVI 485
Cdd:PRK13633 95 --DNQIVA-TIVEEDVAFGPenlgIPPEEIRERVDESLKKVGM-----YEYrrhaPHLLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 486 IADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDM-AVVEriSHRVAVMYLGQIVEIGTRRAVFEN 554
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMeEAVE--ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
335-546 |
2.49e-26 |
|
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: 106.98 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 335 REVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQPLRRDiqfifqdpyASL 414
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEE---------RGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 415 DPRQTVGYSILEPLRVHGLLQGDAgSKRVAWLLERVGlLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSAL 494
Cdd:cd03269 82 YPKMKVIDQLVYLAQLKGLKKEEA-RRRIDEWLERLE-LSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 949724212 495 DVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03269 160 DPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
31-264 |
3.01e-26 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 110.96 E-value: 3.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKS--VTALSLmhLIEQAGGEVSCDEmllrrrnrqvIELGEQSASQMRHVRGADIAM 108
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKStlVRCLNR--LIEPTAGEVLIDG----------EDITKLSKKELRELRRKKMSM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 109 IFQEpmtslnpvF------TVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRipeakaiLS----RYPHQLSGGMRQRVM 178
Cdd:COG4175 110 VFQH--------FallphrTVLENVAFGLEI-QGVPKAERRERAREALELVG-------LAgwedSYPDELSGGMQQRVG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 179 IAMALSCRPAVLIADEPTTALDVTIQAQiLQ--LIKvLQQDMSMGVIFITHDMgvvaD----IADRVLVMYQGEAVETGS 252
Cdd:COG4175 174 LARALATDPDILLMDEAFSALDPLIRRE-MQdeLLE-LQAKLKKTIVFITHDL----DealrLGDRIAIMKDGRIVQIGT 247
|
250
....*....|..
gi 949724212 253 VEQIFHAPQHPY 264
Cdd:COG4175 248 PEEILTNPANDY 259
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-270 |
3.41e-26 |
|
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: 113.32 E-value: 3.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 2 PHSDELDASDVLAVSNLNIAFEQEQQRVsaVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEmllr 81
Cdd:COG4987 323 AEPAPAPGGPSLELEDVSFRYPGAGRPV--LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG---- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 82 rrnrqvIELGEQSASQMRHVrgadIAMIFQEPmtslnPVF--TvgeqIAESIRLHQGASHEEAMVEAkrmLDQVRIPEak 159
Cdd:COG4987 397 ------VDLRDLDEDDLRRR----IAVVPQRP-----HLFdtT----LRENLRLARPDATDEELWAA---LERVGLGD-- 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 160 aILSRYPH-----------QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHD 228
Cdd:COG4987 453 -WLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRT--VLLITHR 529
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 949724212 229 MgVVADIADRVLVMYQGEAVETGSVEQIfhAPQHPYTKALLA 270
Cdd:COG4987 530 L-AGLERMDRILVLEDGRIVEQGTHEEL--LAQNGRYRQLYQ 568
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
31-260 |
3.48e-26 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 109.02 E-value: 3.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSvTALSLM-HLIEQAGGEV--------SCDEMLLRRRNRQVIelgeQSASqmrhv 101
Cdd:COG1125 17 AVDDLSLTIPAGEFTVLVGPSGCGKT-TTLRMInRLIEPTSGRIlidgedirDLDPVELRRRIGYVI----QQIG----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 102 rgadiamifqepmtsLNPVFTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIPeAKAILSRYPHQLSGGMRQRVMIAM 181
Cdd:COG1125 87 ---------------LFPHMTVAENIATVPRL-LGWDKERIRARVDELLELVGLD-PEEYRDRYPHELSGGQQQRVGVAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMgvvaD----IADRVLVMYQGEAVETGSVEQIF 257
Cdd:COG1125 150 ALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDI----DealkLGDRIAVMREGRIVQYDTPEEIL 225
|
...
gi 949724212 258 HAP 260
Cdd:COG1125 226 ANP 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-256 |
3.75e-26 |
|
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: 107.27 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQQrvsAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEmllrrrnrqvIELGE 92
Cdd:cd03256 1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDG----------TDINK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 93 QSASQMRHVRgADIAMIFQEPmtSLNPVFTVGEQIAeSIRLHQ--------GASHEEAMVEAKRMLDQVRIPEaKAilSR 164
Cdd:cd03256 68 LKGKALRQLR-RQIGMIFQQF--NLIERLSVLENVL-SGRLGRrstwrslfGLFPKEEKQRALAALERVGLLD-KA--YQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQ 244
Cdd:cd03256 141 RADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKD 220
|
250
....*....|..
gi 949724212 245 GEAVETGSVEQI 256
Cdd:cd03256 221 GRIVFDGPPAEL 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
29-256 |
5.79e-26 |
|
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: 112.20 E-value: 5.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVScdemllrrrnrqvIELGEQSASQMRhvRGAD--- 105
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVN-------------VRVGDEWVDMTK--PGPDgrg 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 106 -----IAMIFQEpmTSLNPVFTVGEQIAESIRLHqgASHEEAMVEAKRMLDQVRIPEAKA--ILSRYPHQLSGGMRQRVM 178
Cdd:TIGR03269 362 rakryIGILHQE--YDLYPHRTVLDNLTEAIGLE--LPDELARMKAVITLKMVGFDEEKAeeILDKYPDELSEGERHRVA 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 179 IAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQI 256
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
313-564 |
6.83e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.49 E-value: 6.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 313 ILRVRNLVTRFPLRSgilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRidtLA 392
Cdd:PRK13642 4 ILEVENLVFKYEKES--------DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEL---LT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 393 ASKLQPLRRDIQFIFQDPyasldPRQTVGYSILEPLRVHGLLQG---DAGSKRVAWLLERVGLLpEHAWRYPHEFSGGQR 469
Cdd:PRK13642 73 AENVWNLRRKIGMVFQNP-----DNQFVGATVEDDVAFGMENQGiprEEMIKRVDEALLAVNML-DFKTREPARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 470 QRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGTRR 549
Cdd:PRK13642 147 QRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPS 225
|
250 260
....*....|....*....|...
gi 949724212 550 AVFENPQH--------PYTRKLM 564
Cdd:PRK13642 226 ELFATSEDmveigldvPFSSNLM 248
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
337-555 |
7.17e-26 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 109.16 E-value: 7.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 337 VHAVENVSFDLWPGETLSLVGESGCGKSTtgraLLRLV---ES-QRGEIIFNGQRIDTLaasklQPLRRDIQFIFQDpYA 412
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVaglERiTSGEIWIGGRVVNEL-----EPADRDIAMVFQN-YA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 413 sLDPRQTV----GYSilepLRVHGLLQGDAgSKRV---AWLLERVGLLPehawRYPHEFSGGQRQRICIARALALNPKVI 485
Cdd:PRK11650 87 -LYPHMSVrenmAYG----LKIRGMPKAEI-EERVaeaARILELEPLLD----RKPRELSGGQRQRVAMGRAIVREPAVF 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 486 IADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMavVE--RISHRVAVMYLGQIVEIGTRRAVFENP 555
Cdd:PRK11650 157 LFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQ--VEamTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
312-523 |
7.19e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 107.26 E-value: 7.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 312 PILRVRNLVTRFPLRSGilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTL 391
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQ-------PQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 392 AAsklqplrrDIQFIFQDpyASLDPRQTVGYSILEPLRVHGLlqGDAGSKRVA-WLLERVGLlPEHAWRYPHEFSGGQRQ 470
Cdd:COG4525 75 GA--------DRGVVFQK--DALLPWLNVLDNVAFGLRLRGV--PKAERRARAeELLALVGL-ADFARRRIWQLSGGMRQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 949724212 471 RICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHD 523
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
31-256 |
7.43e-26 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 108.25 E-value: 7.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGevscdemllrrrnrQVIELGEQSASQMRHVRgADIAMIF 110
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSG--------------TARVAGYDVVREPRKVR-RSIGIVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEPmtSLNPVFTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIPEAKailSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:TIGR01188 73 QYA--SVDEDLTGRENLEMMGRL-YGLPKDEAEERAEELLELFELGEAA---DRPVGTYSGGMRRRLDIAASLIHQPDVL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 191 IADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQI 256
Cdd:TIGR01188 147 FLDEPTTGLDPRTRRAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-252 |
8.54e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 111.98 E-value: 8.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 5 DELDASDVLAVSNL----NIAFEQEQQRvSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLI-EQAGGEVSCDEML 79
Cdd:PRK13657 321 DPPGAIDLGRVKGAvefdDVSFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKS-TLINLLQRVfDPQSGRILIDGTD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 80 LRRRNRQvielgeqsasQMRHvrgaDIAMIFQEPMTsLNpvftvgEQIAESIRL-HQGASHEEAMVEAKRmldqvriPEA 158
Cdd:PRK13657 399 IRTVTRA----------SLRR----NIAVVFQDAGL-FN------RSIEDNIRVgRPDATDEEMRAAAER-------AQA 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 159 KAILSRYPH-----------QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVifITH 227
Cdd:PRK13657 451 HDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI--IAH 528
|
250 260
....*....|....*....|....*
gi 949724212 228 DMGVVADiADRVLVMYQGEAVETGS 252
Cdd:PRK13657 529 RLSTVRN-ADRILVFDNGRVVESGS 552
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
31-246 |
1.01e-25 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 103.48 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVscdemllrrrnrqvielgeqsasqmrHVRGADIAmif 110
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI--------------------------LIDGKDIA--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 qepmtslnpvftvgeqiaesirlhqgasheeamveakrmldQVRIPEAKAILSrYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:cd00267 65 -----------------------------------------KLPLEELRRRIG-YVPQLSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 191 IADEPTTALDVTIQAQILQLIKVLQQDMSMgVIFITHDMGVVADIADRVLVMYQGE 246
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGRT-VIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
311-556 |
1.10e-25 |
|
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: 105.83 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPlrsgilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDT 390
Cdd:COG0410 1 MPMLEVENLHAGYG-----------GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 391 LAASKLqpLRRDIQF------IFqdpyasldPRQTVgysiLEPLRVHGLLQGDAgsKRVAWLLERV-GLLP---EHAWRY 460
Cdd:COG0410 70 LPPHRI--ARLGIGYvpegrrIF--------PSLTV----EENLLLGAYARRDR--AEVRADLERVyELFPrlkERRRQR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 461 PHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLG 540
Cdd:COG0410 134 AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERG 212
|
250
....*....|....*.
gi 949724212 541 QIVEIGTRRAVFENPQ 556
Cdd:COG0410 213 RIVLEGTAAELLADPE 228
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
32-277 |
1.23e-25 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 108.93 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 32 VRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVScdemllrrrnrqvIELGEQSASQMR-HVRGadIAMIF 110
Cdd:TIGR03258 21 LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGLTGR-------------IAIADRDLTHAPpHKRG--LALLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEpmTSLNPVFTVGEQIAESIRlhqgASHEEAMVEAKRMLDQVRIPEAKAILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:TIGR03258 86 QN--YALFPHLKVEDNVAFGLR----AQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 191 IADEPTTALDVTIQAQILQLIKVLQQDM-SMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQHPYTKALL 269
Cdd:TIGR03258 160 LLDEPLSALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFL 239
|
....*...
gi 949724212 270 AAVPQLGA 277
Cdd:TIGR03258 240 GAANILPA 247
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
36-260 |
1.46e-25 |
|
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: 108.26 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 36 SFRLKRGETLAIVGESGSGKSvtalSLMHLIeqAG------GEVSCDEMLL----RRRNRQVielgeqsasqmrHVRGad 105
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKT----TLLRAI--AGlerpdsGRIRLGGEVLqdsaRGIFLPP------------HRRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 106 IAMIFQEPmtSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDqvrIpeaKAILSRYPHQLSGGMRQRVMIAMALSC 185
Cdd:COG4148 79 IGYVFQEA--RLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLG---I---GHLLDRRPATLSGGERQRVAIGRALLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAP 260
Cdd:COG4148 151 SPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-256 |
2.18e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 106.73 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRQVI-----ElgeqsasqmrhvRGad 105
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIgylpeE------------RG-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 106 iamifqepmtsLNPVFTVGEQIAESIRLHqGASHEEAMVEAKRMLDQVRIPE--AKAIlsrypHQLSGGMRQRVMIAMAL 183
Cdd:COG4152 82 -----------LYPKMKVGEQLVYLARLK-GLSKAEAKRRADEWLERLGLGDraNKKV-----EELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 184 SCRPAVLIADEPTTALDVtIQAQILQliKVLQQDMSMG--VIFITHDMGVVADIADRVLVMYQGEAVETGSVEQI 256
Cdd:COG4152 145 LHDPELLILDEPFSGLDP-VNVELLK--DVIRELAAKGttVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
47-279 |
2.30e-25 |
|
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: 107.19 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 47 IVGESGSGKSVTALSLMHLIEQAGGEvscdemllrrrnrqvIELGEQSASQM-RHVRGadIAMIFQEpmTSLNPVFTVGE 125
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGS---------------IMLDGEDVTNVpPHLRH--INMVFQS--YALFPHMTVEE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 126 QIAESIRLhQGASHEEAMVEAKRMLDQVRIPEAKailSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQA 205
Cdd:TIGR01187 62 NVAFGLKM-RKVPRAEIKPRVLEALRLVQLEEFA---DRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRD 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 949724212 206 QILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQHPYTKALLAAVPQLGAMN 279
Cdd:TIGR01187 138 QMQLELKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATV 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
312-566 |
2.82e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 105.50 E-value: 2.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 312 PILRVRNLVTRFPlrsgilnrvTREVhaVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQ-----RGEIIFNGQ 386
Cdd:PRK14258 6 PAIKVNNLSFYYD---------TQKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 387 RIDTLAASkLQPLRRDIQFIFQDPYasldprqtvgysiLEPLRVHGLLQgdAGSKRVAWL--LERVGLLpEHA------W 458
Cdd:PRK14258 75 NIYERRVN-LNRLRRQVSMVHPKPN-------------LFPMSVYDNVA--YGVKIVGWRpkLEIDDIV-ESAlkdadlW 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 459 --------RYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLM--LDLQRELGIayLFISHDMAVVE 528
Cdd:PRK14258 138 deikhkihKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTM--VIVSHNLHQVS 215
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 949724212 529 RISHRVAVMY-----LGQIVEIGTRRAVFENPQHPYTRKLMAA 566
Cdd:PRK14258 216 RLSDFTAFFKgnenrIGQLVEFGLTKKIFNSPHDSRTREYVLS 258
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-266 |
2.90e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 104.99 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 11 DVLAVSNLNIAFEQeqqrVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIE-----QAGGEV--------SCDE 77
Cdd:PRK14247 2 NKIEIRDLKVSFGQ----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVyldgqdifKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 78 MLLRRRnrqvielgeqsasqmrhvrgadIAMIFQEPmtslNPV--FTVGEQIAESIRLHQGA-SHEEAMVEAKRMLDQVR 154
Cdd:PRK14247 78 IELRRR----------------------VQMVFQIP----NPIpnLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 155 I-PEAKAILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVA 233
Cdd:PRK14247 132 LwDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMT--IVLVTHFPQQAA 209
|
250 260 270
....*....|....*....|....*....|...
gi 949724212 234 DIADRVLVMYQGEAVETGSVEQIFHAPQHPYTK 266
Cdd:PRK14247 210 RISDYVAFLYKGQIVEWGPTREVFTNPRHELTE 242
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
31-246 |
3.16e-25 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 102.46 E-value: 3.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRqvielgeqsasqmRHVRGAdIAMIF 110
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDL-------------ESLRKN-IAYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEPMtslnpVF--TVGEQIaesirlhqgasheeamveakrmldqvripeakailsryphqLSGGMRQRVMIAMALSCRPA 188
Cdd:cd03228 83 QDPF-----LFsgTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 189 VLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADiADRVLVMYQGE 246
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKT--VIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
28-289 |
3.53e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.09 E-value: 3.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 28 RVSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqAGgevscdemlLRRRNRQVIELGEQSASQMrHVRGADIA 107
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKT----TLLRII--AG---------LEHQTSGHIRFHGTDVSRL-HARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 108 MIFQEpmTSLNPVFTVGEQIAESIRL---HQGASHEEAMVEAKRMLDQVRIPEakaILSRYPHQLSGGMRQRVMIAMALS 184
Cdd:PRK10851 78 FVFQH--YALFRHMTVFDNIAFGLTVlprRERPNAAAIKAKVTQLLEMVQLAH---LADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQHPY 264
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRF 232
|
250 260
....*....|....*....|....*....
gi 949724212 265 TKALLAAVPQL-GAMNGHEL---PRRFPL 289
Cdd:PRK10851 233 VLEFMGEVNRLqGTIRGGQFhvgAHRWPL 261
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
336-556 |
3.54e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 105.68 E-value: 3.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 EVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASK-LQPLRRDIQFIFQDPYASL 414
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnLKKLRKKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 415 DpRQTVGYSILEPLRVHGLLQGDAGSKRVAWLlERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSAL 494
Cdd:PRK13641 99 F-ENTVLKDVEFGPKNFGFSEDEAKEKALKWL-KKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 495 DVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQ 556
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
339-547 |
3.70e-25 |
|
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: 103.73 E-value: 3.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAaskLQPLRRDIQFIFQDPY------- 411
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSRISIIPQDPVlfsgtir 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 412 ASLDPRQTVG----YSILEplRVHgllqgdagskrvawLLERVGLLPEHAwRYPHE-----FSGGQRQRICIARALALNP 482
Cdd:cd03244 96 SNLDPFGEYSdeelWQALE--RVG--------------LKEFVESLPGGL-DTVVEeggenLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 483 KVIIADESVSALDVSIRGQIINLmldLQREL-GIAYLFISHdmavveRI-----SHRVAVMYLGQIVEIGT 547
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKT---IREAFkDCTVLTIAH------RLdtiidSDRILVLDKGRVVEFDS 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
339-547 |
4.19e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 109.87 E-value: 4.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLaasKLQPLRRDIQFIFQDPY---ASLd 415
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDL---TLESLRRQIGVVPQDTFlfsGTI- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 416 pRQTVGYSileplrvhgllQGDAGSKRVAWLLERVGLlpehawrypHEF-------------------SGGQRQRICIAR 476
Cdd:COG1132 431 -RENIRYG-----------RPDATDEEVEEAAKAAQA---------HEFiealpdgydtvvgergvnlSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 477 ALALNPKVIIADESVSALDVSIRGQIINLMLDLQRelGIAYLFISHdmavveRIS-----HRVAVMYLGQIVEIGT 547
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAH------RLStirnaDRILVLDDGRIVEQGT 557
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
310-597 |
5.05e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.09 E-value: 5.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 310 GEPILRVRNLVTRFPlrsgilNRVTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEI----IFNG 385
Cdd:PRK13631 18 DDIILRVKNLYCVFD------EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 386 QRIDTLAAS---------KLQPLRRDIQFIFQDPYASLDpRQTVGYSIL-EPLRVhGLLQGDAgSKRVAWLLERVGLLPE 455
Cdd:PRK13631 92 DKKNNHELItnpyskkikNFKELRRRVSMVFQFPEYQLF-KDTIEKDIMfGPVAL-GVKKSEA-KKLAKFYLNKMGLDDS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 456 HAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVA 535
Cdd:PRK13631 169 YLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVI 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 536 VMYLGQIVEIGTRRAVFENpQHPYTRKLMAAVPVA----DPSHHRPQRVLLSDDIPSNIRKRGEEI 597
Cdd:PRK13631 248 VMDKGKILKTGTPYEIFTD-QHIINSTSIQVPRVIqvinDLIKKDPKYKKLYQKQPRTIEQLADAI 312
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
310-542 |
6.97e-25 |
|
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: 101.74 E-value: 6.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 310 GEPILRVRNLVTRfplrsgilnrvtrevHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRID 389
Cdd:cd03215 1 GEPVLEVRGLSVK---------------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 390 tlAASKLQPLRRDIQFIFQDpyasldpRQTVG----YSILEPLRVHGLLqgdagskrvawllervgllpehawryphefS 465
Cdd:cd03215 66 --RRSPRDAIRAGIAYVPED-------RKREGlvldLSVAENIALSSLL------------------------------S 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 466 GGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:cd03215 107 GGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-272 |
1.10e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 104.02 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 9 ASDVLAVSNLNIAFEQEqqrvSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRN---- 84
Cdd:PRK14271 18 AAPAMAAVNLTLGFAGK----TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSifny 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 85 RQVIELGEQsasqmrhvrgadIAMIFQEPmtslNPV-FTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEA-KAIL 162
Cdd:PRK14271 94 RDVLEFRRR------------VGMLFQRP----NPFpMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAvKDRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 163 SRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADIADRVLVM 242
Cdd:PRK14271 158 SDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLT--VIIVTHNLAQAARISDRAALF 235
|
250 260 270
....*....|....*....|....*....|
gi 949724212 243 YQGEAVETGSVEQIFHAPQHPYTKALLAAV 272
Cdd:PRK14271 236 FDGRLVEEGPTEQLFSSPKHAETARYVAGL 265
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
299-549 |
1.14e-24 |
|
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: 108.65 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 299 EPQTEQDTVVEGEPILRVRNLVTRFPlrsgilnrvTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQR 378
Cdd:TIGR02203 316 EKDTGTRAIERARGDVEFRNVTFRYP---------GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 379 GEIIFNGqriDTLAASKLQPLRRDIQFIFQDPYASLDP-RQTVGYSILEplrvhgllqgDAGSKRV------AWLLERVG 451
Cdd:TIGR02203 387 GQILLDG---HDLADYTLASLRRQVALVSQDVVLFNDTiANNIAYGRTE----------QADRAEIeralaaAYAQDFVD 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 452 LLP--------EHAWRypheFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRelGIAYLFISHD 523
Cdd:TIGR02203 454 KLPlgldtpigENGVL----LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHR 527
|
250 260
....*....|....*....|....*.
gi 949724212 524 MAVVERiSHRVAVMYLGQIVEIGTRR 549
Cdd:TIGR02203 528 LSTIEK-ADRIVVMDDGRIVERGTHN 552
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-266 |
1.17e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 103.59 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 9 ASDVLAVSNLNIAFEQEqqrvSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRrNRQVI 88
Cdd:PRK14246 7 AEDVFNISRLYLYINDK----AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYF-GKDIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 89 ELgeqSASQMRHvrgaDIAMIFQEPmtSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRI-PEAKAILSRYPH 167
Cdd:PRK14246 82 QI---DAIKLRK----EVGMVFQQP--NPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPAS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADIADRVLVMYQGEA 247
Cdd:PRK14246 153 QLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIA--IVIVSHNPQQVARVADYVAFLYNGEL 230
|
250
....*....|....*....
gi 949724212 248 VETGSVEQIFHAPQHPYTK 266
Cdd:PRK14246 231 VEWGSSNEIFTSPKNELTE 249
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
19-248 |
1.26e-24 |
|
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: 101.95 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 19 NIAFEQEQQRvSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDemllrrrnrqvielGEQSASQM 98
Cdd:cd03226 4 NISFSYKKGT-EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLN--------------GKPIKAKE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 99 RHVRgadIAMIFQEPMTSLnpvF--TVGEQIAESIRLhqgASHEEAMVEAkrMLDQVRIPEAKailSRYPHQLSGGMRQR 176
Cdd:cd03226 69 RRKS---IGYVMQDVDYQL---FtdSVREELLLGLKE---LDAGNEQAET--VLKDLDLYALK---ERHPLSLSGGQKQR 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqQDMSMGVIFITHDMGVVADIADRVLVMYQGEAV 248
Cdd:cd03226 135 LAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
31-252 |
1.71e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 107.94 E-value: 1.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSvTALSL-MHLIEQAGGEVSCDEMLLRRRNRQviELGEQsasqmrhvrgadIAMI 109
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKS-TLVNLlLRFYDPTSGRILIDGVDIRDLTLE--SLRRQ------------IGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 110 FQEPMtslnpVF--TvgeqIAESIRL-HQGASHEEaMVEAKRMLdqvripEAKAILSRYPHQ-----------LSGGMRQ 175
Cdd:COG1132 420 PQDTF-----LFsgT----IRENIRYgRPDATDEE-VEEAAKAA------QAHEFIEALPDGydtvvgergvnLSGGQRQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADiADRVLVMYQGEAVETGS 252
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRT--TIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
13-251 |
1.94e-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: 101.68 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRQVIE-LG 91
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRrLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 EQSASqmrhvrgadiamifqepmTSLNPVFTVGEQIAESIRLHqGASHEEAMVEAKRMLDQVRIpeaKAILSRYPHQLSG 171
Cdd:cd03266 82 FVSDS------------------TGLYDRLTARENLEYFAGLY-GLKGDELTARLEELADRLGM---EELLDRRVGGFST 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:cd03266 140 GMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-257 |
1.99e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 103.29 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 19 NIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTAlSLMHLIEQAggevSCDEMLLrrrNRQVIelgeqSASQM 98
Cdd:PRK13648 12 NVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIA-KLMIGIEKV----KSGEIFY---NNQAI-----TDDNF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 99 RHVRgADIAMIFQEPMTSLnpvftVGEQIAESIRL---HQGASHEEAMVEAKRMLDQVRIPEAKailSRYPHQLSGGMRQ 175
Cdd:PRK13648 79 EKLR-KHIGIVFQNPDNQF-----VGSIVKYDVAFgleNHAVPYDEMHRRVSEALKQVDMLERA---DYEPNALSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADiADRVLVMYQGEAVETGSVEQ 255
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTE 228
|
..
gi 949724212 256 IF 257
Cdd:PRK13648 229 IF 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
313-552 |
2.03e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.39 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 313 ILRVRNLVTRFPlrsgilnrvtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDtLA 392
Cdd:PRK13636 5 ILKVEELNYNYS----------DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 393 ASKLQPLRRDIQFIFQDPyasldPRQTVGYSILEPLRVHGL---LQGDAGSKRVAWLLERVGLlpEHAWRYP-HEFSGGQ 468
Cdd:PRK13636 74 RKGLMKLRESVGMVFQDP-----DNQLFSASVYQDVSFGAVnlkLPEDEVRKRVDNALKRTGI--EHLKDKPtHCLSFGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 469 RQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTR 548
Cdd:PRK13636 147 KKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
....
gi 949724212 549 RAVF 552
Cdd:PRK13636 227 KEVF 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-261 |
2.08e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 103.34 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 14 AVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTAlslmHLIEqagGEVSCDEMLLRRRNRQVIELGEQ 93
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTIS----KLIN---GLLLPDDNPNSKITVDGITLTAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 94 SASQMRHVRGadiaMIFQEPMTSLNPVfTVGEQIAESIRlHQGASHEEAMVEAKRMLDQVRIPEakaILSRYPHQLSGGM 173
Cdd:PRK13640 78 TVWDIREKVG----IVFQNPDNQFVGA-TVGDDVAFGLE-NRAVPRPEMIKIVRDVLADVGMLD---YIDSEPANLSGGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGvVADIADRVLVMYQGEAVETGSV 253
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSP 227
|
....*...
gi 949724212 254 EQIFHAPQ 261
Cdd:PRK13640 228 VEIFSKVE 235
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
335-553 |
2.47e-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: 101.92 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 335 REVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLaasKLQPLRRDIQFIFQDPYasL 414
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI---SRKSLRSMIGVVLQDTF--L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 415 DPRqtvgySILEPLRVHGLlqgDAGSKRVAWLLERVGL------LPEHAWRYPHE----FSGGQRQRICIARALALNPKV 484
Cdd:cd03254 89 FSG-----TIMENIRLGRP---NATDEEVIEAAKEAGAhdfimkLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 485 IIADESVSALDVSIRGQIINLMLDLQRelGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGTRRAVFE 553
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
341-523 |
3.35e-24 |
|
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: 100.63 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 341 ENVSFDLWPGETLSLVGESGCGKSTtgraLLR----LVESQRGEIIFNGQRIDTLAASklqpLRRDIQFIFqdPYASLDP 416
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTT----LLRilagLLPPSAGEVLWNGEPIRDARED----YRRRLAYLG--HADGLKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 417 RQTVgysiLEPLRVHGLLQGDAGSKRVAW-LLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALD 495
Cdd:COG4133 89 ELTV----RENLRFWAALYGLRADREAIDeALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
170 180
....*....|....*....|....*...
gi 949724212 496 VSIRGQIINLMLDLQRELGIAyLFISHD 523
Cdd:COG4133 164 AAGVALLAELIAAHLARGGAV-LLTTHQ 190
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
342-547 |
4.08e-24 |
|
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: 101.15 E-value: 4.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 342 NVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLaasKLQPLRRDIQFIFQDPYASLDprqTVG 421
Cdd:cd03253 19 DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV---TLDSLRRAIGVVPQDTVLFND---TIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 422 YSIL---------------EPLRVHGLLQG--DAGSKRVAwllERvGLlpehawryphEFSGGQRQRICIARALALNPKV 484
Cdd:cd03253 93 YNIRygrpdatdeevieaaKAAQIHDKIMRfpDGYDTIVG---ER-GL----------KLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 485 IIADESVSALDVSIRGQIINLMLDLQRelGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGT 547
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
9-228 |
4.88e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 101.01 E-value: 4.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 9 ASDVLAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRqvi 88
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDE--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 89 elgEQSASqmrhVRGADIAMIFQEPMtsLNPVFTVGEQIaESIRLHQGASHEEAMVEAKRMLDQVRIPEAkaiLSRYPHQ 168
Cdd:PRK10584 80 ---EARAK----LRAKHVGFVFQSFM--LIPTLNALENV-ELPALLRGESSRQSRNGAKALLEQLGLGKR---LDHLPAQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHD 228
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
313-551 |
5.13e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 102.49 E-value: 5.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 313 ILRVRNLVTRFplrsgilnrvtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDtla 392
Cdd:COG4152 1 MLELKGLTKRF-----------GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 393 asklqplrrdiqfifqdpyasLDPRQTVGY-----------SILEPL----RVHGLLQGDAgSKRVAWLLERVGlLPEHA 457
Cdd:COG4152 67 ---------------------PEDRRRIGYlpeerglypkmKVGEQLvylaRLKGLSKAEA-KRRADEWLERLG-LGDRA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 458 WRYPHEFSGGQRQRICIARALALNPKVIIADESVSALD-VSirgqiINLMLDLQREL---GIAYLFISHDMAVVERISHR 533
Cdd:COG4152 124 NKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDpVN-----VELLKDVIRELaakGTTVIFSSHQMELVEELCDR 198
|
250
....*....|....*...
gi 949724212 534 VAVMYLGQIVEIGTRRAV 551
Cdd:COG4152 199 IVIINKGRKVLSGSVDEI 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
33-544 |
5.82e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.92 E-value: 5.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 33 RNLSFRLKRGETLAIVGESGSGKSvtalSLMHLI----EQAGGEVSCDemllrrrnrqvielgeqsasqmrhvRGADIAM 108
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKS----TLLKILagelEPDSGEVSIP-------------------------KGLRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 109 IFQEPmtSLNPVFTVGEQIAESIR------------LHQGASHEEAMVE-------------------AKRMLDQVRIPE 157
Cdd:COG0488 66 LPQEP--PLDDDLTVLDTVLDGDAelraleaeleelEAKLAEPDEDLERlaelqeefealggweaearAEEILSGLGFPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 158 AkaILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDV-TIQ--AQILqlikvlqQDMSMGVIFITHD------ 228
Cdd:COG0488 144 E--DLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIEwlEEFL-------KNYPGTVLVVSHDryfldr 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 229 -MGVVADIADRVLVMYQG------------EAVETGSVEQI-------------FHAPQHPYTKAlLAAVPQLGAMNGHE 282
Cdd:COG0488 215 vATRILELDRGKLTLYPGnysayleqraerLEQEAAAYAKQqkkiakeeefirrFRAKARKAKQA-QSRIKALEKLEREE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 283 LPRR--FPLISLHDPSHVepqteqdtvveGEPILRVRNLVTRFPlrsgilnrvTREVhaVENVSFDLWPGETLSLVGESG 360
Cdd:COG0488 294 PPRRdkTVEIRFPPPERL-----------GKKVLELEGLSKSYG---------DKTL--LDDLSLRIDRGDRIGLIGPNG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 361 CGKSTTGRALLRLVESQRGEIIFnGQRIdtlaasklqplrrDIQFIFQDpYASLDPRQTVgysiLEPLRvhgLLQGDAGS 440
Cdd:COG0488 352 AGKSTLLKLLAGELEPDSGTVKL-GETV-------------KIGYFDQH-QEELDPDKTV----LDELR---DGAPGGTE 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 441 KRVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQrelGiAYLFI 520
Cdd:COG0488 410 QEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP---G-TVLLV 485
|
570 580
....*....|....*....|....
gi 949724212 521 SHDMAVVERISHRVAVMYLGQIVE 544
Cdd:COG0488 486 SHDRYFLDRVATRILEFEDGGVRE 509
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
34-257 |
6.97e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.21 E-value: 6.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 34 NLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLrrrnrqVIELGEQSASQMRHvrgaDIAMIFQEP 113
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI------TPETGNKNLKKLRK----KVSLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 114 MTSLnpvF--TVGEQIaESIRLHQGASHEEAMVEAKRMLDQVRIPEAkaILSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
Cdd:PRK13641 95 EAQL---FenTVLKDV-EFGPKNFGFSEDEAKEKALKWLKKVGLSED--LISKSPFELSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 192 ADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIF 257
Cdd:PRK13641 169 LDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
339-547 |
7.68e-24 |
|
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: 100.64 E-value: 7.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLqplrrdiqfifqdpyasldpRQ 418
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL--------------------RR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 419 TVGYSILEPLRVHGLLQGDAGSKRVAWLLERVgllpEHAWRYP--HEF-------------------SGGQRQRICIARA 477
Cdd:cd03252 77 QVGVVLQENVLFNRSIRDNIALADPGMSMERV----IEAAKLAgaHDFiselpegydtivgeqgaglSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 478 LALNPKVIIADESVSALDVSIRGQIINLMLDLQRelGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGT 547
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGS 219
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
33-240 |
9.52e-24 |
|
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: 99.23 E-value: 9.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 33 RNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQ-AGGEVSCDEMLlrrrnrqVIELGEQSASQMRHvrgADIAMIFQ 111
Cdd:TIGR03608 15 DDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLLEKfDSGQVYLNGQE-------TPPLNSKKASKFRR---EKLGYLFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 112 epmtslNPVFTVGEQIAESIRL---HQGASHEEAMVEAKRMLDQVRIpeaKAILSRYPHQLSGGMRQRVMIAMALSCRPA 188
Cdd:TIGR03608 84 ------NFALIENETVEENLDLglkYKKLSKKEKREKKKEALEKVGL---NLKLKQKIYELSGGEQQRVALARAILKPPP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 949724212 189 VLIADEPTTALDVTIQAQILQLIKVLqQDMSMGVIFITHDMgVVADIADRVL 240
Cdd:TIGR03608 155 LILADEPTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDP-EVAKQADRVI 204
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
31-257 |
1.03e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 101.62 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSvTALSLMH--LIEQAGGEVSCDemllrrrnrQVIELGEQSASQMRHVRgADIAM 108
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKS-TMIQLTNglIISETGQTIVGD---------YAIPANLKKIKEVKRLR-KEIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 109 IFQEPMTSLnpvftVGEQIAESIR---LHQGASHEEAMVEAKRMLDQVRIPEAKAilSRYPHQLSGGMRQRVMIAMALSC 185
Cdd:PRK13645 95 VFQFPEYQL-----FQETIEKDIAfgpVNLGENKQEAYKKVPELLKLVQLPEDYV--KRSPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIF 257
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
33-228 |
1.33e-23 |
|
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: 99.09 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 33 RNLSFRLKRGETLAIVGESGSGKSvTAL-SLMHLIEQAGGEVSCDemllrrrnrqvielGEQSASQMRHVRgADIAMIFQ 111
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKT-TLLrILAGLLPPSAGEVLWN--------------GEPIRDAREDYR-RRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 112 EPMtsLNPVFTVGEQIAESIRLHQGASHEEAMVEAkrmLDQVRIPEAkaiLSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
Cdd:COG4133 83 ADG--LKPELTVRENLRFWAALYGLRADREAIDEA---LEAVGLAGL---ADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 949724212 192 ADEPTTALDVTIQAQILQLIKVLQQDMSMgVIFITHD 228
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQ 190
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
340-557 |
1.45e-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: 99.46 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLqplrrdiqFIFQDpyASLDPRQT 419
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQN--YSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 420 VGYSIlePLRVHGLLQGDAGSKRVAWLLERVGL--LPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVS 497
Cdd:TIGR01184 71 VRENI--ALAVDRVLPDLSKSERRAIVEEHIALvgLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 498 IRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVM------YLGQIVEIG-----TRRAVFENPQH 557
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILEVPfprprDRLEVVEDPSY 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
339-561 |
2.22e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 99.86 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLR---LVESQR--GEIIFNGQridTLAASKLQP--LRRDIQFIFQDPY 411
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGFRveGKVTFHGK---NLYAPDVDPveVRRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 412 ASldPRqtvgySILEPL----RVHGLlQGDAG-----SKRVAWLLERV-------GLlpehawryphEFSGGQRQRICIA 475
Cdd:PRK14243 102 PF--PK-----SIYDNIaygaRINGY-KGDMDelverSLRQAALWDEVkdklkqsGL----------SLSGGQQQRLCIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 476 RALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIayLFISHDMAVVERISHRVAVM---------YLGQIVEIG 546
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFD 241
|
250
....*....|....*
gi 949724212 547 TRRAVFENPQHPYTR 561
Cdd:PRK14243 242 RTEKIFNSPQQQATR 256
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
29-246 |
2.92e-23 |
|
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: 98.09 E-value: 2.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQAG-GEVSCD-EMLLRRRNRQVielgeqsASQMRHvrgadI 106
Cdd:TIGR02673 15 VAALHDVSLHIRKGEFLFLTGPSGAGKT-TLLKLLYGALTPSrGQVRIAgEDVNRLRGRQL-------PLLRRR-----I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 107 AMIFQEpmTSLNPVFTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIPE-AKAilsrYPHQLSGGMRQRVMIAMALSC 185
Cdd:TIGR02673 82 GVVFQD--FRLLPDRTVYENVALPLEV-RGKKEREIQRRVGAALRQVGLEHkADA----FPEQLSGGEQQRVAIARAIVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQQdMSMGVIFITHDMGVVADIADRVLVMYQGE 246
Cdd:TIGR02673 155 SPPLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
32-262 |
2.94e-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: 98.69 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 32 VRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQ--AGGevscdemlLRRRNRQVIElgeqsasqmrhvRGADIAMI 109
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKS-TLLNLISGLAQptSGG--------VILEGKQITE------------PGPDRMVV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 110 FQEpmTSLNPVFTVGEQIA---ESIRLHQGASHEEAMVEakRMLDQVRIPEAKailSRYPHQLSGGMRQRVMIAMALSCR 186
Cdd:TIGR01184 60 FQN--YSLLPWLTVRENIAlavDRVLPDLSKSERRAIVE--EHIALVGLTEAA---DKRPGQLSGGMKQRVAIARALSIR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 187 PAVLIADEPTTALDV----TIQAQILQLIkvlqQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQI-FHAPQ 261
Cdd:TIGR01184 133 PKVLLLDEPFGALDAltrgNLQEELMQIW----EEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPR 208
|
.
gi 949724212 262 H 262
Cdd:TIGR01184 209 D 209
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
350-546 |
2.98e-23 |
|
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: 98.33 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 350 GETLSLVGESGCGKSTtgraLLRLVE----SQRGEIIFNGQRIDTLaasklQPLRRDIQFIFQDP--YASLDPRQTVGYS 423
Cdd:cd03298 24 GEITAIVGPSGSGKST----LLNLIAgfetPQSGRVLINGVDVTAA-----PPADRPVSMLFQENnlFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 424 ILEPLRVHGLLQgdagsKRVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQII 503
Cdd:cd03298 95 LSPGLKLTAEDR-----QAIEVALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 949724212 504 NLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
342-556 |
5.73e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 99.32 E-value: 5.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 342 NVSFDlwPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFnGQRidTLAASK----LQPLRRDIQFIFQDPYASLDpR 417
Cdd:PRK13634 27 NVSIP--SGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GER--VITAGKknkkLKPLRKKVGIVFQFPEHQLF-E 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 418 QTVGYSI-LEPLRVhGLLQGDAgSKRVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDV 496
Cdd:PRK13634 101 ETVEKDIcFGPMNF-GVSEEDA-KQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 497 SIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQ 556
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
34-260 |
6.02e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.56 E-value: 6.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 34 NLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQ-AGGEVSCDemllrrrnrqvielGE---QSASQMRhvrgaDIAMI 109
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKT-TVLRLVAGLEKpTEGQIFID--------------GEdvtHRSIQQR-----DICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 110 FQEpmTSLNPVFTVGEQIAESIRLhQGASHEEAmveakrmldQVRIPEAKAIL------SRYPHQLSGGMRQRVMIAMAL 183
Cdd:PRK11432 84 FQS--YALFPHMSLGENVGYGLKM-LGVPKEER---------KQRVKEALELVdlagfeDRYVDQISGGQQQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAP 260
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
311-555 |
7.08e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.14 E-value: 7.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFplrSGILnrvtrevhAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDT 390
Cdd:PRK11300 3 QPLLSVSGLMMRF---GGLL--------AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 391 LAASKLQplRRDIQFIFQDpyASLDPRQTVgysiLEPLRV-----------HGLLQGDA-------GSKRVAWLLERVGL 452
Cdd:PRK11300 72 LPGHQIA--RMGVVRTFQH--VRLFREMTV----IENLLVaqhqqlktglfSGLLKTPAfrraeseALDRAATWLERVGL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 453 LpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISH 532
Cdd:PRK11300 144 L-EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISD 222
|
250 260
....*....|....*....|...
gi 949724212 533 RVAVMYLGQIVEIGTRRAVFENP 555
Cdd:PRK11300 223 RIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
12-265 |
9.43e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.92 E-value: 9.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIEQAG---------GEVSCDEMLLRR 82
Cdd:PRK14239 5 ILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKS----TLLRSINRMNdlnpevtitGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 83 RNRQVIELGEQsasqmrhvrgadIAMIFQEPmtslNPV-FTVGEQIAESIRLhQGASHEEAMVEA-KRMLDQVRI-PEAK 159
Cdd:PRK14239 77 PRTDTVDLRKE------------IGMVFQQP----NPFpMSIYENVVYGLRL-KGIKDKQVLDEAvEKSLKGASIwDEVK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 160 AILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMgvIFITHDMGVVADIADRV 239
Cdd:PRK14239 140 DRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRT 217
|
250 260
....*....|....*....|....*.
gi 949724212 240 LVMYQGEAVETGSVEQIFHAPQHPYT 265
Cdd:PRK14239 218 GFFLDGDLIEYNDTKQMFMNPKHKET 243
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
339-547 |
9.88e-23 |
|
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: 97.30 E-value: 9.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLaasKLQPLRRDIQFIFQDPYASLDP-R 417
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY---TLASLRRQIGLVSQDVFLFNDTvA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 418 QTVGYSILeplrvhgllqgDAGSKRVawllervgllpEHAWR--YPHEF-------------------SGGQRQRICIAR 476
Cdd:cd03251 94 ENIAYGRP-----------GATREEV-----------EEAARaaNAHEFimelpegydtvigergvklSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 477 ALALNPKVIIADESVSALDVSIRGQIINLMLDLQRelGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGT 547
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGT 219
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-257 |
1.06e-22 |
|
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: 96.91 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 19 NIAFEQEQQRvSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRqvIELGEQsasqm 98
Cdd:cd03254 7 NVNFSYDEKK-PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISR--KSLRSM----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 99 rhvrgadIAMIFQEPmtslnpvFTVGEQIAESIRL-HQGASHEEAMVEAK--RMLDQV-RIPEA-KAILSRYPHQLSGGM 173
Cdd:cd03254 79 -------IGVVLQDT-------FLFSGTIMENIRLgRPNATDEEVIEAAKeaGAHDFImKLPNGyDTVLGENGGNLSQGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADiADRVLVMYQGEAVETGSV 253
Cdd:cd03254 145 RQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRT--SIIIAHRLSTIKN-ADKILVLDDGKIIEEGTH 221
|
....
gi 949724212 254 EQIF 257
Cdd:cd03254 222 DELL 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
336-554 |
1.27e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 98.54 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 EVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRI--DTLAASKLQPLRRDIQFIFQDPYAS 413
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpaNLKKIKEVKRLRKEIGLVFQFPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 414 LDpRQTVGYSI-LEPlrVHGLLQGDAGSKRVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVS 492
Cdd:PRK13645 103 LF-QETIEKDIaFGP--VNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 493 ALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFEN 554
Cdd:PRK13645 180 GLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
31-260 |
2.23e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 99.25 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQA-GGEVSCDemllrrrNRQVIELgeqSASQmRHVRgadiaMI 109
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKT-TVLRLIAGFETPdSGRIMLD-------GQDITHV---PAEN-RHVN-----TV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 110 FQEpmTSLNPVFTVGEQIAESIRLhQGASHEEAmveAKRMLDQVRIPEAKAILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
Cdd:PRK09452 92 FQS--YALFPHMTVFENVAFGLRM-QKTPAAEI---TPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 190 LIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAP 260
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-246 |
2.35e-22 |
|
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: 94.81 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAfeqeqqrvSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCD-EMLLRRRNRQVIEL 90
Cdd:cd03215 4 VLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgKPVTRRSPRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 91 GEQSASQMRHVRGadiamifqepmtsLNPVFTVGEQIAesirlhqgasheeamveakrmldqvripeakailsrYPHQLS 170
Cdd:cd03215 76 GIAYVPEDRKREG-------------LVLDLSVAENIA------------------------------------LSSLLS 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRVLVMYQGE 246
Cdd:cd03215 107 GGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
29-246 |
3.06e-22 |
|
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: 95.17 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQ-AGGEVSCDEMLLRRRNRQVIELGEQSasqmrhvrgadIA 107
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKS-TLLKLIYKEELpTSGTIRVNGQDVSDLRGRAIPYLRRK-----------IG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 108 MIFQEpmTSLNPVFTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIPEAKailSRYPHQLSGGMRQRVMIAMALSCRP 187
Cdd:cd03292 82 VVFQD--FRLLPDRNVYENVAFALEV-TGVPPREIRKRVPAALELVGLSHKH---RALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 188 AVLIADEPTTALDVTIQAQILQLIKVLQQdMSMGVIFITHDMGVVADIADRVLVMYQGE 246
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
336-568 |
3.45e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.16 E-value: 3.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 EVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASK-LQPLRRDIQFIFQDPYASL 414
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyIRPVRKRIGMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 415 DpRQTVGYSILEPLRVHGLLQGDAGSKRVAWLLErVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSAL 494
Cdd:PRK13646 99 F-EDTVEREIIFGPKNFKMNLDEVKNYAHRLLMD-LGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 949724212 495 DVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFEnpQHPYTRKLMAAVP 568
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK--DKKKLADWHIGLP 248
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-256 |
3.64e-22 |
|
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: 95.19 E-value: 3.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCD-EMLLRRRNRQVIELG 91
Cdd:cd03224 1 LEVENLNAGYGKSQ----ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgRDITGLPPHERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 eqsasqmrhvrgadIAMIFQEPMtsLNPVFTVgeqiAESIRLhqgASHEEAMVEAKRMLDQV--RIPEAKAILSRYPHQL 169
Cdd:cd03224 77 --------------IGYVPEGRR--IFPELTV----EENLLL---GAYARRRAKRKARLERVyeLFPRLKERRKQLAGTL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVE 249
Cdd:cd03224 134 SGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVL 212
|
....*..
gi 949724212 250 TGSVEQI 256
Cdd:cd03224 213 EGTAAEL 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-266 |
3.99e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 96.06 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 18 LNIAFEQEQQRV-----SAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIE-----QAGGEVSCDEMLLRRRNRQV 87
Cdd:PRK14267 1 MKFAIETVNLRVyygsnHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 88 IELGEQsasqmrhvrgadIAMIFQEPmtslNPV--FTVGEQIAESIRLHQgasheeaMVEAKRMLDQV---------RIP 156
Cdd:PRK14267 81 IEVRRE------------VGMVFQYP----NPFphLTIYDNVAIGVKLNG-------LVKSKKELDERvewalkkaaLWD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 157 EAKAILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADIA 236
Cdd:PRK14267 138 EVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYT--IVLVTHSPAQAARVS 215
|
250 260 270
....*....|....*....|....*....|
gi 949724212 237 DRVLVMYQGEAVETGSVEQIFHAPQHPYTK 266
Cdd:PRK14267 216 DYVAFLYLGKLIEVGPTRKVFENPEHELTE 245
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
336-556 |
4.58e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.41 E-value: 4.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 EVHAVENVSFDLWPGETLSLVGESGCGKSTTGR---ALLRLVESQRGEIIFNGQridTLAASKLQPLRRDIQFIFQDPya 412
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKlinGLLLPDDNPNSKITVDGI---TLTAKTVWDIREKVGIVFQNP-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 413 sldPRQTVGYSILEPLrVHGL----LQGDAGSKRVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIAD 488
Cdd:PRK13640 94 ---DNQFVGATVGDDV-AFGLenraVPRPEMIKIVRDVLADVGML-DYIDSEPANLSGGQKQRVAIAGILAVEPKIIILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 489 ESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVErISHRVAVMYLGQIVEIGTRRAVFENPQ 556
Cdd:PRK13640 169 ESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
29-543 |
6.01e-22 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 99.48 E-value: 6.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHL---IEQAG---GEVSCDEMLLRRRNrqvIELGEQsasqmrhvR 102
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKS----TLMKVlsgVYPHGsyeGEILFDGEVCRFKD---IRDSEA--------L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 103 GadIAMIFQE----PMTSlnpvftvgeqIAESIRL-HQGASH-----EEAMVEAKRMLDQVRIPEAKAILSRyphQLSGG 172
Cdd:NF040905 79 G--IVIIHQElaliPYLS----------IAENIFLgNERAKRgvidwNETNRRARELLAKVGLDESPDTLVT---DIGVG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVL-QQDMSmgVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:NF040905 144 KQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELkAQGIT--SIIISHKLNEIRRVADSITVLRDGRTIETL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 252 SVEQifhapqhpytkallAAVPQ---LGAMNGHELPRRFPlisLHDPShvepqteqdtvvEGEPILRVRNLVTRFPLRSG 328
Cdd:NF040905 222 DCRA--------------DEVTEdriIRGMVGRDLEDRYP---ERTPK------------IGEVVFEVKNWTVYHPLHPE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 329 ilnrvtREVhaVENVSFDLWPGETLSLVGESGCGK-----STTGRALLRLVesqRGEIIFNGQRIDTLAASKlqPLRRDI 403
Cdd:NF040905 273 ------RKV--VDDVSLNVRRGEIVGIAGLMGAGRtelamSVFGRSYGRNI---SGTVFKDGKEVDVSTVSD--AIDAGL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 404 QfifqdpYASLDpRQTVGYSILEPLRVHGLLqgdAGSKRVAwlleRVGLLPEH-----AWRYPHEF-------------- 464
Cdd:NF040905 340 A------YVTED-RKGYGLNLIDDIKRNITL---ANLGKVS----RRGVIDENeeikvAEEYRKKMniktpsvfqkvgnl 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 465 SGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
Cdd:NF040905 406 SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
312-536 |
7.90e-22 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 99.28 E-value: 7.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 312 PILRVRNLVTRFPLRSgilnrvtrevHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQridTL 391
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRR----------PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV---PL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 392 AASKLQPLRRDIQFIFQDPYasldprqTVGYSILEPLRvhgLLQGDAGSKRVAWLLERVGL------LPEH----AWRYP 461
Cdd:TIGR02857 387 ADADADSWRDQIAWVPQHPF-------LFAGTIAENIR---LARPDASDAEIREALERAGLdefvaaLPQGldtpIGEGG 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 462 HEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRelGIAYLFISHDMAVVERISHRVAV 536
Cdd:TIGR02857 457 AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
12-245 |
8.55e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 94.50 E-value: 8.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqaGG--EVSCDEMLLRRRNrqvie 89
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKS----TLLHLL---GGldTPTSGDVIFNGQP----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 90 LGEQSASQMRHVRGADIAMIFQepMTSLNPVFTVGEQIAESIrLHQGASHEEAMVEAKRMLDQVRIpEAKAilSRYPHQL 169
Cdd:PRK11629 73 MSKLSSAAKAELRNQKLGFIYQ--FHHLLPDFTALENVAMPL-LIGKKKPAEINSRALEMLAAVGL-EHRA--NHRPSEL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGvVADIADRVLVMYQG 245
Cdd:PRK11629 147 SGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ-LAKRMSRQLEMRDG 221
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
32-272 |
8.95e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.18 E-value: 8.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 32 VRNLSFRLKRGETLAIVGESGSGKSvtalSLMHL----IEQAGGEVSCDEMllrrrnrqviELGEQSASQMRHVRgadiA 107
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKS----TLLKLltgeLTPSSGEVRLNGR----------PLAAWSPWELARRR----A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 108 MIFQEpmTSLNPVFTVgeqiAESIRL-----HQGASHEEAMVEakRMLDQVripEAKAILSRYPHQLSGGMRQRVMIAMA 182
Cdd:COG4559 79 VLPQH--SSLAFPFTV----EEVVALgraphGSSAAQDRQIVR--EALALV---GLAHLAGRSYQTLSGGEQQRVQLARV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 183 L-------SCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMsMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQ 255
Cdd:COG4559 148 LaqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRG-GGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
250
....*....|....*..
gi 949724212 256 IFhapqhpyTKALLAAV 272
Cdd:COG4559 227 VL-------TDELLERV 236
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
339-547 |
1.02e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 99.27 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLaasKLQPLRRDIQFIFQDpyASLDPRq 418
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV---TRASLRRNIAVVFQD--AGLFNR- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 419 tvgySILEPLRVHgllQGDAGSKRVAWLLERVGLLpEHAWRYPHEF-----------SGGQRQRICIARALALNPKVIIA 487
Cdd:PRK13657 424 ----SIEDNIRVG---RPDATDEEMRAAAERAQAH-DFIERKPDGYdtvvgergrqlSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 488 DESVSALDVSIRGQiINLMLDLQRElGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGT 547
Cdd:PRK13657 496 DEATSALDVETEAK-VKAALDELMK-GRTTFIIAHRLSTV-RNADRILVFDNGRVVESGS 552
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
31-328 |
1.11e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.57 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRQvielgeqsaSQMRHVRgADIAMIF 110
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQ---------KEIKPVR-KKVGVVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEPMTSLNPVfTVGEQIAESIRlHQGASHEEAMVEAKRMLDQVRIpeAKAILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:PRK13643 91 QFPESQLFEE-TVLKDVAFGPQ-NFGIPKEKAEKIAAEKLEMVGL--ADEFWEKSPFELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 191 IADEPTTALDVTIQAQILQLIKVLQQdMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHapqhpytkalla 270
Cdd:PRK13643 167 VLDEPTAGLDPKARIEMMQLFESIHQ-SGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ------------ 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 271 avpQLGAMNGHELprrfpliSLHDPSHVEPQTEQDTVVEGE--PILRVR--NLVTRFPLRSG 328
Cdd:PRK13643 234 ---EVDFLKAHEL-------GVPKATHFADQLQKTGAVTFEklPITRAElvTLLTSLSVNSG 285
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
9-313 |
1.40e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 96.83 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 9 ASDVLAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQ-AGGEVSCDemllrrrnrqv 87
Cdd:PRK11607 16 LTPLLEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKS-TLLRMLAGFEQpTAGQIMLD----------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 88 ielGEQSASQMRHVRgaDIAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASHE-EAMVEakRMLDQVRIPE-AKailsRY 165
Cdd:PRK11607 80 ---GVDLSHVPPYQR--PINMMFQS--YALFPHMTVEQNIAFGLKQDKLPKAEiASRVN--EMLGLVHMQEfAK----RK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQI-LQLIKVLQQdmsMGV--IFITHDMGVVADIADRVLVM 242
Cdd:PRK11607 147 PHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILER---VGVtcVMVTHDQEEAMTMAGRIAIM 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 243 YQGEAVETGSVEQIFHAPQHPYTKALLAAVpqlGAMNGHELPRRFPLISLHDPSHVEP-QTEQD-TVVEGEPI 313
Cdd:PRK11607 224 NRGKFVQIGEPEEIYEHPTTRYSAEFIGSV---NVFEGVLKERQEDGLVIDSPGLVHPlKVDADaSVVDNVPV 293
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
340-523 |
1.63e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.63 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLaasKLQPLRRDIQFIFQDPYASLDprqT 419
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTL---KPEIYRQQVSYCAQTPTLFGD---T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 420 VGYSILEPLRVHGlLQGDagSKRVAWLLERVGlLPEHAWRYP-HEFSGGQRQRICIARALALNPKVIIADESVSALDVSI 498
Cdd:PRK10247 97 VYDNLIFPWQIRN-QQPD--PAIFLDDLERFA-LPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180
....*....|....*....|....*
gi 949724212 499 RGQIINLMLDLQRELGIAYLFISHD 523
Cdd:PRK10247 173 KHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
341-557 |
1.86e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 94.45 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 341 ENVSFDLWPGETLSLVGESGCGKSTtgraLLRLVESQ----RGEIIFNGQRIDTLAASKLQPLRRDIQFIFQDpyASLDP 416
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTT----LLRLIGGQiapdHGEILFDGENIPAMSRSRLYTVRKRMSMLFQS--GALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 417 RQTVGYSILEPLRVHGLLQGDAGSKRVAWLLERVGLLPEhAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDV 496
Cdd:PRK11831 98 DMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGA-AKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 497 SIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQH 557
Cdd:PRK11831 177 ITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDP 237
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
311-550 |
1.87e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.08 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPlrsgilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTtgraLLRLVE------SQRGEIIFN 384
Cdd:PRK13549 3 EYLLEMKNITKTFG-----------GVKALDNVSLKVRAGEIVSLCGENGAGKST----LMKVLSgvyphgTYEGEIIFE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 385 GQridTLAASKLQPL-RRDIQFIFQDpyASLDPRQTVGYSIL---EPLRvHGLLQGDAGSKRVAWLLERVGLLPEHAWRY 460
Cdd:PRK13549 68 GE---ELQASNIRDTeRAGIAIIHQE--LALVKELSVLENIFlgnEITP-GGIMDYDAMYLRAQKLLAQLKLDINPATPV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 461 pHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLG 540
Cdd:PRK13549 142 -GNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDG 219
|
250
....*....|
gi 949724212 541 QivEIGTRRA 550
Cdd:PRK13549 220 R--HIGTRPA 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
28-251 |
1.87e-21 |
|
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: 92.73 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 28 RVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDemllrrrNRQVIELGEQSASQMRHVRGadia 107
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD-------GKPLDIAARNRIGYLPEERG---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 108 mifqepmtsLNPVFTVGEQIAESIRLHqGASHEEAMVEAKRMLDQVRIPEAKailSRYPHQLSGGMRQRVMIAMALSCRP 187
Cdd:cd03269 81 ---------LYPKMKVIDQLVYLAQLK-GLKKEEARRRIDEWLERLELSEYA---NKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 949724212 188 AVLIADEPTTALDVTIQAQILQLIKVLqQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
31-257 |
2.01e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.91 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVscdemllrRRNRQVIELGEQSASQMRHvrgaDIAMIF 110
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI--------LFDGKPIDYSRKGLMKLRE----SVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEPMTSLNPVfTVGEQIAESIrLHQGASHEEAMVEAKRMLDQVRIPEAKailSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:PRK13636 89 QDPDNQLFSA-SVYQDVSFGA-VNLKLPEDEVRKRVDNALKRTGIEHLK---DKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 191 IADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIF 257
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
35-279 |
2.15e-21 |
|
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: 95.95 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 35 LSFRLKRGETLAIVGESGSGKSvTALSLMH-LIEQAGGEVSCDEMLLRRRNRQVIELGEQSAsqmrhvrgadIAMIFQEp 113
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKT-TLIRLIAgLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRR----------IGYVFQE- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 114 mTSLNPVFTVGEQIAESIRLHQGASHEEAMVEAKRMLDqvripeAKAILSRYPHQLSGGMRQRVMIAMALSCRPAVLIAD 193
Cdd:TIGR02142 84 -ARLFPHLSVRGNLRYGMKRARPSERRISFERVIELLG------IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 194 EPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQHPYtkallAAVP 273
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW-----LARE 231
|
....*.
gi 949724212 274 QLGAMN 279
Cdd:TIGR02142 232 DQGSLI 237
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
29-250 |
2.32e-21 |
|
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: 91.34 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqAG------GEVSCDEMLLRRRN-RQVIELGeqsasqmrhv 101
Cdd:cd03216 13 VKALDGVSLSVRRGEVHALLGENGAGKS----TLMKIL--SGlykpdsGEILVDGKEVSFASpRDARRAG---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 102 rgadIAMIfqepmtslnpvftvgeqiaesirlhqgasheeamveakrmldqvripeakailsrypHQLSGGMRQRVMIAM 181
Cdd:cd03216 77 ----IAMV---------------------------------------------------------YQLSVGERQMVEIAR 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRVLVMYQGEAVET 250
Cdd:cd03216 96 ALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-567 |
2.76e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.39 E-value: 2.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRL---VESQR--GEIIFNGQRIdtLAASKLQPLRRDIQFIFQDPyasl 414
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkVSGYRysGDVLLGGRSI--FNYRDVLEFRRRVGMLFQRP---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 415 DP-RQTVGYSILEPLRVHGLLQGDAGSKRVAWLLERVGL---LPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADES 490
Cdd:PRK14271 111 NPfPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 491 VSALDVSIRGQIINLMLDLQRELGIayLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQHPYTRKLMAAV 567
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRLTV--IIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGL 265
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
29-260 |
3.44e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.10 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVscdemLLRrrnrqvielGEQ-SASQMRHVRGAdIA 107
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV-----LIR---------GEPiTKENIREVRKF-VG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 108 MIFQEPMtslNPVF--TVGEQIA-ESIRLhqgASHEEAMveAKRMLDQVRIPEAKAILSRYPHQLSGGMRQRVMIAMALS 184
Cdd:PRK13652 82 LVFQNPD---DQIFspTVEQDIAfGPINL---GLDEETV--AHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAP 260
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
339-524 |
3.48e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 93.23 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKlqplrrdiQFIFQDpyASLDPRQ 418
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER--------GVVFQN--EGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 419 TVGYSILEPLRvhglLQGDAGSKRVAW---LLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADESVSALD 495
Cdd:PRK11248 86 NVQDNVAFGLQ----LAGVEKMQRLEIahqMLKKVGLEGAEK-RYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180
....*....|....*....|....*....
gi 949724212 496 VSIRGQIINLMLDLQRELGIAYLFISHDM 524
Cdd:PRK11248 161 AFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
31-256 |
3.78e-21 |
|
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: 92.93 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIEQaggevscdeMLLRRRNRQVIELGEQSASQMRHVRgADIAMIF 110
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKS----TLTKLIQR---------FYVPENGRVLVDGHDLALADPAWLR-RQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEpmtslNPVFTvgEQIAESIRLHQGASHEEAMVEAKRMLDQ----VRIPEA-KAILSRYPHQLSGGMRQRVMIAMALSC 185
Cdd:cd03252 83 QE-----NVLFN--RSIRDNIALADPGMSMERVIEAAKLAGAhdfiSELPEGyDTIVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 186 RPAVLIADEPTTALDVTIQAQILQLIkvlqQDMSMG--VIFITHDMGVVADiADRVLVMYQGEAVETGSVEQI 256
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNM----HDICAGrtVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
340-542 |
4.23e-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: 90.74 E-value: 4.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLqplrrdiqfifqdpyasldpRQT 419
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL--------------------GDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 420 VGYsileplrvhgLLQGD---AGSkrvawLLERVgllpehawrypheFSGGQRQRICIARALALNPKVIIADESVSALDV 496
Cdd:cd03246 78 VGY----------LPQDDelfSGS-----IAENI-------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 949724212 497 SIRGQIINLMLDLqRELGIAYLFISHDMAVVERIShRVAVMYLGQI 542
Cdd:cd03246 130 EGERALNQAIAAL-KAAGATRIVIAHRPETLASAD-RILVLEDGRV 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
306-523 |
4.58e-21 |
|
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: 97.05 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 306 TVVEGEPILRVRNLVTRFPLRSGILNrvtrevhaveNVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNG 385
Cdd:TIGR02868 327 AVGLGKPTLELRDLSAGYPGAPPVLD----------GVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 386 QRIDTLAASKlqpLRRDIQFIFQDPYasldprqTVGYSILEPLRvhgLLQGDAGSKRVAWLLERVGLLpEHAWRYPH--- 462
Cdd:TIGR02868 397 VPVSSLDQDE---VRRRVSVCAQDAH-------LFDTTVRENLR---LARPDATDEELWAALERVGLA-DWLRALPDgld 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 463 --------EFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIayLFISHD 523
Cdd:TIGR02868 463 tvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTV--VLITHH 529
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
33-256 |
7.81e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 97.10 E-value: 7.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 33 RNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRQVIElgeqsasqmRHVrgadiAMIFQE 112
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLH---------RQV-----ALVGQE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 113 PMtslnpVF--TVGEQIAESIRlhqgaSHEEAMVEAKRMLdqvriPEAKAILSRYPH-----------QLSGGMRQRVMI 179
Cdd:TIGR00958 564 PV-----LFsgSVRENIAYGLT-----DTPDEEIMAAAKA-----ANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAI 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 180 AMALSCRPAVLIADEPTTALDVTIQAqilqlikVLQQDMS---MGVIFITHDMGVVADiADRVLVMYQGEAVETGSVEQI 256
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSALDAECEQ-------LLQESRSrasRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
31-257 |
7.91e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.89 E-value: 7.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSvTALSLMH-LIEQAGGEVSCDEMLLRRRNRQvielgeqsaSQMRHVRgADIAMI 109
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKS-TIMQLLNgLHVPTQGSVRVDDTLITSTSKN---------KDIKQIR-KKVGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 110 FQEPMTSLnpvF--TVGEQIAESIRlHQGASHEEAMVEAKRMLDQVRIPEAkaILSRYPHQLSGGMRQRVMIAMALSCRP 187
Cdd:PRK13649 91 FQFPESQL---FeeTVLKDVAFGPQ-NFGVSQEEAEALAREKLALVGISES--LFEKNPFELSGGQMRRVAIAGILAMEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 188 AVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIF 257
Cdd:PRK13649 165 KILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
29-545 |
8.28e-21 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 95.95 E-value: 8.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVscdemllrrrnrqvIELGEQ-SASQMRHVRGADIA 107
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI--------------LFQGKEiDFKSSKEALENGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 108 MIFQEpmtsLNPVF--TVGEQIAESIRLHQG--ASHEEAMVEAKRMLDQVRI---PEAKAIlsryphQLSGGMRQRVMIA 180
Cdd:PRK10982 77 MVHQE----LNLVLqrSVMDNMWLGRYPTKGmfVDQDKMYRDTKAIFDELDIdidPRAKVA------TLSVSQMQMIEIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQqDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVE-----Q 255
Cdd:PRK10982 147 KAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAgltmdK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 256 IfhapqhpytkallaavpqLGAMNGHELPRRFPlislhdpshvepqteQDTVVEGEPILRVRNLVTrfplrsgiLNRVTr 335
Cdd:PRK10982 226 I------------------IAMMVGRSLTQRFP---------------DKENKPGEVILEVRNLTS--------LRQPS- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 evhaVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAAskLQPLRRDIQFIFQDP----- 410
Cdd:PRK10982 264 ----IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNA--NEAINHGFALVTEERrstgi 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 411 YASLDprqtVGY-SILEPLRVH----GLLQGDAGSKRVAWLLERVGL-LPEHAWRYpHEFSGGQRQRICIARALALNPKV 484
Cdd:PRK10982 338 YAYLD----IGFnSLISNIRNYknkvGLLDNSRMKSDTQWVIDSMRVkTPGHRTQI-GSLSGGNQQKVIIGRWLLTQPEI 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 485 IIADESVSALDVSIRGQIINLMLDL-QRELGIayLFISHDMAVVERISHRVAVMYLGQIVEI 545
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-255 |
1.06e-20 |
|
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: 91.52 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 19 NIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRrrnrqvielgEQSASQM 98
Cdd:cd03251 5 NVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVR----------DYTLASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 99 RhvrgADIAMIFQEpmtslnpVFTVGEQIAESIRL-HQGASHEEAMVEAkrmldqvRIPEAKAILSRYPH---------- 167
Cdd:cd03251 75 R----RQIGLVSQD-------VFLFNDTVAENIAYgRPGATREEVEEAA-------RAANAHEFIMELPEgydtvigerg 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 168 -QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADiADRVLVMYQGE 246
Cdd:cd03251 137 vKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRT--TFVIAHRLSTIEN-ADRIVVLEDGK 213
|
....*....
gi 949724212 247 AVETGSVEQ 255
Cdd:cd03251 214 IVERGTHEE 222
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
340-567 |
1.14e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.00 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQplrRDIQFIFQDPyasLDP--- 416
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA---RRLALLPQHH---LTPegi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 417 --RQTVGYSILEPLRVHGLLqGDAGSKRVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSAL 494
Cdd:PRK11231 92 tvRELVAYGRSPWLSLWGRL-SAEDNARVNQAMEQTRIN-HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 495 DVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTrravfenPQHPYTRKLMAAV 567
Cdd:PRK11231 170 DINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT-------PEEVMTPGLLRTV 234
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-293 |
1.82e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.37 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIEqagGEVSCDemllrrrnRQVIELG 91
Cdd:PRK13548 2 MLEARNLSVRLGGRT----LLDDVSLTLRPGEVVAILGPNGAGKS----TLLRALS---GELSPD--------SGEVRLN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 EQSASQMRHVRGADI-AMIFQEpmTSLNPVFTVgEQIAESIRLHQGASHEEAMVEAKRMLDQVripEAKAILSRYPHQLS 170
Cdd:PRK13548 63 GRPLADWSPAELARRrAVLPQH--SSLSFPFTV-EEVVAMGRAPHGLSRAEDDALVAAALAQV---DLAHLAGRDYPQLS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 171 GGMRQRVMIAMAL------SCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQ 244
Cdd:PRK13548 137 GGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQ 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 949724212 245 GEAVETGSVEQIFhapqhpyTKALLAAVPQLGAMNGHELPRRFPLISLH 293
Cdd:PRK13548 217 GRLVADGTPAEVL-------TPETLRRVYGADVLVQPHPETGAPLVLPR 258
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
41-251 |
1.96e-20 |
|
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: 89.86 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 41 RGETLAIVGESGSGKSvtalSLMHLIeqAGGEVSCDEMLLrrrnrqvieLGEQSasqMRHVRGAD--IAMIFQEpmTSLN 118
Cdd:cd03298 23 QGEITAIVGPSGSGKS----TLLNLI--AGFETPQSGRVL---------INGVD---VTAAPPADrpVSMLFQE--NNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 119 PVFTVGEQI--AESIRLHQGASHEEAMveaKRMLDQVRIPEakaILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPT 196
Cdd:cd03298 83 AHLTVEQNVglGLSPGLKLTAEDRQAI---EVALARVGLAG---LEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 197 TALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
29-252 |
2.28e-20 |
|
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: 90.68 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNrqvielgeqsasqMRHVRgADIAM 108
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN-------------LRWLR-SQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 109 IFQEPM---TSlnpvftvgeqIAESIRLHQGASHEEAMVEAKRMldqvriPEAKAILSRYPH-----------QLSGGMR 174
Cdd:cd03249 82 VSQEPVlfdGT----------IAENIRYGKPDATDEEVEEAAKK------ANIHDFIMSLPDgydtlvgergsQLSGGQK 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 175 QRVMIAMALSCRPAVLIADEPTTALDvTIQAQILQliKVLQQDM-SMGVIFITHDMGVVADiADRVLVMYQGEAVETGS 252
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALD-AESEKLVQ--EALDRAMkGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
336-543 |
2.46e-20 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 89.96 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 EVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKlqpLRRDIQFIFQDP---YA 412
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD---LRRNIGYVPQDVtlfYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 413 SLDPRQTVGYS------ILEPLRVHGLLQgdagskrvawllervgLLPEHawryPHEF-----------SGGQRQRICIA 475
Cdd:cd03245 93 TLRDNITLGAPladderILRAAELAGVTD----------------FVNKH----PNGLdlqigergrglSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 476 RALALNPKVIIADESVSALDVSIRGQIINlmlDLQREL-GIAYLFISHDMAVVERIShRVAVMYLGQIV 543
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKE---RLRQLLgDKTLIIITHRPSLLDLVD-RIIVMDSGRIV 217
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
36-246 |
3.12e-20 |
|
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: 89.54 E-value: 3.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 36 SFRLKRGETLAIVGESGSGKSvTALSLMH-LIEQAGGEVSCDEMLLRRrnrqvielgeqSASQMRHVrgadiAMIFQEpm 114
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKS-TLLNLIAgFIEPASGSIKVNDQSHTG-----------LAPYQRPV-----SMLFQE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 115 TSLNPVFTVGEQIAESIR--LHQGASHEEAMVEAKRmldQVRIPEakaILSRYPHQLSGGMRQRVMIAMALSCRPAVLIA 192
Cdd:TIGR01277 79 NNLFAHLTVRQNIGLGLHpgLKLNAEQQEKVVDAAQ---QVGIAD---YLDRLPEQLSGGQRQRVALARCLVRPNPILLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 949724212 193 DEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGE 246
Cdd:TIGR01277 153 DEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
338-546 |
3.44e-20 |
|
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: 89.17 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 338 HAVENVSFDLWPGeTLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdtlaASKLQPLRRDIQFIFQDPyaSLDPR 417
Cdd:cd03264 14 RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLRRRIGYLPQEF--GVYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 418 QTVgysiLEPLRVHGLLQGDAGS---KRVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSAL 494
Cdd:cd03264 87 FTV----REFLDYIAWLKGIPSKevkARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 949724212 495 DVSIRGQIINLMldlqRELGIAYLFI--SHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03264 162 DPEERIRFRNLL----SELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
339-549 |
4.02e-20 |
|
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: 94.81 E-value: 4.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLqplRRDIQFIFQDPYasldprq 418
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL---RQFINYLPQEPY------- 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 419 TVGYSILEPLrvhgLLQGDAG-SKRVAWLLERVGLLPEHAWRYPHEF-----------SGGQRQRICIARALALNPKVII 486
Cdd:TIGR01193 559 IFSGSILENL----LLGAKENvSQDEIWAACEIAEIKDDIENMPLGYqtelseegssiSGGQKQRIALARALLTDSKVLI 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 487 ADESVSALDVSIRGQIINLMLDLQRELGIaylFISHDMAVVERiSHRVAVMYLGQIVEIGTRR 549
Cdd:TIGR01193 635 LDESTSNLDTITEKKIVNNLLNLQDKTII---FVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHD 693
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-255 |
4.53e-20 |
|
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: 89.60 E-value: 4.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 19 NIAFEQEQQRvSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEmllrRRNRQVielgeqsasQM 98
Cdd:cd03253 5 NVTFAYDPGR-PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG----QDIREV---------TL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 99 RHVRGAdIAMIFQEpmtslNPVFTvgEQIAESIRLHQGASHEEAMVEAKRMLDQ----VRIPEA-KAILSRYPHQLSGGM 173
Cdd:cd03253 71 DSLRRA-IGVVPQD-----TVLFN--DTIGYNIRYGRPDATDEEVIEAAKAAQIhdkiMRFPDGyDTIVGERGLKLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADiADRVLVMYQGEAVETGSV 253
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRT--TIVIAHRLSTIVN-ADKIIVLKDGRIVERGTH 219
|
..
gi 949724212 254 EQ 255
Cdd:cd03253 220 EE 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-242 |
4.90e-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: 93.89 E-value: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 2 PHSDELDA----SDVLAVSNLNIAFEQeqqRVSAVRNLSFRLKRGETLAIVGESGSGKSvTALS-LMHLIEQAGGEVSCD 76
Cdd:TIGR02857 307 PLAGKAPVtaapASSLEFSGVSVAYPG---RRPALRPVSFTVPPGERVALVGPSGAGKS-TLLNlLLGFVDPTEGSIAVN 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 77 emllrrrnrqvielGEQSASQMRHVRGADIAMIFQEPmtslnpvFTVGEQIAESIRLHQGASHEEAMVEAKRM-----LD 151
Cdd:TIGR02857 383 --------------GVPLADADADSWRDQIAWVPQHP-------FLFAGTIAENIRLARPDASDAEIREALERagldeFV 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 152 QVRIPEAKAILSRYPHQLSGGMRQRVMIAMALsCRPA-VLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMG 230
Cdd:TIGR02857 442 AALPQGLDTPIGEGGAGLSGGQAQRLALARAF-LRDApLLLLDEPTAHLDAETEAEVLEALRALAQGRT--VLLVTHRLA 518
|
250
....*....|..
gi 949724212 231 VVADiADRVLVM 242
Cdd:TIGR02857 519 LAAL-ADRIVVL 529
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
339-555 |
5.42e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.43 E-value: 5.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGqrIDTLAASKLQPLRRDIQFIFQDPYAsldprQ 418
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIRKLVGIVFQNPET-----Q 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 419 TVGYSILEPLRV---HGLLQGDAGSKRVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALD 495
Cdd:PRK13644 90 FVGRTVEEDLAFgpeNLCLPPIEIRKRVDRALAEIGL-EKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 496 VSIRGQIINLMLDLQRElGIAYLFISHDMAVVErISHRVAVMYLGQIVEIGTRRAVFENP 555
Cdd:PRK13644 169 PDSGIAVLERIKKLHEK-GKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-246 |
6.48e-20 |
|
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: 89.31 E-value: 6.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 22 FEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSC-DEMLLRRRNRQVielgeqsaSQMRH 100
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVaGLVPWKRRKKFL--------RRIGV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 101 VRGADIAMIFQEPmtslnpvftvgeqIAESIRLHQgASHEEAMVEAKRMLDQ-VRIPEAKAILSRYPHQLSGGMRQRVMI 179
Cdd:cd03267 99 VFGQKTQLWWDLP-------------VIDSFYLLA-AIYDLPPARFKKRLDElSELLDLEELLDTPVRQLSLGQRMRAEI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 180 AMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGE 246
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
314-547 |
6.85e-20 |
|
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: 88.24 E-value: 6.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFplrSGILNRVTRevhaveNVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLaa 393
Cdd:cd03369 7 IEVENLSVRY---APDLPPVLK------NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 sKLQPLRRDIQFIFQDPY-------ASLDPRQTvgYS---ILEPLRVHGllqgdAGSKrvawllervgllpehawryphe 463
Cdd:cd03369 76 -PLEDLRSSLTIIPQDPTlfsgtirSNLDPFDE--YSdeeIYGALRVSE-----GGLN---------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 464 FSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMldlqREL--GIAYLFISHDMAVVERIShRVAVMYLGQ 541
Cdd:cd03369 126 LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTI----REEftNSTILTIAHRLRTIIDYD-KILVMDAGE 200
|
....*.
gi 949724212 542 IVEIGT 547
Cdd:cd03369 201 VKEYDH 206
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-543 |
7.15e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 93.05 E-value: 7.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQA-GGEVSCDEMLLRRRN-RQVIELGeqsasqmrhvrgadI 106
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKS-TLLKILSGNYQPdAGSILIDGQEMRFAStTAALAAG--------------V 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 107 AMIFQEpmTSLNPVFTVgeqiAESIRLHQ-----GASHEEAMV-EAKRMLDQVRI---PEAKaiLSRyphqLSGGMRQRV 177
Cdd:PRK11288 82 AIIYQE--LHLVPEMTV----AENLYLGQlphkgGIVNRRLLNyEAREQLEHLGVdidPDTP--LKY----LSIGQRQMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 178 MIAMALScRPAVLIA-DEPTTALDVTIQAQILQLIKVLQQDMSMgVIFITHDMGVVADIADRVLVMYQGEAVET-GSVEQ 255
Cdd:PRK11288 150 EIAKALA-RNARVIAfDEPTSSLSAREIEQLFRVIRELRAEGRV-ILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 256 IFHApqhpytkallaavpQL-GAMNGHElprrfplisLHDPSHVEPQTeqdtvvEGEPILRVRNLVTRfPLRsgilnrvt 334
Cdd:PRK11288 228 VDRD--------------QLvQAMVGRE---------IGDIYGYRPRP------LGEVRLRLDGLKGP-GLR-------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 335 revhavENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDtlAASKLQPLRRDIQFIFQDPYA-S 413
Cdd:PRK11288 270 ------EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID--IRSPRDAIRAGIMLCPEDRKAeG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 414 LDPRQTVGYSILEPLRVH----GLLQGDAGSKRVAwlLERVGLL------PEHAWRYpheFSGGQRQRICIARALALNPK 483
Cdd:PRK11288 342 IIPVHSVADNINISARRHhlraGCLINNRWEAENA--DRFIRSLniktpsREQLIMN---LSGGNQQKAILGRWLSEDMK 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 484 VIIADESVSALDVSIRGQIINLMLDLQrELGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
Cdd:PRK11288 417 VILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
12-259 |
8.20e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.77 E-value: 8.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNiafeqeqqRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRN-RQVIEL 90
Cdd:COG1129 256 VLEVEGLS--------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 91 GeqsasqmrhvrgadIAMIfqeP----MTSLNPVFTVGEQIAESI--RLHQGA--SHEEAMVEAKRMLDQVRI----PEA 158
Cdd:COG1129 328 G--------------IAYV---PedrkGEGLVLDLSIRENITLASldRLSRGGllDRRRERALAEEYIKRLRIktpsPEQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 159 KAIlsryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADR 238
Cdd:COG1129 391 PVG------NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDR 463
|
250 260
....*....|....*....|....*.
gi 949724212 239 VLVMYQGEAV-----ETGSVEQIFHA 259
Cdd:COG1129 464 ILVMREGRIVgeldrEEATEEAIMAA 489
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
31-251 |
8.24e-20 |
|
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: 88.02 E-value: 8.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGeTLAIVGESGSGKSvtalSLMHLIeqAGgevscdemlLRRRNRQVIELGEQSASQMRHVRGADIAMIF 110
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKT----TLMRIL--AT---------LTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEPMTSlnPVFTVGEQIAESIRLHqGASHEEAMVEAKRMLDQVRIPEAKailSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:cd03264 79 QEFGVY--PNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELVNLGDRA---KKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 191 IADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELGEDRI--VILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
336-547 |
8.37e-20 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 93.85 E-value: 8.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 EVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLA----ASKLQPLRRDIqFIFQ--- 408
Cdd:TIGR03796 491 EPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPrevlANSVAMVDQDI-FLFEgtv 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 409 -DPYASLDPrqtvgySILEPlrvhGLLQgdagSKRVAWLLERVGLLPEhawRYPHE-------FSGGQRQRICIARALAL 480
Cdd:TIGR03796 570 rDNLTLWDP------TIPDA----DLVR----ACKDAAIHDVITSRPG---GYDAElaegganLSGGQRQRLEIARALVR 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 481 NPKVIIADESVSALDVSIRGQII-NLmldlqRELGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGT 547
Cdd:TIGR03796 633 NPSILILDEATSALDPETEKIIDdNL-----RRRGCTCIIVAHRLSTI-RDCDEIIVLERGKVVQRGT 694
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
338-548 |
1.11e-19 |
|
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: 88.35 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 338 HAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASklQPLRRDIQF------IFqdpy 411
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPH--ERARAGIAYvpqgreIF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 412 asldPRQTVgysiLEPLRVHGLLQGDAGSKRVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESV 491
Cdd:TIGR03410 88 ----PRLTV----EENLLTGLAALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 492 SALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTR 548
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAG 216
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
27-259 |
1.16e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.60 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 27 QRVSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLM-HLIEQAGGEVscdemllrrrnrqvielgeqsasqmrHVRGAD 105
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKS-TLLKLIaGILEPTSGRV--------------------------EVNGRV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 106 IAMIfqEPMTSLNPVFTVGEQIAESIRLHqGASHEEAmveaKRMLDQVripEAKAILSRYPHQ----LSGGMRQRVMIAM 181
Cdd:COG1134 90 SALL--ELGAGFHPELTGRENIYLNGRLL-GLSRKEI----DEKFDEI---VEFAELGDFIDQpvktYSSGMRARLAFAV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHA 259
Cdd:COG1134 160 ATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
336-556 |
1.20e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.24 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 EVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKlqplrRDIQFIFQDpYAsLD 415
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-----RGVGMVFQS-YA-LY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 416 PRQTVGYSILEPLRVHGLLQGDAgSKRV---AWLLERVGLLPehawRYPHEFSGGQRQRICIARALALNPKVIIADESVS 492
Cdd:PRK11000 88 PHLSVAENMSFGLKLAGAKKEEI-NQRVnqvAEVLQLAHLLD----RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 949724212 493 ALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQ 556
Cdd:PRK11000 163 NLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
31-245 |
1.34e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.01 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQ--AGGEVSCDEMLLRRRNRQVIELGEQsasqmrhvrgadIAM 108
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKS-TLLKLICGIERpsAGKIWFSGHDITRLKNREVPFLRRQ------------IGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 109 IFQEPMTSLNPvfTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIPEaKAilSRYPHQLSGGMRQRVMIAMALSCRPA 188
Cdd:PRK10908 84 IFQDHHLLMDR--TVYDNVAIPLII-AGASGDDIRRRVSAALDKVGLLD-KA--KNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 189 VLIADEPTTALDVTIQAQILQLIKVLQQdMSMGVIFITHDMGVVADIADRVLVMYQG 245
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
336-552 |
1.87e-19 |
|
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: 92.07 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 EVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdtlAASKLQPLRRDIQFIFQDPYA-SL 414
Cdd:TIGR02204 352 DQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDL---RQLDPAELRARMALVPQDPVLfAA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 415 DPRQTVGYSileplRVHGLLQGDAGSKRVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADES 490
Cdd:TIGR02204 429 SVMENIRYG-----RPDATDEEVEAAARAAHAHEFISALPEGYDTYLGErgvtLSGGQRQRIAIARAILKDAPILLLDEA 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 491 VSALDvSIRGQIINLMLDLQRElGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGTRRAVF 552
Cdd:TIGR02204 504 TSALD-AESEQLVQQALETLMK-GRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAELI 562
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
344-543 |
2.29e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 87.33 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 344 SFDLWPGETLSLVGESGCGKSTtgraLLRLV----ESQRGEIIFNGQriDTLAASklqPLRRDIQFIFQDP--YASLDPR 417
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKST----LLNLIagflTPASGSLTLNGQ--DHTTTP---PSRRPVSMLFQENnlFSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 418 QTVGYSiLEPlrvhGLLQGDAGSKRVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVS 497
Cdd:PRK10771 90 QNIGLG-LNP----GLKLNAAQREKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 949724212 498 IRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
Cdd:PRK10771 164 LRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
311-542 |
2.82e-19 |
|
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: 87.14 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPLRSgilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdt 390
Cdd:cd03248 9 KGIVKFQNVTFAYPTRP--------DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 391 lAASKLQPLRRDIQFIFQDPyasldprQTVGYSILEPLrVHGLLQGDAGS-KRVAWLLERVGLLPEHAWRYPHE------ 463
Cdd:cd03248 79 -SQYEHKYLHSKVSLVGQEP-------VLFARSLQDNI-AYGLQSCSFECvKEAAQKAHAHSFISELASGYDTEvgekgs 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 464 -FSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELgiAYLFISHDMAVVERiSHRVAVMYLGQI 542
Cdd:cd03248 150 qLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
336-546 |
3.30e-19 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 85.44 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 EVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASklqpLRRDIQFIFQDPYasld 415
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LSSLISVLNQRPY---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 416 prqtvgysileplrvhgLLQGDagskrvawLLERVGLlpehawryphEFSGGQRQRICIARALALNPKVIIADESVSALD 495
Cdd:cd03247 86 -----------------LFDTT--------LRNNLGR----------RFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 949724212 496 VSIRGQIINLMLDLQRELGIayLFISHDMAVVERIShRVAVMYLGQIVEIG 546
Cdd:cd03247 131 PITERQLLSLIFEVLKDKTL--IWITHHLTGIEHMD-KILFLENGKIIMQG 178
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
13-242 |
3.77e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 86.38 E-value: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAfeqeQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLM--HLIE--QAGGEVSCDEmllRRRNRQVI 88
Cdd:COG4136 2 LSLENLTIT----LGGRPLLAPLSLTVAPGEILTLMGPSGSGKS-TLLAAIagTLSPafSASGEVLLNG---RRLTALPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 89 ELgeqsasqmRHvrgadIAMIFQEPMtsLNPVFTVGEQIAESIRLHQGASHEEAMVEAkrMLDQVRIPeakAILSRYPHQ 168
Cdd:COG4136 74 EQ--------RR-----IGILFQDDL--LFPHLSVGENLAFALPPTIGRAQRRARVEQ--ALEEAGLA---GFADRDPAT 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDmgvVADI--ADRVLVM 242
Cdd:COG4136 134 LSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD---EEDApaAGRVLDL 206
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-256 |
5.55e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 88.22 E-value: 5.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 22 FEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMH-LIEQAGGEVSCDEMLLRRRnrqvielgeqsasQMRH 100
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKS-TTIKMLTgILVPTSGEVRVLGYVPFKR-------------RKEF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 101 VRgaDIAMIF-QEpmTSLN---PVftvgeqiAESIRLHQ------GASHEEAMVEAKRMLD-------QVRipeakails 163
Cdd:COG4586 94 AR--RIGVVFgQR--SQLWwdlPA-------IDSFRLLKaiyripDAEYKKRLDELVELLDlgelldtPVR--------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 164 ryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMY 243
Cdd:COG4586 154 ----QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVID 229
|
250
....*....|...
gi 949724212 244 QGEAVETGSVEQI 256
Cdd:COG4586 230 HGRIIYDGSLEEL 242
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
330-546 |
8.29e-19 |
|
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: 85.30 E-value: 8.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 330 LNRVTREVHAvENVSFDLW--PGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAasklqPLRRDIQFIF 407
Cdd:TIGR01277 3 LDKVRYEYEH-LPMEFDLNvaDGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA-----PYQRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 408 QDP--YASLDPRQTVGYSILEPLRVHGLLQgdagsKRVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVI 485
Cdd:TIGR01277 77 QENnlFAHLTVRQNIGLGLHPGLKLNAEQQ-----EKVVDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPIL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 486 IADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:TIGR01277 151 LLDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-245 |
1.01e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 89.68 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 2 PHSDELDASDVLAVSNLNiafeqeqqrVSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIEQA----GGEVSCDE 77
Cdd:PRK10762 247 PRLDKAPGEVRLKVDNLS---------GPGVNDVSFTLRKGEILGVSGLMGAGRT----ELMKVLYGAlprtSGYVTLDG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 78 MLLRRRNRQ-VIELGEQSASQMRHVRGADIAMIFQEPM--TSLNPVFTVGEQIAesirlHQgasHEEAMVEAKRMLDQVR 154
Cdd:PRK10762 314 HEVVTRSPQdGLANGIVYISEDRKRDGLVLGMSVKENMslTALRYFSRAGGSLK-----HA---DEQQAVSDFIRLFNIK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 155 IPEAKAILSryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVAD 234
Cdd:PRK10762 386 TPSMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLG 460
|
250
....*....|.
gi 949724212 235 IADRVLVMYQG 245
Cdd:PRK10762 461 MSDRILVMHEG 471
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-257 |
1.47e-18 |
|
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: 89.42 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQQRVsaVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRQviELGe 92
Cdd:COG4618 331 LSVENLTVVPPGSKRPI--LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDRE--ELG- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 93 qsasqmRHVrG---ADIAMifqepmtslnpvF--TVGEQIAesiRLhqGASHEEAMVEAKRMldqVRIPEAkaILsRYP- 166
Cdd:COG4618 406 ------RHI-GylpQDVEL------------FdgTIAENIA---RF--GDADPEKVVAAAKL---AGVHEM--IL-RLPd 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 167 ----------HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmsmG--VIFITHDMGVVAd 234
Cdd:COG4618 456 gydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR---GatVVVITHRPSLLA- 531
|
250 260
....*....|....*....|...
gi 949724212 235 IADRVLVMYQGEAVETGSVEQIF 257
Cdd:COG4618 532 AVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
349-534 |
1.54e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.83 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 349 PGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQPLR-RDIQFIFQDpyASLDPRQTVgysiLEP 427
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQS--FMLIPTLNA----LEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 428 LRVHGLLQGDAGSK---RVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIIN 504
Cdd:PRK10584 109 VELPALLRGESSRQsrnGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
|
170 180 190
....*....|....*....|....*....|
gi 949724212 505 LMLDLQRELGIAYLFISHDMAVVERISHRV 534
Cdd:PRK10584 188 LLFSLNREHGTTLILVTHDLQLAARCDRRL 217
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
340-547 |
1.66e-18 |
|
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: 89.42 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQridTLAASKLQPLRRDIQFIFQDPYasLDPRqt 419
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGV---DLAIADPAWLRRQMGVVLQENV--LFSR-- 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 420 vgySILEPLRvhgLLQGDAGSKRVAWLLERVGLLpEHAWRYPHEF-----------SGGQRQRICIARALALNPKVIIAD 488
Cdd:TIGR01846 546 ---SIRDNIA---LCNPGAPFEHVIHAAKLAGAH-DFISELPQGYntevgekganlSGGQRQRIAIARALVGNPRILIFD 618
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 489 ESVSALDVSIRGQIINLMLDLQRelGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGT 547
Cdd:TIGR01846 619 EATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTV-RACDRIIVLEKGQIAESGR 674
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
309-550 |
1.72e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.93 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 309 EGEPILRVRNLVTRFPlrsgilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRI 388
Cdd:COG3845 1 MMPPALELRGITKRFG-----------GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 389 DtlAASKLQPLRRDIQFIFQDPyaSLDPRQTV------GysiLEPLRvHGLLQGDAGSKRVAWLLERVGL-LPEHAwrYP 461
Cdd:COG3845 70 R--IRSPRDAIALGIGMVHQHF--MLVPNLTVaenivlG---LEPTK-GGRLDRKAARARIRELSERYGLdVDPDA--KV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 462 HEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQ 541
Cdd:COG3845 140 EDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGK 218
|
....*....
gi 949724212 542 IVeiGTRRA 550
Cdd:COG3845 219 VV--GTVDT 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
31-260 |
1.95e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.81 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVscdemLLRRrnrqvIELGEqsASQMRHVRGAdIAMIF 110
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV-----LVSG-----IDTGD--FSKLQGIRKL-VGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEPMTSLnpvftVGEQIAESIrlhqgASHEEAM----VEAKRMLDQVrIPEAKAILSRY--PHQLSGGMRQRVMIAMALS 184
Cdd:PRK13644 84 QNPETQF-----VGRTVEEDL-----AFGPENLclppIEIRKRVDRA-LAEIGLEKYRHrsPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADiADRVLVMYQGEAVETGSVEQIFHAP 260
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
334-555 |
2.18e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 85.62 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 334 TREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdtlAASKLQPLRRDIQFIFQDP--- 410
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TKENIREVRKFVGLVFQNPddq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 411 YASLDPRQTVGYSilePLRVHglLQGDAGSKRVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADES 490
Cdd:PRK13652 91 IFSPTVEQDIAFG---PINLG--LDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 491 VSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENP 555
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
314-555 |
2.81e-18 |
|
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: 84.13 E-value: 2.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFPlrsgilnrvTREVhaVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAA 393
Cdd:cd03218 1 LRAENLSKRYG---------KRKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 SKLQplRRDIQFIFQDpyASLDPRQTVGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLlpEH-AWRYPHEFSGGQRQRI 472
Cdd:cd03218 70 HKRA--RLGIGYLPQE--ASIFRKLTVEENILAVLEIRGLSKKER-EEKLEELLEEFHI--THlRKSKASSLSGGERRRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 473 CIARALALNPKVIIADESVSALDVSIRGQIINLMLDLqRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVF 552
Cdd:cd03218 143 EIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
...
gi 949724212 553 ENP 555
Cdd:cd03218 222 ANE 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
31-229 |
2.84e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 84.75 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIE-----QAGgevscdemllrrrnrqVIELGEQSASQmrhvRGAD 105
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKT----TLLNLIAgfvpyQHG----------------SITLDGKPVEG----PGAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 106 IAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIPEAKAilsRYPHQLSGGMRQRVMIAMALSC 185
Cdd:PRK11248 72 RGVVFQN--EGLLPWRNVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAEK---RYIWQLSGGQRQRVGIARALAA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 949724212 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDM 229
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
341-547 |
3.46e-18 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 88.47 E-value: 3.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 341 ENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLaasKLQPLRRDIQFIFQDPyasldprQTV 420
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL---DVQAVRRQLGVVLQNG-------RLM 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 421 GYSILEPLRVHGLLQGDAgskrvAWLLERVGLLPEHAWRYP---H--------EFSGGQRQRICIARALALNPKVIIADE 489
Cdd:TIGR03797 540 SGSIFENIAGGAPLTLDE-----AWEAARMAGLAEDIRAMPmgmHtvisegggTLSGGQRQRLLIARALVRKPRILLFDE 614
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 490 SVSALDVsiRGQIInLMLDLQReLGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGT 547
Cdd:TIGR03797 615 ATSALDN--RTQAI-VSESLER-LKVTRIVIAHRLSTI-RNADRIYVLDAGRVVQQGT 667
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
168-547 |
4.01e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 88.64 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDM-SMGVIFITHDMgvvaDIADR---VLVMY 243
Cdd:NF033858 136 KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVATAYM----EEAERfdwLVAMD 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 244 QGEAVETGSveqifhapqhpyTKALLAavpQLGAMNgheLPRRFplISL--------HDPSHVEPQTEQDtvvEGEPILR 315
Cdd:NF033858 212 AGRVLATGT------------PAELLA---RTGADT---LEAAF--IALlpeekrrgHQPVVIPPRPADD---DDEPAIE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 316 VRNLVTRFplrsGilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTlaask 395
Cdd:NF033858 269 ARGLTMRF----G-------DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA----- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 396 lqplrRDIqfifqdpyaslDPRQTVGY-----------SILEPLRVHGLL---QGDAGSKRVAWLLERVGLLpEHAWRYP 461
Cdd:NF033858 333 -----GDI-----------ATRRRVGYmsqafslygelTVRQNLELHARLfhlPAAEIAARVAEMLERFDLA-DVADALP 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 462 HEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAyLFIS-HDMAVVERIShRVAVMYLG 540
Cdd:NF033858 396 DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFIStHFMNEAERCD-RISLMHAG 473
|
....*..
gi 949724212 541 QIVEIGT 547
Cdd:NF033858 474 RVLASDT 480
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
32-257 |
4.33e-18 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 83.98 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 32 VRNLSFRLKRGETLAIVGESGSGKSvTALSL------------MHLIEQAGGEVSCDEmlLRRRnrqvieLGeqsasqmr 99
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKS-TLLSLitgdlpptygndVRLFGERRGGEDVWE--LRKR------IG-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 100 HVrGADIAMIFQEPMTSLNPV---FTvgeqiaESIRLHQGASHEEAMvEAKRMLDQVRIpeaKAILSRYPHQLSGGMRQR 176
Cdd:COG1119 82 LV-SPALQLRFPRDETVLDVVlsgFF------DSIGLYREPTDEQRE-RARELLELLGL---AHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDmgvVADIAD---RVLVMYQGEAVETGSV 253
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHH---VEEIPPgitHVLLLKDGRVVAAGPK 227
|
....
gi 949724212 254 EQIF 257
Cdd:COG1119 228 EEVL 231
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
31-252 |
5.18e-18 |
|
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: 83.31 E-value: 5.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRQVIelgeqsasqmrhvRGAdIAMIF 110
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL-------------RSR-ISIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEPMT-------SLNP--VFTvGEQIAESIRLHQGASHeeamVEAKRMLDQVRIPEAKAilsryphQLSGGMRQRVMIAM 181
Cdd:cd03244 85 QDPVLfsgtirsNLDPfgEYS-DEELWQALERVGLKEF----VESLPGGLDTVVEEGGE-------NLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADiADRVLVMYQGEAVETGS 252
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCT--VLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
13-247 |
5.40e-18 |
|
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: 81.88 E-value: 5.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQQRVsaVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRQviELGE 92
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPN--ELGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 93 QSASQMRHVrgadiaMIFqepmtslnpvftvGEQIAESIrlhqgasheeamveakrmldqvripeakailsryphqLSGG 172
Cdd:cd03246 77 HVGYLPQDD------ELF-------------SGSIAENI-------------------------------------LSGG 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMgVIFITHDMGVVAdIADRVLVMYQGEA 247
Cdd:cd03246 101 QRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGAT-RIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
350-542 |
6.19e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.96 E-value: 6.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 350 GETLSLVGESGCGKSTTGRALLRLVESQRGEIifngqridtLAASK-LQPLRRDIQFIFQDpyASLDPRQTVGYSIlepl 428
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL---------LAGTApLAEAREDTRLMFQD--ARLLPWKKVIDNV---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 429 rvhGLlqGDAGSKRVAWL--LERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLM 506
Cdd:PRK11247 103 ---GL--GLKGQWRDAALqaLAAVGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLI 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 949724212 507 LDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:PRK11247 177 ESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-257 |
8.71e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 83.90 E-value: 8.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRQVIELG 91
Cdd:PRK13638 1 MLATSDLWFRYQDEP----VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 EQsasqmrhvrgadIAMIFQEPMTSLnpVFT-VGEQIAESIRlHQGASHEEAmveAKRMLDQVRIPEAKailsRYPHQ-- 168
Cdd:PRK13638 77 QQ------------VATVFQDPEQQI--FYTdIDSDIAFSLR-NLGVPEAEI---TRRVDEALTLVDAQ----HFRHQpi 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 --LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIK-VLQQDMSmgVIFITHDMGVVADIADRVLVMYQG 245
Cdd:PRK13638 135 qcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRrIVAQGNH--VIISSHDIDLIYEISDAVYVLRQG 212
|
250
....*....|..
gi 949724212 246 EAVETGSVEQIF 257
Cdd:PRK13638 213 QILTHGAPGEVF 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
36-256 |
8.93e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 82.71 E-value: 8.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 36 SFRLKRGETLAIVGESGSGKSvTALSLMH-LIEQAGGEvscdeMLLRRRNRQvielgEQSASQmRHVrgadiAMIFQEpm 114
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS-TLLNLIAgFLTPASGS-----LTLNGQDHT-----TTPPSR-RPV-----SMLFQE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 115 TSLNPVFTVGEQIAesIRLHQG----ASHEEAMveaKRMLDQVRIPEakaILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:PRK10771 80 NNLFSHLTVAQNIG--LGLNPGlklnAAQREKL---HAIARQMGIED---LLARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 191 IADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQI 256
Cdd:PRK10771 152 LLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
12-246 |
9.00e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.52 E-value: 9.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNiAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIE-QAGGEVSCDEMLLRRRN-RQVIE 89
Cdd:PRK13549 259 ILEVRNLT-AWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNpQQAIA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 90 LGeqsasqmrhvrgadIAMIFQE-PMTSLNPVFTVGEQIAESI--------RLHQGASHEEAMVEAKRMldQVRIPEAKA 160
Cdd:PRK13549 338 QG--------------IAMVPEDrKRDGIVPVMGVGKNITLAAldrftggsRIDDAAELKTILESIQRL--KVKTASPEL 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 161 ILSRyphqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQdMSMGVIFITHDMGVVADIADRVL 240
Cdd:PRK13549 402 AIAR----LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVL 476
|
....*.
gi 949724212 241 VMYQGE 246
Cdd:PRK13549 477 VMHEGK 482
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-522 |
9.36e-18 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 86.61 E-value: 9.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 16 SNLNIAfeQEQQRVSAVRNL---SFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDemlLRRRNRQVIELGE 92
Cdd:PRK10938 2 SSLQIS--QGTFRLSDTKTLqlpSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ---FSHITRLSFEQLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 93 QSASQMRHVRGADiamifqepMTSLNPVFTvGEQIAESIRLHqgaSHEEAMVEakRMLDQVRIpeaKAILSRYPHQLSGG 172
Cdd:PRK10938 77 KLVSDEWQRNNTD--------MLSPGEDDT-GRTTAEIIQDE---VKDPARCE--QLAQQFGI---TALLDRRFKYLSTG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRVLVMYQGEAVETGS 252
Cdd:PRK10938 140 ETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 253 VEQIFhapqhpyTKALLAAVPQLGAMNGHELPRRFplislhDPSHvepqteQDTVVEGEPILRVRNLVTRFPLRSgILNR 332
Cdd:PRK10938 219 REEIL-------QQALVAQLAHSEQLEGVQLPEPD------EPSA------RHALPANEPRIVLNNGVVSYNDRP-ILHN 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 333 VTREVHavenvsfdlwPGETLSLVGESGCGKSTtgraLLRLVES---------------QR--GEIIFN-GQRIDTLAAS 394
Cdd:PRK10938 279 LSWQVN----------PGEHWQIVGPNGAGKST----LLSLITGdhpqgysndltlfgrRRgsGETIWDiKKHIGYVSSS 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 395 klqplrrdiqfIFQDPYASLDPRQTV--GY--SIleplrvhGLLQG--DAGSKRVAWLLERVGLLPEHAWRYPHEFSGGQ 468
Cdd:PRK10938 345 -----------LHLDYRVSTSVRNVIlsGFfdSI-------GIYQAvsDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQ 406
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 469 RQRICIARALALNPKVIIADESVSALDVSIRgQIINLMLD-LQRELGIAYLFISH 522
Cdd:PRK10938 407 QRLALIVRALVKHPTLLILDEPLQGLDPLNR-QLVRRFVDvLISEGETQLLFVSH 460
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
340-522 |
1.24e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 80.66 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFngqridtlaasklqPLRRDIQFIFQDPYASLdprqt 419
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM--------------PEGEDLLFLPQRPYLPL----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 420 vgysileplrvhgllqgdagskrvawllervGLLPEhAWRYP--HEFSGGQRQRICIARALALNPKVIIADESVSALDVS 497
Cdd:cd03223 78 -------------------------------GTLRE-QLIYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180
....*....|....*....|....*
gi 949724212 498 IRGQiinlMLDLQRELGIAYLFISH 522
Cdd:cd03223 126 SEDR----LYQLLKELGITVISVGH 146
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
336-555 |
1.88e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 86.31 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 EVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLaasKLQPLRRDIQFIFQDPyasLD 415
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY---DHHYLHRQVALVGQEP---VL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 416 PRQTVGYSILEPLRVHGLLQGDAGSKRvAWLLERVGLLP--------EHAwrypHEFSGGQRQRICIARALALNPKVIIA 487
Cdd:TIGR00958 567 FSGSVRENIAYGLTDTPDEEIMAAAKA-ANAHDFIMEFPngydtevgEKG----SQLSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 488 DESVSALDVsirgQIINLMLDLQRELGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGTRRAVFENP 555
Cdd:TIGR00958 642 DEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
339-553 |
2.02e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.24 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASK-LQPLRRDIQFIFQDPYASLDpR 417
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeIKPVRKKVGVVFQFPESQLF-E 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 418 QTVGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVS 497
Cdd:PRK13643 100 ETVLKDVAFGPQNFGIPKEKA-EKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 498 IRGQIINLMLDLQrELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFE 553
Cdd:PRK13643 179 ARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-266 |
2.03e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.39 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 19 NIAFEQEQQRVsaVRNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQAGGEVscdemllrrRNRQVIELGEQSASQM 98
Cdd:PRK14258 12 NLSFYYDTQKI--LEGVSMEIYQSKVTAIIGPSGCGKS-TFLKCLNRMNELESEV---------RVEGRVEFFNQNIYER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 99 R----HVRgADIAMIFQEPmtSLNPVfTVGEQIAESIRL---HQGASHE---EAMVEAKRMLDQVRIPEAKAILsryphQ 168
Cdd:PRK14258 80 RvnlnRLR-RQVSMVHPKP--NLFPM-SVYDNVAYGVKIvgwRPKLEIDdivESALKDADLWDEIKHKIHKSAL-----D 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEA- 247
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENr 230
|
250 260
....*....|....*....|...
gi 949724212 248 ----VETGSVEQIFHAPQHPYTK 266
Cdd:PRK14258 231 igqlVEFGLTKKIFNSPHDSRTR 253
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
340-552 |
2.69e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.36 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDtLAASKLQPLRRDIQFIFQDP-----YASL 414
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALRQQVATVFQDPeqqifYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 415 DprQTVGYSilepLRVHGLLQGDAgSKRVAWLLERVgllpeHAWRYPHE----FSGGQRQRICIARALALNPKVIIADES 490
Cdd:PRK13638 96 D--SDIAFS----LRNLGVPEAEI-TRRVDEALTLV-----DAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 491 VSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVF 552
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
13-252 |
3.16e-17 |
|
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: 80.53 E-value: 3.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQQRVsaVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMllrrrNRQVIELGE 92
Cdd:cd03369 7 IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI-----DISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 93 QSASqmrhvrgadIAMIFQEPM-------TSLNPV--FTvGEQIAESIRLHQGASHeeamveakrmldqvripeakails 163
Cdd:cd03369 80 LRSS---------LTIIPQDPTlfsgtirSNLDPFdeYS-DEEIYGALRVSEGGLN------------------------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 164 ryphqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMgvIFITHDMGVVADIaDRVLVMY 243
Cdd:cd03369 126 -----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTI--LTIAHRLRTIIDY-DKILVMD 197
|
....*....
gi 949724212 244 QGEAVETGS 252
Cdd:cd03369 198 AGEVKEYDH 206
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
311-543 |
3.61e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.84 E-value: 3.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPlrsgilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDT 390
Cdd:PRK09700 3 TPYISMAGIGKSFG-----------PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 391 LA---ASKLqplrrDIQFIFQDpYASLDPrqtvgYSILEPLRVHGLLQGDAGS----------KRVAWLLERVGLLpeha 457
Cdd:PRK09700 72 LDhklAAQL-----GIGIIYQE-LSVIDE-----LTVLENLYIGRHLTKKVCGvniidwremrVRAAMMLLRVGLK---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 458 wRYPHEFSG----GQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHR 533
Cdd:PRK09700 137 -VDLDEKVAnlsiSHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDR 214
|
250
....*....|
gi 949724212 534 VAVMYLGQIV 543
Cdd:PRK09700 215 YTVMKDGSSV 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
29-260 |
3.95e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 83.35 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqAG------GEVSCDEmllRRRNRqvIELGEQsasqmrhvr 102
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKS----TLLRMV--AGleritsGEIWIGG---RVVNE--LEPADR--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 103 gaDIAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASHEEAmveAKRMLDQVRIPEAKAILSRYPHQLSGGMRQRVMIAMA 182
Cdd:PRK11650 77 --DIAMVFQN--YALYPHMSVRENMAYGLKI-RGMPKAEI---EERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAP 260
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-256 |
4.20e-17 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 84.77 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 19 NIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEmllrrrnrqvIELGEQSASQM 98
Cdd:TIGR02203 335 NVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG----------HDLADYTLASL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 99 RhvrgADIAMIFQEpmtslnpVFTVGEQIAESIRLHQGASHEEAMVEakrmlDQVRIPEAKAILSRYP---HQ------- 168
Cdd:TIGR02203 405 R----RQVALVSQD-------VVLFNDTIANNIAYGRTEQADRAEIE-----RALAAAYAQDFVDKLPlglDTpigengv 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 -LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADiADRVLVMYQGEA 247
Cdd:TIGR02203 469 lLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRT--TLVIAHRLSTIEK-ADRIVVMDDGRI 545
|
....*....
gi 949724212 248 VETGSVEQI 256
Cdd:TIGR02203 546 VERGTHNEL 554
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
35-272 |
4.31e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.04 E-value: 4.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 35 LSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQAGGEVscdemLLRRRNrqvieLGEQSASQMRHVRgadiAMIFQEPM 114
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKS-TLLARMAGLLPGQGEI-----LLNGRP-----LSDWSAAELARHR----AYLSQQQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 115 TSLN-PVFtvgeqiaESIRLHQGASHEEAMVEA--KRMLDQVRIpEAKaiLSRYPHQLSGGMRQRVMIAMAL-----SCR 186
Cdd:COG4138 80 PPFAmPVF-------QYLALHQPAGASSEAVEQllAQLAEALGL-EDK--LSRPLTQLSGGEWQRVRLAAVLlqvwpTIN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 187 P--AVLIADEPTTALDVTIQAQILQLIKVL-QQDMSmgVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFhapqhp 263
Cdd:COG4138 150 PegQLLLLDEPMNSLDVAQQAALDRLLRELcQQGIT--VVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM------ 221
|
....*....
gi 949724212 264 yTKALLAAV 272
Cdd:COG4138 222 -TPENLSEV 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
334-553 |
4.49e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 84.69 E-value: 4.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 334 TREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLaasKLQPLRRDIQFIFQDPYAS 413
Cdd:PRK11176 353 GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDY---TLASLRNQVALVSQNVHLF 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 414 LDprqTVGYSIleplrvhgllqgdAGSKRVAWLLERVgllpEHAWRYPH--EF-------------------SGGQRQRI 472
Cdd:PRK11176 430 ND---TIANNI-------------AYARTEQYSREQI----EEAARMAYamDFinkmdngldtvigengvllSGGQRQRI 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 473 CIARALALNPKVIIADESVSALDV-SIRgqIINLMLD-LQRELGIayLFISHDMAVVERiSHRVAVMYLGQIVEIGTRRA 550
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTeSER--AIQAALDeLQKNRTS--LVIAHRLSTIEK-ADEILVVEDGEIVERGTHAE 564
|
...
gi 949724212 551 VFE 553
Cdd:PRK11176 565 LLA 567
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-256 |
4.72e-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: 4.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQQRVsaVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNR------ 85
Cdd:TIGR01842 316 HLSVENVTIVPPGGKKPT--LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRetfgkh 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 86 -----QVIELGEQSASQmrhvrgaDIAMiFQEPMTSlnpvftvgEQIAESIRLHQgaSHEeaMVEAKRMLDQVRIPEAKA 160
Cdd:TIGR01842 394 igylpQDVELFPGTVAE-------NIAR-FGENADP--------EKIIEAAKLAG--VHE--LILRLPDGYDTVIGPGGA 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 161 ilsryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQdMSMGVIFITHDMGVVAdIADRVL 240
Cdd:TIGR01842 454 -------TLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKA-RGITVVVITHRPSLLG-CVDKIL 524
|
250
....*....|....*.
gi 949724212 241 VMYQGEAVETGSVEQI 256
Cdd:TIGR01842 525 VLQDGRIARFGERDEV 540
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
27-251 |
4.75e-17 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 80.65 E-value: 4.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 27 QRVSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqAG------GEVScdemllrrrnrqvielgeqsasqmrh 100
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKS----TLLRLL--AGiyppdsGTVT-------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 101 VRGADIAMIfqEPMTSLNPVFTVGEQIAESIRLHqGASHEEAmveaKRMLDQVripEAKAILSRYPHQ----LSGGMRQR 176
Cdd:cd03220 81 VRGRVSSLL--GLGGGFNPELTGRENIYLNGRLL-GLSRKEI----DEKIDEI---IEFSELGDFIDLpvktYSSGMKAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMgVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKT-VILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-251 |
5.34e-17 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 80.33 E-value: 5.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 19 NIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRQVIelgeqsasqM 98
Cdd:cd03245 7 NVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---------R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 99 RHvrgadIAMIFQEPMtslnpVF--TVGEQIAesirLHQGASHEEAMVEAkrmldqVRIPEAKAILSRYPH--------- 167
Cdd:cd03245 78 RN-----IGYVPQDVT-----LFygTLRDNIT----LGAPLADDERILRA------AELAGVTDFVNKHPNgldlqiger 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 168 --QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMgvIFITHDMGVVaDIADRVLVMYQG 245
Cdd:cd03245 138 grGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTL--IIITHRPSLL-DLVDRIIVMDSG 214
|
....*.
gi 949724212 246 EAVETG 251
Cdd:cd03245 215 RIVADG 220
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
31-251 |
5.85e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 82.06 E-value: 5.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSC---DEMLLRRRNRQVIELGEQ--SASQMRHVRGAD 105
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEKVLEKLviQKTRFKKIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 106 -----IAMIFQEPMTSLnpvF--TVGEQIAESIRlHQGASHEEAMVEAKRMLDQVRIPEAkaILSRYPHQLSGGMRQRVM 178
Cdd:PRK13651 102 eirrrVGVVFQFAEYQL---FeqTIEKDIIFGPV-SMGVSKEEAKKRAAKYIELVGLDES--YLQRSPFELSGGQKRRVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 179 IAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQdMSMGVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
13-260 |
6.41e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.35 E-value: 6.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQeqqrVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDemllrrrNRQVIELGE 92
Cdd:PRK09536 4 IDVSDLSVEFGD----TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVA-------GDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 93 QSASQMrhvrgadIAMIFQEpmTSLNPVFTVgEQIAE------SIRLHQGASHEEAMVEakRMLDQVripEAKAILSRYP 166
Cdd:PRK09536 73 RAASRR-------VASVPQD--TSLSFEFDV-RQVVEmgrtphRSRFDTWTETDRAAVE--RAMERT---GVAQFADRPV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFItHDMGVVADIADRVLVMYQGE 246
Cdd:PRK09536 138 TSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGR 216
|
250
....*....|....
gi 949724212 247 AVETGSVEQIFHAP 260
Cdd:PRK09536 217 VRAAGPPADVLTAD 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-278 |
6.61e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.83 E-value: 6.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQeqQRVsaVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMllrrrnrqviELGE 92
Cdd:PRK11231 3 LRTENLTVGYGT--KRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDK----------PISM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 93 QSASQM-RHvrgadIAMIFQEPMTSLNpvFTVGEQIA--ESIRL-HQG--ASHEEAMVEakRMLDQVRIPEakaILSRYP 166
Cdd:PRK11231 69 LSSRQLaRR-----LALLPQHHLTPEG--ITVRELVAygRSPWLsLWGrlSAEDNARVN--QAMEQTRINH---LADRRL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRVLVMYQGE 246
Cdd:PRK11231 137 TDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
250 260 270
....*....|....*....|....*....|..
gi 949724212 247 AVETGSVEQIFhapqhpyTKALLAAVPQLGAM 278
Cdd:PRK11231 216 VMAQGTPEEVM-------TPGLLRTVFDVEAE 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
314-553 |
7.12e-17 |
|
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: 84.08 E-value: 7.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFplrsgilnrvtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRaLLRLVESQR---GEIIFN------ 384
Cdd:TIGR03269 1 IEVKNLTKKF-----------DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMH-VLRGMDQYEptsGRIIYHvalcek 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 385 ----------------------GQRIDTLAASK--LQPLRRDIQFIFQDPYAsLDPRQTVGYSILEPLRVHGLlQGDAGS 440
Cdd:TIGR03269 69 cgyverpskvgepcpvcggtlePEEVDFWNLSDklRRRIRKRIAIMLQRTFA-LYGDDTVLDNVLEALEEIGY-EGKEAV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 441 KRVAWLLERVGLlpEHawRYPH---EFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAY 517
Cdd:TIGR03269 147 GRAVDLIEMVQL--SH--RITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISM 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 949724212 518 LFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFE 553
Cdd:TIGR03269 223 VLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
336-543 |
7.39e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.39 E-value: 7.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 EVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQPLRRD-IQFIFQDPY--A 412
Cdd:PRK10535 20 QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREhFGFIFQRYHllS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 413 SLDPRQTVgysilEPLRVHGLLQGDAGSKRVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVS 492
Cdd:PRK10535 100 HLTAAQNV-----EVPAVYAGLERKQRLLRAQELLQRLGL-EDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 949724212 493 ALDvSIRGQIINLMLDLQRELGIAYLFISHDMAVVERiSHRVAVMYLGQIV 543
Cdd:PRK10535 174 ALD-SHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
31-251 |
7.56e-17 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 79.57 E-value: 7.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDemllrrrnrqvielgeQSASQMRHVRGADIAMIF 110
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFD----------------GKSYQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEPmtSLNPVFTVGEQIAESIRLHqGASHEEAMveakRMLDQVRipeakaiLSRYPH----QLSGGMRQRVMIAMALSCR 186
Cdd:cd03268 79 EAP--GFYPNLTARENLRLLARLL-GIRKKRID----EVLDVVG-------LKDSAKkkvkGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 187 PAVLIADEPTTALDVTIQAQILQLIKVLqQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
31-254 |
7.57e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 80.94 E-value: 7.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTalsLMHLieqaggevscDEMLLRRRNRQVIELGEQSASQMRHVRGAdIAMIF 110
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTL---LLHL----------NGIYLPQRGRVKVMGREVNAENEKWVRSK-VGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEPMtslNPVF--TVGEQIAESIRlHQGASHEEAMVEAKRMLDQVRIpeaKAILSRYPHQLSGGMRQRVMIAMALSCRPA 188
Cdd:PRK13647 86 QDPD---DQVFssTVWDDVAFGPV-NMGLDKDEVERRVEEALKAVRM---WDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 189 VLIADEPTTALDVTIQAQILQLIKVLQQDMSMgVIFITHDMGVVADIADRVLVMYQGEAVETGSVE 254
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQGKT-VIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
32-246 |
1.03e-16 |
|
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: 79.44 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 32 VRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLrrrnrqvielgeqSASQMRHVRgADIAMIFQ 111
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI-------------SQYEHKYLH-SKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 112 EPMTSLNpvfTVGEQIAESIrlhQGASHEEAMVEAKRMldqvripEAKAILSRYPH-----------QLSGGMRQRVMIA 180
Cdd:cd03248 96 EPVLFAR---SLQDNIAYGL---QSCSFECVKEAAQKA-------HAHSFISELASgydtevgekgsQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVaDIADRVLVMYQGE 246
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRT--VLVIAHRLSTV-ERADQILVLDGGR 225
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
37-256 |
1.10e-16 |
|
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: 79.51 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 37 FRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRQVIELGEqsasqmRHVRGADIamifqePMTS 116
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYVPQ------RHEFAWDF------PISV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 117 LNPVFTVGEQIAESIRLHQGASHEeAMVEAkrmLDQVRIPEakaiLSRYP-HQLSGGMRQRVMIAMALSCRPAVLIADEP 195
Cdd:TIGR03771 69 AHTVMSGRTGHIGWLRRPCVADFA-AVRDA---LRRVGLTE----LADRPvGELSGGQRQRVLVARALATRPSVLLLDEP 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 196 TTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRVlVMYQGEAVETGSVEQI 256
Cdd:TIGR03771 141 FTGLDMPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQL 199
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
337-550 |
1.11e-16 |
|
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: 83.34 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 337 VHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVE--SQRGEIIFNGQRIDtlAASKLQPLRRDIQFIFQDpyASL 414
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLK--ASNIRDTERAGIVIIHQE--LTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 415 DPRQTVGYSIL---EPLRVHGLLQGDAGSKRVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESV 491
Cdd:TIGR02633 90 VPELSVAENIFlgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 492 SALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQivEIGTRRA 550
Cdd:TIGR02633 170 SSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ--HVATKDM 225
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
33-261 |
1.18e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 82.00 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 33 RNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqAGGE-VSCDEMLLrrrnrqvielGEQsasQMRHVRGAD--IAMI 109
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKS----TLLRMI--AGLEdITSGDLFI----------GEK---RMNDVPPAErgVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 110 FQEpmTSLNPVFTVGEQIAESIRLhqgASHEEAmvEAKRMLDQV-RIPEAKAILSRYPHQLSGGMRQRVMIAMALSCRPA 188
Cdd:PRK11000 81 FQS--YALYPHLSVAENMSFGLKL---AGAKKE--EINQRVNQVaEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 189 VLIADEPTTALD----VTIQAQILQLIKVLQQDMsmgvIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPQ 261
Cdd:PRK11000 154 VFLLDEPLSNLDaalrVQMRIEISRLHKRLGRTM----IYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
313-543 |
1.76e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.74 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 313 ILRVRNLVTRFplrsgilNRVT-REVHAVENVSFDLWPGETLSLVGESGCGKSTtgraLLRLV----ESQRGEIIFNGQR 387
Cdd:COG1101 1 MLELKNLSKTF-------NPGTvNEKRALDGLNLTIEEGDFVTVIGSNGAGKST----LLNAIagslPPDSGSILIDGKD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 388 IDTLAASKlqplR-RDIQFIFQDPYASLDPRQTvgysILEPL-------RVHGLLQGDAGSKR------VAWL---LE-- 448
Cdd:COG1101 70 VTKLPEYK----RaKYIGRVFQDPMMGTAPSMT----IEENLalayrrgKRRGLRRGLTKKRRelfrelLATLglgLEnr 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 449 ---RVGLLpehawryphefSGGQRQriciarALAL------NPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLF 519
Cdd:COG1101 142 ldtKVGLL-----------SGGQRQ------ALSLlmatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLM 204
|
250 260
....*....|....*....|....*.
gi 949724212 520 ISHDM--AVveRISHRVAVMYLGQIV 543
Cdd:COG1101 205 VTHNMeqAL--DYGNRLIMMHEGRII 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
33-246 |
2.31e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 79.34 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 33 RNLSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQA-GGEvscdemLLRrrnrqvielGEQSASQMRHvrgaDIAMIFQ 111
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKS-TLLRLLAGLETPsAGE------LLA---------GTAPLAEARE----DTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 112 EpmTSLNPVFTVGEQIAESIRLHQGASHEEAMvEAKRMLDqvRIPEakailsrYPHQLSGGMRQRVMIAMALSCRPAVLI 191
Cdd:PRK11247 89 D--ARLLPWKKVIDNVGLGLKGQWRDAALQAL-AAVGLAD--RANE-------WPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 192 ADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGE 246
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
340-552 |
2.96e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.05 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQPLRrdiqfifqdpyASLdPRQT 419
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR-----------AVL-PQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 420 vgySILEPLRVH-----GLLQGDAGSKRVAWL----LERVGLLpEHAWRYPHEFSGGQRQRICIARALA------LNPKV 484
Cdd:PRK13548 86 ---SLSFPFTVEevvamGRAPHGLSRAEDDALvaaaLAQVDLA-HLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 485 IIADESVSALDvsIRGQIINLML--DLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVF 552
Cdd:PRK13548 162 LLLDEPTSALD--LAHQHHVLRLarQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
33-271 |
4.43e-16 |
|
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: 81.79 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 33 RNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRrrnrqviELGEQSasqmrhVRGAdIAMIFQE 112
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIR-------DVTQAS------LRAA-IGIVPQD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 113 pmTSLnpvF--TVGEQIAESiRLhqGASHEEaMVEAKRM--LDQ--VRIPEA----------KailsryphqLSGGMRQR 176
Cdd:COG5265 441 --TVL---FndTIAYNIAYG-RP--DASEEE-VEAAARAaqIHDfiESLPDGydtrvgerglK---------LSGGEKQR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADiADRVLVMYQGEAVETGSveqi 256
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRT--TLVIAHRLSTIVD-ADEILVLEAGRIVERGT---- 575
|
250
....*....|....*
gi 949724212 257 fHApqhpytkALLAA 271
Cdd:COG5265 576 -HA-------ELLAQ 582
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-246 |
5.02e-16 |
|
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: 81.02 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 2 PHSDELDASDVLAVSNLNiAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIE-QAGGEVSCDEMLL 80
Cdd:TIGR02633 247 PHEPHEIGDVILEARNLT-CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPV 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 81 RRRN-RQVIELGeqsasqmrhvrgadIAMIFQE-PMTSLNPVFTVGEQIA-ESIRLHQGASHEEAMVEAKRMLDQVRIPE 157
Cdd:TIGR02633 326 DIRNpAQAIRAG--------------IAMVPEDrKRHGIVPILGVGKNITlSVLKSFCFKMRIDAAAELQIIGSAIQRLK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 158 AKAILSRYP-HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIA 236
Cdd:TIGR02633 392 VKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLS 470
|
250
....*....|
gi 949724212 237 DRVLVMYQGE 246
Cdd:TIGR02633 471 DRVLVIGEGK 480
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-261 |
5.48e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 77.71 E-value: 5.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 10 SDVLAVSNLNIAFEQeqqrVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCD-EMLLRRRNRQVI 88
Cdd:COG0410 1 MPMLEVENLHAGYGG----IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgEDITGLPPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 89 ELGeqsasqMRHV---RGadiamIFQEpMTslnpvftvgeqIAESIRLhqGASHEEAMVEAKRMLDQV--RIPEAKAILS 163
Cdd:COG0410 77 RLG------IGYVpegRR-----IFPS-LT-----------VEENLLL--GAYARRDRAEVRADLERVyeLFPRLKERRR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqQDMSMGVIFITHDMGVVADIADRVLVMY 243
Cdd:COG0410 132 QRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLE 210
|
250
....*....|....*...
gi 949724212 244 QGEAVETGSVEQIFHAPQ 261
Cdd:COG0410 211 RGRIVLEGTAAELLADPE 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
12-267 |
6.18e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 78.29 E-value: 6.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSvTALS----LMHLIE--QAGGEV----------SC 75
Cdd:PRK14243 10 VLRTENLNVYYGSFL----AVKNVWLDIPKNQITAFIGPSGCGKS-TILRcfnrLNDLIPgfRVEGKVtfhgknlyapDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 76 DEMLLRRRnrqvielgeqsasqmrhvrgadIAMIFQEPmtslNPvF--TVGEQIAESIRLHQGASHEEAMVEakRMLDQV 153
Cdd:PRK14243 85 DPVEVRRR----------------------IGMVFQKP----NP-FpkSIYDNIAYGARINGYKGDMDELVE--RSLRQA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 154 RI-PEAKAILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVV 232
Cdd:PRK14243 136 ALwDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYT--IIIVTHNMQQA 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 949724212 233 ADIADRVLVM---------YQGEAVETGSVEQIFHAPQHPYTKA 267
Cdd:PRK14243 214 ARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQATRD 257
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
13-260 |
6.57e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 77.72 E-value: 6.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQeqqrVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEmllrrrnrQVIE-LG 91
Cdd:PRK11300 6 LSVSGLMMRFGG----LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG--------QHIEgLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 EQSASQMRHVRGADIAMIFQEpMTSLNPVFtvgeqIAESIRLHQG------------ASHEEAMVEAKRMLDQVRIpeaK 159
Cdd:PRK11300 74 GHQIARMGVVRTFQHVRLFRE-MTVIENLL-----VAQHQQLKTGlfsgllktpafrRAESEALDRAATWLERVGL---L 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 160 AILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRV 239
Cdd:PRK11300 145 EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRI 224
|
250 260
....*....|....*....|.
gi 949724212 240 LVMYQGEAVETGSVEQIFHAP 260
Cdd:PRK11300 225 YVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-252 |
6.67e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 81.22 E-value: 6.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 19 NIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLrrRNRQVIELGEQSA--S 96
Cdd:PRK11176 346 NVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL--RDYTLASLRNQVAlvS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 97 QMRHVRGADIAMifqepmtslNPVFTVGEQIA-ESIRLHQGASHeeAMVEAKRM---LDQVrIPEAKAIlsryphqLSGG 172
Cdd:PRK11176 424 QNVHLFNDTIAN---------NIAYARTEQYSrEQIEEAARMAY--AMDFINKMdngLDTV-IGENGVL-------LSGG 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADiADRVLVMYQGEAVETGS 252
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRT--SLVIAHRLSTIEK-ADEILVVEDGEIVERGT 561
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
311-556 |
8.32e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 77.38 E-value: 8.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPlrsgilnrvTREVhaVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDT 390
Cdd:COG1137 1 MMTLEAENLVKSYG---------KRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 391 LaasklqPL----RRDIQFIFQDPyaSLDPRQTVGYSILEPLRVHGLlQGDAGSKRVAWLLERVGLlpEH-AWRYPHEFS 465
Cdd:COG1137 70 L------PMhkraRLGIGYLPQEA--SIFRKLTVEDNILAVLELRKL-SKKEREERLEELLEEFGI--THlRKSKAYSLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 466 GGQRQRICIARALALNPKVIIADESVSALD---VS-IRGQIINLmldlqRELGIAYLFISHDmaVVE--RISHRVAVMYL 539
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLDEPFAGVDpiaVAdIQKIIRHL-----KERGIGVLITDHN--VREtlGICDRAYIISE 211
|
250
....*....|....*..
gi 949724212 540 GQIVEIGTRRAVFENPQ 556
Cdd:COG1137 212 GKVLAEGTPEEILNNPL 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
314-553 |
9.68e-16 |
|
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: 80.56 E-value: 9.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFPlrsgilnrvTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAA 393
Cdd:COG4618 331 LSVENLTVVPP---------GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 SKLQP----LRRDIQFI----------FQDPyaslDPRQtvgysILEPLR---VHGLLQ----------GDAGSkrvawl 446
Cdd:COG4618 402 EELGRhigyLPQDVELFdgtiaeniarFGDA----DPEK-----VVAAAKlagVHEMILrlpdgydtriGEGGA------ 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 447 lervGLlpehawryphefSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLqRELGIAYLFISHDMAV 526
Cdd:COG4618 467 ----RL------------SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSL 529
|
250 260
....*....|....*....|....*..
gi 949724212 527 VeRISHRVAVMYLGQIVEIGTRRAVFE 553
Cdd:COG4618 530 L-AAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
32-257 |
1.14e-15 |
|
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: 76.81 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 32 VRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEvscdemllrrrnrqvIELGEQSASQMRHVRGADIAMIF- 110
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGK---------------ILLDGQDITKLPMHKRARLGIGYl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 -QEPmtSLNPVFTVGEQIAESIRLHqGASHEEAMVEAKRMLDQVRIpeaKAILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
Cdd:cd03218 81 pQEA--SIFRKLTVEENILAVLEIR-GLSKKEREEKLEELLEEFHI---THLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 190 LIADEPTTALDVTIQAQILQLIKVLqQDMSMGvIFIT-HDMGVVADIADRVLVMYQGEAVETGSVEQIF 257
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
8-255 |
1.50e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.09 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 8 DASDVLAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEqAGGEVSCDEMLlrrrNRQV 87
Cdd:TIGR00955 17 DGSWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSP-KGVKGSGSVLL----NGMP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 88 IElgeqsASQMRHVRgadiAMIFQEPMtsLNPVFTVGEQIAES--IRLHQGASHEEAMVEAKRMLDQVRIPEAKAILSRY 165
Cdd:TIGR00955 92 ID-----AKEMRAIS----AYVQQDDL--FIPTLTVREHLMFQahLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 166 PHQ---LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVM 242
Cdd:TIGR00955 161 PGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILM 240
|
250
....*....|...
gi 949724212 243 YQGEAVETGSVEQ 255
Cdd:TIGR00955 241 AEGRVAYLGSPDQ 253
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
342-547 |
1.59e-15 |
|
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: 79.86 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 342 NVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLaasKLQPLRRDIQFIFQDPYASLDprqTVG 421
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDV---TQASLRAAIGIVPQDTVLFND---TIA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 422 YSIleplrvhglLQGDAGSK--------RVAWLLERVGLLPEhawRYPHE-------FSGGQRQRICIARALALNPKVII 486
Cdd:COG5265 450 YNI---------AYGRPDASeeeveaaaRAAQIHDFIESLPD---GYDTRvgerglkLSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 487 ADESVSALDVSIRGQIinlmldlQRELGIA-----YLFISHdmavveRIS-----HRVAVMYLGQIVEIGT 547
Cdd:COG5265 518 FDEATSALDSRTERAI-------QAALREVargrtTLVIAH------RLStivdaDEILVLEAGRIVERGT 575
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
13-248 |
1.91e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.77 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEvscdemlLRRRNRQVIELGE 92
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGT-------YRVAGQDVATLDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 93 QSASQMRHvrgADIAMIFQEpmTSLNPVFTvGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEAkaiLSRYPHQLSGG 172
Cdd:PRK10535 78 DALAQLRR---EHFGFIFQR--YHLLSHLT-AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDR---VEYQPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqQDMSMGVIFITHDMGVVADiADRVLVMYQGEAV 248
Cdd:PRK10535 149 QQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-248 |
2.14e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 76.66 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQQR-VSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqaGGEVSCDEmllrrrnrQVIELG 91
Cdd:COG1101 2 LELKNLSKTFNPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKS----TLLNAI---AGSLPPDS--------GSILID 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 EQSASQMR-HVRGADIAMIFQEPMTSLNPVFTVGEQIA------ESIRLHQGASHEE-----AMVEA------KRMLDQV 153
Cdd:COG1101 67 GKDVTKLPeYKRAKYIGRVFQDPMMGTAPSMTIEENLAlayrrgKRRGLRRGLTKKRrelfrELLATlglgleNRLDTKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 154 RipeakailsryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVA 233
Cdd:COG1101 147 G-------------LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQAL 213
|
250
....*....|....*
gi 949724212 234 DIADRVLVMYQGEAV 248
Cdd:COG1101 214 DYGNRLIMMHEGRII 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
340-553 |
2.32e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.15 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKlqplRRDIQFIFQdpYASLDPrqt 419
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA----RQRVGVVPQ--FDNLDP--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 420 vGYSILEPLRVHGL---LQGDAGSKRVAWLLErVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDV 496
Cdd:PRK13537 94 -DFTVRENLLVFGRyfgLSAAAARALVPPLLE-FAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 497 SIRgqiiNLMLDLQREL---GIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFE 553
Cdd:PRK13537 172 QAR----HLMWERLRSLlarGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
357-559 |
6.38e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.45 E-value: 6.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 357 GESGCGKSTTGRALLRLVESQRGEIIFNGQR-IDTLAASKLQPLRRDIQFIFQDpyASLDPRqtvgYsileplRVHGLLQ 435
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFDAEKGICLPPEKRRIGYVFQD--ARLFPH----Y------KVRGNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 436 GDAGSKRVAWLLERVGLLP-EHAW-RYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQREL 513
Cdd:PRK11144 99 YGMAKSMVAQFDKIVALLGiEPLLdRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREI 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 949724212 514 GIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQ-HPY 559
Cdd:PRK11144 179 NIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmRPW 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
336-553 |
6.54e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.55 E-value: 6.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 EVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASK-LQPLRRDIQFIFQDPYASL 414
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdIKQIRKKVGLVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 415 DpRQTVGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSAL 494
Cdd:PRK13649 99 F-EETVLKDVAFGPQNFGVSQEEA-EALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 495 DVSIRGQIINLMLDLQrELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFE 553
Cdd:PRK13649 177 DPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
328-543 |
7.50e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 74.29 E-value: 7.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 328 GILNRVTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGqridtLAASKLQP-LRRDIQFI 406
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----LVPWKRRKkFLRRIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 407 F---QDPYASLDPRQtvGYSILEplRVHGLLQGDAGsKRVAWLLERVGLlpEHAWRYP-HEFSGGQRQRICIARALALNP 482
Cdd:cd03267 100 FgqkTQLWWDLPVID--SFYLLA--AIYDLPPARFK-KRLDELSELLDL--EELLDTPvRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 483 KVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
314-601 |
8.18e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 75.51 E-value: 8.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFPLRSGIlnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEI--IFNGQRIDTL 391
Cdd:PRK13651 3 IKVKNIVKIFNKKLPT------ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 392 AAS-------------------KLQPLRRDIQFIFQdpYASLDP-RQTVGYSILEPLRVHGLLQGDAgSKRVAWLLERVG 451
Cdd:PRK13651 77 TKEkekvleklviqktrfkkikKIKEIRRRVGVVFQ--FAEYQLfEQTIEKDIIFGPVSMGVSKEEA-KKRAAKYIELVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 452 LLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERIS 531
Cdd:PRK13651 154 LDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWT 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 532 HRVAVMYLGQIVEIGTRRAVFENPQHPYTRKLMaavpvadpshhrPQRVLlsdDIPSNIRKRGEEISPVS 601
Cdd:PRK13651 233 KRTIFFKDGKIIKDGDTYDILSDNKFLIENNME------------PPKLL---NFVNKLEKKGIDVPKVT 287
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
340-522 |
9.96e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.15 E-value: 9.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFngqridtlaasklqPLRRDIQFIFQDPY---ASLdp 416
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR--------------PAGARVLFLPQRPYlplGTL-- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 417 RQTVGYsilePLRVHgllqgDAGSKRVAWLLERVGL--LPEH-----AWryPHEFSGGQRQRICIARALALNPKVIIADE 489
Cdd:COG4178 443 REALLY----PATAE-----AFSDAELREALEAVGLghLAERldeeaDW--DQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190
....*....|....*....|....*....|....
gi 949724212 490 SVSALDVSIRGQIINLmldLQREL-GIAYLFISH 522
Cdd:COG4178 512 ATSALDEENEAALYQL---LREELpGTTVISVGH 542
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
340-551 |
1.01e-14 |
|
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: 77.39 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQP----LRRDIQFI--------- 406
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKhigyLPQDVELFpgtvaenia 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 407 -FQDpyaSLDPRQTVGYSILEplRVHGLLQ----------GDAGSkrvawllervGLlpehawryphefSGGQRQRICIA 475
Cdd:TIGR01842 414 rFGE---NADPEKIIEAAKLA--GVHELILrlpdgydtviGPGGA----------TL------------SGGQRQRIALA 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 476 RALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERIShRVAVMYLGQIVEIGTRRAV 551
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCVD-KILVLQDGRIARFGERDEV 540
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-251 |
1.03e-14 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 72.35 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQQRVsaVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIEQA----GGEVSCDEMLlrrrnrqVI 88
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKS----TLLQLLTGDlkpqQGEITLDGVP-------VS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 89 ELGEQSASQmrhvrgadIAMIFQEPMtslnpVFtvgeqiAESIRLHQGAsheeamveakrmldqvripeakailsryphQ 168
Cdd:cd03247 68 DLEKALSSL--------ISVLNQRPY-----LF------DTTLRNNLGR------------------------------R 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADiADRVLVMYQGEAV 248
Cdd:cd03247 99 FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKT--LIWITHHLTGIEH-MDKILFLENGKII 175
|
...
gi 949724212 249 ETG 251
Cdd:cd03247 176 MQG 178
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
32-256 |
1.15e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 73.96 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 32 VRNLSFRLKRGETLAIVGESGSGKSvTALSLM-HLIEQAGGEVSCDEMLLRRrnrqvielgeqsasqmrhVRGADIAMIF 110
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKS-TLLSMIsRLLPPDSGEVLVDGLDVAT------------------TPSRELAKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 ----QEPmtSLNPVFTVGEqiaesirL--------HQGASHEEamveakrmlDQVRIPEAKAILS------RYPHQLSGG 172
Cdd:COG4604 78 ailrQEN--HINSRLTVRE-------LvafgrfpySKGRLTAE---------DREIIDEAIAYLDledladRYLDELSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGS 252
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
....
gi 949724212 253 VEQI 256
Cdd:COG4604 220 PEEI 223
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
313-547 |
1.50e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.58 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 313 ILRVRNLVTRFPLRSGILNRV-----------TREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEI 381
Cdd:COG1134 4 MIEVENVSKSYRLYHEPSRSLkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 382 IFNGqridtlaasklqplrrdiqfifqdpyasldprqtvgysileplrvhgllqgdagskRVAWLLE-RVGLLPEH---- 456
Cdd:COG1134 84 EVNG--------------------------------------------------------RVSALLElGAGFHPELtgre 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 457 ----------------AWRYPH--EFSG--------------GQRQRICIARALALNPKVIIADESVSALDVSIRGQIIN 504
Cdd:COG1134 108 niylngrllglsrkeiDEKFDEivEFAElgdfidqpvktyssGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLA 187
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 949724212 505 LMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGT 547
Cdd:COG1134 188 RIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD 229
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
313-543 |
1.65e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 74.74 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 313 ILRVRNLVTRFPLRS----------GILNRVTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEII 382
Cdd:COG4586 1 IIEVENLSKTYRVYEkepglkgalkGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 383 FNG-----QRIDtlaasklqpLRRDIQFIF-QdpyasldpRQTVGY--SILEPLRVHGLLQG---DAGSKRVAWLLERVG 451
Cdd:COG4586 81 VLGyvpfkRRKE---------FARRIGVVFgQ--------RSQLWWdlPAIDSFRLLKAIYRipdAEYKKRLDELVELLD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 452 LlpEHAWRYP-HEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERI 530
Cdd:COG4586 144 L--GELLDTPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAL 221
|
250
....*....|...
gi 949724212 531 SHRVAVMYLGQIV 543
Cdd:COG4586 222 CDRVIVIDHGRII 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
342-546 |
1.72e-14 |
|
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: 73.07 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 342 NVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQ---RGEIIFNGQridtlaASKLQPLRRDIQFIFQDPY--ASLDP 416
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQ------PRKPDQFQKCVAYVRQDDIllPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 417 RQTVGYSIlePLRVHGLLQGDAGSKRVA-WLLERVGLLPEHAWRYPHeFSGGQRQRICIARALALNPKVIIADESVSALD 495
Cdd:cd03234 99 RETLTYTA--ILRLPRKSSDAIRKKRVEdVLLRDLALTRIGGNLVKG-ISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 949724212 496 VSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
340-556 |
2.44e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.00 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLaasklqPL----RRDIQFIFQDpyASLD 415
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL------PLharaRRGIGYLPQE--ASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 416 PRQTVGYSILEPLRVHGLLQGDAGSKRVAWLLERVGLlpEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADESVSAL 494
Cdd:PRK10895 91 RRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI--EHLRdSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 495 DvSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQ 556
Cdd:PRK10895 169 D-PISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
313-544 |
2.70e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.60 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 313 ILRVRNLVTRFPlrsGilnrvtreVHAVENVSFDLWPGETLSLVGESGCGKSTtgraLLRLVE------SQRGEIIFNGQ 386
Cdd:NF040905 1 ILEMRGITKTFP---G--------VKALDDVNLSVREGEIHALCGENGAGKST----LMKVLSgvyphgSYEGEILFDGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 387 --RIDTLAASKlqplRRDIQFIFQDpyASLDPRQTVGYSIL---EPLRvHGLLQGDAGSKRVAWLLERVGlLPEHawryP 461
Cdd:NF040905 66 vcRFKDIRDSE----ALGIVIIHQE--LALIPYLSIAENIFlgnERAK-RGVIDWNETNRRARELLAKVG-LDES----P 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 462 HEFSG----GQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLqRELGIAYLFISHDMAVVERISHRVAVM 537
Cdd:NF040905 134 DTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVL 212
|
....*..
gi 949724212 538 YLGQIVE 544
Cdd:NF040905 213 RDGRTIE 219
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
159-264 |
3.53e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 74.14 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 159 KAILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADR 238
Cdd:PRK11144 119 EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADR 198
|
90 100
....*....|....*....|....*..
gi 949724212 239 VLVMYQGEAVETGSVEQIFHAPQ-HPY 264
Cdd:PRK11144 199 VVVLEQGKVKAFGPLEEVWASSAmRPW 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
29-251 |
3.60e-14 |
|
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: 72.30 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAG---GEVSCDEMLLRRrnrqvielgEQSASQMRHVRGAD 105
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP---------DQFQKCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 106 IamifqepmtsLNPVFTVGEQIAESIRLhqgASHEEAMVEAKRMLDQVRIPEAKAILS---RYPHQLSGGMRQRVMIAMA 182
Cdd:cd03234 91 I----------LLPGLTVRETLTYTAIL---RLPRKSSDAIRKKRVEDVLLRDLALTRiggNLVKGISGGERRRVSIAVQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 183 LSCRPAVLIADEPTTALDVTIQaqiLQLIKVLQQDMSMGVIFIT--HDMGV-VADIADRVLVMYQGEAVETG 251
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTA---LNLVSTLSQLARRNRIVILtiHQPRSdLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
35-256 |
5.62e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.89 E-value: 5.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 35 LSFRLKRGETLAIVGESGSGKSvTALSLMHLIEQAGGEVSCDEMLLRrrnrqvielgEQSASQMRHVRGAdiaMIFQEPM 114
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKS-TLLARMAGLLPGSGSIQFAGQPLE----------AWSAAELARHRAY---LSQQQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 115 TSLNPVFtvgeqiaESIRLHQGASHEEAMVEA--KRMLDQVRIPEAkaiLSRYPHQLSGGMRQRVMIAMA-LSCRPAV-- 189
Cdd:PRK03695 81 PFAMPVF-------QYLTLHQPDKTRTEAVASalNEVAEALGLDDK---LGRSVNQLSGGEWQRVRLAAVvLQVWPDInp 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 190 ----LIADEPTTALDVTIQAQILQLIKVLQQdMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQI 256
Cdd:PRK03695 151 agqlLLLDEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
31-242 |
6.16e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 70.73 E-value: 6.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqAGgevscdemLLRrrnrqvielgeQSASQMRHVRGADIAMIF 110
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKS----TLLKVL--AG--------VLR-----------PTSGTVRRAGGARVAYVP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEpmTSLNPVF--TVGEQIAESIRLHQGAS-----HEEAMVEakRMLDQVRIpeaKAILSRYPHQLSGGMRQRVMIAMAL 183
Cdd:NF040873 62 QR--SEVPDSLplTVRDLVAMGRWARRGLWrrltrDDRAAVD--DALERVGL---ADLAGRQLGELSGGQRQRALLAQGL 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADiADRVLVM 242
Cdd:NF040873 135 AQEADLLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
323-505 |
8.65e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 74.36 E-value: 8.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 323 FPLRSGILNRVTREVH-------AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLaasK 395
Cdd:PRK10789 307 VPEGRGELDVNIRQFTypqtdhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---Q 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 396 LQPLRRDIQFIFQDPYASLDprqTVGYSIleplrvhGLLQGDAGSK------RVAWLLERVGLLPEHawrYPHE------ 463
Cdd:PRK10789 384 LDSWRSRLAVVSQTPFLFSD---TVANNI-------ALGRPDATQQeiehvaRLASVHDDILRLPQG---YDTEvgergv 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 949724212 464 -FSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQII-NL 505
Cdd:PRK10789 451 mLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILhNL 494
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-261 |
8.87e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.46 E-value: 8.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 19 NIAFEQEQQRVsaVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDE-----MLLRRRNRQVIELGEQ 93
Cdd:PRK10895 8 NLAKAYKGRRV--VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedislLPLHARARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 94 SASQMRHVrgadiamifqepmtslnpvfTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEAKAILSRyphQLSGGM 173
Cdd:PRK10895 86 EASIFRRL--------------------SVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQ---SLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSV 253
Cdd:PRK10895 143 RRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTP 221
|
....*...
gi 949724212 254 EQIFHAPQ 261
Cdd:PRK10895 222 TEILQDEH 229
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
340-546 |
1.10e-13 |
|
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: 70.25 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRL--VESQRGEIIFNGQriDTLAASKLQPLRRDIQFIFQdpyasldpr 417
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGE--DITDLPPEERARLGIFLAFQ--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 418 qtvgysilEPLRVHGLlqgdagskRVAWLLervgllpehawRYPHE-FSGGQRQRICIARALALNPKVIIADESVSALDV 496
Cdd:cd03217 85 --------YPPEIPGV--------KNADFL-----------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 949724212 497 -SIR--GQIINLMldlqRELGIAYLFISHDMAVVERI-SHRVAVMYLGQIVEIG 546
Cdd:cd03217 138 dALRlvAEVINKL----REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-255 |
1.19e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 73.69 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 6 ELDASDVLAVSNLNIAFEQEQQRVsavRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqAG------GEVSCDEml 79
Cdd:COG4178 356 ETSEDGALALEDLTLRTPDGRPLL---EDLSLSLKPGERLLITGPSGSGKS----TLLRAI--AGlwpygsGRIARPA-- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 80 lrrrnrqvielgeqsasqmrhvrGADIAMIFQEPMTslnPVFTVGEQIAesiRLHQGASHEEAmvEAKRMLDQVRIPEAK 159
Cdd:COG4178 425 -----------------------GARVLFLPQRPYL---PLGTLREALL---YPATAEAFSDA--ELREALEAVGLGHLA 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 160 AILS---RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlQQDMSMGVIFITHDmGVVADIA 236
Cdd:COG4178 474 ERLDeeaDWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR--EELPGTTVISVGHR-STLAAFH 550
|
250
....*....|....*....
gi 949724212 237 DRVLVMYQGEAVETGSVEQ 255
Cdd:COG4178 551 DRVLELTGDGSWQLLPAEA 569
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
35-260 |
1.37e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 71.36 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 35 LSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRN-----RQVIELGEQ--SASQMrhvrgadia 107
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSskafaRKVAYLPQQlpAAEGM--------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 108 mifqepmtslnpvfTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEAKAILSRYPHQLSGGMRQRVMIAMALSCRP 187
Cdd:PRK10575 101 --------------TVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 188 AVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAP 260
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
343-568 |
1.54e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 74.24 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 343 VSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdtlAASKLQPLRRDIQFIFQDPYASldpRQTVGY 422
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV---AKFGLTDLRRVLSIIPQSPVLF---SGTVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 423 SIlEPLRVHGllqgDAGskrvAW-LLERVGL----------LPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESV 491
Cdd:PLN03232 1329 NI-DPFSEHN----DAD----LWeALERAHIkdvidrnpfgLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 492 SALDVSIRGQIINLMLDLQRELGIayLFISHDMAVVERIShRVAVMYLGQIVEIGTRRAVFENPQHPYTRKLMAAVP 568
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIREEFKSCTM--LVIAHRLNTIIDCD-KILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGP 1473
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
30-259 |
1.62e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.07 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 30 SAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRQVIelgeqsasqmrhvrgadIAMI 109
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-----------------VAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 110 FQ-EPMTSLNPVFTvgEQIAESIR------LHQGASHEEAMVEAKrmLDQVRIPEAKailSRYPHQLSGGMRQRVMIAMA 182
Cdd:PRK15056 84 PQsEEVDWSFPVLV--EDVVMMGRyghmgwLRRAKKRDRQIVTAA--LARVDMVEFR---HRQIGELSGGQKKRVFLARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLqQDMSMGVIFITHDMGVVADIADRVlVMYQGEAVETGSVEQIFHA 259
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFTA 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
311-544 |
1.83e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.02 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPlrsgilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRI-- 388
Cdd:PRK11288 2 SPYLSFDGIGKTFP-----------GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrf 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 389 -DTLAAsklqpLRRDIQFIFQDpyASLDPRQTVGYSILE---PLRvHGLLQGDAGSKRVAWLLERVGLL--PEHAWRYph 462
Cdd:PRK11288 71 aSTTAA-----LAAGVAIIYQE--LHLVPEMTVAENLYLgqlPHK-GGIVNRRLLNYEAREQLEHLGVDidPDTPLKY-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 463 eFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:PRK11288 141 -LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
..
gi 949724212 543 VE 544
Cdd:PRK11288 219 VA 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
342-527 |
2.06e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.53 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 342 NVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQridtlaasklqpLRrdIQFIFQDPYasLDPRQtvg 421
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------LR--IGYVPQKLY--LDTTL--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 422 ysilePLRVHGLLQGDAGSKRVAWL--LERVGllPEHAWRYP-HEFSGGQRQRICIARALALNPKVIIADESVSALDVSI 498
Cdd:PRK09544 83 -----PLTVNRFLRLRPGTKKEDILpaLKRVQ--AGHLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....*....
gi 949724212 499 RGQIINLMLDLQRELGIAYLFISHDMAVV 527
Cdd:PRK09544 156 QVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
34-528 |
2.08e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.06 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 34 NLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqaGGEVSCDEMLLRRRNRQVIELGEQSASqmRHVRGAdiamifqep 113
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKS----TLMKIL---NGEVLLDDGRIIYEQDLIVARLQQDPP--RNVEGT--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 114 mtslnpVFT-----VGEQiAESIRLHQGASHEEAMVEAKRMLDQV-----------------RIPEAKAILSRYPHQ--- 168
Cdd:PRK11147 83 ------VYDfvaegIEEQ-AEYLKRYHDISHLVETDPSEKNLNELaklqeqldhhnlwqlenRINEVLAQLGLDPDAals 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 -LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlqqDMSMGVIFITHDMGVVADIADR-------VL 240
Cdd:PRK11147 156 sLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK----TFQGSIIFISHDRSFIRNMATRivdldrgKL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 241 VMYQGEavetgsveqifhapqhpYTKALLAAVPQL--GAMNGHELPRRFplislhdpshvePQTE---------QDTVVE 309
Cdd:PRK11147 232 VSYPGN-----------------YDQYLLEKEEALrvEELQNAEFDRKL------------AQEEvwirqgikaRRTRNE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 310 GepilRVRNLVTRFPLRSGILNRV----------TRE---VHAVENVSFDLwPGETL--------------SLVGESGCG 362
Cdd:PRK11147 283 G----RVRALKALRRERSERREVMgtakmqveeaSRSgkiVFEMENVNYQI-DGKQLvkdfsaqvqrgdkiALIGPNGCG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 363 KSTTGRALLRLVESQRGEIifngqRIDTlaasKLqplrrDIQFIfqDPY-ASLDPRQTVGYSILEplrvhgllqgdaGSK 441
Cdd:PRK11147 358 KTTLLKLMLGQLQADSGRI-----HCGT----KL-----EVAYF--DQHrAELDPEKTVMDNLAE------------GKQ 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 442 RVAwllerVGLLPEHAWRYPHEF--------------SGGQRQRICIARaLALNP-KVIIADESVSALDVSirgqiinlM 506
Cdd:PRK11147 410 EVM-----VNGRPRHVLGYLQDFlfhpkramtpvkalSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDVE--------T 475
|
570 580
....*....|....*....|....*.
gi 949724212 507 LDLQRELGIAY----LFISHDMAVVE 528
Cdd:PRK11147 476 LELLEELLDSYqgtvLLVSHDRQFVD 501
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-246 |
2.16e-13 |
|
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: 69.12 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQQRVSA--VRNLSFRLKRGETLAIVGESGSGKSvtalSLMH-LIEQAGGEVSCDEMLLRRRNRQVI 88
Cdd:cd03213 3 TLSFRNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKS----TLLNaLAGRRTGLGVSGEVLINGRPLDKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 89 ELGEQSASQMRHvrgaDIAMifqepmtslnPVFTVgeqiaesirlhqgashEEAMVEAKRMldqvripeakailsrypHQ 168
Cdd:cd03213 79 SFRKIIGYVPQD----DILH----------PTLTV----------------RETLMFAAKL-----------------RG 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQdMSMGVIFITHDM-GVVADIADRVLVMYQGE 246
Cdd:cd03213 112 LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPsSEIFELFDKLLLLSQGR 189
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
303-547 |
2.61e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 72.94 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 303 EQDTVVEGEPILRVRNLVTRFPlrsgilnrvTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEII 382
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYP---------DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 383 FNGQRIDTLAASKlqpLRRDIQFIFQDPY---ASL------------DPRQTVgysILEPLRVHGLLQGDAGSKrvAWLL 447
Cdd:PRK11160 399 LNGQPIADYSEAA---LRQAISVVSQRVHlfsATLrdnlllaapnasDEALIE---VLQQVGLEKLLEDDKGLN--AWLG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 448 E--RvgllpehawryphEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRelGIAYLFISHDMA 525
Cdd:PRK11160 471 EggR-------------QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLT 535
|
250 260
....*....|....*....|..
gi 949724212 526 VVERIShRVAVMYLGQIVEIGT 547
Cdd:PRK11160 536 GLEQFD-RICVMDNGQIIEQGT 556
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
330-528 |
3.45e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 330 LNRVTRevHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQridtlaasklqplrrDIQFifqd 409
Cdd:COG2401 38 LRVVER--YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVP---------------DNQF---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 410 pyasldPRQTvgySILEPLrvhgLLQGDAgsKRVAWLLERVGLLPEHAW-RYPHEFSGGQRQRICIARALALNPKVIIAD 488
Cdd:COG2401 97 ------GREA---SLIDAI----GRKGDF--KDAVELLNAVGLSDAVLWlRRFKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 949724212 489 ESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVE 528
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVID 201
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
33-259 |
3.97e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.02 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 33 RNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDemllrrrnrqvielGEQSASQMRHVRGADIAMIFQE 112
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLD--------------GEHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 113 PMTSLNpvFTVGEQIAESIRLHQG------ASHEEAMVEAKRMLDQVRIPEAKAilsrypHQLSGGMRQRVMIAMALSCR 186
Cdd:PRK10253 90 ATTPGD--ITVQELVARGRYPHQPlftrwrKEDEEAVTKAMQATGITHLADQSV------DTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 187 PAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHA 259
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-251 |
4.44e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 70.63 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 6 ELDASDVLAVSNLNIAF---EQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCdemllrr 82
Cdd:PRK13536 28 EAKASIPGSMSTVAIDLagvSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 83 rnrqvieLGEQSASQMRHVRgADIAMIFQepMTSLNPVFTVGEQIAESIRLHQGASHE-EAMVEAkrMLDQVRIpEAKAi 161
Cdd:PRK13536 101 -------LGVPVPARARLAR-ARIGVVPQ--FDNLDLEFTVRENLLVFGRYFGMSTREiEAVIPS--LLEFARL-ESKA- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 162 lSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQdMSMGVIFITHDMGVVADIADRVLV 241
Cdd:PRK13536 167 -DARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCV 244
|
250
....*....|
gi 949724212 242 MYQGEAVETG 251
Cdd:PRK13536 245 LEAGRKIAEG 254
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
314-495 |
5.18e-13 |
|
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: 67.96 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLvtRFPLRSGILNRVTREVHaveNVSFDLWPGETLSLVGESGCGKSTTGRAL--LRLVESQRGEIIFNGQRIDtl 391
Cdd:cd03213 4 LSFRNL--TVTVKSSPSKSGKQLLK---NVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 392 aaskLQPLRRDIQFIFQDPYasLDPRQTVgysiLEPLRVHGLLQGdagskrvawllervgllpehawrypheFSGGQRQR 471
Cdd:cd03213 77 ----KRSFRKIIGYVPQDDI--LHPTLTV----RETLMFAAKLRG---------------------------LSGGERKR 119
|
170 180
....*....|....*....|....
gi 949724212 472 ICIARALALNPKVIIADESVSALD 495
Cdd:cd03213 120 VSIALELVSNPSLLFLDEPTSGLD 143
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
34-260 |
6.03e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.80 E-value: 6.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 34 NLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqAGgevscdeMLLRRRNRQV--IELGEQSASQMRHvrgaDIAMIFQ 111
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKT----SLLNAL--LG-------FLPYQGSLKIngIELRELDPESWRK----HLSWVGQ 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 112 EPMTslnpvftVGEQIAESIRLHQGASHEEAMVEAkrmLDQVRIPEakaILSRYPH-----------QLSGGMRQRVMIA 180
Cdd:PRK11174 431 NPQL-------PHGTLRDNVLLGNPDASDEQLQQA---LENAWVSE---FLPLLPQgldtpigdqaaGLSVGQAQRLALA 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADIaDRVLVMYQGEAVETGSVEQIFHAP 260
Cdd:PRK11174 498 RALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQT--TLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
335-546 |
8.25e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 67.94 E-value: 8.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 335 REVHAVENVSFDLWPGETLSLVGESGCGKSTtgraLLRLV----ESQRGEIIFNGQRIDTLAASklqplrrdiqfifqdp 410
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKST----LLRLLagiyPPDSGTVTVRGRVSSLLGLG---------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 411 yASLDPRQTVGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLlpEHAWRYP-HEFSGGQRQRICIARALALNPKVIIADE 489
Cdd:cd03220 93 -GGFNPELTGRENIYLNGRLLGLSRKEI-DEKIDEIIEFSEL--GDFIDLPvKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 490 SVSALDVSIRGQIINLMLDLQRELGIAyLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLRELLKQGKTV-ILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
312-617 |
1.02e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 70.26 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 312 PILRVRNLVTRFPlrsgilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTL 391
Cdd:PRK09536 2 PMIDVSDLSVEFG-----------DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 392 AASKLQplrRDIQFIFQDPYASL--DPRQTVGYSiLEPLRVHGLLQGDAGSKRVAWLLERVGLlPEHAWRYPHEFSGGQR 469
Cdd:PRK09536 71 SARAAS---RRVASVPQDTSLSFefDVRQVVEMG-RTPHRSRFDTWTETDRAAVERAMERTGV-AQFADRPVTSLSGGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 470 QRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRR 549
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPA 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 550 AVFENPQHPYTRKLMAAVpVADPSHHRPQRVLLSDDIPS--------NIRKRGEEISPVSLQLVGPGHYV-ARPLPE 617
Cdd:PRK09536 225 DVLTADTLRAAFDARTAV-GTDPATGAPTVTPLPDPDRTeaaadtrvHVVGGGQPAARAVSRLVAAGASVsVGPVPE 300
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-255 |
1.14e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 70.62 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 19 NIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIEQAGgEVSCDEMLLRRRNrqvieLGEQSASQM 98
Cdd:PRK11160 343 NVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTRAW-DPQQGEILLNGQP-----IADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 99 RhvrgADIAMIFQEpmtslnpVFTVGEQIAESIRLHQGASHEEAMVEakrMLDQV---RIPEAKAILS-------RyphQ 168
Cdd:PRK11160 413 R----QAISVVSQR-------VHLFSATLRDNLLLAAPNASDEALIE---VLQQVgleKLLEDDKGLNawlgeggR---Q 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 LSGGMRQRVMIAMALsCRPA-VLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADIaDRVLVMYQGEA 247
Cdd:PRK11160 476 LSGGEQRRLGIARAL-LHDApLLLLDEPTEGLDAETERQILELLAEHAQNKT--VLMITHRLTGLEQF-DRICVMDNGQI 551
|
....*...
gi 949724212 248 VETGSVEQ 255
Cdd:PRK11160 552 IEQGTHQE 559
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
329-552 |
1.47e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.37 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 329 ILNRVT---REVH-AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQridtlaasklqPLRRDIQ 404
Cdd:PRK15056 8 VVNDVTvtwRNGHtALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ-----------PTRQALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 405 fifQDPYASLDPRQTVGYSIlePLRVH-----------GLLQGDAGSKR--VAWLLERVGLLpEHAWRYPHEFSGGQRQR 471
Cdd:PRK15056 77 ---KNLVAYVPQSEEVDWSF--PVLVEdvvmmgryghmGWLRRAKKRDRqiVTAALARVDMV-EFRHRQIGELSGGQKKR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 472 ICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHrVAVMYLGQIVEIGTRRAV 551
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETT 228
|
.
gi 949724212 552 F 552
Cdd:PRK15056 229 F 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-252 |
1.80e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 68.68 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 20 IAFEQEQQRVSA---VRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVS-CDEMLLRRrnrqvielgeqsa 95
Cdd:PRK13537 8 IDFRNVEKRYGDklvVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlCGEPVPSR------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 96 sqMRHVRgADIAMIFQepMTSLNPVFTVGEQIAESIRlHQGASHEEAMVEAKRMLDQVRIpEAKAilSRYPHQLSGGMRQ 175
Cdd:PRK13537 75 --ARHAR-QRVGVVPQ--FDNLDPDFTVRENLLVFGR-YFGLSAAAARALVPPLLEFAKL-ENKA--DAKVGELSGGMKR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqqdMSMG--VIFITHDMGVVADIADRVLVMYQGEAVETGS 252
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSL---LARGktILLTTHFMEEAERLCDRLCVIEEGRKIAEGA 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
335-495 |
2.82e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.06 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 335 REVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRidTLAASKLQPLRRDIQFIFQDP---- 410
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH--NLKDINLKWWRSKIGVVSQDPllfs 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 411 -------------------------------YASLDPRQTVGYS-------ILEPLRVHGLLQGDAG------------S 440
Cdd:PTZ00265 474 nsiknnikyslyslkdlealsnyynedgndsQENKNKRNSCRAKcagdlndMSNTTDSNELIEMRKNyqtikdsevvdvS 553
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 441 KRVAwLLERVGLLPEhawRY-------PHEFSGGQRQRICIARALALNPKVIIADESVSALD 495
Cdd:PTZ00265 554 KKVL-IHDFVSALPD---KYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
10-244 |
3.19e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.06 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 10 SDVLAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSVTAlslmhlieqaggevscdemllrrrnRQVIE 89
Cdd:PRK09544 2 TSLVSLENVSVSFGQRR----VLSDVSLELKPGKILTLLGPNGAGKSTLV-------------------------RVVLG 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 90 LGEQSASQMRHVRGADIAMIFQEpmTSLNPvfTVGEQIAESIRLHQGASHEEAMVEAKRMldqvripEAKAILSRYPHQL 169
Cdd:PRK09544 53 LVAPDEGVIKRNGKLRIGYVPQK--LYLDT--TLPLTVNRFLRLRPGTKKEDILPALKRV-------QAGHLIDAPMQKL 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQ 244
Cdd:PRK09544 122 SGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
343-556 |
3.49e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.81 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 343 VSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdtlAASKLQPLRRDIQFIFQDPY-------ASLD 415
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI---GAYGLRELRRQFSMIPQDPVlfdgtvrQNVD 1405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 416 PrqtvgysILEplrvhgllqgdAGSKRVAWLLERVGLLPehawRYPHE--------------FSGGQRQRICIARA-LAL 480
Cdd:PTZ00243 1406 P-------FLE-----------ASSAEVWAALELVGLRE----RVASEsegidsrvleggsnYSVGQRQLMCMARAlLKK 1463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 481 NPKVIIADESVSALDVSIRGQIINLMldlqRELGIAYLFIShdmavverISHR---VA------VMYLGQIVEIGTRRAV 551
Cdd:PTZ00243 1464 GSGFILMDEATANIDPALDRQIQATV----MSAFSAYTVIT--------IAHRlhtVAqydkiiVMDHGAVAEMGSPREL 1531
|
....*
gi 949724212 552 FENPQ 556
Cdd:PTZ00243 1532 VMNRQ 1536
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
145-536 |
4.55e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 145 EAKRMLDQVRIPEAKAILSRYPHQLSGGMRQRVMIAMALScRPA-VLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVI 223
Cdd:PRK13409 189 ERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALL-RDAdFYFFDEPTSYLDIRQRLNVARLIRELAEGKY--VL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 224 FITHDMGVVADIADRVLVMYqGEAvetgSVEQIFhapQHPYtkallaavpqlGAMNG------HELP------RRFPLI- 290
Cdd:PRK13409 266 VVEHDLAVLDYLADNVHIAY-GEP----GAYGVV---SKPK-----------GVRVGineylkGYLPeenmriRPEPIEf 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 291 SLHDPshvEPQTEQDTVVEGEPIlrVRNLVTrFPLrsgilnrvtrEVHAVEnvsfdLWPGETLSLVGESGCGKSTTGRAL 370
Cdd:PRK13409 327 EERPP---RDESERETLVEYPDL--TKKLGD-FSL----------EVEGGE-----IYEGEVIGIVGPNGIGKTTFAKLL 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 371 LRLVESQRGEIIFNgQRIdtlaASKLQPLRRDIQFIFQDPYASLDPRQTVGY---SILEPLRVHGLLQgdagsKRVAwll 447
Cdd:PRK13409 386 AGVLKPDEGEVDPE-LKI----SYKPQYIKPDYDGTVEDLLRSITDDLGSSYyksEIIKPLQLERLLD-----KNVK--- 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 448 ervgllpehawryphEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVV 527
Cdd:PRK13409 453 ---------------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMI 517
|
....*....
gi 949724212 528 ERISHRVAV 536
Cdd:PRK13409 518 DYISDRLMV 526
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
339-534 |
5.77e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 64.95 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIifngqRIDTLAASKLQPLRRDIqfifqDPYASLDPRQ 418
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----RRAGGARVAYVPQRSEV-----PDSLPLTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 419 TVGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSI 498
Cdd:NF040873 77 LVAMGRWARRGLWRRLTRDD-RAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 949724212 499 RGQIINLMLDLQRElGIAYLFISHDMAVVERISHRV 534
Cdd:NF040873 155 RERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
31-228 |
6.20e-12 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 68.16 E-value: 6.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDemllrrrnrqvielGEQSASQMRHVRGADIAMIF 110
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD--------------GVPVSSLDQDEVRRRVSVCA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEPMtslnpVFtvGEQIAESIRLHQG-ASHEEAMveakRMLDQVRIPEakaILSRYPH-----------QLSGGMRQRVM 178
Cdd:TIGR02868 416 QDAH-----LF--DTTVRENLRLARPdATDEELW----AALERVGLAD---WLRALPDgldtvlgeggaRLSGGERQRLA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 949724212 179 IAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvLQQDMSMGVIFITHD 228
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
32-227 |
6.73e-12 |
|
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: 64.10 E-value: 6.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 32 VRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEmllrrrnrqvielgeqsasqmrhvrGADIAMIFQ 111
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-------------------------GEDLLFLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 112 EPMTslnPVFTVGEQIAesirlhqgasheeamveakrmldqvripeakailsrYP--HQLSGGMRQRVMIAMALSCRPAV 189
Cdd:cd03223 72 RPYL---PLGTLREQLI------------------------------------YPwdDVLSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 949724212 190 LIADEPTTALDVTIQAQILQLIKvlqqDMSMGVIFITH 227
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
350-547 |
7.28e-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: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 350 GETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdtlAASKLQPLRRDIQFIFQDPY-------ASLDPRQTvgY 422
Cdd:TIGR00957 1312 GEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI---AKIGLHDLRFKITIIPQDPVlfsgslrMNLDPFSQ--Y 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 423 SileplrvhgllqgdagSKRVAWLLER------VGLLPEhawRYPHE-------FSGGQRQRICIARALALNPKVIIADE 489
Cdd:TIGR00957 1387 S----------------DEEVWWALELahlktfVSALPD---KLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDE 1447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 490 SVSALDVSIrGQIINLMLDLQRElGIAYLFISHDMAVVERIShRVAVMYLGQIVEIGT 547
Cdd:TIGR00957 1448 ATAAVDLET-DNLIQSTIRTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGA 1502
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
338-549 |
8.19e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.91 E-value: 8.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 338 HAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDtlaASKLQPLRRDIQFIFQDPyasldPR 417
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN---AENEKWVRSKVGLVFQDP-----DD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 418 QTVGYSILE-----PLRVHglLQGDAGSKRVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVS 492
Cdd:PRK13647 91 QVFSSTVWDdvafgPVNMG--LDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 493 ALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRR 549
Cdd:PRK13647 168 YLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-260 |
8.37e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 67.82 E-value: 8.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 21 AFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLMhlieQAGGEVSCDEMLLRRRNRQVIELGEQSASqmrh 100
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKS-TLLSLI----QRHFDVSEGDIRFHDIPLTKLQLDSWRSR---- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 101 vrgadIAMIFQEPmtslnpvFTVGEQIAESIRLHQGASHEEAMVEAKRML----DQVRIPEAkailsrYPHQ-------L 169
Cdd:PRK10789 391 -----LAVVSQTP-------FLFSDTVANNIALGRPDATQQEIEHVARLAsvhdDILRLPQG------YDTEvgergvmL 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADiADRVLVMYQGEAVE 249
Cdd:PRK10789 453 SGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRT--VIISAHRLSALTE-ASEILVMQHGHIAQ 529
|
250
....*....|.
gi 949724212 250 TGSVEQIFHAP 260
Cdd:PRK10789 530 RGNHDQLAQQS 540
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
311-548 |
9.50e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 9.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFPlrsgilnrvtrEVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDt 390
Cdd:PRK10762 2 QALLQLKGIDKAFP-----------GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 391 laasklqplrrdiqfiFQDPYASldprQTVGYSIL--------------------EPLRVHGLLQGDAGSKRVAWLLERV 450
Cdd:PRK10762 70 ----------------FNGPKSS----QEAGIGIIhqelnlipqltiaeniflgrEFVNRFGRIDWKKMYAEADKLLARL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 451 GLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRE-LGIAYlfISHDMAVVER 529
Cdd:PRK10762 130 NL-RFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQgRGIVY--ISHRLKEIFE 206
|
250
....*....|....*....
gi 949724212 530 ISHRVAVMYLGQIveIGTR 548
Cdd:PRK10762 207 ICDDVTVFRDGQF--IAER 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
341-551 |
1.17e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.39 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 341 ENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQplrRDIQFIFQDpyASLDPRQTV 420
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA---RRIGLLAQN--ATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 421 ------GYSILEPLRVHGLLQGDAGskrVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSAL 494
Cdd:PRK10253 99 qelvarGRYPHQPLFTRWRKEDEEA---VTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 495 DVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAV 551
Cdd:PRK10253 175 DISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-249 |
1.32e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.40 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 11 DVLAVSNLNIAFEQEQQrvsaVRNLSFRLKRGETLAIVGESGSGKSvTALS-LMHLIEQAGGEVscdemllrrrnrqviE 89
Cdd:COG0488 314 KVLELEGLSKSYGDKTL----LDDLSLRIDRGDRIGLIGPNGAGKS-TLLKlLAGELEPDSGTV---------------K 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 90 LGEqsasqmrhvrGADIAMIFQEpMTSLNPVFTVGEQIAesiRLHQGASHEEAMVEAKRML---DQVRipeaKAIlsryp 166
Cdd:COG0488 374 LGE----------TVKIGYFDQH-QEELDPDKTVLDELR---DGAPGGTEQEVRGYLGRFLfsgDDAF----KPV----- 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDV-TIQAqilqLIKVLqQDMSMGVIFITHDMGVVADIADRVLVMYQG 245
Cdd:COG0488 431 GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA----LEEAL-DDFPGTVLLVSHDRYFLDRVATRILEFEDG 505
|
....
gi 949724212 246 EAVE 249
Cdd:COG0488 506 GVRE 509
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
339-547 |
1.36e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.19 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLwPGETL--------------SLVGESGCGKSTTGRALLRLVESQRGEIIFNGQridTLAASKLQPLRRDIQ 404
Cdd:PRK10575 13 ALRNVSFRV-PGRTLlhplsltfpagkvtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQ---PLESWSSKAFARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 405 FIFQD-PYASldprqtvGYSILEPLRV-----HGLLQ--GDAGSKRVAWLLERVGLLPeHAWRYPHEFSGGQRQRICIAR 476
Cdd:PRK10575 89 YLPQQlPAAE-------GMTVRELVAIgrypwHGALGrfGAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 477 ALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGT 547
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
165-242 |
1.64e-11 |
|
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: 62.47 E-value: 1.64e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQdmsmGVIFITHDMGVVADIADRVLVM 242
Cdd:cd03221 67 YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIEL 140
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
12-255 |
2.45e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.29 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNiafeqeQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRN-RQVIEL 90
Cdd:PRK10982 250 ILEVRNLT------SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINH 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 91 GEQSASQMRHVRGadiamIFQEPMTSLNPVFTVGEQIAESIRLhqgASHEEAMVEAKRMLDQVRI--PEAKAILSryphQ 168
Cdd:PRK10982 324 GFALVTEERRSTG-----IYAYLDIGFNSLISNIRNYKNKVGL---LDNSRMKSDTQWVIDSMRVktPGHRTQIG----S 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRVLVMYQGEA- 247
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVa 470
|
250
....*....|
gi 949724212 248 --VETGSVEQ 255
Cdd:PRK10982 471 giVDTKTTTQ 480
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
340-551 |
2.79e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.95 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTtgraLL----RLVESQRGEIIFNGQRIDTLA----ASKLQPLRRDIQFIfqdpy 411
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKST----LLsmisRLLPPDSGEVLVDGLDVATTPsrelAKRLAILRQENHIN----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 412 ASLDPRQTVG-----YSileplrvHGLLqGDAGSKRVAWLLERVGLLP-EHawRYPHEFSGGQRQRICIARALALNPKVI 485
Cdd:COG4604 88 SRLTVRELVAfgrfpYS-------KGRL-TAEDREIIDEAIAYLDLEDlAD--RYLDELSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 486 IADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAV 551
Cdd:COG4604 158 LLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
325-554 |
3.53e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.88 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 325 LRSGILNRVTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRG-----EIIFNGQRIDTLAASKLQPL 399
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiELLGRTVQREGRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 400 RRDIQFIFQDpyASLDPRQTVGYSIL------EPL-RVHGLLQGDAGSKRVAWLLERVGLLpEHAWRYPHEFSGGQRQRI 472
Cdd:PRK09984 85 RANTGYIFQQ--FNLVNRLSVLENVLigalgsTPFwRTCFSWFTREQKQRALQALTRVGMV-HFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 473 CIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAvF 552
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ-F 240
|
..
gi 949724212 553 EN 554
Cdd:PRK09984 241 DN 242
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
34-288 |
4.00e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.02 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 34 NLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqaGGEVSCD--EMLLRRRNrqvieLGEQSASQMRHVRgADIAMIFQ 111
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKT----TLLRLI---GGQIAPDhgEILFDGEN-----IPAMSRSRLYTVR-KRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 112 EP--MTSLNPVFTVGEQIAESIRLHQGASHEEAMVEakrmLDQVRIPEAKAILsryPHQLSGGMRQRVMIAMALSCRPAV 189
Cdd:PRK11831 92 SGalFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMK----LEAVGLRGAAKLM---PSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 190 LIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIfHAPQHPYTKALL 269
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL-QANPDPRVRQFL 243
|
250
....*....|....*....
gi 949724212 270 AavpqlGAMNGhELPRRFP 288
Cdd:PRK11831 244 D-----GIADG-PVPFRYP 256
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
32-256 |
4.68e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.12 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 32 VRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDE-------MLLRRRnrqvieLGeqsasqmrhvrga 104
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGedithlpMHKRAR------LG------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 105 dIAMIFQEPmtSlnpVF---TVGEQIAeSIRLHQGASHEEAMVEAKRMLDQVRIpeaKAILSRYPHQLSGGMRQRVMIAM 181
Cdd:COG1137 80 -IGYLPQEA--S---IFrklTVEDNIL-AVLELRKLSKKEREERLEELLEEFGI---THLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 182 ALSCRPAVLIADEPTTALD---VT-IQAQILQLikvlqQDMSMGVIfIT-HDMGVVADIADRVLVMYQGEAVETGSVEQI 256
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDpiaVAdIQKIIRHL-----KERGIGVL-ITdHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
31-259 |
5.39e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 65.51 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGET--------------LAIVGESGSGKSVTALSLMHLIEQAGGEVSCDemllrrrNRQVIELGEQSAS 96
Cdd:PRK10790 342 DIDNVSFAYRDDNLvlqninlsvpsrgfVALVGHTGSGKSTLASLLMGYYPLTEGEIRLD-------GRPLSSLSHSVLR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 97 QmrhvrgaDIAMIFQEPMTSLNPVF---TVGEQIAESirlhqgasHEEAMVEAKRMLDQVR-IPEAkaILSRYPHQ---L 169
Cdd:PRK10790 415 Q-------GVAMVQQDPVVLADTFLanvTLGRDISEE--------QVWQALETVQLAELARsLPDG--LYTPLGEQgnnL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMgvIFITHDMGVVADiADRVLVMYQGEAVE 249
Cdd:PRK10790 478 SVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTL--VVIAHRLSTIVE-ADTILVLHRGQAVE 554
|
250
....*....|
gi 949724212 250 TGSVEQIFHA 259
Cdd:PRK10790 555 QGTHQQLLAA 564
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-258 |
5.54e-11 |
|
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: 62.28 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 10 SDVLAVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSvtaLSLMHLIEQAGGEVSCdemllrrrNRQVIE 89
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCS---TLLKALANRTEGNVSV--------EGDIHY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 90 LGEQSASQMRHVRGaDIAMIFQEpmTSLNPVFTVGEQIAESIRLhQGasheeamveakrmldqvripeakailSRYPHQL 169
Cdd:cd03233 70 NGIPYKEFAEKYPG-EIIYVSEE--DVHFPTLTVRETLDFALRC-KG--------------------------NEFVRGI 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVA-DIADRVLVMYQGeav 248
Cdd:cd03233 120 SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIyDLFDKVLVLYEG--- 196
|
250
....*....|
gi 949724212 249 etgsvEQIFH 258
Cdd:cd03233 197 -----RQIYY 201
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
314-554 |
5.88e-11 |
|
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: 63.39 E-value: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 314 LRVRNLVTRFplrSGILNRVTREVHAVENvsfdlwPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAa 393
Cdd:cd03288 20 IKIHDLCVRY---ENNLKPVLKHVKAYIK------PGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 394 skLQPLRRDIQFIFQDPYA-------SLDPRQTVGYSIL-EPLRVHGLlqgdagsKRVAWLLErvGLLPEHAWRYPHEFS 465
Cdd:cd03288 90 --LHTLRSRLSIILQDPILfsgsirfNLDPECKCTDDRLwEALEIAQL-------KNMVKSLP--GGLDAVVTEGGENFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 466 GGQRQRICIARALALNPKVIIADESVSALDVSIRgqiiNLmldLQRELGIAYLfishDMAVVErISHRVAVMYLGQIVEI 545
Cdd:cd03288 159 VGQRQLFCLARAFVRKSSILIMDEATASIDMATE----NI---LQKVVMTAFA----DRTVVT-IAHRVSTILDADLVLV 226
|
....*....
gi 949724212 546 GTRRAVFEN 554
Cdd:cd03288 227 LSRGILVEC 235
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
343-547 |
7.18e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.53 E-value: 7.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 343 VSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAaskLQPLRRDIQFIFQDPYASldpRQTVGY 422
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKVLGIIPQAPVLF---SGTVRF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 423 SiLEPLRVHgllqGDAGskrvAW-LLERVGL----------LPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESV 491
Cdd:PLN03130 1332 N-LDPFNEH----NDAD----LWeSLERAHLkdvirrnslgLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 492 SALDVSIRGQIinlmldlQRElgIAYLFISHDMAVverISHR---------VAVMYLGQIVEIGT 547
Cdd:PLN03130 1403 AAVDVRTDALI-------QKT--IREEFKSCTMLI---IAHRlntiidcdrILVLDAGRVVEFDT 1455
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
339-528 |
7.26e-11 |
|
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: 61.99 E-value: 7.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASklqpLRRDIQFIFQDPyaSLDPRQ 418
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE----PHENILYLGHLP--GLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 419 TVgysiLEPLRVHGLLQGDAgsKRVAW-LLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVS 497
Cdd:TIGR01189 89 SA----LENLHFWAAIHGGA--QRTIEdALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180 190
....*....|....*....|....*....|..
gi 949724212 498 IRGQIINLMLD-LQRElGIAYLFISHDMAVVE 528
Cdd:TIGR01189 162 GVALLAGLLRAhLARG-GIVLLTTHQDLGLVE 192
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-242 |
9.15e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.90 E-value: 9.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 3 HSDELDASD-VLAV-SNLNIAFEQEQQRVsaVRNLSFRLKRGETLAIVGESGSGKSVTalsLMHLIEQAGGEVSCDEMLL 80
Cdd:COG2401 17 YSSVLDLSErVAIVlEAFGVELRVVERYV--LRDLNLEIEPGEIVLIVGASGSGKSTL---LRLLAGALKGTPVAGCVDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 81 rrrnrQVIELGEQSAsqmrhvrgadiamifqepmtslnpvftvgeqIAESIrlhqgaSHEEAMVEAKRMLDQVRIPEAKA 160
Cdd:COG2401 92 -----PDNQFGREAS-------------------------------LIDAI------GRKGDFKDAVELLNAVGLSDAVL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 161 ILSRYPHqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiQAQILQL-IKVLQQDMSMGVIFITHDMGVVADIADRV 239
Cdd:COG2401 130 WLRRFKE-LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ-TAKRVARnLQKLARRAGITLVVATHHYDVIDDLQPDL 207
|
...
gi 949724212 240 LVM 242
Cdd:COG2401 208 LIF 210
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
340-522 |
1.61e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 64.00 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALlrlvesqrGEI--IFNGQRIdtlaasklQPLRRDIQFIFQDPYASL--- 414
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRIL--------GELwpVYGGRLT--------KPAKGKLFYVPQRPYMTLgtl 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 415 ----------DPRQTVGYS------ILEPLRVHGLLQGDAGSKRVA-WLlervgllpehawrypHEFSGGQRQRICIARA 477
Cdd:TIGR00954 532 rdqiiypdssEDMKRRGLSdkdleqILDNVQLTHILEREGGWSAVQdWM---------------DVLSGGEKQRIAMARL 596
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 949724212 478 LALNPKVIIADESVSALDVSIRGQIINLMldlqRELGIAYLFISH 522
Cdd:TIGR00954 597 FYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
340-544 |
1.84e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.93 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdtlaASKLQPLRRDIQFIFQdpYASLDPRQT 419
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLARARIGVVPQ--FDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 420 VGYSILEPLRVHGLLQGDAgSKRVAWLLERVGLLPEHAWRYPhEFSGGQRQRICIARALALNPKVIIADESVSALDVSIR 499
Cdd:PRK13536 131 VRENLLVFGRYFGMSTREI-EAVIPSLLEFARLESKADARVS-DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHAR 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 949724212 500 gqiiNLMLDLQREL---GIAYLFISHDMAVVERISHRVAVMYLG-QIVE 544
Cdd:PRK13536 209 ----HLIWERLRSLlarGKTILLTTHFMEEAERLCDRLCVLEAGrKIAE 253
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
332-557 |
1.99e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.77 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 332 RVTREVHAV-ENVSFDLWPGETLSLVGESGCGKSTTGRALL-RLVESQ-------RGEIIFNGQRIDTLAASKLQPLRRD 402
Cdd:PRK13547 8 HVARRHRAIlRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 403 IQFIFQDPYAsLDPRQTVGYSILEPLRVHGLLQGDAGSkrVAW-LLERVGLLPEHAwRYPHEFSGGQRQRICIARALA-- 479
Cdd:PRK13547 88 LPQAAQPAFA-FSAREIVLLGRYPHARRAGALTHRDGE--IAWqALALAGATALVG-RDVTTLSGGELARVQFARVLAql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 480 -------LNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVF 552
Cdd:PRK13547 164 wpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL 243
|
....*
gi 949724212 553 EnPQH 557
Cdd:PRK13547 244 T-PAH 247
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
315-568 |
3.21e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 63.14 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 315 RVRNLVTRFPLRSGILNrvtrevhaveNVSFDLWPGETLSLVGESGCGKSTTGRALlrlveSQR--------GEIIFNGQ 386
Cdd:TIGR00955 26 RLRGCFCRERPRKHLLK----------NVSGVAKPGELLAVMGSSGAGKTTLMNAL-----AFRspkgvkgsGSVLLNGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 387 RIDtlaaskLQPLRRDIQFIFQDP--YASLDPRQTVGYSILepLRVHGLLQGDAGSKRVAWLLERVGLLPEHAWRYPHE- 463
Cdd:TIGR00955 91 PID------AKEMRAISAYVQQDDlfIPTLTVREHLMFQAH--LRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPg 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 464 ----FSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAVMYL 539
Cdd:TIGR00955 163 rvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAE 242
|
250 260 270
....*....|....*....|....*....|.
gi 949724212 540 GQIVEIGTrravfenPQH--PYTRKLMAAVP 568
Cdd:TIGR00955 243 GRVAYLGS-------PDQavPFFSDLGHPCP 266
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
299-547 |
3.85e-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: 63.49 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 299 EPQTEQDTVVEGE-----------PILRVRNLVTRFPLRSGilnrvtrevHAVENVSFDLWPGETLSLVGESGCGKSTTG 367
Cdd:TIGR01257 1912 EPIFDEDDDVAEErqriisggnktDILRLNELTKVYSGTSS---------PAVDRLCVGVRPGECFGLLGVNGAGKTTTF 1982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 368 RALLRLVESQRGEIIFNGQRIDTLAASKLQPLRRDIQFIFQDPYasLDPRqtvgysilEPLRVHGLLQGDAGS--KRVA- 444
Cdd:TIGR01257 1983 KMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDL--LTGR--------EHLYLYARLRGVPAEeiEKVAn 2052
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 445 WLLERVGlLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDM 524
Cdd:TIGR01257 2053 WSIQSLG-LSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSM 2130
|
250 260
....*....|....*....|...
gi 949724212 525 AVVERISHRVAVMYLGQIVEIGT 547
Cdd:TIGR01257 2131 EECEALCTRLAIMVKGAFQCLGT 2153
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
12-255 |
4.36e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.80 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLRRRNRQvielg 91
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQRE----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 EQSASQMRHVRgADIAMIFQEpmTSLNPVFTVGEQIaesirLHQGASHEEAMVEAKRMLDQVRIPEAKAILSR-----YP 166
Cdd:PRK09984 75 GRLARDIRKSR-ANTGYIFQQ--FNLVNRLSVLENV-----LIGALGSTPFWRTCFSWFTREQKQRALQALTRvgmvhFA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 167 HQ----LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVM 242
Cdd:PRK09984 147 HQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL 226
|
250
....*....|...
gi 949724212 243 YQGEAVETGSVEQ 255
Cdd:PRK09984 227 RQGHVFYDGSSQQ 239
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
340-513 |
7.67e-10 |
|
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: 59.27 E-value: 7.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQPLRR-DIQFIFQDPY---ASLD 415
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRySVAYAAQKPWllnATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 416 PRQTVGySILEPLRVHGLLqgDAGSkrvawLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADESV 491
Cdd:cd03290 97 ENITFG-SPFNKQRYKAVT--DACS-----LQPDIDLLPFGDQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180
....*....|....*....|....*..
gi 949724212 492 SALDVSIRGQ-----IINLMLDLQREL 513
Cdd:cd03290 169 SALDIHLSDHlmqegILKFLQDDKRTL 195
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
32-254 |
8.16e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 58.69 E-value: 8.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 32 VRNLSFRLKRGETLAIVGESGSGKSVTALSLMHL--IEQAGGEvscdemllrrrnrqvIELGEQSASQM----RHVRGad 105
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGE---------------ILFKGEDITDLppeeRARLG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 106 IAMIFQEPmtslnpvftvgeqiaesirlhqgasheeamveakrmldqVRIPEAK-AILSRYPHQ-LSGGMRQRVMIAMAL 183
Cdd:cd03217 79 IFLAFQYP---------------------------------------PEIPGVKnADFLRYVNEgFSGGEKKRNEILQLL 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADI-ADRVLVMYQGEAVETGSVE 254
Cdd:cd03217 120 LLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKE 190
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
29-245 |
8.19e-10 |
|
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: 59.27 E-value: 8.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMLLrrrnrqvielGEQSASQMRHVRGADIAM 108
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNE----------SEPSFEATRSRNRYSVAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 109 IFQEPMTsLNPvfTVGEQIAESIRLHQgaSHEEAMVEAKRML---------DQVRIPEaKAIlsryphQLSGGMRQRVMI 179
Cdd:cd03290 84 AAQKPWL-LNA--TVEENITFGSPFNK--QRYKAVTDACSLQpdidllpfgDQTEIGE-RGI------NLSGGQRQRICV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 180 AMALSCRPAVLIADEPTTALDVTIQAQILQ--LIKVLQQDMSMgVIFITHDMGVVADiADRVLVMYQG 245
Cdd:cd03290 152 ARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRT-LVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
246-276 |
9.63e-10 |
|
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: 55.45 E-value: 9.63e-10
10 20 30
....*....|....*....|....*....|.
gi 949724212 246 EAVETGSVEQIFHAPQHPYTKALLAAVPQLG 276
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIK 31
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
12-234 |
1.07e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.66 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLniAFEQEQQRVsaVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLI----EQAGGEVS-CDEMLLRRR--- 83
Cdd:PRK13538 1 MLEARNL--ACERDERIL--FSGLSFTLNAGELVQIEGPNGAGKT----SLLRILaglaRPDAGEVLwQGEPIRRQRdey 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 84 NRQVIELGEQSAsqmrhvrgadiamifqepmtsLNPVFTVGEQIAESIRLHQGAShEEAMVEAkrmLDQVRipeakaiLS 163
Cdd:PRK13538 73 HQDLLYLGHQPG---------------------IKTELTALENLRFYQRLHGPGD-DEALWEA---LAQVG-------LA 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 164 RY---P-HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLikvLQQDMSMG--VIFITH-DMGVVAD 234
Cdd:PRK13538 121 GFedvPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEAL---LAQHAEQGgmVILTTHqDLPVASD 195
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
311-552 |
1.18e-09 |
|
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: 59.33 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNlVTrfplrsgilnrVTR-EVHAVENVSFDLWPGETLSLVGESGCGKSTtgraLLRLV-----ESQRGEIIFN 384
Cdd:COG1119 1 DPLLELRN-VT-----------VRRgGKTILDDISWTVKPGEHWAILGPNGAGKST----LLSLItgdlpPTYGNDVRLF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 385 GQRidtLAASKLQPLRRDIQFIFQDPYASLDPRQTV-------GYSILeplrvhGLLQ--GDAGSKRVAWLLERVGLLpE 455
Cdd:COG1119 65 GER---RGGEDVWELRKRIGLVSPALQLRFPRDETVldvvlsgFFDSI------GLYRepTDEQRERARELLELLGLA-H 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 456 HAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMA-VVERISHrV 534
Cdd:COG1119 135 LADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGITH-V 213
|
250
....*....|....*...
gi 949724212 535 AVMYLGQIVEIGTRRAVF 552
Cdd:COG1119 214 LLLKDGRVVAAGPKEEVL 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
342-547 |
1.25e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.01 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 342 NVSFDLWPGETLSLVGESGCGKSTTGRALLRLVeSQRGEIIFNGQRIDTLAaskLQPLRRDIQFIFQDPyaSLdPRQTVG 421
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELD---PESWRKHLSWVGQNP--QL-PHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 422 YSILeplrvhgLLQGDAGSKRV------AWLLERVGLLP--------EHAWRypheFSGGQRQRICIARALALNPKVIIA 487
Cdd:PRK11174 441 DNVL-------LGNPDASDEQLqqalenAWVSEFLPLLPqgldtpigDQAAG----LSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 488 DESVSALDVSIRGQIINLMLDLQRelGIAYLFISH---DMAVVERIshrvAVMYLGQIVEIGT 547
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHqleDLAQWDQI----WVMQDGQIVQQGD 566
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
159-536 |
1.46e-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: 60.95 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 159 KAILSRYPHQLSGGMRQRVMIAMALScRPA-VLIADEPTTALDVTIQAQILQLIKVLQQDMSMgVIFITHDMGVVADIAD 237
Cdd:COG1245 203 ENILDRDISELSGGELQRVAIAAALL-RDAdFYFFDEPSSYLDIYQRLNVARLIRELAEEGKY-VLVVEHDLAILDYLAD 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 238 RVLVMYqGEAVETGSVEQIfhapqhpytKALLAAVPQLgaMNGHeLP------RRFPLI-SLHDPShvepqteqdTVVEG 310
Cdd:COG1245 281 YVHILY-GEPGVYGVVSKP---------KSVRVGINQY--LDGY-LPeenvriRDEPIEfEVHAPR---------REKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 311 EPILRVRNLVTRFP-----LRSGILNRvtrevhavenvsfdlwpGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNg 385
Cdd:COG1245 339 ETLVEYPDLTKSYGgfsleVEGGEIRE-----------------GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED- 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 386 QRIdtlaASKLQPLRRDI-----QFIFQdpyASLDPRQTVGY--SILEPLRVHGLLQgdagsKRVAwllervgllpehaw 458
Cdd:COG1245 401 LKI----SYKPQYISPDYdgtveEFLRS---ANTDDFGSSYYktEIIKPLGLEKLLD-----KNVK-------------- 454
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 459 ryphEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERISHRVAV 536
Cdd:COG1245 455 ----DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
32-252 |
1.56e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.11 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 32 VRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMllrrrnrQVIELGeqsasqmRHVRGADIAMIFQ 111
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGL-------NIAKIG-------LHDLRFKITIIPQ 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 112 EPM-------TSLNPVFTVG-EQIAESIRLhqgaSHEEAMVEAkrMLDQVRIPEAKAilsryPHQLSGGMRQRVMIAMAL 183
Cdd:TIGR00957 1368 DPVlfsgslrMNLDPFSQYSdEEVWWALEL----AHLKTFVSA--LPDKLDHECAEG-----GENLSVGQRQLVCLARAL 1436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmgVIFITHDMGVVADIAdRVLVMYQGEAVETGS 252
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCT--VLTIAHRLNTIMDYT-RVIVLDKGEVAEFGA 1502
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
31-211 |
1.65e-09 |
|
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: 57.75 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqAGgevscdemlLRRRNRQVIELGEQSASQMRHVRGADIAMIF 110
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKT----TLLRIL--AG---------LLRPDSGEVRWNGTPLAEQRDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 111 QEPmtSLNPVFTVGEQIAESIRLHQGASHE-EAMVEAKRMLDQVRIPeakailsryPHQLSGGMRQRVMIAMALSCRPAV 189
Cdd:TIGR01189 80 HLP--GLKPELSALENLHFWAAIHGGAQRTiEDALAAVGLTGFEDLP---------AAQLSAGQQRRLALARLWLSRRPL 148
|
170 180
....*....|....*....|..
gi 949724212 190 LIADEPTTALDVTIQAQILQLI 211
Cdd:TIGR01189 149 WILDEPTTALDKAGVALLAGLL 170
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
13-246 |
2.16e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 57.48 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQQRVSAV-RNLSFRLKRGETLAIVGESGSGKSVTALSLMhlieqagGEvscdemlLRRRNRQVielg 91
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTlKDINLEVPKGELVAIVGPVGSGKSSLLSALL-------GE-------LEKLSGSV---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 92 eqsasqmrHVRGAdIAMIFQEPmtslnpvFTVGEQIAESIRLHQGASHE--EAMVEA-------KRM--LDQVRIPEaKA 160
Cdd:cd03250 63 --------SVPGS-IAYVSQEP-------WIQNGTIRENILFGKPFDEEryEKVIKAcalepdlEILpdGDLTEIGE-KG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 161 IlsryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQliKVLQQDMSMG--VIFITHDMGVVADiADR 238
Cdd:cd03250 126 I------NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFE--NCILGLLLNNktRILVTHQLQLLPH-ADQ 196
|
....*...
gi 949724212 239 VLVMYQGE 246
Cdd:cd03250 197 IVVLDNGR 204
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
138-256 |
2.64e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.36 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 138 SHEEAMVEAKRMLDQVRIPEAKAilsRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQD 217
Cdd:NF000106 117 SRKDARARADELLERFSLTEAAG---RAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD 193
|
90 100 110
....*....|....*....|....*....|....*....
gi 949724212 218 MSMgVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQI 256
Cdd:NF000106 194 GAT-VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
543-572 |
2.64e-09 |
|
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: 53.56 E-value: 2.64e-09
10 20 30
....*....|....*....|....*....|
gi 949724212 543 VEIGTRRAVFENPQHPYTRKLMAAVPVADP 572
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDP 30
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
292-547 |
3.42e-09 |
|
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: 60.41 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 292 LHDPSHvePQTEQDTVVEGE-----PILRVRNLVTRF-PLRSGILNRVtrevhaveNVSFdlWPGETLSLVGESGCGKST 365
Cdd:TIGR01257 904 MEDPEH--PEGINDSFFERElpglvPGVCVKNLVKIFePSGRPAVDRL--------NITF--YENQITAFLGHNGAGKTT 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 366 TGRALLRLVESQRGEIIFNGQRIDTlaasKLQPLRRDIQFIFQdpYASLDPRQTVGYSILEPLRVHGLLQGDAGSKRVAw 445
Cdd:TIGR01257 972 TLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQSLGMCPQ--HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEA- 1044
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 446 LLERVGLlpeHAWR--YPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRelGIAYLFISHD 523
Cdd:TIGR01257 1045 MLEDTGL---HHKRneEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHH 1119
|
250 260
....*....|....*....|....
gi 949724212 524 MAVVERISHRVAVMYLGQIVEIGT 547
Cdd:TIGR01257 1120 MDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
343-556 |
3.55e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 57.64 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 343 VSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQrGEIIFNGQRIDTLAASKLQplRRDIQFIFQDPYASLDPRqtvgY 422
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAWSAAELA--RHRAYLSQQQTPPFAMPV----F 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 423 SILEpLRVHGLLQGDAGSKRVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARAL-----ALNP--KVIIADESVSALD 495
Cdd:PRK03695 88 QYLT-LHQPDKTRTEAVASALNEVAEALGLDDKLG-RSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 949724212 496 VSIRG---QIINLMLdlqrELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFENPQ 556
Cdd:PRK03695 166 VAQQAaldRLLSELC----QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
32-262 |
4.15e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.91 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 32 VRNLSFRLKRGETLAIVGESGSGKSVtalslmhLIEQAGGEVSCDEMLLRRRNRQVIELGEQSASQMRHVRGADIAMIFQ 111
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKST-------LLKALAGDLTGGGAPRGARVTGDVTLNGEPLAAIDAPRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 112 EPMTSLNPvFTVGEQIAESIRLHQGASHEEAMVEAKRMLDQVRIPEAKAILSRYPHQLSGGMRQRVMIAMALS------- 184
Cdd:PRK13547 90 QAAQPAFA-FSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 185 --CRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFhAPQH 262
Cdd:PRK13547 169 aaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL-TPAH 247
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
34-228 |
5.24e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.03 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 34 NLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDemllrrrNRQVIELGEQSASQmrhvrgaDIAMIFQEP 113
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFE-------GEDISTLKPEIYRQ-------QVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 114 MtslnpVF--TVGEQIAESIRLHQGASHEEAMVeakRMLDQVRIPEAkaILSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
Cdd:PRK10247 91 T-----LFgdTVYDNLIFPWQIRNQQPDPAIFL---DDLERFALPDT--ILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 949724212 192 ADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHD 228
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-283 |
5.61e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.60 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 35 LSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEMllrrrnrQVIELGeqsASQMRHVrgadIAMIFQEPM 114
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDC-------DVAKFG---LTDLRRV----LSIIPQSPV 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 115 TSLNPVFTVGEQIAEsirlHQGASHEEAMVEAkrmldqvripEAKAILSRYPHQL-----------SGGMRQRVMIAMAL 183
Cdd:PLN03232 1321 LFSGTVRFNIDPFSE----HNDADLWEALERA----------HIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARAL 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 184 SCRPAVLIADEPTTALDVTIQAQILQLIKvlQQDMSMGVIFITHDMGVVADiADRVLVMYQGEAVETGSVEQIFHAPqhp 263
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIR--EEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD--- 1460
|
250 260
....*....|....*....|
gi 949724212 264 yTKALLAAVPQLGAMNGHEL 283
Cdd:PLN03232 1461 -TSAFFRMVHSTGPANAQYL 1479
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
13-254 |
6.36e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 57.00 E-value: 6.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMhlieqagG----EVSCDEMLLRRRNrqVI 88
Cdd:COG0396 1 LEIKNLHVSVEGKE----ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLM-------GhpkyEVTSGSILLDGED--IL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 89 ELG-EQSAsqmrhvrGADIAMIFQepmtslNPV----FTVGE--QIAESIRLHQGASHEEAMVEAKRMLDQVRIPEAkaI 161
Cdd:COG0396 68 ELSpDERA-------RAGIFLAFQ------YPVeipgVSVSNflRTALNARRGEELSAREFLKLLKEKMKELGLDED--F 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 162 LSRYPHQ-LSGGMRQRVMIAMALSCRPAVLIADEPTTALDV-TIQAQILQLIKVLQQDmsMGVIFITH-----DMGVvad 234
Cdd:COG0396 133 LDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIdALRIVAEGVNKLRSPD--RGILIITHyqrilDYIK--- 207
|
250 260
....*....|....*....|
gi 949724212 235 iADRVLVMYQGEAVETGSVE 254
Cdd:COG0396 208 -PDFVHVLVDGRIVKSGGKE 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
342-543 |
6.60e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 56.12 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 342 NVSFDLWPGETLSLVGESGCGKSTTGRALLRLVE---SQRGEIIFNGQRIDTLAasklQPLRRDIQFIFQDP--YASLDP 416
Cdd:cd03233 25 DFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIPYKEFA----EKYPGEIIYVSEEDvhFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 417 RQTVGYSIleplrvhgLLQGDAGSKRVawllervgllpehawryphefSGGQRQRICIARALALNPKVIIADESVSALDV 496
Cdd:cd03233 101 RETLDFAL--------RCKGNEFVRGI---------------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 949724212 497 SIRGQIINLMLDLQRELGIAyLFISHDMAVVErISH---RVAVMYLGQIV 543
Cdd:cd03233 152 STALEILKCIRTMADVLKTT-TFVSLYQASDE-IYDlfdKVLVLYEGRQI 199
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-261 |
7.16e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 57.03 E-value: 7.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 39 LKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVscdemllrrrnrqvielgeqsasqmrhvrGADIAMIFQEPMTsLN 118
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-----------------------------EIELDTVSYKPQY-IK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 119 PVF--TVGEQIAESIRLHQGASHEEAMVEAKRMLDQvripeakaILSRYPHQLSGGMRQRVMIAMALScRPA-VLIADEP 195
Cdd:cd03237 72 ADYegTVRDLLSSITKDFYTHPYFKTEIAKPLQIEQ--------ILDREVPELSGGELQRVAIAACLS-KDAdIYLLDEP 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 196 TTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVmYQGEAvetgSVEQIFHAPQ 261
Cdd:cd03237 143 SAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV-FEGEP----SVNGVANPPQ 203
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
541-590 |
1.01e-08 |
|
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: 52.75 E-value: 1.01e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 949724212 541 QIVEIGTRRAVFENPQHPYTRKLMAAVPVADpshhRPQRVLLSddIPSNI 590
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIK----KRDRKLIS--IPGEV 44
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
29-266 |
1.17e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.50 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 29 VSAVRNLSFRLKRGETLAIVGESGSGKSvTALSLM---------HLI---EQAGGEVSCDEMLLRRRNRQVIELGEQSAS 96
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKS-TVMSLLmrfydlkndHHIvfkNEHTNDMTNEQDYQGDEEQNVGMKNVNEFS 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 97 QMRHVRGADIAMIFQEP--------------MTSLNPVFTVGEQ--------IAESIRLhqgaSHEEAMVE-AKRMLDQV 153
Cdd:PTZ00265 1260 LTKEGGSGEDSTVFKNSgkilldgvdicdynLKDLRNLFSIVSQepmlfnmsIYENIKF----GKEDATREdVKRACKFA 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 154 RIPEAKAILSR--------YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFI 225
Cdd:PTZ00265 1336 AIDEFIESLPNkydtnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI 1415
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 949724212 226 TH--------DMGVVADIADRVLVMYQGEavetGSVEQIFHAPQHPYTK 266
Cdd:PTZ00265 1416 AHriasikrsDKIVVFNNPDRTGSFVQAH----GTHEELLSVQDGVYKK 1460
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
33-211 |
1.31e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.27 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 33 RNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEmllrrrnrQVIELGEqSASQMRHVRGADiAMifqe 112
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG--------GDIDDPD-VAEACHYLGHRN-AM---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 113 pmtslNPVFTVGEQIAESIRLHQGasHEEAMVEAkrmLDQVRIPEAKAILSRYphqLSGGMRQRVMIA-MALSCRPaVLI 191
Cdd:PRK13539 85 -----KPALTVAENLEFWAAFLGG--EELDIAAA---LEAVGLAPLAHLPFGY---LSAGQKRRVALArLLVSNRP-IWI 150
|
170 180
....*....|....*....|
gi 949724212 192 ADEPTTALDVTIQAQILQLI 211
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELI 170
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
35-239 |
1.46e-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: 55.19 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 35 LSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVScdemllrrrnrqvieLGEQSASQMRHVRGADIAMIFQEPm 114
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVL---------------LNGGPLDFQRDSIARGLLYLGHAP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 115 tSLNPVFTVGEQIAESIRLHQGASHEEAmveakrmLDQVRIpeaKAILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADE 194
Cdd:cd03231 83 -GIKTTLSVLENLRFWHADHSDEQVEEA-------LARVGL---NGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 949724212 195 PTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRV 239
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
341-532 |
1.47e-08 |
|
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: 53.99 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 341 ENVSFDLWPGETLSLVGESGCGKSTtgraLLRLVesqrgeiifngqridtlaASKLQPLRRDIQfifqdpyasLDPRQTV 420
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKST----LLKLI------------------AGELEPDEGIVT---------WGSTVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 421 GYsileplrvhgllqgdagskrvawllervgllpehawrYPHeFSGGQRQRICIARALALNPKVIIADESVSALDVSIRG 500
Cdd:cd03221 66 GY-------------------------------------FEQ-LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIE 107
|
170 180 190
....*....|....*....|....*....|....*.
gi 949724212 501 QIINLMLDLQRelgiAYLFISHDM----AVVERISH 532
Cdd:cd03221 108 ALEEALKEYPG----TVILVSHDRyfldQVATKIIE 139
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
312-547 |
1.49e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.80 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 312 PILRVRNLVTRfplrsgilnrvTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRAL-----LRLVEsqrGEIIFNGQ 386
Cdd:CHL00131 6 PILEIKNLHAS-----------VNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpaYKILE---GDILFKGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 387 RIDTLAASklQPLRRDIQFIFQDPY------------ASLDPRQT-VGYSILEPLRVHGLLQgdagSKrvawlLERVGLL 453
Cdd:CHL00131 72 SILDLEPE--ERAHLGIFLAFQYPIeipgvsnadflrLAYNSKRKfQGLPELDPLEFLEIIN----EK-----LKLVGMD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 454 PEHAWRYPHE-FSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQI---INLMLDLQRelgiAYLFISHDMAVVER 529
Cdd:CHL00131 141 PSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIaegINKLMTSEN----SIILITHYQRLLDY 216
|
250
....*....|....*....
gi 949724212 530 IS-HRVAVMYLGQIVEIGT 547
Cdd:CHL00131 217 IKpDYVHVMQNGKIIKTGD 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-252 |
1.50e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.10 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQQrvSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGevscdemllrrrnrQVIELGE 92
Cdd:TIGR01257 929 VCVKNLVKIFEPSGR--PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSG--------------TVLVGGK 992
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 93 QSASQMRHVRGAdIAMIFQEpmtslNPVF---TVGEQIAESIRLhQGASHEEAMVEAKRMLDQVRIPEAKailSRYPHQL 169
Cdd:TIGR01257 993 DIETNLDAVRQS-LGMCPQH-----NILFhhlTVAEHILFYAQL-KGRSWEEAQLEMEAMLEDTGLHHKR---NEEAQDL 1062
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVE 249
Cdd:TIGR01257 1063 SGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYC 1140
|
...
gi 949724212 250 TGS 252
Cdd:TIGR01257 1141 SGT 1143
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
304-553 |
2.01e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.42 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 304 QDTVVEGEpilRVRNLVTR---------FPLRSGilnRVtrevhAVENVSFDLWPGET--------------LSLVGESG 360
Cdd:PRK10790 309 QQAVVAGE---RVFELMDGprqqygnddRPLQSG---RI-----DIDNVSFAYRDDNLvlqninlsvpsrgfVALVGHTG 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 361 CGKSTTGRALLRLVESQRGEIIFNGQRIDTLAAsklQPLRRDIQFIFQDPY---ASLDPRQTVGYSILEplrvhgllqgd 437
Cdd:PRK10790 378 SGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SVLRQGVAMVQQDPVvlaDTFLANVTLGRDISE----------- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 438 agsKRVAWLLERVGL------LPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADESVSALDvSIRGQIINLML 507
Cdd:PRK10790 444 ---EQVWQALETVQLaelarsLPDGLYTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANID-SGTEQAIQQAL 519
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 508 DLQRElgiaylfisHDMAVVerISHRVA---------VMYLGQIVEIGTRRAVFE 553
Cdd:PRK10790 520 AAVRE---------HTTLVV--IAHRLStiveadtilVLHRGQAVEQGTHQQLLA 563
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
336-554 |
2.31e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.27 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 EVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLqpLRRDIQFIFQDpyASLD 415
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI--MREAVAIVPEG--RRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 416 PRQTVGysilEPLRVHGLL-QGDAGSKRVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSAL 494
Cdd:PRK11614 93 SRMTVE----ENLAMGGFFaERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 495 DVSIRGQIINLMLDLqRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFEN 554
Cdd:PRK11614 169 APIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-261 |
2.84e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 32 VRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVscdemllRRRNRQVIELGeqsasqMRHVRgADIAMIFQ 111
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEI-------RVNGREIGAYG------LRELR-RQFSMIPQ 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 112 EPMtslnpVF--TVGEQIAESIRlhqgASHEE--AMVEAKRMLDQVrIPEAKAILSRYPH---QLSGGMRQRVMIAMALS 184
Cdd:PTZ00243 1392 DPV-----LFdgTVRQNVDPFLE----ASSAEvwAALELVGLRERV-ASESEGIDSRVLEggsNYSVGQRQLMCMARALL 1461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 185 CRPAVLI-ADEPTT----ALDVTIQAQILQLIKvlqqdmSMGVIFITHDMGVVADIaDRVLVMYQGEAVETGSVEQIFHA 259
Cdd:PTZ00243 1462 KKGSGFIlMDEATAnidpALDRQIQATVMSAFS------AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMN 1534
|
..
gi 949724212 260 PQ 261
Cdd:PTZ00243 1535 RQ 1536
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
341-528 |
2.90e-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: 54.42 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 341 ENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQPLRrdiqfifqdpYASLDPRQTV 420
Cdd:cd03231 17 SGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLL----------YLGHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 421 GYSILEPLRVHGLLQGDAGskrVAWLLERVGLLP-EHawRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIR 499
Cdd:cd03231 87 TLSVLENLRFWHADHSDEQ---VEEALARVGLNGfED--RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|....*....
gi 949724212 500 GQIINLMLDLQRELGIAYLFISHDMAVVE 528
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTHQDLGLSE 190
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
341-506 |
3.08e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.11 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 341 ENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDtlaasklqplrrDIQFIFQDPYAS----LDP 416
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID------------DPDVAEACHYLGhrnaMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 417 RQTVgysiLEPLRVHGLLQGDAGSkRVAWLLERVGLLP-EHawRYPHEFSGGQRQRICIARALALNPKVIIADESVSALD 495
Cdd:PRK13539 87 ALTV----AENLEFWAAFLGGEEL-DIAAALEAVGLAPlAH--LPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170
....*....|.
gi 949724212 496 VSIRGQIINLM 506
Cdd:PRK13539 160 AAAVALFAELI 170
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
341-541 |
3.53e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.04 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 341 ENVSFDLWPGETLSLVGESGCGKSTtgraLLR----LVESQRGEIIFNGQRIDTLAASklqpLRRDIQFIFQdpYASLDP 416
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTS----LLRilagLARPDAGEVLWQGEPIRRQRDE----YHQDLLYLGH--QPGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 417 RQTVgysiLEPLRVHGLLQGDAGSKRVAWLLERVGLLP-EHAwryP-HEFSGGQRQRICIARALALNPKVIIADESVSAL 494
Cdd:PRK13538 88 ELTA----LENLRFYQRLHGPGDDEALWEALAQVGLAGfEDV---PvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 949724212 495 DVSIRGQIINLMLDLQRELGIAYLFISHDMavvERISHRVAVMYLGQ 541
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGMVILTTHQDL---PVASDKVRKLRLGQ 204
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
349-497 |
4.25e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.43 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 349 PGETLSLVGESGCGKSTTGRALLRLVESQ--RGEIIFNGQRIDtlaasklQPLRRDIQFIFQDP--YASLDPRQTVGYSI 424
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPT-------KQILKRTGFVTQDDilYPHLTVRETLVFCS 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 425 LepLRVHGLLQGDAGSKRVAWLLERVGLLPEHAWRYPHEF----SGGQRQRICIARALALNPKVIIADESVSALDVS 497
Cdd:PLN03211 166 L--LRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
11-260 |
4.48e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.58 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 11 DVLAVSNLNIAFEQEQQR-VSAVRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIEQ--------------------- 68
Cdd:PTZ00265 379 DIKKIQFKNVRFHYDTRKdVEIYKDLNFTLTEGKTYAFVGESGCGKS----TILKLIERlydptegdiiindshnlkdin 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 69 ------AGGEVSCDEMLLRRRNRQVI---------------ELGE-----QSASQMRHVRGADIAMIFQEPMTSlnpvfT 122
Cdd:PTZ00265 455 lkwwrsKIGVVSQDPLLFSNSIKNNIkyslyslkdlealsnYYNEdgndsQENKNKRNSCRAKCAGDLNDMSNT-----T 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 123 VGEQIAESIRLHQGASHEEAMVEAKRML--DQVR-IPEA-KAILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTA 198
Cdd:PTZ00265 530 DSNELIEMRKNYQTIKDSEVVDVSKKVLihDFVSaLPDKyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSS 609
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 199 LDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVAdIADRVLVMYQGEAVETGSVEQIFHAP 260
Cdd:PTZ00265 610 LDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIR-YANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
34-531 |
4.75e-08 |
|
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: 56.10 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 34 NLSFRlkRGETLAIVGESGSGKSvTALSLMHLIEQA-GGEVSCDE-----MLLRR----RNRQVIELGEQSASQMRHV-- 101
Cdd:TIGR03719 25 SLSFF--PGAKIGVLGLNGAGKS-TLLRIMAGVDKDfNGEARPQPgikvgYLPQEpqldPTKTVRENVEEGVAEIKDAld 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 102 RGADIAMIFQEPMTSLNPVFTVGEQIAESIRlHQGASHEEAMVEakRMLDQVRIPEAKAILSRyphqLSGGMRQRVMIAM 181
Cdd:TIGR03719 102 RFNEISAKYAEPDADFDKLAAEQAELQEIID-AADAWDLDSQLE--IAMDALRCPPWDADVTK----LSGGERRRVALCR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIkvlqQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVE-----TGSVEQ- 255
Cdd:TIGR03719 175 LLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPwegnySSWLEQk 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 256 ------------------------IFHAP--QHPYTKALLAAVPQlgaMNGHELPRRFPLISLHDPshVEPQTeqdtvve 309
Cdd:TIGR03719 251 qkrleqeekeesarqktlkrelewVRQSPkgRQAKSKARLARYEE---LLSQEFQKRNETAEIYIP--PGPRL------- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 310 GEPILRVRNLVTRFPLRsgILnrvtrevhaVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNgqriD 389
Cdd:TIGR03719 319 GDKVIEAENLTKAFGDK--LL---------IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG----E 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 390 TLAASKLQPLRrdiqfifqdpyASLDPRQTVGYSILEplrvhGLLQGDAGSKRV---AWL----------LERVGLLpeh 456
Cdd:TIGR03719 384 TVKLAYVDQSR-----------DALDPNKTVWEEISG-----GLDIIKLGKREIpsrAYVgrfnfkgsdqQKKVGQL--- 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 457 awryphefSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQrelGIAyLFISHDMAVVERIS 531
Cdd:TIGR03719 445 --------SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFA---GCA-VVISHDRWFLDRIA 507
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
248-277 |
6.18e-08 |
|
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: 49.71 E-value: 6.18e-08
10 20 30
....*....|....*....|....*....|
gi 949724212 248 VETGSVEQIFHAPQHPYTKALLAAVPQLGA 277
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDP 30
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
170-523 |
6.26e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.56 E-value: 6.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiqaQILQLIKVLqQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVE 249
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWL-KSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 250 -TGSV----------------------EQIFHApQHPYTKALLAAVPQLGAMNGHELPRRFPLISlhdPSHV-------- 298
Cdd:PRK10636 227 yTGNYssfevqratrlaqqqamyesqqERVAHL-QSYIDRFRAKATKAKQAQSRIKMLERMELIA---PAHVdnpfhfsf 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 299 -EPQTEQDtvvegePILRVRNlvtrfpLRSGILNRVTrevhaVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQ 377
Cdd:PRK10636 303 rAPESLPN------PLLKMEK------VSAGYGDRII-----LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPV 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 378 RGEI-IFNGQRIDTLAASKLQPLRRD---IQFIfqdpyASLDPRQTVgysilEPLR--VHGL-LQGDagskRVAWLLERv 450
Cdd:PRK10636 366 SGEIgLAKGIKLGYFAQHQLEFLRADespLQHL-----ARLAPQELE-----QKLRdyLGGFgFQGD----KVTEETRR- 430
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 451 gllpehawrypheFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRelgiAYLFISHD 523
Cdd:PRK10636 431 -------------FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHD 486
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
41-246 |
7.06e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.99 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 41 RGETLAIVGESGSGKSVTALSLMHLIEQAGGEVscdemllrrrnrqvielgeqsasqmrhvrgadiamifqepmtslnpv 120
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV----------------------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 121 ftvgeqiaesirlhqgasheeAMVEAKRMLDQVRIPEAKAILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALD 200
Cdd:smart00382 34 ---------------------IYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLD 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 201 VTIQAQILQLI-----KVLQQDMSMGVIFITHDM-----GVVADIADRVLVMYQGE 246
Cdd:smart00382 93 AEQEALLLLLEelrllLLLKSEKNLTVILTTNDEkdlgpALLRRRFDRRIVLLLIL 148
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
460-536 |
7.35e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 7.35e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 460 YPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERiSHRVAV 536
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1430
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
316-507 |
1.11e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 53.70 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 316 VRNLVTRFplrsgilnrvTREVHAV-ENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQrGEIIFNGQRIDTLAas 394
Cdd:cd03289 5 VKDLTAKY----------TEGGNAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVP-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 395 kLQPLRRDIQ------FIFQDPY-ASLDPRQTvgYSILEPLRVhgllQGDAGSKRVA--------WLLERVGLLPEHawr 459
Cdd:cd03289 72 -LQKWRKAFGvipqkvFIFSGTFrKNLDPYGK--WSDEEIWKV----AEEVGLKSVIeqfpgqldFVLVDGGCVLSH--- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 949724212 460 yphefsgGQRQRICIARALALNPKVIIADESVSALDvSIRGQIINLML 507
Cdd:cd03289 142 -------GHKQLMCLARSVLSKAKILLLDEPSAHLD-PITYQVIRKTL 181
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
298-553 |
1.29e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.95 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 298 VEPQT-EQDTVVEGEPilrvrNLVTrfpLRSGILNRVTREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVES 376
Cdd:TIGR00957 619 LEPDSiERRTIKPGEG-----NSIT---VHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 377 QRGEIIFNGQRIDTLAASKLQ--PLRRDIQFIFQdpyasldprqtvgysiLEPLRVHGLLQGDAgskrvawLLERVGLLP 454
Cdd:TIGR00957 691 VEGHVHMKGSVAYVPQQAWIQndSLRENILFGKA----------------LNEKYYQQVLEACA-------LLPDLEILP 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 455 EHAWRYPHE----FSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQREL-GIAYLFISHDMAVVER 529
Cdd:TIGR00957 748 SGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHGISYLPQ 827
|
250 260
....*....|....*....|....
gi 949724212 530 ISHrVAVMYLGQIVEIGTRRAVFE 553
Cdd:TIGR00957 828 VDV-IIVMSGGKISEMGSYQELLQ 850
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
42-251 |
1.47e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.50 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 42 GETLAIVGESGSGKSVTALSLMHLIEQAG--GEVSCDEmllRRRNRQVIElgeqsasqmrhvrgaDIAMIFQEPMtsLNP 119
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANN---RKPTKQILK---------------RTGFVTQDDI--LYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 120 VFTVGEQI--AESIRLHQGASHEEAMVEAKRMLDQVRIP--EAKAILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEP 195
Cdd:PLN03211 154 HLTVRETLvfCSLLRLPKSLTKQEKILVAESVISELGLTkcENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 196 TTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYQGEAVETG 251
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
340-522 |
1.77e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.87 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQplrrdiQFIFQDPYASLDPRQT 419
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQK------QLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 420 vgysilepLRVHGL--LQGDAGSKRVAWLLERVGLlpEHAWRYP-HEFSGGQRQRICIARALALNPKVIIADESVSALDv 496
Cdd:PRK13540 91 --------LRENCLydIHFSPGAVGITELCRLFSL--EHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD- 159
|
170 180
....*....|....*....|....*.
gi 949724212 497 SIRGQIINLMLDLQRELGIAYLFISH 522
Cdd:PRK13540 160 ELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
339-550 |
3.20e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.44 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 339 AVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDtlaASKLQPLRRDIQFIFQDpyasldprq 418
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYRKLFSAVFTD--------- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 419 tvgysileplrVH--GLLQGDAG----SKRVAWLLERVGL---LPEHAWRYPH-EFSGGQRQRICIARALALNPKVIIAD 488
Cdd:PRK10522 406 -----------FHlfDQLLGPEGkpanPALVEKWLERLKMahkLELEDGRISNlKLSKGQKKRLALLLALAEERDILLLD 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 489 ESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDMAVVERiSHRVAVMYLGQIVEI-GTRRA 550
Cdd:PRK10522 475 EWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSELtGEERD 536
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
12-248 |
7.47e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.10 E-value: 7.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQQRVsAVRNLSFRLKRGETLAIVGESGSGKSVTALSLM-----HLIeqaGGEVSCDEMLLRRRN-R 85
Cdd:NF040905 257 VFEVKNWTVYHPLHPERK-VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrsygRNI---SGTVFKDGKEVDVSTvS 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 86 QVIELGEQSASQMRHVRGadiamifqepmtsLNpvftVGEQIAESIRL--HQGAS-------HEEAMVeAKRMLDQVRIP 156
Cdd:NF040905 333 DAIDAGLAYVTEDRKGYG-------------LN----LIDDIKRNITLanLGKVSrrgvideNEEIKV-AEEYRKKMNIK 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 157 ----EAKAIlsryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqQDMSMGVIFITHDMGVV 232
Cdd:NF040905 395 tpsvFQKVG------NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINEL-AAEGKGVIVISSELPEL 467
|
250
....*....|....*.
gi 949724212 233 ADIADRVLVMYQGEAV 248
Cdd:NF040905 468 LGMCDRIYVMNEGRIT 483
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
141-243 |
9.08e-07 |
|
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: 49.28 E-value: 9.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 141 EAMVEAKRMLDQVRIPEAKAILSRYP--HQLSGGMRQRVMIAMAL---SCRPAVLIA-DEPTTALDVTIQAQILQLIKVL 214
Cdd:cd03227 48 AQSATRRRSGVKAGCIVAAVSAELIFtrLQLSGGEKELSALALILalaSLKPRPLYIlDEIDRGLDPRDGQALAEAILEH 127
|
90 100
....*....|....*....|....*....
gi 949724212 215 QQDMSMgVIFITHDMGvVADIADRVLVMY 243
Cdd:cd03227 128 LVKGAQ-VIVITHLPE-LAELADKLIHIK 154
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
341-543 |
9.72e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 9.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 341 ENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQridtLAASKLQplrrdiqfifQDPyasldPRQTV 420
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQD----LIVARLQ----------QDP-----PRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 421 G------------------------------YS---------ILEPLRVHGLLQGDAgskRVAWLLERVGLLPEHAWRyp 461
Cdd:PRK11147 81 GtvydfvaegieeqaeylkryhdishlvetdPSeknlnelakLQEQLDHHNLWQLEN---RINEVLAQLGLDPDAALS-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 462 hEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRelgiAYLFISHDMAVVERISHRVAVMYLGQ 541
Cdd:PRK11147 156 -SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGK 230
|
..
gi 949724212 542 IV 543
Cdd:PRK11147 231 LV 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
340-503 |
1.04e-06 |
|
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: 52.22 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 340 VENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVeSQRGEIIFNGQRIDTLAaskLQPLRRDIQ------FIFQDPY-A 412
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVT---LQTWRKAFGvipqkvFIFSGTFrK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 413 SLDPRQTvgYSILEPLRVhgllQGDAGSKRVA--------WLLERVGLLpehawrypheFSGGQRQRICIARALALNPKV 484
Cdd:TIGR01271 1311 NLDPYEQ--WSDEEIWKV----AEEVGLKSVIeqfpdkldFVLVDGGYV----------LSNGHKQLMCLARSILSKAKI 1374
|
170
....*....|....*....
gi 949724212 485 IIADESVSALDvSIRGQII 503
Cdd:TIGR01271 1375 LLLDEPSAHLD-PVTLQII 1392
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
32-256 |
1.13e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 50.63 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 32 VRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIEqagGEVSCDEMLLRRRNRqvIELGEQSASQMrhvrgadiamifq 111
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKT----SLLMLIL---GELEPSEGKIKHSGR--ISFSSQFSWIM------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 112 ePMTslnpvftvgeqIAESIRLhqGASHEE----AMVEAKRM-LDQVRIPEA-KAILSRYPHQLSGGMRQRVMIAMALSC 185
Cdd:cd03291 111 -PGT-----------IKENIIF--GVSYDEyrykSVVKACQLeEDITKFPEKdNTVLGEGGITLSGGQRARISLARAVYK 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 186 RPAVLIADEPTTALDVTIQAQILQ--LIKVLQQDMSmgvIFITHDMGVVAdIADRVLVMYQGEAVETGSVEQI 256
Cdd:cd03291 177 DADLYLLDSPFGYLDVFTEKEIFEscVCKLMANKTR---ILVTSKMEHLK-KADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
157-243 |
1.17e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.44 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 157 EAKAILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIA 236
Cdd:cd03236 128 ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLS 206
|
....*..
gi 949724212 237 DRVLVMY 243
Cdd:cd03236 207 DYIHCLY 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
161-246 |
1.26e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 161 ILSRYPHQLSGGMRQRVMIAMALScRPAVL-IADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRV 239
Cdd:PRK13409 446 LLDKNVKDLSGGELQRVAIAACLS-RDADLyLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRL 524
|
....*..
gi 949724212 240 LVmYQGE 246
Cdd:PRK13409 525 MV-FEGE 530
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-240 |
1.34e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEmllrrrNRQVIELGE 92
Cdd:PRK15064 320 LEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSE------NANIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 93 QSASQmrhvrgadiamiFQEPMTslnpVFtvgeqiaESIRLHQGASHEEAMVEAK--RML---DQVRIPeAKAilsryph 167
Cdd:PRK15064 390 DHAYD------------FENDLT----LF-------DWMSQWRQEGDDEQAVRGTlgRLLfsqDDIKKS-VKV------- 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 168 qLSGGMRQRVMIAMALSCRPAVLIADEPTTALDV-TIQAQILQLikvlqqDMSMG-VIFITHDMGVVADIADRVL 240
Cdd:PRK15064 439 -LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMeSIESLNMAL------EKYEGtLIFVSHDREFVSSLATRII 506
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
342-495 |
2.00e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 48.78 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 342 NVSFDLWPGETLSLVGESGCGKSTtgraLLRlVESQR-------GEIIFNGQRIDtlaasklQPLRRDIQFIFQDPyaSL 414
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTT----LLD-VLAGRktagvitGEILINGRPLD-------KNFQRSTGYVEQQD--VH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 415 DPRQTVgysiLEPLRVHGLLQGdagskrvawllervgllpehawrypheFSGGQRQRICIARALALNPKVIIADESVSAL 494
Cdd:cd03232 91 SPNLTV----REALRFSALLRG---------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGL 139
|
.
gi 949724212 495 D 495
Cdd:cd03232 140 D 140
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
35-256 |
2.61e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.89 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 35 LSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDEmllrrrnrqvIELGEQSASQMRHVRGadiaMIFQepm 114
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG----------CDISKFGLMDLRKVLG----IIPQ--- 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 115 tslNPVFTVGeqiaeSIRL-------HQGASHEEAMvEAKRMLDQVRIPEA--KAILSRYPHQLSGGMRQRVMIAMALSC 185
Cdd:PLN03130 1321 ---APVLFSG-----TVRFnldpfneHNDADLWESL-ERAHLKDVIRRNSLglDAEVSEAGENFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 186 RPAVLIADEPTTALDVTIQAQILQLIKvlQQDMSMGVIFITHDMGVVADiADRVLVMYQGEAVETGSVEQI 256
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTIR--EEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENL 1459
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
341-504 |
2.69e-06 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 48.62 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 341 ENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGqridTLAASKLQP------LRRDIqfIFQDPYasl 414
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG----SIAYVSQEPwiqngtIRENI--LFGKPF--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 415 DP---RQTVGYSILEP-LRVhgLLQGDA---GSKRVAwllervgllpehawrypheFSGGQRQRICIARALALNPKVIIA 487
Cdd:cd03250 93 DEeryEKVIKACALEPdLEI--LPDGDLteiGEKGIN-------------------LSGGQKQRISLARAVYSDADIYLL 151
|
170
....*....|....*..
gi 949724212 488 DESVSALDVSIRGQIIN 504
Cdd:cd03250 152 DDPLSAVDAHVGRHIFE 168
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
336-546 |
3.15e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.73 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 EVHAVENVSFDLWPGETLSLVGESGCGKSTtGRALLRLVESQRGEiifNGQRIDTLAASKlQPLRRDIqfifqDPYASLD 415
Cdd:NF000106 25 EVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGR---RPWRF*TWCANR-RALRRTI-----G*HRPVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 416 PRQTVGYSILEPLRVHG----LLQGDAGSkRVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESV 491
Cdd:NF000106 95 *GRRESFSGRENLYMIGr*ldLSRKDARA-RADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 492 SALDVSIRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
344-587 |
3.73e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 344 SFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQPLRRDIqfiFQDPYASL------DPR 417
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDE---WQRNNTDMlspgedDTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 418 QTVGYSILEPLRVHGLLQGDAGSKRVAWLLERvgllpehawRYPHeFSGGQRQRICIARALALNPKVIIADESVSALDVS 497
Cdd:PRK10938 100 RTTAEIIQDEVKDPARCEQLAQQFGITALLDR---------RFKY-LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 498 IRGQIINLMLDLQRElGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFEN---PQHPYTRKLM-AAVPVADps 573
Cdd:PRK10938 170 SRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQalvAQLAHSEQLEgVQLPEPD-- 246
|
250
....*....|....
gi 949724212 574 hHRPQRVLLSDDIP 587
Cdd:PRK10938 247 -EPSARHALPANEP 259
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
13-265 |
3.74e-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: 48.75 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 13 LAVSNLNIAFEQEQQRVsaVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVSCDemllrrrnrqvielGE 92
Cdd:cd03288 20 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVID--------------GI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 93 QSASQMRHVRGADIAMIFQEPMTslnpvftvgeqIAESIRLHQGAsheEAMVEAKRMLDQVRIPEAKAILSRYPHQL--- 169
Cdd:cd03288 84 DISKLPLHTLRSRLSIILQDPIL-----------FSGSIRFNLDP---ECKCTDDRLWEALEIAQLKNMVKSLPGGLdav 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 170 --------SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaQILQLIkVLQQDMSMGVIFITHDMGVVADiADRVLV 241
Cdd:cd03288 150 vteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-NILQKV-VMTAFADRTVVTIAHRVSTILD-ADLVLV 226
|
250 260
....*....|....*....|....
gi 949724212 242 MYQGEAVETGSVEQIFHAPQHPYT 265
Cdd:cd03288 227 LSRGILVECDTPENLLAQEDGVFA 250
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
169-251 |
3.97e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.70 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 LSGGMRQRVMIA--MALSCRPAVLIADEPTTALDvtiQAQILQLIKVLQQ--DMSMGVIFITHDMGVVaDIADRVLVM-- 242
Cdd:cd03238 88 LSGGELQRVKLAseLFSEPPGTLFILDEPSTGLH---QQDINQLLEVIKGliDLGNTVILIEHNLDVL-SSADWIIDFgp 163
|
90
....*....|...
gi 949724212 243 ----YQGEAVETG 251
Cdd:cd03238 164 gsgkSGGKVVFSG 176
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
32-256 |
4.69e-06 |
|
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: 49.91 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 32 VRNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIEqagGEVSCDEMLLRRRNRqvIELGEQSASQMrhvrgadiamifq 111
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKS----SLLMMIM---GELEPSEGKIKHSGR--ISFSPQTSWIM------------- 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 112 ePMTslnpvftvgeqIAESIRLhqGASHEE----AMVEAKRM-LDQVRIPEA-KAILSRYPHQLSGGMRQRVMIAMALSC 185
Cdd:TIGR01271 500 -PGT-----------IKDNIIF--GLSYDEyrytSVIKACQLeEDIALFPEKdKTVLGEGGITLSGGQRARISLARAVYK 565
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 186 RPAVLIADEPTTALDVTIQAQILQ--LIKVLqqdMSMGVIFITHDMGVVADiADRVLVMYQGEAVETGSVEQI 256
Cdd:TIGR01271 566 DADLYLLDSPFTHLDVVTEKEIFEscLCKLM---SNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSEL 634
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
349-538 |
5.25e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 48.13 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 349 PGETLSLVGESGCGKSTTGRALlrlvesqRGEIIFNGQR----------IDTLAASKLQP-----LRRDIQFIFQDPYAS 413
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKIL-------AGKLKPNLGKfddppdwdeiLDEFRGSELQNyftklLEGDVKVIVKPQYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 414 LDPRQTVGySILEPL-RVHGLLQGDAGSKRvawlLERVGLLPEHAwrypHEFSGGQRQRICIARALALNPKVIIADESVS 492
Cdd:cd03236 98 LIPKAVKG-KVGELLkKKDERGKLDELVDQ----LELRHVLDRNI----DQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 949724212 493 ALDVsirGQIINlMLDLQREL---GIAYLFISHDMAVVERISHRVAVMY 538
Cdd:cd03236 169 YLDI---KQRLN-AARLIRELaedDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-262 |
5.65e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 23 EQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKS----VTALSLMHLIEQAGGEVSCDemllrrrnrqvielGEQSASQM 98
Cdd:TIGR00956 68 FRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCStllkTIASNTDGFHIGVEGVITYD--------------GITPEEIK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 99 RHVRGaDIAMIFQepmTSLN-PVFTVGEQIAESIRLH------QGASHEEamvEAKRMLDQV------RIPEAKAILSRY 165
Cdd:TIGR00956 134 KHYRG-DVVYNAE---TDVHfPHLTVGETLDFAARCKtpqnrpDGVSREE---YAKHIADVYmatyglSHTRNTKVGNDF 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiQAQILQLIKVLQQDMSmgvifITHDMGVVA---------DIA 236
Cdd:TIGR00956 207 VRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLD---SATALEFIRALKTSAN-----ILDTTPLVAiyqcsqdayELF 278
|
250 260
....*....|....*....|....*.
gi 949724212 237 DRVLVMYQGeavetgsvEQIFHAPQH 262
Cdd:TIGR00956 279 DKVIVLYEG--------YQIYFGPAD 296
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
12-251 |
5.80e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.25 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 12 VLAVSNLNIAFEQEQqrvsAVRNLSFRLKRGETLAIVGESGSGKSVTALSLM--HLIEQAGGEVscdemllRRRNRQVIE 89
Cdd:PRK09580 1 MLSIKDLHVSVEDKA----ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTV-------EFKGKDLLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 90 LGEQSASqmrhvrGADIAMIFQEPM------------TSLNPVFTVGEQiaesirlhqgasheeamvEAKRMLDQVRIPE 157
Cdd:PRK09580 70 LSPEDRA------GEGIFMAFQYPVeipgvsnqfflqTALNAVRSYRGQ------------------EPLDRFDFQDLME 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 158 AKAILSRYPHQL---------SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqQDMSMGVIFITHD 228
Cdd:PRK09580 126 EKIALLKMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHY 204
|
250 260
....*....|....*....|....
gi 949724212 229 MGVVADIA-DRVLVMYQGEAVETG 251
Cdd:PRK09580 205 QRILDYIKpDYVHVLYQGRIVKSG 228
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
28-253 |
5.83e-06 |
|
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: 47.64 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 28 RVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHlieqAGGEVSCDEML---LRRRnrqvieLGEQSASQMRHVRGA 104
Cdd:cd03270 7 REHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIY----AEGQRRYVESLsayARQF------LGQMDKPDVDSIEGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 105 DIAMIFQEPMTSLNPVFTVGE--QIAESIRLHQGashEEAMVEAKRMLDQVRIPEAKaiLSRYPHQLSGGMRQRVMIAMA 182
Cdd:cd03270 77 SPAIAIDQKTTSRNPRSTVGTvtEIYDYLRLLFA---RVGIRERLGFLVDVGLGYLT--LSRSAPTLSGGEAQRIRLATQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949724212 183 LSCR-PAVL-IADEPTTALDvtiQAQILQLIKVLQ--QDMSMGVIFITHDMGVVAdIADRVLVMYQGEAVETGSV 253
Cdd:cd03270 152 IGSGlTGVLyVLDEPSIGLH---PRDNDRLIETLKrlRDLGNTVLVVEHDEDTIR-AADHVIDIGPGAGVHGGEI 222
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
169-256 |
8.10e-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: 49.24 E-value: 8.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 LSGGMRQRVMIAMALSCR---PAVLIADEPTTALDVtiqAQILQLIKVLQQDMSMG--VIFITHDMGVVAdIADRVLVM- 242
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHF---DDIKKLLEVLQRLVDKGntVVVIEHNLDVIK-TADYIIDLg 905
|
90
....*....|....*....
gi 949724212 243 -----YQGEAVETGSVEQI 256
Cdd:TIGR00630 906 peggdGGGTVVASGTPEEV 924
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
73-240 |
9.47e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.06 E-value: 9.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 73 VSCDEMLLRRRNRQVIELgeqsasqmrHVRGADIAMIFQepMTSLNpvftvgeqiAESIRLHQGASHEEamVEAKRMLDQ 152
Cdd:PRK00635 741 IPCPSCLGKRFLPQVLEV---------RYKGKNIADILE--MTAYE---------AEKFFLDEPSIHEK--IHALCSLGL 798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 153 VRIPeakaiLSRYPHQLSGGMRQRVMIAMAL---SCRPAVLIADEPTTALDVtiqAQILQLIKVLQQDMSMG--VIFITH 227
Cdd:PRK00635 799 DYLP-----LGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHT---HDIKALIYVLQSLTHQGhtVVIIEH 870
|
170
....*....|...
gi 949724212 228 DMGVVaDIADRVL 240
Cdd:PRK00635 871 NMHVV-KVADYVL 882
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
169-261 |
1.34e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.03 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSMGVIFITHDMGVVADIADRVLVMYqGEAv 248
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE-GEP- 149
|
90
....*....|...
gi 949724212 249 etgSVEQIFHAPQ 261
Cdd:cd03222 150 ---GVYGIASQPK 159
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
350-536 |
1.40e-05 |
|
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: 47.02 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 350 GETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIdtlaASKLQPLRRDIQFIFQDPYASLDPRQ-TVGY---SIL 425
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV----SYKPQYIKADYEGTVRDLLSSITKDFyTHPYfktEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 426 EPLRVHGLLQgdagskrvawllervgllpehawRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIR---GQI 502
Cdd:cd03237 101 KPLQIEQILD-----------------------REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmaSKV 157
|
170 180 190
....*....|....*....|....*....|....
gi 949724212 503 INLMLDLQRElgiAYLFISHDMAVVERISHRVAV 536
Cdd:cd03237 158 IRRFAENNEK---TAFVVEHDIIMIDYLADRLIV 188
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-257 |
2.06e-05 |
|
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: 48.02 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 14 AVSNLNIAFEQEQQRVSAVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGEVscdemllrrrnrqvielgeq 93
Cdd:TIGR00957 636 SITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------------- 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 94 sasqmrHVRGAdIAMIFQEPMT---SLNPVFTVGEQIAEsiRLHQGASHEEAMVEAKRML---DQVRIPEaKAIlsryph 167
Cdd:TIGR00957 696 ------HMKGS-VAYVPQQAWIqndSLRENILFGKALNE--KYYQQVLEACALLPDLEILpsgDRTEIGE-KGV------ 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQliKVLQqdmSMGV------IFITHDMGVVADIaDRVLV 241
Cdd:TIGR00957 760 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE--HVIG---PEGVlknktrILVTHGISYLPQV-DVIIV 833
|
250
....*....|....*.
gi 949724212 242 MYQGEAVETGSVEQIF 257
Cdd:TIGR00957 834 MSGGKISEMGSYQELL 849
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
446-538 |
3.83e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 446 LLERVGLlpEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVsirGQIINlMLDLQREL--GIAYLFISH 522
Cdd:PRK13409 196 VVERLGL--ENILdRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI---RQRLN-VARLIRELaeGKYVLVVEH 269
|
90
....*....|....*.
gi 949724212 523 DMAVVERISHRVAVMY 538
Cdd:PRK13409 270 DLAVLDYLADNVHIAY 285
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
169-240 |
5.28e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 45.30 E-value: 5.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 169 LSGGMRQRVMIAMALSCR---PAVLIADEPTTALDVtiqAQILQLIKVLQQDMSMG--VIFITHDMGVVAdIADRVL 240
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHF---HDVKKLLEVLQRLVDKGntVVVIEHNLDVIK-CADWII 242
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
28-252 |
6.41e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 44.87 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 28 RVSAVRNLSFRLKRGETLAIVGESGSGKSVtalslmhLIEQAGGEVSCDEMLLRRRNRQVIELgeQSASQMRHvrgaDIA 107
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTT-------LLGTLCGDPRATSGRIVFDGKDITDW--QTAKIMRE----AVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 108 MIfqepmtslnpvftvgeqiAESIRLHQGASHEEAMVE----AKRMLDQVRIPEAKAILSRYPHQ-------LSGGMRQR 176
Cdd:PRK11614 84 IV------------------PEGRRVFSRMTVEENLAMggffAERDQFQERIKWVYELFPRLHERriqragtMSGGEQQM 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949724212 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQDmSMGVIFITHDMGVVADIADRVLVMYQGEAV--ETGS 252
Cdd:PRK11614 146 LAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVleDTGD 222
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
349-536 |
8.00e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.13 E-value: 8.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 349 PGETLSLVGESGCGKSTTGRALLRLVESQRGEIIfngqridtlaasklqplrrdiqfifqdpYASLDPRQTVGYSILEPL 428
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI----------------------------YIDGEDILEEVLDQLLLI 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 429 RVHgllqgdagskrvawllervgllpehawRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQII----- 503
Cdd:smart00382 53 IVG---------------------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleel 105
|
170 180 190
....*....|....*....|....*....|....*....
gi 949724212 504 NLMLDLQRELGIAYLFISH------DMAVVERISHRVAV 536
Cdd:smart00382 106 RLLLLLKSEKNLTVILTTNdekdlgPALLRRRFDRRIVL 144
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-268 |
8.11e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 33 RNLSFRLKRGETLAIVGESGSGKSvtalSLMHLIeqaGGEVSCDEMLLRRRNRQVIELGEQsasqmRHVRGADIAmifQE 112
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKS----TILKLI---SGELQPSSGTVFRSAKVRMAVFSQ-----HHVDGLDLS---SN 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 113 PMTSLNPVFT-VGEQiaeSIRLHQGASHEEAMVEAKRMldqvripeakailsrypHQLSGGMRQRVMIAMALSCRPAVLI 191
Cdd:PLN03073 591 PLLYMMRCFPgVPEQ---KLRAHLGSFGVTGNLALQPM-----------------YTLSGGQKSRVAFAKITFKKPHILL 650
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949724212 192 ADEPTTALDVTIQAQILQLIKVLQQdmsmGVIFITHDMGVVADIADRVLVMYQGEAVEtgsveqiFHAPQHPYTKAL 268
Cdd:PLN03073 651 LDEPSNHLDLDAVEALIQGLVLFQG----GVLMVSHDEHLISGSVDELWVVSEGKVTP-------FHGTFHDYKKTL 716
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
353-435 |
9.31e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 42.71 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 353 LSLVGESGCGKSTTGRALLRLVESQRGEIIFngqrIDTLAASKLQPLRRDIQFIFQDPYASLDPRQTVGYSILEPLRVHG 432
Cdd:pfam13401 8 LVLTGESGTGKTTLLRRLLEQLPEVRDSVVF----VDLPSGTSPKDLLRALLRALGLPLSGRLSKEELLAALQQLLLALA 83
|
...
gi 949724212 433 LLQ 435
Cdd:pfam13401 84 VAV 86
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
314-389 |
1.10e-04 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 45.17 E-value: 1.10e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 314 LRVRNLVTRFPLRSGilnrvtREVHAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRID 389
Cdd:COG4615 328 LELRGVTYRYPGEDG------DEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT 397
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
157-228 |
1.12e-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: 43.75 E-value: 1.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949724212 157 EAKAILSRYPHQLSGGMRQ------RVMIAMALSCRPAVLIADEPTTALDV-TIQAQILQLIKVLQQDMSMGVIFITHD 228
Cdd:cd03240 104 ESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
31-256 |
1.53e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 31 AVRNLSFRLKRGETLAIVGESGSGKSVTALSLMHLIEQAGGE-------VSCDEMLLRRRN---------------RQVI 88
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawlfgqpVDAGDIATRRRVgymsqafslygeltvRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 89 ELgeqsasqmrHVRgadiamIFQEPmtslnpvftvGEQIAESIrlhqgasheEAMVEaKRMLDQVripeakaiLSRYPHQ 168
Cdd:NF033858 361 EL---------HAR------LFHLP----------AAEIAARV---------AEMLE-RFDLADV--------ADALPDS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ-LIKVLQQDmsmGV-IFI-THDMGvVADIADRVLVMYQG 245
Cdd:NF033858 398 LPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRlLIELSRED---GVtIFIsTHFMN-EAERCDRISLMHAG 473
|
250
....*....|.
gi 949724212 246 EAVETGSVEQI 256
Cdd:NF033858 474 RVLASDTPAAL 484
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
338-554 |
1.61e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.50 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 338 HAVENVSFDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIIFNGQRIDTLAASKLQplrrdiqfifqdpyasldpR 417
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLN-------------------G 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 418 QTVGysiLEPLRVHGLLQGdAGSKRVAWLLERVGLLPEHAwRYPHE----FSGGQRQRICIARALALNPKVIIADESVSA 493
Cdd:PRK13545 99 QLTG---IENIELKGLMMG-LTKEKIKEIIPEIIEFADIG-KFIYQpvktYSSGMKSRLGFAISVHINPDILVIDEALSV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949724212 494 LDVSIRGQIINLMLDLqRELGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGTRRAVFEN 554
Cdd:PRK13545 174 GDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
446-538 |
2.34e-04 |
|
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: 44.00 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 446 LLERVGLlpEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRElGIAYLFISHDM 524
Cdd:COG1245 196 LAEKLGL--ENILdRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDL 272
|
90
....*....|....
gi 949724212 525 AVVERISHRVAVMY 538
Cdd:COG1245 273 AILDYLADYVHILY 286
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
40-214 |
3.33e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.94 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 40 KRGETLAIVGESGSGKSvtalSLMHLIEQ--AGGEVSCDEMLLRRRNRQvielgeqSASQMR--HVRGADIAMifqepmt 115
Cdd:TIGR00956 787 KPGTLTALMGASGAGKT----TLLNVLAErvTTGVITGGDRLVNGRPLD-------SSFQRSigYVQQQDLHL------- 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 116 slnPVFTVGEQIAESIRLHQGA--SHEEAMveakRMLDQV-RIPE----AKAILSRYPHQLSGGMRQRVMIAMALSCRPA 188
Cdd:TIGR00956 849 ---PTSTVRESLRFSAYLRQPKsvSKSEKM----EYVEEViKLLEmesyADAVVGVPGEGLNVEQRKRLTIGVELVAKPK 921
|
170 180
....*....|....*....|....*..
gi 949724212 189 VLI-ADEPTTALDVTIQAQILQLIKVL 214
Cdd:TIGR00956 922 LLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
433-496 |
3.51e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 3.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 949724212 433 LLQGDAGSKRVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADESVSALDV 496
Cdd:PLN03073 314 LIDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
169-234 |
5.25e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.14 E-value: 5.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 169 LSGGMRQRVMIAMALSCRP---AVLIADEPTTALDVtiqAQILQLIKVLQQDMSMG--VIFITHDMGVV--AD 234
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHF---EDIRKLLEVLHRLVDKGntVVVIEHNLDVIktAD 900
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
465-514 |
5.31e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.19 E-value: 5.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 949724212 465 SGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMldLQRELG 514
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKC--IKDELR 789
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
465-504 |
6.11e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.04 E-value: 6.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 949724212 465 SGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIIN 504
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFD 781
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
345-495 |
9.08e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 40.99 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 345 FDLWPGETLSLVGESGCGKSTTGRALLRLVESQRGEIifngqRIDTLAASKLQPLRrdiqFIfqdPYASLDPRQTVGYSI 424
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI-----QIDGKTATRGDRSR----FM---AYLGHLPGLKADLST 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949724212 425 LEPLRVHGLLQGDAGSKRVAWLLERVGlLPEHAWRYPHEFSGGQRQRICIARaLALNPKVI-IADESVSALD 495
Cdd:PRK13543 100 LENLHFLCGLHGRRAKQMPGSALAIVG-LAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLD 169
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
336-529 |
1.30e-03 |
|
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: 40.00 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 336 EVHAVENVSFDLwPGETLSLV-GESGCGKSTtgrallrlvesqrgeIIFngqriDTLAASKLQPLRRDIQFIFQDPYASL 414
Cdd:cd03238 7 NVHNLQNLDVSI-PLNVLVVVtGVSGSGKST---------------LVN-----EGLYASGKARLISFLPKFSRNKLIFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 415 DPRQT---VGYSILEPLRVHGLLqgdagskrvawllervgllpehawryphefSGGQRQRICIARALALNPK--VIIADE 489
Cdd:cd03238 66 DQLQFlidVGLGYLTLGQKLSTL------------------------------SGGELQRVKLASELFSEPPgtLFILDE 115
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 949724212 490 SVSALDVSIRGQIINLMLDLqRELGIAYLFISHDMAVVER 529
Cdd:cd03238 116 PSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSS 154
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
464-546 |
1.38e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.93 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 464 FSGGQRQRICIARALALNPKVIIADESVSALDV---SIRGQIINLMLDLQRelgiAYLFISHDMAVVERIS-HRVAVMYL 539
Cdd:PRK09580 146 FSGGEKKRNDILQMAVLEPELCILDESDSGLDIdalKIVADGVNSLRDGKR----SFIIVTHYQRILDYIKpDYVHVLYQ 221
|
....*..
gi 949724212 540 GQIVEIG 546
Cdd:PRK09580 222 GRIVKSG 228
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
445-538 |
1.81e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.86 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 445 WLLERVGLLPEHAwryphEFSGGQRQRICIARALALNPKVIIADESVSALDVSIRGQIINLMLDLQRELGIAYLFISHDM 524
Cdd:cd03222 58 WDGITPVYKPQYI-----DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDL 132
|
90
....*....|....
gi 949724212 525 AVVERISHRVAVMY 538
Cdd:cd03222 133 AVLDYLSDRIHVFE 146
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
169-234 |
2.63e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.78 E-value: 2.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949724212 169 LSGGMRQRVMIAMALSCR---PAVLIADEPTTAL---DvtiqaqILQLIKVLQQDMSMG--VIFITHDMGVV--AD 234
Cdd:COG0178 827 LSGGEAQRVKLASELSKRstgKTLYILDEPTTGLhfhD------IRKLLEVLHRLVDKGntVVVIEHNLDVIktAD 896
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
166-233 |
2.84e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 2.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949724212 166 PHQLSGGMRQrvMIAMALSC-----RPAVLIADEPTTALDVTIQAQILQLIKVLQQDMSmGVIFITHDMGVVA 233
Cdd:pfam13304 234 AFELSDGTKR--LLALLAALlsalpKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGA-QLILTTHSPLLLD 303
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
118-212 |
3.60e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.60 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 118 NPVFTVGEQIAES--IRLHQGASHEEAMVEAKRMLDQVRIPEAKAILSRYP--HQLSGGMRQRVMIAMALSCRPAVLIAD 193
Cdd:PLN03140 965 SPQVTVRESLIYSafLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMD 1044
|
90
....*....|....*....
gi 949724212 194 EPTTALDVTIQAQILQLIK 212
Cdd:PLN03140 1045 EPTSGLDARAAAIVMRTVR 1063
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
169-258 |
4.81e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.11 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQliKVLQQDMSMGV-IFITHDMGVVADIaDRVLVMYQGEA 247
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDELRGKTrVLVTNQLHFLSQV-DRIILVHEGMI 817
|
90
....*....|.
gi 949724212 248 VETGSVEQIFH 258
Cdd:PLN03130 818 KEEGTYEELSN 828
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
85-228 |
4.86e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.72 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 85 RQVIELGeqsasqMRHVRGA-----DIAMIFQEPMTSLNpvftvgEQIAESIRL-----HQGASHEEAMVEakRMLDQVR 154
Cdd:PRK11819 88 RENVEEG------VAEVKAAldrfnEIYAAYAEPDADFD------ALAAEQGELqeiidAADAWDLDSQLE--IAMDALR 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949724212 155 IPEAKAILSryphQLSGGMRQRVmiamALsCR-----PAVLIADEPTTALDvtiqAQ-ILQLIKVLqQDMSMGVIFITHD 228
Cdd:PRK11819 154 CPPWDAKVT----KLSGGERRRV----AL-CRlllekPDMLLLDEPTNHLD----AEsVAWLEQFL-HDYPGTVVAVTHD 219
|
|
|