|
Name |
Accession |
Description |
Interval |
E-value |
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-237 |
2.96e-137 |
|
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: 384.72 E-value: 2.96e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 3 EPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGI 82
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 83 AQAPEGRRIFPDMTVEENLLMGTIPIGN-AHAAEDMQKMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLL 161
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDrAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487090 162 DEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEVRKAYLGG 237
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLGV 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-227 |
2.07e-118 |
|
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: 336.33 E-value: 2.07e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAQA 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 PEGRRIFPDMTVEENLLMGTIPIGNAHAAEDMQKMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPS 165
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487090 166 LGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGN 227
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-237 |
2.85e-101 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 293.71 E-value: 2.85e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASG 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 GIAQAPEGRRIFPDMTVEENLLMGTIPIGNAHAAEDMQKMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLL 160
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 161 LDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEVRKAYLGG 237
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLGG 237
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-235 |
1.54e-77 |
|
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: 233.19 E-value: 1.54e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAQA 85
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 PEGRRIFPDMTVEENLLMGTIPIGNAHAAEDmQKMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPS 165
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRSRKIP-DEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487090 166 LGLAPIVVKQIFQTLRELA-RGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLlgNQEVRKAYL 235
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRaEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL--DEDKVRRYL 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-237 |
5.21e-60 |
|
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: 189.48 E-value: 5.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 2 NEPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGG 81
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 82 IA---QAPegrRIFPDMTVEENLLMGT--------------IPIGNAHAAEDMQKMFDL--FPRLKERRKQRAMTMSGGE 142
Cdd:COG0411 81 IArtfQNP---RLFPELTVLENVLVAAharlgrgllaallrLPRARREEREARERAEELleRVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 143 QQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEqnaHH---ALKLADRGYVMVNGQIRLS 218
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIE---HDmdlVMGLADRIVVLDFGRVIAE 234
|
250
....*....|....*....
gi 2790487090 219 GSGEDLLGNQEVRKAYLGG 237
Cdd:COG0411 235 GTPAEVRADPRVIEAYLGE 253
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-236 |
1.71e-55 |
|
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: 177.35 E-value: 1.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 14 FYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAQAPEGRRIFP 93
Cdd:cd03218 9 RYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLPQEASIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 94 DMTVEENLL--MGTIPIGNAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPI 171
Cdd:cd03218 89 KLTVEENILavLEIRGLSKKEREEKLEELLEEF-HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 172 VVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEVRKAYLG 236
Cdd:cd03218 168 AVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-230 |
9.64e-55 |
|
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: 175.32 E-value: 9.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIA-- 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 84 -QAPegrRIFPDMTVEENLLMGTIPIGNAHA---------AEDMQKMFDL--FPRLKERRKQRAMTMSGGEQQMLAIARA 151
Cdd:cd03219 81 fQIP---RLFPELTVLENVMVAAQARTGSGLllararreeREARERAEELleRVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 152 LMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEV 230
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
15-236 |
8.42e-52 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 167.90 E-value: 8.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 15 YGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGI---AQAPEgrrI 91
Cdd:COG1137 13 YGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIgylPQEAS---I 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 92 FPDMTVEENLL--MGTIPIGNAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLA 169
Cdd:COG1137 90 FRKLTVEDNILavLELRKLSKKEREERLEELLEEF-GITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 170 PIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEVRKAYLG 236
Cdd:COG1137 169 PIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLG 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-225 |
3.71e-51 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 166.01 E-value: 3.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASggIAQA 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR--IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 PEGRRIFPDMTVEENL-LMGTI-PIGNAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDE 163
Cdd:COG1131 79 PQEPALYPDLTVRENLrFFARLyGLPRKEARERIDELLELF-GLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487090 164 PSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
15-236 |
4.59e-50 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 163.60 E-value: 4.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 15 YGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAQAPEGRRIFPD 94
Cdd:TIGR04406 11 YKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYLPQEASIFRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 95 MTVEENLLMGTIPIGNAHAAEDMQKMFDLFPRL--KERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIV 172
Cdd:TIGR04406 91 LTVEENIMAVLEIRKDLDRAEREERLEALLEEFqiSHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487090 173 VKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEVRKAYLG 236
Cdd:TIGR04406 171 VGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLG 234
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-234 |
8.50e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 155.25 E-value: 8.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTH--YVa 78
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigYV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 79 sggiAQAPEGRRIFPdMTVEENLLMGTIPIGNahaaedmqkmfdLFPRLKERRKQRAM-----------------TMSGG 141
Cdd:COG1121 81 ----PQRAEVDWDFP-ITVRDVVLMGRYGRRG------------LFRRPSRADREAVDealervgledladrpigELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 142 EQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRgYVMVNGQIRLSGSG 221
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDR-VLLLNRGLVAHGPP 222
|
250
....*....|...
gi 2790487090 222 EDLLGNQEVRKAY 234
Cdd:COG1121 223 EEVLTPENLSRAY 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-235 |
1.23e-42 |
|
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: 144.62 E-value: 1.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASggIAQ 84
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ--IGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 85 APEGRRIFPDMTVEENL-----LMGTIPIGNAHAAEDMQKMFDLFprlkERRKQRAMTMSGGEQQMLAIARALMSRPTLL 159
Cdd:COG4555 79 LPDERGLYDRLTVRENIryfaeLYGLFDEELKKRIEELIELLGLE----EFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 160 LLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLL---GNQEVRKAYL 235
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELReeiGEENLEDAFV 233
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-233 |
1.08e-41 |
|
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: 141.70 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFY-GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAsggiaq 84
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 85 apegRRI-----FPD-----MTVEENLLMGTIPIGNAHA-----AEDMQKMFDLfprlKERRKQRAMTMSGGEQQMLAIA 149
Cdd:COG1122 75 ----RKVglvfqNPDdqlfaPTVEEDVAFGPENLGLPREeirerVEEALELVGL----EHLADRPPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 150 RALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQE 229
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
....
gi 2790487090 230 VRKA 233
Cdd:COG1122 227 LLEE 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-215 |
1.09e-41 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 139.84 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAqa 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 PEGRRIFPDMTVEENLlmgtipignahaaedmqkmfdlfprlkerrkqramTMSGGEQQMLAIARALMSRPTLLLLDEPS 165
Cdd:cd03230 79 PEEPSLYENLTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790487090 166 LGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-238 |
1.37e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 138.97 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHyvasggIAQ 84
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKD------INK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 85 ApegRR----------IFPDMTVEENLLMGTIPIGNAHAAEDMQKMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARAL 152
Cdd:COG1126 75 L---RRkvgmvfqqfnLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERvgLADKADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 153 MSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGN-QEVR 231
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENpQHER 231
|
....*...
gi 2790487090 232 -KAYLGGV 238
Cdd:COG1126 232 tRAFLSKV 239
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-164 |
2.19e-40 |
|
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: 135.85 E-value: 2.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVaSGGIAQAPEGRRIFPDMTVEEN 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL-RKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 101 LLMGTIPIGNAHAAEDMQ-----KMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEP 164
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARaeealEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-214 |
1.38e-39 |
|
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: 135.67 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 7 EFHEVDVFY--GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVA--SGGI 82
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 83 AQAPEGRRIFPdmTVEENLLMGtiPIGNAHAAEDMQK----MFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTL 158
Cdd:cd03225 81 FQNPDDQFFGP--TVEEEVAFG--LENLGLPEEEIEErveeALELV-GLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487090 159 LLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQ 214
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-215 |
2.24e-39 |
|
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: 135.77 E-value: 2.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLL----MSIFGQPRIR-GGQILFRGEEISHRSTHYVAS- 79
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLrllnRLNDLIPGAPdEGEVLLDGKDIYDLDVDVLELr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 80 ---GGIAQAPEgrrIFPdMTVEENL-----LMGTIPIGNAHA-AEDMQKMFDLFPRLKerRKQRAMTMSGGEQQMLAIAR 150
Cdd:cd03260 81 rrvGMVFQKPN---PFP-GSIYDNVayglrLHGIKLKEELDErVEEALRKAALWDEVK--DRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 151 ALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARgGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-224 |
3.00e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 141.31 E-value: 3.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 2 NEPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGG 81
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 82 IA---QAPEgrrIFPDMTVEENLLMGTIPIG---------NAHAAEDMQKM-FDLFPRlkerrkQRAMTMSGGEQQMLAI 148
Cdd:COG1129 81 IAiihQELN---LVPNLSVAENIFLGREPRRgglidwramRRRARELLARLgLDIDPD------TPVGDLSVAQQQLVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 149 ARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVeqnAHH---ALKLADRGYVMVNGQIRLSGSGEDL 224
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYI---SHRldeVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-234 |
3.27e-39 |
|
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: 135.94 E-value: 3.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS--GGI 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARriAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 83 AQAPEGRrifPDMTVEENLLMGTIP---IGNAHAAEDMQK------MFDLFPrLKERrkqRAMTMSGGEQQMLAIARALM 153
Cdd:COG1120 81 PQEPPAP---FGLTVRELVALGRYPhlgLFGRPSAEDREAveealeRTGLEH-LADR---PVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 154 SRPTLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVeqnAH---HALKLADRGYVMVNGQIRLSGSGEDLLGNQE 229
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMV---LHdlnLAARYADRLVLLKDGRIVAQGPPEEVLTPEL 230
|
....*
gi 2790487090 230 VRKAY 234
Cdd:COG1120 231 LEEVY 235
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-214 |
7.48e-39 |
|
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: 131.98 E-value: 7.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 7 EFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSthyvasggiaqap 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 87 egrrifpdmtveenllmgtipignahaaedmqkmfdlfprLKERRKQRAMT--MSGGEQQMLAIARALMSRPTLLLLDEP 164
Cdd:cd00267 68 ----------------------------------------LEELRRRIGYVpqLSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790487090 165 SLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQ 214
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-215 |
1.14e-38 |
|
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: 133.42 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSThyvasggiaQA 85
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKK---------NI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 PEGRR----------IFPDMTVEENLLMGTIPIGNAHAAEDMQKMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALM 153
Cdd:cd03262 72 NELRQkvgmvfqqfnLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKvgLADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487090 154 SRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-215 |
1.17e-38 |
|
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: 133.41 E-value: 1.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHyvaSGGIAQA 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE---RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 PEGRRIFPDMTVEEN----LLMGTIPIGNAHA-AEDMQKMFDLFPRLKErrkqRAMTMSGGEQQMLAIARALMSRPTLLL 160
Cdd:cd03259 78 FQDYALFPHLTVAENiafgLKLRGVPKAEIRArVRELLELVGLEGLLNR----YPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487090 161 LDEPSLGLAPIVVKQIFQTLREL-ARGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-224 |
3.14e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 133.26 E-value: 3.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 4 PMLEFHEVDV-FYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSThyvasggi 82
Cdd:COG3638 1 PMLELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 83 AQAPEGRR----IF------PDMTVEENLLMGTIP-------IGNAHAAEDMQKMFDLFPR--LKERRKQRAMTMSGGEQ 143
Cdd:COG3638 73 RALRRLRRrigmIFqqfnlvPRLSVLTNVLAGRLGrtstwrsLLGLFPPEDRERALEALERvgLADKAYQRADQLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 144 QMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELAR-GGMTIfLVeqNAHH---ALKLADRGYVMVNGQIRLSG 219
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITV-VV--NLHQvdlARRYADRIIGLRDGRVVFDG 229
|
....*
gi 2790487090 220 SGEDL 224
Cdd:COG3638 230 PPAEL 234
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-215 |
6.18e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 131.70 E-value: 6.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 3 EPMLEFHEVDVFYG----AIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSthyva 78
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLS----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 79 SGGIAQApegRR-----IF------PDMTVEENLLMGTIpIGNAHAAEDMQKMFDLFPR--LKERRKQRAMTMSGGEQQM 145
Cdd:COG1136 77 ERELARL---RRrhigfVFqffnllPELTALENVALPLL-LAGVSRKERRERARELLERvgLGDRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 146 LAIARALMSRPTLLLLDEP--SL----GlapivvKQIFQTLRELAR-GGMTIFLVEQNAHHAlKLADRGYVMVNGQI 215
Cdd:COG1136 153 VAIARALVNRPKLILADEPtgNLdsktG------EEVLELLRELNReLGTTIVMVTHDPELA-ARADRVIRLRDGRI 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-219 |
9.22e-38 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 131.12 E-value: 9.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 7 EFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTH--YVAsggiaQ 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigYVP-----Q 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 85 APEGRRIFPdMTVEENLLMGTIPIGN------------AHAAEDMQKMFDLfprlkerRKQRAMTMSGGEQQMLAIARAL 152
Cdd:cd03235 76 RRSIDRDFP-ISVRDVVLMGLYGHKGlfrrlskadkakVDEALERVGLSEL-------ADRQIGELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 153 MSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRgYVMVNGQIRLSG 219
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-227 |
1.11e-37 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 131.75 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIShrsthyvasGGIAQ 84
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN---------DPKVD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 85 APEGRR----------IFPDMTVEENLLMGTIPIGNAHAAEDMQKMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARAL 152
Cdd:PRK09493 72 ERLIRQeagmvfqqfyLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKvgLAERAHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 153 MSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGN 227
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-215 |
1.88e-37 |
|
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: 130.70 E-value: 1.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFY----GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASG 80
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 G-----IAQAPeGRRIFPDMTVEENLLMGTIPIGNAHAAEDMQK----MFDLFPRLKERRKQRAMTMSGGEQQMLAIARA 151
Cdd:cd03257 81 RkeiqmVFQDP-MSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEavllLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 152 LMSRPTLLLLDEPSLGLAPIVVKQIFQTLREL-ARGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-224 |
3.04e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 133.30 E-value: 3.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRsthyvasg 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 giaqAPEGRRI---------FPDMTVEEN----LLMGTIPigNAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLA 147
Cdd:COG3842 73 ----PPEKRNVgmvfqdyalFPHLTVAENvafgLRMRGVP--KAEIRARVAELLELV-GLEGLADRYPHQLSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 148 IARALMSRPTLLLLDEPsLG-----LAPIVVKQIFQTLRELargGMTIFLVeqnAHH---ALKLADRGYVMVNGQIRLSG 219
Cdd:COG3842 146 LARALAPEPRVLLLDEP-LSaldakLREEMREELRRLQREL---GITFIYV---THDqeeALALADRIAVMNDGRIEQVG 218
|
....*
gi 2790487090 220 SGEDL 224
Cdd:COG3842 219 TPEEI 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-205 |
3.11e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.79 E-value: 3.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFY-GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVasggia 83
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREI------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 84 qaPEGRR----IF------PDMTVEENLLMGTIPIG--NAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARA 151
Cdd:COG2884 75 --PYLRRrigvVFqdfrllPDRTVYENVALPLRVTGksRKEIRRRVREVLDLV-GLSDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487090 152 LMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIF-------LVEQNAHHALKLAD 205
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLiathdleLVDRMPKRVLELED 212
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-219 |
5.03e-37 |
|
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: 128.87 E-value: 5.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAQA 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 PEgrrIFPDMTVEENLLMGTIPIGNAHaaEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPS 165
Cdd:cd03268 81 PG---FYPNLTARENLRLLARLLGIRK--KRIDEVLDVV-GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487090 166 LGLAPIVVKQIFQTLRELARGGMTIFLveqnAHHAL----KLADRGYVMVNGQIRLSG 219
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQGITVLI----SSHLLseiqKVADRIGIINKGKLIEEG 208
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-214 |
6.81e-37 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 127.69 E-value: 6.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIshrsthyvASGGIAQA 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL--------TDLEDELP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 PEGRRI---------FPDMTVEENLLMGtipignahaaedmqkmfdlfprlkerrkqramtMSGGEQQMLAIARALMSRP 156
Cdd:cd03229 73 PLRRRIgmvfqdfalFPHLTVLENIALG---------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 157 TLLLLDEPSLGLAPIVVKQIFQTLREL-ARGGMTIFLVEQNAHHALKLADRGYVMVNGQ 214
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-224 |
1.35e-36 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 128.84 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAI-QALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS----- 79
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 80 GGIAQAPegrRIFPDMTVEENLLMG---TIPIGNAHA----AEDMQKMFDLFPR--LKERRKQRAMTMSGGEQQMLAIAR 150
Cdd:cd03256 81 GMIFQQF---NLIERLSVLENVLSGrlgRRSTWRSLFglfpKEEKQRALAALERvgLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487090 151 ALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLveqNAHH---ALKLADRGYVMVNGQIRLSGSGEDL 224
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIV---SLHQvdlAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-229 |
1.80e-36 |
|
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: 134.26 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 3 EPMLEFHEVDVFY--GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFG---QPRIRGGQILFRGEEISHRSTHYV 77
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 78 AS--GGIAQAPEgRRIFPdMTVEENLLMGtIPIGNAHAAEDMQKMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALM 153
Cdd:COG1123 82 GRriGMVFQDPM-TQLNP-VTVGDQIAEA-LENLGLSRAEARARVLELLEAvgLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 154 SRPTLLLLDEPSLGLAPIVVKQIFQTLRELAR-GGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQE 229
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-227 |
1.99e-36 |
|
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: 134.26 E-value: 1.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 3 EPMLEFHEVDVFY-----GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSthyv 77
Cdd:COG1123 258 EPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLS---- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 78 asgGIAQAPEGRRI-----------FPDMTVEENL-----LMGTIPIGNAHA-AEDMQKMFDLFPRLKERrkqRAMTMSG 140
Cdd:COG1123 334 ---RRSLRELRRRVqmvfqdpysslNPRMTVGDIIaeplrLHGLLSRAERRErVAELLERVGLPPDLADR---YPHELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 141 GEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELAR-GGMTIFLVeqnAHH---ALKLADRGYVMVNGQIR 216
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQReLGLTYLFI---SHDlavVRYIADRVAVMYDGRIV 484
|
250
....*....|.
gi 2790487090 217 LSGSGEDLLGN 227
Cdd:COG1123 485 EDGPTEEVFAN 495
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-234 |
2.73e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 129.46 E-value: 2.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHyvasgGIAQ 84
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRR-----RIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 85 APEGRRIFPDMTVEENL-----LMGtipIGNAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLL 159
Cdd:COG4152 76 LPEERGLYPKMKVGEQLvylarLKG---LSKAEAKRRADEWLERL-GLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 160 LLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEdllgnqEVRKAY 234
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD------EIRRQF 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-220 |
3.19e-36 |
|
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: 127.24 E-value: 3.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 20 ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIshRSTHYVASGGIAQAPEGRRIFPDMTVEE 99
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQSLGYCPQFDALFDELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 100 NL-LMGTIP-IGNAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIF 177
Cdd:cd03263 95 HLrFYARLKgLPKSEIKEEVELLLRVL-GLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIW 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2790487090 178 QTLRELaRGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGS 220
Cdd:cd03263 174 DLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGS 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
18-215 |
3.67e-36 |
|
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: 127.22 E-value: 3.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 18 IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHyvasggiAQAPEGRR----IF- 92
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEK-------ELAAFRRRhigfVFq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 93 -----PDMTVEENLLMGTIPIG--NAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPS 165
Cdd:cd03255 90 sfnllPDLTALENVELPLLLAGvpKKERRERAEELLERV-GLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2790487090 166 LGLAPIVVKQIFQTLRELARG-GMTIFLVEQNaHHALKLADRGYVMVNGQI 215
Cdd:cd03255 169 GNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-236 |
7.91e-36 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 127.41 E-value: 7.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASG 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 GIAQAPEGRRIFPDMTVEENLLMG--------------TIPIGNAHAAEDMQKMFDLFPR--LKERRKQRAMTMSGGEQQ 144
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLVAqhqqlktglfsgllKTPAFRRAESEALDRAATWLERvgLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 145 MLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGED 223
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
250
....*....|...
gi 2790487090 224 LLGNQEVRKAYLG 236
Cdd:PRK11300 241 IRNNPDVIKAYLG 253
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-215 |
1.71e-35 |
|
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: 123.69 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAqa 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 pegrrifpdmTVeenllmgtipignahaaedMQkmfdlfprlkerrkqramtMSGGEQQMLAIARALMSRPTLLLLDEPS 165
Cdd:cd03216 79 ----------MV-------------------YQ-------------------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790487090 166 LGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-231 |
6.42e-35 |
|
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: 124.32 E-value: 6.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHyvasg 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 giAQAPEGRRI---------FPDMTVEENLlmgtipignahaaedmqkMFDL--FPRLKER-RKQRAMTM---------- 138
Cdd:COG1127 76 --ELYELRRRIgmlfqggalFDSLTVFENV------------------AFPLreHTDLSEAeIRELVLEKlelvglpgaa 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 139 -------SGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVM 210
Cdd:COG1127 136 dkmpselSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVL 215
|
250 260
....*....|....*....|...
gi 2790487090 211 VNGQIRLSGSGEDLL--GNQEVR 231
Cdd:COG1127 216 ADGKIIAEGTPEELLasDDPWVR 238
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-214 |
9.39e-35 |
|
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: 122.11 E-value: 9.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYG--AIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS--GG 81
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKniAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 82 IAQAPEgrrIFpDMTVEENLLmgtipignahaaedmqkmfdlfprlkerrkqramtmSGGEQQMLAIARALMSRPTLLLL 161
Cdd:cd03228 81 VPQDPF---LF-SGTIRENIL------------------------------------SGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 162 DEPSLGLAPIVVKQIFQTLRELaRGGMTIFLVeqnAH--HALKLADRGYVMVNGQ 214
Cdd:cd03228 121 DEATSALDPETEALILEALRAL-AKGKTVIVI---AHrlSTIRDADRIIVLDDGR 171
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-215 |
1.32e-34 |
|
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: 123.76 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYGA----IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRST--HYVA 78
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkaFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 79 SGGIAQAPEGRrIFPDMTVEENLLMGTIPIGNAHAAEDMQKMFD---LFPRLKERRKQramTMSGGEQQMLAIARALMSR 155
Cdd:COG1124 81 VQMVFQDPYAS-LHPRHTVDRILAEPLRIHGLPDREERIAELLEqvgLPPSFLDRYPH---QLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487090 156 PTLLLLDEPSLGLAPIVVKQIFQTLREL-ARGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-215 |
5.74e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 121.08 E-value: 5.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISH-------RSTHYVA 78
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmpppewrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 79 sggiaQAPegrRIFPDmTVEENLLMgtiPIGNAHAAEDMQKMFDLFPRL---KERRKQRAMTMSGGEQQMLAIARALMSR 155
Cdd:COG4619 81 -----QEP---ALWGG-TVRDNLPF---PFQLRERKFDRERALELLERLglpPDILDKPVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487090 156 PTLLLLDEPSLGLAPIVVKQIFQTLREL-ARGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-228 |
8.04e-34 |
|
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: 127.57 E-value: 8.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 4 PMLEFHEVDVFY-GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS--G 80
Cdd:COG4988 335 PSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRqiA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 GIAQAPegrRIFPDmTVEENLLMGTIP---------IGNAHAAEDMQKMFD-LFPRLKERrkqrAMTMSGGEQQMLAIAR 150
Cdd:COG4988 415 WVPQNP---YLFAG-TIRENLRLGRPDasdeeleaaLEAAGLDEFVAALPDgLDTPLGEG----GRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 151 ALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLveqnAH--HALKLADRGYVMVNGQIRLSGSGEDLLGNQ 228
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILI----THrlALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-219 |
9.32e-34 |
|
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: 120.46 E-value: 9.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIShrsthYVASGGIAQA 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-----IAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 PEGRRIFPDMTVEENL-----LMGTIPIGNAHAAEDMQKMFDLfprlKERRKQRAMTMSGGEQQMLAIARALMSRPTLLL 160
Cdd:cd03269 76 PEERGLYPKMKVIDQLvylaqLKGLKKEEARRRIDEWLERLEL----SEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 161 LDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSG 219
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
1.52e-33 |
|
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: 119.07 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 2 NEPMLEFHEVDVfygaIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGG 81
Cdd:cd03215 1 GEPVLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 82 IAQAPEGRR---IFPDMTVEENLLMGTIpignahaaedmqkmfdlfprlkerrkqramtMSGGEQQMLAIARALMSRPTL 158
Cdd:cd03215 77 IAYVPEDRKregLVLDLSVAENIALSSL-------------------------------LSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 159 LLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-206 |
1.69e-33 |
|
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: 120.05 E-value: 1.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFY-GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS--GG 81
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLlrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 82 IAQAPEGRRIFPDMTVEENLLMGTIPIGnAHAAEDMQKMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPTLL 159
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRG-KKEREIQRRVGAALRQvgLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2790487090 160 LLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLveqnAHHALKLADR 206
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIV----ATHDLSLVDR 202
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-229 |
2.68e-33 |
|
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: 126.03 E-value: 2.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 4 PMLEFHEVDVFY--GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS-- 79
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRri 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 80 GGIAQAPEgrrIFpDMTVEENLLmgtipIGNAHAAED-MQKMFD---LFPRLKERRK-------QRAMTMSGGEQQMLAI 148
Cdd:COG4987 412 AVVPQRPH---LF-DTTLRENLR-----LARPDATDEeLWAALErvgLGDWLAALPDgldtwlgEGGRRLSGGERRRLAL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 149 ARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARgGMTIFLVeqnAHH--ALKLADRGYVMVNGQIRLSGSGEDLLG 226
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLI---THRlaGLERMDRILVLEDGRIVEQGTHEELLA 558
|
...
gi 2790487090 227 NQE 229
Cdd:COG4987 559 QNG 561
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
15-236 |
7.19e-33 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 119.23 E-value: 7.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 15 YGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAQAPEGRRIFPD 94
Cdd:PRK10895 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 95 MTVEENLlMGTIPIGNAHAAEDMQ----KMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAP 170
Cdd:PRK10895 93 LSVYDNL-MAVLQIRDDLSAEQREdranELMEEF-HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487090 171 IVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEVRKAYLG 236
Cdd:PRK10895 171 ISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLG 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-215 |
9.45e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 123.98 E-value: 9.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 20 ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAQAPEGRR---IFPDMT 96
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAYVPEDRKgegLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 97 VEENLLMGTIP-------IGNAHAAEDMQKMFDLFpRLK-ERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGl 168
Cdd:COG1129 347 IRENITLASLDrlsrgglLDRRRERALAEEYIKRL-RIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRG- 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 169 apIVV---KQIFQTLRELARGGMTIFLV-----EqnahhALKLADRGYVMVNGQI 215
Cdd:COG1129 425 --IDVgakAEIYRLIRELAAEGKAVIVIsselpE-----LLGLSDRILVMREGRI 472
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-225 |
9.48e-33 |
|
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: 119.03 E-value: 9.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 3 EPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQ-PRIRGGQILFRGE--------EISHRs 73
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGErrggedvwELRKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 74 thyvasGGIAQAPEGRRIFPDMTVEENLLMG---TIPIGNAHAAEDMQKMFDLFPRLK-ERRKQRAM-TMSGGEQQMLAI 148
Cdd:COG1119 80 ------IGLVSPALQLRFPRDETVLDVVLSGffdSIGLYREPTDEQRERARELLELLGlAHLADRPFgTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 149 ARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELAR-GGMTIFLVeqnAHHA---LKLADRGYVMVNGQIRLSGSGEDL 224
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVLV---THHVeeiPPGITHVLLLKDGRVVAAGPKEEV 230
|
.
gi 2790487090 225 L 225
Cdd:COG1119 231 L 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-224 |
1.82e-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: 117.72 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAQA 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 pegRRIFPDMTVEENLLMG--TIPIGNAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDE 163
Cdd:cd03300 81 ---YALFPHLTVFENIAFGlrLKKLPKAEIKERVAEALDLV-QLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487090 164 PSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDL 224
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
15-224 |
3.04e-32 |
|
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: 117.09 E-value: 3.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 15 YGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAqaPEGRRIFPD 94
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIV--FQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 95 MTVEENLLM-GTI-PIGNAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIV 172
Cdd:cd03265 88 LTGWENLYIhARLyGVPGAERRERIDELLDFV-GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2790487090 173 VKQIFQTLREL-ARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDL 224
Cdd:cd03265 167 RAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-206 |
4.94e-32 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 116.04 E-value: 4.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 4 PMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS-GGI 82
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRlAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 83 AQAPEgrrIFPDMTVEENLLMGTIPIGNAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLD 162
Cdd:COG4133 81 GHADG---LKPELTVRENLRFWAALYGLRADREAIDEALEAV-GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2790487090 163 EPSLGLAPIVVKQIFQTLRE-LARGGMTIF----LVEQNAHHALKLADR 206
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAhLARGGAVLLtthqPLELAAARVLDLGDF 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-224 |
5.91e-32 |
|
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: 116.45 E-value: 5.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSthyvasgGIAQA 85
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLS-------EAELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 PEGRRI---------FPDMTVEENLLMgtiPIgNAHAAEDMQKMFDL------FPRLKERRKQRAMTMSGGEQQMLAIAR 150
Cdd:cd03261 74 RLRRRMgmlfqsgalFDSLTVFENVAF---PL-REHTRLSEEEIREIvlekleAVGLRGAEDLYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 151 ALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELAR-GGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDL 224
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-210 |
1.03e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 116.73 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFY----GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTH- 75
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 76 -YVasggiAQAPegrRIFPDMTVEENLLMG--TIPIGNAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARAL 152
Cdd:COG1116 83 gVV-----FQEP---ALLPWLTVLDNVALGleLRGVPKAERRERARELLELV-GLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487090 153 MSRPTLLLLDEPslglapivvkqiF-----QT--------LRELARGGMTIFLVEQNAHHALKLADRGYVM 210
Cdd:COG1116 154 ANDPEVLLMDEP------------FgaldaLTrerlqdelLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-210 |
5.37e-31 |
|
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: 113.72 E-value: 5.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYG----AIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIS--HRSTHYVas 79
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTgpGPDRGYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 80 ggiAQAPegrRIFPDMTVEENLLMG--TIPIGNAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPT 157
Cdd:cd03293 79 ---FQQD---ALLPWLTVLDNVALGleLQGVPKAEARERAEELLELV-GLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790487090 158 LLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVM 210
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-235 |
1.23e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.40 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 19 QALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS----GGIAQAPEGRRIFPd 94
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVrktvGIVFQNPDDQLFAP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 95 mTVEENLLMGTIPIGNAHaaEDMQKmfdlfpRLKERRKQRAMT---------MSGGEQQMLAIARALMSRPTLLLLDEPS 165
Cdd:PRK13639 95 -TVEEDVAFGPLNLGLSK--EEVEK------RVKEALKAVGMEgfenkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487090 166 LGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQE-VRKAYL 235
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIEtIRKANL 236
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-215 |
1.92e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 113.21 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 3 EPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIfgqPR----IRG----GQILFRGEEISHRST 74
Cdd:COG1117 9 EPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL---NRmndlIPGarveGEILLDGEDIYDPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 75 HYVA----SGGIAQAPegrRIFPdMTVEENLLMGtIPIGNAHAAEDMQ-------KMFDLFPRLKERRKQRAMTMSGGEQ 143
Cdd:COG1117 86 DVVElrrrVGMVFQKP---NPFP-KSIYDNVAYG-LRLHGIKSKSELDeiveeslRKAALWDEVKDRLKKSALGLSGGQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487090 144 QMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELaRGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL-KKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-219 |
2.04e-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: 110.99 E-value: 2.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 7 EFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAsggiaqap 86
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 87 egRRIfpdmtveenllmGTIPignahaaedmQ--KMFDLFPrLKERRkqrAMTMSGGEQQMLAIARALMSRPTLLLLDEP 164
Cdd:cd03214 73 --RKI------------AYVP----------QalELLGLAH-LADRP---FNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487090 165 SLGLAPIVVKQIFQTLRELAR-GGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSG 219
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-214 |
2.11e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.44 E-value: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTlLMSI-FG--QPriRGGQILFRGEEISHRSTHYV 77
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKST-LMKIlYGlyQP--DSGEILIDGKPVRIRSPRDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 78 ASGGIA---QAPegrRIFPDMTVEENLLMGTIP-----IGNAHAAEDMQKMFDLFPrLKERRKQRAMTMSGGEQQMLAIA 149
Cdd:COG3845 78 IALGIGmvhQHF---MLVPNLTVAENIVLGLEPtkggrLDRKAARARIRELSERYG-LDVDPDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 150 RALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQ 214
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-225 |
3.11e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 114.86 E-value: 3.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIShrsthyvasggIAQA 85
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-----------TNLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 PEGRRI---------FPDMTVEENLLMG--TIPIGNAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMS 154
Cdd:COG1118 72 PRERRVgfvfqhyalFPHMTVAENIAFGlrVRPPSKAEIRARVEELLELV-QLEGLADRYPSQLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 155 RPTLLLLDEPSLGLAPIVVKQIFQTLREL--ARGGMTIF----LVEqnahhALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRRWLRRLhdELGGTTVFvthdQEE-----ALELADRVVVMNQGRIEQVGTPDEVY 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-223 |
3.47e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.87 E-value: 3.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 20 ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTH----YVAsggiaqapegrRIF--- 92
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYkrakYIG-----------RVFqdp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 93 -----PDMTVEENLLMG---------TIPIGNAHAAE--DMQKMFDLfpRLKERRKQRAMTMSGGEQQMLAIARALMSRP 156
Cdd:COG1101 90 mmgtaPSMTIEENLALAyrrgkrrglRRGLTKKRRELfrELLATLGL--GLENRLDTKVGLLSGGQRQALSLLMATLTKP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487090 157 TLLLLDEPSLGLAPIVVKQIFQTLREL-ARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGED 223
Cdd:COG1101 168 KLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDVSGEE 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-215 |
6.46e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 111.79 E-value: 6.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSI--FGQ--PRIR-GGQILFRGEEISHRSTH 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDlnPEVTiTGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 76 YV----ASGGIAQAPEGrriFPdMTVEENLLMGTIPIGNA------HAAEDMQKMFDLFPRLKERRKQRAMTMSGGEQQM 145
Cdd:PRK14239 81 TVdlrkEIGMVFQQPNP---FP-MSIYENVVYGLRLKGIKdkqvldEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 146 LAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELaRGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-225 |
7.33e-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: 116.86 E-value: 7.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 20 ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGgIAQAPEGRRIFPDmTVEE 99
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ-IGVVLQDVFLFSG-TIRE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 100 NLLMGTIPIG---------NAHAAEDMQKM---FDLfpRLKERrkqrAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLG 167
Cdd:COG2274 568 NITLGDPDATdeeiieaarLAGLHDFIEALpmgYDT--VVGEG----GSNLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 168 LAPIVVKQIFQTLRELARgGMTIFLVeqnAH--HALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:COG2274 642 LDAETEAIILENLRRLLK-GRTVIII---AHrlSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-228 |
1.27e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 112.21 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASG 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 GIAqaPEGRRIFPDMTVEENLLMGTIPIG-NAHAAEDMQKMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLL 159
Cdd:PRK13537 83 GVV--PQFDNLDPDFTVRENLLVFGRYFGlSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 160 LLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQ 228
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-215 |
1.33e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 110.87 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLL--MSIFGQPRirGGQIlfrgeEISHRSTHYVASGGIA 83
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLrvLNLLEMPR--SGTL-----NIAGNHFDFSKTPSDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 84 QAPEGRR----------IFPDMTVEENLLMGTIPIGNAHAAEDMQKMFDLFPRLkeRRKQRA----MTMSGGEQQMLAIA 149
Cdd:PRK11124 76 AIRELRRnvgmvfqqynLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERL--RLKPYAdrfpLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487090 150 RALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-228 |
3.97e-29 |
|
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: 109.31 E-value: 3.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQ-ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIS-------HRSTHYV 77
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReqdpvelRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 78 asggIAQAPegrrIFPDMTVEENLlmGTIPignahaaedmqkmfDLFPRLKERRKQRAM-------------------TM 138
Cdd:cd03295 81 ----IQQIG----LFPHMTVEENI--ALVP--------------KLLKWPKEKIRERADellalvgldpaefadryphEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 139 SGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQIRL 217
Cdd:cd03295 137 SGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQ 216
|
250
....*....|.
gi 2790487090 218 SGSGEDLLGNQ 228
Cdd:cd03295 217 VGTPDEILRSP 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-215 |
4.13e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 109.33 E-value: 4.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLL-------MSIFGQPRIRGGQILFRgEEISHRsthyva 78
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLrvlnlleTPDSGQLNIAGHQFDFS-QKPSEK------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 79 sggiaQAPEGRR----------IFPDMTVEENLLMGTIPIGNAHAAEDMQKMFDLFPRLKERRKQRA--MTMSGGEQQML 146
Cdd:COG4161 76 -----AIRLLRQkvgmvfqqynLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRfpLHLSGGQQQRV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 147 AIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
15-224 |
5.81e-29 |
|
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: 108.97 E-value: 5.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 15 YGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAQapeGRRIFPD 94
Cdd:cd03296 12 FGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQ---HYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 95 MTVEENLLMGTipignahaaeDMQKMFDLFPRLKERRKQRAM---------------TMSGGEQQMLAIARALMSRPTLL 159
Cdd:cd03296 89 MTVFDNVAFGL----------RVKPRSERPPEAEIRAKVHELlklvqldwladrypaQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487090 160 LLDEPSLGLAPIVVKQIFQTLRELA-RGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDL 224
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
16-219 |
8.85e-29 |
|
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: 107.84 E-value: 8.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 16 GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHyvASGGIAQAPEGRRIFPDM 95
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE--ARRRLGFVSDSTGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 96 TVEENLL-MGTIPIGNAHAAED-MQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVV 173
Cdd:cd03266 94 TARENLEyFAGLYGLKGDELTArLEELADRL-GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2790487090 174 KQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSG 219
Cdd:cd03266 173 RALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-236 |
1.22e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 107.92 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYGaiQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHrsthyvasggiaQ 84
Cdd:COG3840 1 MLRLDDLTYRYG--DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA------------L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 85 APEGRRI---------FPDMTVEENLLMGTIPIGNAhAAEDMQKMFDLFPRL----KERRKQRAmtMSGGEQQMLAIARA 151
Cdd:COG3840 67 PPAERPVsmlfqennlFPHLTVAQNIGLGLRPGLKL-TAEQRAQVEQALERVglagLLDRLPGQ--LSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 152 L-MSRPtLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVeqnAHH---ALKLADRGYVMVNGQIRLSGSGEDLLG 226
Cdd:COG3840 144 LvRKRP-ILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMV---THDpedAARIADRVLLVADGRIAADGPTAALLD 219
|
250
....*....|..
gi 2790487090 227 --NQEVRKAYLG 236
Cdd:COG3840 220 gePPPALAAYLG 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-219 |
1.53e-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: 107.38 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 23 QVSLQVNqGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGeeishrsTHYVASG-GIAQAPEGRRI---------F 92
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG-------TVLFDSRkKINLPPQQRKIglvfqqyalF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 93 PDMTVEENLLMGTIPIGNAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIV 172
Cdd:cd03297 88 PHLNVRENLAFGLKRKRNREDRISVDELLDLL-GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2790487090 173 VKQIFQTLREL-ARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSG 219
Cdd:cd03297 167 RLQLLPELKQIkKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-224 |
1.94e-28 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 112.07 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 4 PMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIA 83
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 84 QAPEGRRIFPDMTVEENLLMGTipignAHAAEDMQKMFDLfprLKERRKQRAMTMSGG-----EQQMLAIARALMSRPTL 158
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFGL-----PKRQASMQKMKQL---LAALGCQLDLDSSAGslevaDRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487090 159 LLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDL 224
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-215 |
2.19e-28 |
|
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: 106.57 E-value: 2.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 14 FYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIsHRSTHYVASGGIAQAPeGRRIFP 93
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-KAKERRKSIGYVMQDV-DYQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 94 DmTVEENLLMGTIPIGNAHA-AEDMQKMFDLFpRLKERRKQramTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIV 172
Cdd:cd03226 87 D-SVREELLLGLKELDAGNEqAETVLKDLDLY-ALKERHPL---SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2790487090 173 VKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:cd03226 162 MERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-215 |
5.14e-28 |
|
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: 106.36 E-value: 5.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFY----GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHY 76
Cdd:COG4181 4 SSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 77 VASGgiaqapEGRRI------F---PDMTVEENLLMgtiPI---GNAHAAEDMQKMFDlfpR--LKERRKQRAMTMSGGE 142
Cdd:COG4181 84 RARL------RARHVgfvfqsFqllPTLTALENVML---PLelaGRRDARARARALLE---RvgLGHRLDHYPAQLSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 143 QQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEqnahHALKLA---DRGYVMVNGQI 215
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVT----HDPALAarcDRVLRLRAGRL 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-206 |
1.01e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 105.67 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFY--GAIQA--LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHY 76
Cdd:PRK11629 1 MNKILLQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 77 VAS------GGIAQApegRRIFPDMTVEENLLMGTIpIGNAHAAEDMQKMFDLFPR--LKERRKQRAMTMSGGEQQMLAI 148
Cdd:PRK11629 81 KAElrnqklGFIYQF---HHLLPDFTALENVAMPLL-IGKKKPAEINSRALEMLAAvgLEHRANHRPSELSGGERQRVAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487090 149 ARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVeqnAHHALKLADR 206
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLV---VTHDLQLAKR 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-234 |
1.42e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 103.27 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVA------ 78
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELArrravl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 79 --SGGIAqapegrriFPdMTVEENLLMGTIPIGNAHAAED------MQKMfDLfPRLKERRKQramTMSGGEQQMLAIAR 150
Cdd:COG4559 81 pqHSSLA--------FP-FTVEEVVALGRAPHGSSAAQDRqivreaLALV-GL-AHLAGRSYQ---TLSGGEQQRVQLAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 151 AL-------MSRPTLLLLDEP--SLGLAPivVKQIFQTLRELARGGMTIFLVeqnaHHALKL----ADRGYVMVNGQIRL 217
Cdd:COG4559 147 VLaqlwepvDGGPRWLFLDEPtsALDLAH--QHAVLRLARQLARRGGGVVAV----LHDLNLaaqyADRILLLHQGRLVA 220
|
250
....*....|....*..
gi 2790487090 218 SGSGEDLLGNQEVRKAY 234
Cdd:COG4559 221 QGTPEEVLTDELLERVY 237
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-220 |
1.50e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 105.41 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHrsthyvasg 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 giaQAPEGRRI---------FPDMTVEEN----LLMGTIPigNAHAAE---DMQKMFdlfpRLKERRKQRAMTMSGGEQQ 144
Cdd:PRK09452 81 ---VPAENRHVntvfqsyalFPHMTVFENvafgLRMQKTP--AAEITPrvmEALRMV----QLEEFAQRKPHQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 145 MLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGS 220
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-227 |
1.53e-26 |
|
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: 104.36 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFY----GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFG---QPRIRGGQILFRGEEISHRSthyv 77
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKLS---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 78 asggiaqaPEGRR---------IFPD--------MTVEEnLLMGTIPI-GNAHAAEDMQKMFDLF-----PRLKERRKQR 134
Cdd:COG0444 77 --------EKELRkirgreiqmIFQDpmtslnpvMTVGD-QIAEPLRIhGGLSKAEARERAIELLervglPDPERRLDRY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 135 AMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVeqnAHH---ALKLADRGYVM 210
Cdd:COG0444 148 PHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFI---THDlgvVAEIADRVAVM 224
|
250
....*....|....*..
gi 2790487090 211 VNGQIRLSGSGEDLLGN 227
Cdd:COG0444 225 YAGRIVEEGPVEELFEN 241
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-225 |
1.56e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 107.17 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFY-GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS--GGI 82
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRqiGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 83 AQAPEgrrIFpDMTVEENLLMGTIPIGN---------AHAAEDMQKMfdlfP-----RLKErrkqRAMTMSGGEQQMLAI 148
Cdd:COG1132 420 PQDTF---LF-SGTIRENIRYGRPDATDeeveeaakaAQAHEFIEAL----PdgydtVVGE----RGVNLSGGQRQRIAI 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 149 ARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARgGMTIFLVeqnAH--HALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVI---AHrlSTIRNADRILVLDDGRIVEQGTHEELL 562
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-234 |
2.73e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.92 E-value: 2.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 4 PMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHyVASGGIA 83
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR-AASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 84 QAPEGRRIFPDMTVEENLLMGTIPignaHAAEdmqkmFDLFPRLKERRKQRAM--------------TMSGGEQQMLAIA 149
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTP----HRSR-----FDTWTETDRAAVERAMertgvaqfadrpvtSLSGGERQRVLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 150 RALMSRPTLLLLDEPSlglAPIVVKQIFQTL---RELARGGMTIFLveqnAHHALKLADRgY-----VMVNGQIRLSGSG 221
Cdd:PRK09536 152 RALAQATPVLLLDEPT---ASLDINHQVRTLelvRRLVDDGKTAVA----AIHDLDLAAR-YcdelvLLADGRVRAAGPP 223
|
250
....*....|...
gi 2790487090 222 EDLLGNQEVRKAY 234
Cdd:PRK09536 224 ADVLTADTLRAAF 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-215 |
5.08e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.11 E-value: 5.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 3 EPMLEFHEVDVF-YGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGG 81
Cdd:COG3845 255 EVVLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 82 IAQAPEGRR---IFPDMTVEENLLMGTI---PIGN---------AHAAEDMQKMFDLFPRlkeRRKQRAMTMSGGEQQML 146
Cdd:COG3845 335 VAYIPEDRLgrgLVPDMSVAENLILGRYrrpPFSRggfldrkaiRAFAEELIEEFDVRTP---GPDTPARSLSGGNQQKV 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 147 AIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-225 |
6.27e-26 |
|
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: 100.87 E-value: 6.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHyvaSGGIAQAPEGRRIFPDMTVEEN 100
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE---KRDISYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 101 LLMGtIPIGNAHAAEDMQKMFDLFPRLKER----RKQRamTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQI 176
Cdd:cd03299 92 IAYG-LKKRKVDKKEIERKVLEIAEMLGIDhllnRKPE--TLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790487090 177 FQTLRELAR-GGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:cd03299 169 REELKKIRKeFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-224 |
2.07e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 101.69 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRsthyvasggiaq 84
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDL------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 85 APEGRRI---------FPDMTVEENL-----LMGTIPIGNAHAAEDMQKMFDLFPRLKERRKQramtMSGGEQQMLAIAR 150
Cdd:COG3839 71 PPKDRNIamvfqsyalYPHMTVYENIafplkLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQ----LSGGQRQRVALGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487090 151 ALMSRPTLLLLDEPslgLAPIVVK---QIFQTLREL-ARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDL 224
Cdd:COG3839 147 ALVREPKVFLLDEP---LSNLDAKlrvEMRAEIKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-234 |
2.09e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 99.85 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 4 PMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASggia 83
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 84 qapegRR---------IFPdMTVEENLLMGTIPIGNAHAAED------MQKMfDLFPrLKERRKQramTMSGGEQQMLAI 148
Cdd:PRK13548 77 -----RRavlpqhsslSFP-FTVEEVVAMGRAPHGLSRAEDDalvaaaLAQV-DLAH-LAGRDYP---QLSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 149 ARALM------SRPTLLLLDEP--SLGLApivvKQ--IFQTLRELARggmtiflvEQNAH-----HALKLA----DRGYV 209
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEPtsALDLA----HQhhVLRLARQLAH--------ERGLAvivvlHDLNLAaryaDRIVL 213
|
250 260
....*....|....*....|....*
gi 2790487090 210 MVNGQIRLSGSGEDLLGNQEVRKAY 234
Cdd:PRK13548 214 LHQGRLVADGTPAEVLTPETLRRVY 238
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-222 |
2.09e-25 |
|
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: 98.75 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQP--RIRGGQILFRGEEISHRSTHYVASGGIA---QAPEGrriFPDM 95
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGIFlafQYPPE---IPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 96 TVEENLlmgtipignahaaEDMQKMFdlfprlkerrkqramtmSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQ 175
Cdd:cd03217 93 KNADFL-------------RYVNEGF-----------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2790487090 176 IFQTLRELARGGMTIFLVeqnAHHA--LKL--ADRGYVMVNGQIRLSGSGE 222
Cdd:cd03217 143 VAEVINKLREEGKSVLII---THYQrlLDYikPDRVHVLYDGRIVKSGDKE 190
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-228 |
4.20e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.06 E-value: 4.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSThyVASGGIAQA 85
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR--LARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 PEGRRIFPDMTVEENLLMGTIPIG-NAHAAEDMQKMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEP 164
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRYFGmSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487090 165 SLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQ 228
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-231 |
7.64e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 100.68 E-value: 7.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 4 PMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHyvasggia 83
Cdd:PRK11607 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 84 QAP-----EGRRIFPDMTVEENLLMG--TIPIGNAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRP 156
Cdd:PRK11607 90 QRPinmmfQSYALFPHMTVEQNIAFGlkQDKLPKAEIASRVNEMLGLV-HMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487090 157 TLLLLDEPSLGLAPIVVKQI-FQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEVR 231
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-219 |
7.86e-25 |
|
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: 96.61 E-value: 7.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYG--AIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRS---THYVASg 80
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEkalSSLISV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 gIAQAPegrRIFpDMTVEENLlmgtipignahaaedmqkmfdlfprlkERRkqramtMSGGEQQMLAIARALMSRPTLLL 160
Cdd:cd03247 80 -LNQRP---YLF-DTTLRNNL---------------------------GRR------FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487090 161 LDEPSLGLAPIVVKQIFQTLRELARGGMTIFLveqnAHH--ALKLADRGYVMVNGQIRLSG 219
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWI----THHltGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-219 |
1.30e-24 |
|
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: 96.79 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 25 SLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSthyVASGGIAQAPEGRRIFPDMTVEENLLMG 104
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP---PADRPVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 105 TIPiGNAHAAEDMQKMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRE 182
Cdd:cd03298 95 LSP-GLKLTAEDRQAIEVALARvgLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 2790487090 183 LAR-GGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSG 219
Cdd:cd03298 174 LHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-206 |
1.30e-24 |
|
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: 97.09 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGA-IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISH---RSTHYVASGg 81
Cdd:cd03292 1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgRAIPYLRRK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 82 IAQAPEGRRIFPDMTVEENLLMGTIPIGNAHAaEDMQKMFDLFPRLKERRKQRAMTM--SGGEQQMLAIARALMSRPTLL 159
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVTGVPPR-EIRKRVPAALELVGLSHKHRALPAelSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2790487090 160 LLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLveqnAHHALKLADR 206
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVV----ATHAKELVDT 201
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
14-224 |
1.73e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.95 E-value: 1.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 14 FYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS--GGIAQAPEGRRI 91
Cdd:PRK13652 13 YSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKfvGLVFQNPDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 92 FPdmTVEENLLMGTIPIG-----NAHAAEDMQKMFDlfprLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSL 166
Cdd:PRK13652 93 SP--TVEQDIAFGPINLGldeetVAHRVSSALHMLG----LEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 167 GLAPIVVKQIFQTLRELA-RGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDL 224
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLPeTYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-219 |
5.10e-24 |
|
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: 95.34 E-value: 5.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETvALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASggIAQA 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR--IGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 PEGRRIFPDMTVEENL----LMGTIPIGNAHAAEDMqkMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLL 161
Cdd:cd03264 78 PQEFGVYPNFTVREFLdyiaWLKGIPSKEVKARVDE--VLELV-NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487090 162 DEPSLGLAP---IVVKQIfqtLRELARGGMTIF---LVEQNAHHALKLAdrgyVMVNGQIRLSG 219
Cdd:cd03264 155 DEPTAGLDPeerIRFRNL---LSELGEDRIVILsthIVEDVESLCNQVA----VLNKGKLVFEG 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-210 |
7.67e-24 |
|
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: 95.19 E-value: 7.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 18 IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFR--GEEIShrsthyvasggIAQAPEGR------ 89
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVD-----------LAQASPREilalrr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 90 ----------RIFPDMT----VEENLLMGTIPIGNAHA-AEDM-------QKMFDLFPRlkerrkqramTMSGGEQQMLA 147
Cdd:COG4778 93 rtigyvsqflRVIPRVSaldvVAEPLLERGVDREEARArARELlarlnlpERLWDLPPA----------TFSGGEQQRVN 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487090 148 IARALMSRPTLLLLDEPSLGLAP---IVVKQIfqtLRELARGGMT---IFlveqnaHHA---LKLADRGYVM 210
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAanrAVVVEL---IEEAKARGTAiigIF------HDEevrEAVADRVVDV 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-230 |
7.90e-24 |
|
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: 95.30 E-value: 7.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 7 EFHEVDVFYGA---IQALKQVSLQVNQGETVALIGANGAGKSTLLMSI--FGQPRirGGQILFRGEEISHRSTHYVAS-- 79
Cdd:cd03249 2 EFKNVSFRYPSrpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerFYDPT--SGEILLDGVDIRDLNLRWLRSqi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 80 GGIAQAPEgrrIFpDMTVEENLLMGtipIGNAHAAEDMQ--------KMFDLFP-RLKERRKQRAMTMSGGEQQMLAIAR 150
Cdd:cd03249 80 GLVSQEPV---LF-DGTIAENIRYG---KPDATDEEVEEaakkanihDFIMSLPdGYDTLVGERGSQLSGGQKQRIAIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 151 ALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLveqnAH--HALKLADRGYVMVNGQIRLSGSGEDLLGNQ 228
Cdd:cd03249 153 ALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVI----AHrlSTIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
..
gi 2790487090 229 EV 230
Cdd:cd03249 229 GV 230
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-210 |
8.80e-24 |
|
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: 98.90 E-value: 8.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 4 PMLEFHEVDVFY-GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHyVASGGI 82
Cdd:TIGR02857 320 SSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD-SWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 83 AQAPEGRRIFPDmTVEENLLMGTiPIGNAHAAEDMQKMFDLFPRLKERRK-------QRAMTMSGGEQQMLAIARALMSR 155
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRLAR-PDASDAEIREALERAGLDEFVAALPQgldtpigEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 156 PTLLLLDEPSLGLAPIVVKQIFQTLRELARgGMTIFLVeqnAH--HALKLADRGYVM 210
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLV---THrlALAALADRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-225 |
1.32e-23 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 94.60 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 19 QALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGgIAQAPEGRRIFPDmTVE 98
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRA-IGVVPQDTVLFND-TIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 99 ENLLMGTIPIGN---------AHAAEDMQKMFDLFprlKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLA 169
Cdd:cd03253 93 YNIRYGRPDATDeevieaakaAQIHDKIMRFPDGY---DTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487090 170 PIVVKQIFQTLRELARGGMTIFLveqnAH--HALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:cd03253 170 THTEREIQAALRDVSKGRTTIVI----AHrlSTIVNADKIIVLKDGRIVERGTHEELL 223
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-205 |
1.51e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.10 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 4 PMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRG-----GQILFRGEEISHRSTHY-V 77
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLnR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 78 ASGGIAQAPEGRRIFPdMTVEENLLMGTIPIG------NAHAAEDMQKMFDLFPRLKERRKQRAMTMSGGEQQMLAIARA 151
Cdd:PRK14258 86 LRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwrpkleIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 152 LMSRPTLLLLDEPSLGLAPIV---VKQIFQTLRelARGGMTIFLVEQNAHHALKLAD 205
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIAsmkVESLIQSLR--LRSELTMVIVSHNLHQVSRLSD 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-226 |
2.14e-23 |
|
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: 96.33 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 24 VSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEeishrsTHYVASGGIAQAPEGRRI---------FPD 94
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR------TLFDSRKGIFLPPEKRRIgyvfqearlFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 95 MTVEENLLMG---TIPIGNAHAAEDMQKMFDLFPrLKERRKQRamtMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPI 171
Cdd:TIGR02142 90 LSVRGNLRYGmkrARPSERRISFERVIELLGIGH-LLGRLPGR---LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487090 172 VVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLG 226
Cdd:TIGR02142 166 RKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-222 |
2.57e-23 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 97.38 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAQAPEGRR---IFPDMTV 97
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 98 EENL----------LMGTIpignAHAAEDM--QKMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPS 165
Cdd:PRK10762 348 KENMsltalryfsrAGGSL----KHADEQQavSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 166 LGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIrlsgSGE 222
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI----SGE 476
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
21-234 |
2.78e-23 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 94.25 E-value: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQP--RIRGGQILFRGEEISHRSTHYVASGGI---AQAPEGrriFPDM 95
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPsyEVTSGTILFKGQDLLELEPDERARAGLflaFQYPEE---IPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 96 TVEEnLLMGTIPIGNAHAAEDMQKMFDLFPRLKERRKQRAMT-----------MSGGEQQMLAIARALMSRPTLLLLDEP 164
Cdd:TIGR01978 93 SNLE-FLRSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDeeflnrsvnegFSGGEKKRNEILQMALLEPKLAILDEI 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487090 165 SLGLAPIVVKQIFQTLRELARGGMTIFLVeqnAHHA--LKL--ADRGYVMVNGQIRLSGSGEdlLGNQEVRKAY 234
Cdd:TIGR01978 172 DSGLDIDALKIVAEGINRLREPDRSFLII---THYQrlLNYikPDYVHVLLDGRIVKSGDVE--LAKELEAKGY 240
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-227 |
3.58e-23 |
|
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: 93.41 E-value: 3.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYG----AIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSthyvasg 80
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLS------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 GIAQAPEGRRI---------FPDMTVEENLlmgTIPIGNAHA--AEDMQKMFDL--FPRLKERRKQRAMTMSGGEQQMLA 147
Cdd:cd03258 74 GKELRKARRRIgmifqhfnlLSSRTVFENV---ALPLEIAGVpkAEIEERVLELleLVGLEDKADAYPAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 148 IARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLREL-ARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLG 226
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
.
gi 2790487090 227 N 227
Cdd:cd03258 231 N 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-193 |
6.03e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.52 E-value: 6.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 3 EPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGI 82
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 83 AQAPEGRRIFPDMTVEENLLMGTIP--IG-------NAHAAEDMQKM-FDLFPRLKERRkqramtMSGGEQQMLAIARAL 152
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLGQLPhkGGivnrrllNYEAREQLEHLgVDIDPDTPLKY------LSIGQRQMVEIAKAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2790487090 153 MSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLV 193
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYV 196
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-216 |
6.49e-23 |
|
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: 92.32 E-value: 6.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRsthYVASGGIAQA 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL---PPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 PEGRRIFPDMTVEENL-----LMGTIPIGNAHAAEDMQKMFDLFPRLKERRKQramtMSGGEQQMLAIARALMSRPTLLL 160
Cdd:cd03301 78 FQNYALYPHMTVYDNIafglkLRKVPKDEIDERVREVAELLQIEHLLDRKPKQ----LSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 161 LDEPSLGLAPIVVKQIFQTLREL-ARGGMTIFLVEQNAHHALKLADRGYVMVNGQIR 216
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
15-206 |
6.62e-23 |
|
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: 92.29 E-value: 6.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 15 YGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSThyvasggiAQAPEGRR---- 90
Cdd:TIGR03608 8 FGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNS--------KKASKFRReklg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 91 -IFPDM------TVEENLLMGTIPIgNAHAAEDMQKMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLL 161
Cdd:TIGR03608 80 yLFQNFalieneTVEENLDLGLKYK-KLSKKEKREKKKEALEKvgLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2790487090 162 DEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHAlKLADR 206
Cdd:TIGR03608 159 DEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADR 202
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-219 |
9.58e-23 |
|
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: 92.33 E-value: 9.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 19 QALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGqpRIRG-----GQILFRGEEISHRSTHYVasggIAQAPEGRRIFP 93
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG--RVEGggttsGQILFNGQPRKPDQFQKC----VAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 94 DMTVEENLLMGTIPIGNAHAAEDMQKMFDLFPRLKE-----RRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGL 168
Cdd:cd03234 95 GLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDlaltrIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2790487090 169 APIVVKQIFQTLRELARGGMTIFL-VEQNAHHALKLADRGYVMVNGQIRLSG 219
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-215 |
1.11e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 95.75 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 24 VSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAQAPEGRR---IFPDMTVEEN 100
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 101 LLMG----TIPIGN--------AHAAEDMQKMfdlfpRLKER-RKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLG 167
Cdd:PRK11288 352 INISarrhHLRAGClinnrweaENADRFIRSL-----NIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2790487090 168 LAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:PRK11288 427 IDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-225 |
1.50e-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: 91.90 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 7 EFHEVDVFY-GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGgIAQA 85
Cdd:cd03254 4 EFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM-IGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 PEGRRIFPDmTVEENLLMGTipigNAHAAEDMQKM-----FDLFPR-----LKERRKQRAMTMSGGEQQMLAIARALMSR 155
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGR----PNATDEEVIEAakeagAHDFIMklpngYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487090 156 PTLLLLDEPSLGLAPIVVKQIFQTLRELaRGGMTIFLVeqnAHH--ALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIII---AHRlsTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
19-231 |
1.68e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 92.12 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 19 QALKQVSLQVNQGETVALIGANGAGKSTLLMSI--FGQP---RIRGGQILFRGEE-ISHRSTHYVA----SGGIAQapeG 88
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlLEQPeagTIRVGDITIDTARsLSQQKGLIRQlrqhVGFVFQ---N 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 89 RRIFPDMTVEENLLMGTIPIGNAHAAEDMQKMFDLFPRLKERRKQRAMT--MSGGEQQMLAIARALMSRPTLLLLDEPSL 166
Cdd:PRK11264 94 FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPrrLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487090 167 GLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGN-QEVR 231
Cdd:PRK11264 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADpQQPR 239
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-236 |
2.38e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.36 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 20 ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS---GGIAQAPEGRriFPDMT 96
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRklvGIVFQNPETQ--FVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 97 VEENLLMGtiPIGNAHAAEDMQKMFDLF---PRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVV 173
Cdd:PRK13644 95 VEEDLAFG--PENLCLPPIEIRKRVDRAlaeIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487090 174 KQIFQTLRELARGGMTIFLVEQNAHHaLKLADRGYVMVNGQIRLSGSGEDLLGNQEVRkaYLG 236
Cdd:PRK13644 173 IAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ--TLG 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-224 |
2.43e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.61 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAQA 85
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 pegRRIFPDMTVEENLLMGTI-------PIGNAHAAEDMQ--KMFDLfPRLKERRKQRamtMSGGEQQMLAIARALMSRP 156
Cdd:PRK10851 83 ---YALFRHMTVFDNIAFGLTvlprrerPNAAAIKAKVTQllEMVQL-AHLADRYPAQ---LSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 157 TLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDL 224
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-189 |
2.73e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 94.61 E-value: 2.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTlLMSIFGQPRIRG---GQILFRGEEISHRSTHYV 77
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKST-LMKVLSGVYPHGtyeGEIIFEGEELQASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 78 ASGGIAQAPEGRRIFPDMTVEENLLMGTIPIgnAHAAEDMQKMFDLFPRLKERRK------QRAMTMSGGEQQMLAIARA 151
Cdd:PRK13549 80 ERAGIAIIHQELALVKELSVLENIFLGNEIT--PGGIMDYDAMYLRAQKLLAQLKldinpaTPVGNLGLGQQQLVEIAKA 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 2790487090 152 LMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMT 189
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIA 195
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-222 |
2.96e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 91.28 E-value: 2.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQP--RIRGGQILFRGEEISHRSTHYVASGGIA---QAPEgrRIfPDM 95
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERARAGIFlafQYPV--EI-PGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 96 TVEeNLLMGTIpigNAHAAEDMqKMFDLFPRLKERRKQRAMTM-----------SGGEQQMLAIARALMSRPTLLLLDEP 164
Cdd:COG0396 93 SVS-NFLRTAL---NARRGEEL-SAREFLKLLKEKMKELGLDEdfldryvnegfSGGEKKRNEILQMLLLEPKLAILDET 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487090 165 SLGLAPIVVKQIFQTLRELARGGMTIFLVeqnAHHA--LKL--ADRGYVMVNGQIRLSGSGE 222
Cdd:COG0396 168 DSGLDIDALRIVAEGVNKLRSPDRGILII---THYQriLDYikPDFVHVLVDGRIVKSGGKE 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-226 |
3.81e-22 |
|
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: 90.75 E-value: 3.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYG--AIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIfgqPR---IRGGQILFRGEEISHRSTHYVASg 80
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI---PRfydVDSGRILIDGHDVRDYTLASLRR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 GIAQAPEGRRIFPDmTVEENLLMGTIPIG---------NAHAAEDMQKMFDlfpRLKERRKQRAMTMSGGEQQMLAIARA 151
Cdd:cd03251 77 QIGLVSQDVFLFND-TVAENIAYGRPGATreeveeaarAANAHEFIMELPE---GYDTVIGERGVKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 152 LMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARgGMTIFLVeqnAHH--ALKLADRGYVMVNGQIRLSGSGEDLLG 226
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVI---AHRlsTIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-215 |
7.63e-22 |
|
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: 89.57 E-value: 7.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGA--IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRStHYVASGGIA 83
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD-PADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 84 QAPEGRRIFPDmTVEENLLMGTIPIGNA---HAAE--DMQKMFDLFPRLKERR-KQRAMTMSGGEQQMLAIARALMSRPT 157
Cdd:cd03245 82 YVPQDVTLFYG-TLRDNITLGAPLADDErilRAAElaGVTDFVNKHPNGLDLQiGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487090 158 LLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAhhALKLADRGYVMVNGQI 215
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPS--LLDLVDRIIVMDSGRI 216
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-231 |
8.03e-22 |
|
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: 92.09 E-value: 8.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 23 QVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEeishrsTHYVASGGIAQAPEGRRI---------FP 93
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE------VLQDSARGIFLPPHRRRIgyvfqearlFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 94 DMTVEENLLMGTIPIGNAHAAEDMQKMFDLF---PRLKerrkQRAMTMSGGEQQMLAIARALMSRPTLLLLDEP--SLGL 168
Cdd:COG4148 91 HLSVRGNLLYGRKRAPRAERRISFDEVVELLgigHLLD----RRPATLSGGERQRVAIGRALLSSPRLLLMDEPlaALDL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 169 ApivVKQ-IFQTLRELAR-GGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEVR 231
Cdd:COG4148 167 A---RKAeILPYLERLRDeLDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLL 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-227 |
8.59e-22 |
|
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: 93.21 E-value: 8.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYGA----IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFG----QPRIRGGQILFRGEEISHr 72
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRllpdPAAHPSGSILFDGQDLLG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 73 sthyvasggiaqAPE-------GRRI---F--------PDMTVEENLLMGTIPIGNAHAAEDMQKMFDLF-----PRLKE 129
Cdd:COG4172 81 ------------LSErelrrirGNRIamiFqepmtslnPLHTIGKQIAEVLRLHRGLSGAAARARALELLervgiPDPER 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 130 RRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLREL-ARGGMTIFLVEqnahHAL----KLA 204
Cdd:COG4172 149 RLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLIT----HDLgvvrRFA 224
|
250 260
....*....|....*....|...
gi 2790487090 205 DRGYVMVNGQIRLSGSGEDLLGN 227
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFAA 247
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-224 |
8.75e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.19 E-value: 8.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 22 KQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAQAPEGRR---IFPDMTVE 98
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQssgLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 99 EN---LLMGTIPIGNAHAAEdmQKMFDLFPR---LK-ERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPI 171
Cdd:PRK15439 360 WNvcaLTHNRRGFWIKPARE--NAVLERYRRalnIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2790487090 172 VVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDL 224
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-205 |
1.70e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.84 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 3 EPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLmSIFGQ-----PRIRG-GQILFRGEEISHRSTHY 76
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTIL-RCFNRlndliPGFRVeGKVTFHGKNLYAPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 77 VAS----GGIAQAPEGrriFPDmTVEENLLMGtiPIGNAHAAeDMQKMFD-------LFPRLKERRKQRAMTMSGGEQQM 145
Cdd:PRK14243 87 VEVrrriGMVFQKPNP---FPK-SIYDNIAYG--ARINGYKG-DMDELVErslrqaaLWDEVKDKLKQSGLSLSGGQQQR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 146 LAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARgGMTIFLVEQNAHHALKLAD 205
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE-QYTIIIVTHNMQQAARVSD 218
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-220 |
1.71e-21 |
|
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: 88.70 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFY--GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS--GG 81
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSriSI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 82 IAQAPEgrrIFPDmTVEENLlmgtIPIGNA------HAAEDMQkmfdlfprLKERRKQRAMTM-----------SGGEQQ 144
Cdd:cd03244 83 IPQDPV---LFSG-TIRSNL----DPFGEYsdeelwQALERVG--------LKEFVESLPGGLdtvveeggenlSVGQRQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487090 145 MLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRElARGGMTIFLVeqnAH--HALKLADRGYVMVNGQIRLSGS 220
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTI---AHrlDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-219 |
1.91e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.78 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFY-GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVA--SGG 81
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 82 IAQAPEGRRIFPDMTVEENLLMGTIPIGNAhaAEDMQKMFDLFPR---LKERRKQRAMTMSGGEQQMLAIARALMSRPTL 158
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGAS--GDDIRRRVSAALDkvgLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487090 159 LLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVeqnAHHALKLADRGY-VMVNGQIRLSG 219
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMA---THDIGLISRRSYrMLTLSDGHLHG 217
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-236 |
2.06e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.87 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 25 SLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEisHRSThyvasgGIAQAP-----EGRRIFPDMTVEE 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--HTTT------PPSRRPvsmlfQENNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 100 NLLMGTIPiG---NAHAAEDMQKMF------DLFPRLKERrkqramtMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAP 170
Cdd:PRK10771 91 NIGLGLNP-GlklNAAQREKLHAIArqmgieDLLARLPGQ-------LSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 171 IVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEVRKAYLG 236
Cdd:PRK10771 163 ALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALLG 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-228 |
2.26e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 92.20 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 2 NEPMLEFHEVDVFY--GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISH------RS 73
Cdd:PRK11160 335 DQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADyseaalRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 74 THYVASggiaQAPEgrrIFPDmTVEENLLMGTIPIGNAHAAEDMQ-----KMFDLFPRLK----ERRKQramtMSGGEQQ 144
Cdd:PRK11160 415 AISVVS----QRVH---LFSA-TLRDNLLLAAPNASDEALIEVLQqvgleKLLEDDKGLNawlgEGGRQ----LSGGEQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 145 MLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLveqnAH--HALKLADRGYVMVNGQIRLSGSGE 222
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMI----THrlTGLEQFDRICVMDNGQIIEQGTHQ 558
|
....*.
gi 2790487090 223 DLLGNQ 228
Cdd:PRK11160 559 ELLAQQ 564
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-227 |
2.58e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 89.26 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISH-RSTH---Y 76
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvRDKDgqlK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 77 VASGGIAQAPEGR--------RIFPDMTVEENLLMGTIPI---GNAHAAEDMQKMFDLFPRLKERRKQRAMTMSGGEQQM 145
Cdd:PRK10619 81 VADKNQLRLLRTRltmvfqhfNLWSHMTVLENVMEAPIQVlglSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 146 LAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
..
gi 2790487090 226 GN 227
Cdd:PRK10619 241 GN 242
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-235 |
4.94e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.00 E-value: 4.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 22 KQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAQAPEGRR---IFPDMTVE 98
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 99 ENL-------------LMGTI-PIGNAHAAEDMQKMFDLFPRLKErrkQRAMTMSGGEQQMLAIARALMSRPTLLLLDEP 164
Cdd:PRK09700 360 QNMaisrslkdggykgAMGLFhEVDEQRTAENQRELLALKCHSVN---QNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487090 165 SLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEVRKAYL 235
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEIMAWAL 507
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-190 |
5.64e-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: 90.88 E-value: 5.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 3 EPMLEFHEVDVFY-GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS-- 79
Cdd:TIGR02868 332 KPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRrv 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 80 GGIAQAPEgrrIFpDMTVEENLLmgtipIGNAHAA-EDMQKMF----------DLFPRLKERRKQRAMTMSGGEQQMLAI 148
Cdd:TIGR02868 412 SVCAQDAH---LF-DTTVRENLR-----LARPDATdEELWAALervgladwlrALPDGLDTVLGEGGARLSGGERQRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2790487090 149 ARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTI 190
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVV 524
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-229 |
5.94e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.57 E-value: 5.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 20 ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYV----ASGGIAQAPEgRRIFPDm 95
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSdirkKVGLVFQYPE-YQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 96 TVEENLLMGTIPIGnahaaedmqkmfdLFPRLKERRKQRAMTM----------------SGGEQQMLAIARALMSRPTLL 159
Cdd:PRK13637 100 TIEKDIAFGPINLG-------------LSEEEIENRVKRAMNIvgldyedykdkspfelSGGQKRRVAIAGVVAMEPKIL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487090 160 LLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQE 229
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVE 237
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-214 |
9.74e-21 |
|
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: 90.27 E-value: 9.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTlLMSIFGQPRIRG---GQILFRGEEISHRSTHYVASGG 81
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKST-LMKILSGVYPHGtwdGEIYWSGSPLKASNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 82 IAQAPEGRRIFPDMTVEENLLMG---TIPIGNAHAAEDMQKMFDLFPRLK---ERRKQRAMTMSGGEQQMLAIARALMSR 155
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGneiTLPGGRMAYNAMYLRAKNLLRELQldaDNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 156 PTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQ 214
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-215 |
1.01e-20 |
|
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: 87.55 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 19 QALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSthyvasggiaqaPEGRRIF------ 92
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLD------------RKQRRAFrrdvql 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 93 ----------PDMTVE-------ENLLMGTIPIGNAHAAEdMQKMFDLFPRLKERRKQRamtMSGGEQQMLAIARALMSR 155
Cdd:TIGR02769 93 vfqdspsavnPRMTVRqiigeplRHLTSLDESEQKARIAE-LLDMVGLRSEDADKLPRQ---LSGGQLQRINIARALAVK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487090 156 PTLLLLDEPSLGLAPIVVKQIFQTLREL-ARGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:TIGR02769 169 PKLIVLDEAVSNLDMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-215 |
1.11e-20 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 86.07 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQpRIRG---GQILFRGEEISHRSTHYVasggIAQAPEGRRIFPDMTV 97
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGR-RTGLgvsGEVLINGRPLDKRSFRKI----IGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 98 EENLLMgtipignahAAEdmqkmfdlfprLKerrkqramTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIF 177
Cdd:cd03213 100 RETLMF---------AAK-----------LR--------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 2790487090 178 QTLRELARGGMT-IFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:cd03213 152 SLLRRLADTGRTiICSIHQPSSEIFELFDKLLLLSQGRV 190
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-231 |
1.22e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.84 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASG 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 GIAQAPEGRRIFPDMTVEENLLMGTIPIG-----NAHAAEDMQK---MFDLFPRLKERRKQRAMTMSGGEQQMLAIARAL 152
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLYIGRHLTKkvcgvNIIDWREMRVraaMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 153 MSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEVR 231
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-231 |
1.50e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 88.39 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 19 QALKQVSLQVN-----QGETvALIGANGAGKSTLLMSIFG-----QPRIR-GGQILFRGEEishrsthyvasgGIAQAPE 87
Cdd:PRK11144 8 QQLGDLCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGltrpqKGRIVlNGRVLFDAEK------------GICLPPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 88 GRRI---------FPDMTVEENLLMGTipignahaAEDMQKMFD----------LFPRLkerrkqrAMTMSGGEQQMLAI 148
Cdd:PRK11144 75 KRRIgyvfqdarlFPHYKVRGNLRYGM--------AKSMVAQFDkivallgiepLLDRY-------PGSLSGGEKQRVAI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 149 ARALMSRPTLLLLDEP--SLGLAPivVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:PRK11144 140 GRALLTAPELLLMDEPlaSLDLPR--KRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVW 217
|
....*.
gi 2790487090 226 GNQEVR 231
Cdd:PRK11144 218 ASSAMR 223
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-225 |
1.52e-20 |
|
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: 89.78 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGA--IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIfgqPR---IRGGQILFRGEEISHRSTHYVASG 80
Cdd:TIGR02203 331 VEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLI---PRfyePDSGQILLDGHDLADYTLASLRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 gIAQAPEGRRIFPDmTVEENLL---MGTIP---IGNAHAAEDMQKMFDLFPR-LKERRKQRAMTMSGGEQQMLAIARALM 153
Cdd:TIGR02203 408 -VALVSQDVVLFND-TIANNIAygrTEQADraeIERALAAAYAQDFVDKLPLgLDTPIGENGVLLSGGQRQRLAIARALL 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487090 154 SRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLveqnAHH--ALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLMQGRTTLVI----AHRlsTIEKADRIVVMDDGRIVERGTHNELL 555
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-237 |
1.69e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.89 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLL------MSIFGQPRIRG-----GQILFRGEEISHRST 74
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrlIELYPEARVSGevyldGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 75 HYVasggIAQAPEGrriFPDMTVEENLLMGTIPIGNAHAAEDMQKMF-------DLFPRLKERRKQRAMTMSGGEQQMLA 147
Cdd:PRK14247 84 VQM----VFQIPNP---IPNLSIFENVALGLKLNRLVKSKKELQERVrwalekaQLWDEVKDRLDAPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 148 IARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARgGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGN 227
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
250
....*....|..
gi 2790487090 228 --QEVRKAYLGG 237
Cdd:PRK14247 236 prHELTEKYVTG 247
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-229 |
1.85e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 87.83 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 17 AIQALKQVSLQVNQGETVALIGANGAGKSTLL--MSIFGQPRIRGGQILFRGEEISHRSTHY--VASGGIAQAPEGRRI- 91
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIehLNALLLPDTGTIEWIFKDEKNKKKTKEKekVLEKLVIQKTRFKKIk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 92 --------------FPDM-----TVEENLLMGTIPIG--NAHAAEDMQKMFDLFPrLKERRKQRA-MTMSGGEQQMLAIA 149
Cdd:PRK13651 99 kikeirrrvgvvfqFAEYqlfeqTIEKDIIFGPVSMGvsKEEAKKRAAKYIELVG-LDESYLQRSpFELSGGQKRRVALA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 150 RALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQE 229
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDNK 257
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-164 |
2.75e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.97 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 15 YGAIQALKQVSLQVNQGETVALIGANGAGKSTLLmsifgqpRIRGGQI-LFRGeEISHRSTHYVASggIAQAPEgrrIFP 93
Cdd:COG0488 8 FGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLL-------KILAGELePDSG-EVSIPKGLRIGY--LPQEPP---LDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 94 DMTVEENLLMGTIPIGN------------AHAAEDMQKMFDLFPRLK-------ERRKQRAM---------------TMS 139
Cdd:COG0488 75 DLTVLDTVLDGDAELRAleaeleeleaklAEPDEDLERLAELQEEFEalggweaEARAEEILsglgfpeedldrpvsELS 154
|
170 180
....*....|....*....|....*
gi 2790487090 140 GGEQQMLAIARALMSRPTLLLLDEP 164
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEP 179
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-164 |
5.33e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.46 E-value: 5.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQ--PRIRG-GQILFRGEEISHRsthyvasgg 81
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSAsGEVLLNGRRLTAL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 82 iaqAPEGRRI---------FPDMTVEENLLmgtipignahaaedmqkmFDLFPRL-KERRKQRAM--------------- 136
Cdd:COG4136 72 ---PAEQRRIgilfqddllFPHLSVGENLA------------------FALPPTIgRAQRRARVEqaleeaglagfadrd 130
|
170 180 190
....*....|....*....|....*....|
gi 2790487090 137 --TMSGGEQQMLAIARALMSRPTLLLLDEP 164
Cdd:COG4136 131 paTLSGGQRARVALLRALLAEPRALLLDEP 160
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-215 |
8.26e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 86.39 E-value: 8.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVD-VFYGA---IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSthyvaSG 80
Cdd:PRK11153 1 MIELKNISkVFPQGgrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALS-----EK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 GIAQApegRR----IFPDM------TVEENLLMgtiP--IGNAHAAEDMQKMFDLFPR--LKERRKQRAMTMSGGEQQML 146
Cdd:PRK11153 76 ELRKA---RRqigmIFQHFnllssrTVFDNVAL---PleLAGTPKAEIKARVTELLELvgLSDKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487090 147 AIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEqnahHAL----KLADRGYVMVNGQI 215
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLIT----HEMdvvkRICDRVAVIDAGRL 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-215 |
9.22e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.12 E-value: 9.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 16 GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSThyvasggiAQAPEGRR----I 91
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR--------AQRKAFRRdiqmV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 92 F--------PDMTVEENL------LMGTIPIGNAHAAEDMQKMFDLFPRLKERRKQRamtMSGGEQQMLAIARALMSRPT 157
Cdd:PRK10419 95 FqdsisavnPRKTVREIIreplrhLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ---LSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 158 LLLLDEPSLGLAPIVVKQIFQTLREL-ARGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-227 |
9.63e-20 |
|
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: 87.43 E-value: 9.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 16 GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFG-QPRirGGQILFRGEEISHRSTHyvasggiAQAPEGRRI--- 91
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRlIPS--EGEIRFDGQDLDGLSRR-------ALRPLRRRMqvv 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 92 F--------PDMTVEEnllmgTIpignahaAEDMQKmfdLFPRLKER-RKQRAMTM------------------SGGEQQ 144
Cdd:COG4172 368 FqdpfgslsPRMTVGQ-----II-------AEGLRV---HGPGLSAAeRRARVAEAleevgldpaarhryphefSGGQRQ 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 145 MLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLREL-ARGGMT-IFLveqnaHHALK----LADRGYVMVNGQIRLS 218
Cdd:COG4172 433 RIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAyLFI-----SHDLAvvraLAHRVMVMKDGKVVEQ 507
|
....*....
gi 2790487090 219 GSGEDLLGN 227
Cdd:COG4172 508 GPTEQVFDA 516
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-213 |
9.92e-20 |
|
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: 84.44 E-value: 9.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIShrsthyvasggiAQAPEGRRIF------PD 94
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT------------EPGPDRMVVFqnysllPW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 95 MTVEENLLMGTIPIGNAHAAEDMQKMFD---LFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPI 171
Cdd:TIGR01184 69 LTVRENIALAVDRVLPDLSKSERRAIVEehiALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2790487090 172 VVKQIFQTLRELAR-GGMTIFLVEQNAHHALKLADRGYVMVNG 213
Cdd:TIGR01184 149 TRGNLQEELMQIWEeHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-214 |
1.51e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.60 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 2 NEPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGG 81
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 82 IAQAPEGRRIFPDMTVEENLLMGTIPIgNAHAAEDMQKMFD----LFPRLKERR--KQRAMTMSGGEQQMLAIARALMSR 155
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLGREFV-NRFGRIDWKKMYAeadkLLARLNLRFssDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487090 156 PTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEqnahHALK----LADRGYVMVNGQ 214
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYIS----HRLKeifeICDDVTVFRDGQ 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-214 |
1.54e-19 |
|
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: 83.29 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 20 ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGeeishrSTHYVAsggiaQAPegrRIFPDmTVEE 99
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------SIAYVS-----QEP---WIQNG-TIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 100 NLLMGtipignahAAEDMQKM------------FDLFPRLKERR-KQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSL 166
Cdd:cd03250 85 NILFG--------KPFDEERYekvikacalepdLEILPDGDLTEiGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2790487090 167 GLAPIVVKQIFQT-LRELARGGMTIFLVEQNAHHaLKLADRGYVMVNGQ 214
Cdd:cd03250 157 AVDAHVGRHIFENcILGLLLNNKTRILVTHQLQL-LPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-215 |
1.58e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 84.68 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFY--GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVA 78
Cdd:PRK13635 1 MKEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 79 S--GGIAQAPEGRriFPDMTVEENLLMGTIPIGNAHaaEDMQKmfdlfpRLKERRKQRAMT---------MSGGEQQMLA 147
Cdd:PRK13635 81 RqvGMVFQNPDNQ--FVGATVQDDVAFGLENIGVPR--EEMVE------RVDQALRQVGMEdflnrephrLSGGQKQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 148 IARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELAR-GGMTIFLVEQNAHHALKlADRGYVMVNGQI 215
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDEAAQ-ADRVIVMNKGEI 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-238 |
2.60e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 83.74 E-value: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLL------MSIFGQPRIRGGQILFrGEEISHRSTHYV-- 77
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrlLELNEEARVEGEVRLF-GRNIYSPDVDPIev 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 78 --ASGGIAQAPEGrriFPDMTVEENLLMGTIPIGNAHAAEDMQKMFD-------LFPRLKERRKQRAMTMSGGEQQMLAI 148
Cdd:PRK14267 84 rrEVGMVFQYPNP---FPHLTIYDNVAIGVKLNGLVKSKKELDERVEwalkkaaLWDEVKDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 149 ARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELaRGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGN- 227
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENp 239
|
250
....*....|..
gi 2790487090 228 -QEVRKAYLGGV 238
Cdd:PRK14267 240 eHELTEKYVTGA 251
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-227 |
3.26e-19 |
|
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: 83.85 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 16 GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEI---SHRSTHYVASGGIAQAPEGRRIF 92
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamSRKELRELRRKKISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 93 PDMTVEENLLMGtIPIGNAHAAEDMQKMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAP 170
Cdd:cd03294 115 PHRTVLENVAFG-LEVQGVPRAEREERAAEALELvgLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487090 171 IVVKQIFQTLREL-ARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGN 227
Cdd:cd03294 194 LIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-220 |
3.57e-19 |
|
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: 85.65 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 18 IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQ-PRIRGGQILFRGEEISHRSTHYVASGGIAQAPEGRR---IFP 93
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 94 DMTVEENLLMGTIP----IGNAHAAEDMQKMFDLFPRLKERRKQRAM---TMSGGEQQMLAIARALMSRPTLLLLDEPSL 166
Cdd:TIGR02633 353 ILGVGKNITLSVLKsfcfKMRIDAAAELQIIGSAIQRLKVKTASPFLpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790487090 167 GLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRgyVMVNGQIRLSGS 220
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDR--VLVIGEGKLKGD 484
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-225 |
4.35e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 83.98 E-value: 4.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 18 IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFG--QPriRGGQILFRGEEISHRSTHYVasggiaqapegRRI---- 91
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGilVP--TSGEVRVLGYVPFKRRKEFA-----------RRIgvvf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 92 ------FPDMTVEENL-LMGTI-PIGNAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGeQQMLA-IARALMSRPTLLLLD 162
Cdd:COG4586 102 gqrsqlWWDLPAIDSFrLLKAIyRIPDAEYKKRLDELVELL-DLGELLDTPVRQLSLG-QRMRCeLAAALLHRPKILFLD 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487090 163 EPSLGLAPIVVKQIFQTLREL-ARGGMTIFL-------VEQnahhalkLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYnRERGTTILLtshdmddIEA-------LCDRVIVIDHGRIIYDGSLEELK 243
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-238 |
4.36e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 84.36 E-value: 4.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFY----GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSthyvaSG 80
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALS-----ER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 GIAQApegRR----IF------PDMTVEENLlmgtipignahaaedmqkmfdLFP-RL----KERRKQRAMTM------- 138
Cdd:COG1135 76 ELRAA---RRkigmIFqhfnllSSRTVAENV---------------------ALPlEIagvpKAEIRKRVAELlelvgls 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 139 ----------SGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLREL-ARGGMTIFLVEQNAHHALKLADRG 207
Cdd:COG1135 132 dkadaypsqlSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInRELGLTIVLITHEMDVVRRICDRV 211
|
250 260 270
....*....|....*....|....*....|...
gi 2790487090 208 YVMVNGQIRLSGSGEDLLGN--QEVRKAYLGGV 238
Cdd:COG1135 212 AVLENGRIVEQGPVLDVFANpqSELTRRFLPTV 244
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-224 |
5.35e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.39 E-value: 5.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSthyVASG 80
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS---IQQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 GIAQAPEGRRIFPDMTVEENLLMGTipignahaaeDMQKmfdlfpRLKERRKQR---AMTM--------------SGGEQ 143
Cdd:PRK11432 79 DICMVFQSYALFPHMSLGENVGYGL----------KMLG------VPKEERKQRvkeALELvdlagfedryvdqiSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 144 QMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLREL-ARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGE 222
Cdd:PRK11432 143 QRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQ 222
|
..
gi 2790487090 223 DL 224
Cdd:PRK11432 223 EL 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
19-222 |
5.79e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.14 E-value: 5.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 19 QALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGqpRIRGGQILFRGEEISHRSTHyvASGGIAQAPEGRR-----IFP 93
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSG--LITGDKSAGSHIELLGRTVQ--REGRLARDIRKSRantgyIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 94 D------MTVEENLLMGTIpignaHAAEDMQKMFDLFPRLKERRK--------------QRAMTMSGGEQQMLAIARALM 153
Cdd:PRK09984 94 QfnlvnrLSVLENVLIGAL-----GSTPFWRTCFSWFTREQKQRAlqaltrvgmvhfahQRVSTLSGGQQQRVAIARALM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 154 SRPTLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGE 222
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-219 |
7.88e-19 |
|
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: 81.81 E-value: 7.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 15 YGAIQALKQVSLQVNQGETVALIGANGAGKSTLLmsifgqpRIRGGQIL-FRGEEISHRSTHYV--ASGGIAqapegrri 91
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLL-------RLLAGIYPpDSGTVTVRGRVSSLlgLGGGFN-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 92 fPDMTVEENL-LMGTIpigNAHAAEDMQKMFDL---FPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEpslG 167
Cdd:cd03220 97 -PELTGRENIyLNGRL---LGLSRKEIDEKIDEiieFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE---V 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 168 LApiVVKQIFQ-----TLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSG 219
Cdd:cd03220 170 LA--VGDAAFQekcqrRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
8.29e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.97 E-value: 8.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYG-AIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYV-- 77
Cdd:PRK13636 1 MEDYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMkl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 78 --ASGGIAQAPEgRRIFpDMTVEENLLMGTIPIGnaHAAEDMQKMFDlfpRLKER------RKQRAMTMSGGEQQMLAIA 149
Cdd:PRK13636 81 reSVGMVFQDPD-NQLF-SASVYQDVSFGAVNLK--LPEDEVRKRVD---NALKRtgiehlKDKPTHCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 150 RALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQ 228
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
....*...
gi 2790487090 229 EV-RKAYL 235
Cdd:PRK13636 234 EMlRKVNL 241
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-215 |
1.38e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 84.01 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 20 ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAQAPEGRR---IFPDMT 96
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEERRstgIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 97 VEENLLMGTI-----PIG---NAHAAEDMQKMFDLFpRLKERRKQRAM-TMSGGEQQMLAIARALMSRPTLLLLDEPSLG 167
Cdd:PRK10982 343 IGFNSLISNIrnyknKVGlldNSRMKSDTQWVIDSM-RVKTPGHRTQIgSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2790487090 168 LAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:PRK10982 422 IDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-235 |
1.52e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 81.96 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 2 NEPMLEFHEVDVFYGAIQ--ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS 79
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 80 --GGIAQAPEGRriFPDMTVEENllmgtIPIGNAHAAEDMQKMFDLFPRL------KERRKQRAMTMSGGEQQMLAIARA 151
Cdd:PRK13632 84 kiGIIFQNPDNQ--FIGATVEDD-----IAFGLENKKVPPKKMKDIIDDLakkvgmEDYLDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 152 LMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELAR-GGMTIFLVEQNAHHALkLADRGYVMVNGQIRLSGSGEDLLGNQE- 229
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEi 235
|
....*.
gi 2790487090 230 VRKAYL 235
Cdd:PRK13632 236 LEKAKI 241
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-216 |
2.21e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.44 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 24 VSLQVNQGETVALIGANGAGKSTLLMSIFGQ-PRIRGGQILFRGEEISHRSTHYVASGGIAQAPEGRR---IFPDMTVEE 99
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKrdgIVPVMGVGK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 100 NLLMGTIP----IGNAHAAEDMQKMFDLFPRLKERR---KQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIV 172
Cdd:PRK13549 361 NITLAALDrftgGSRIDDAAELKTILESIQRLKVKTaspELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGA 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2790487090 173 VKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIR 216
Cdd:PRK13549 441 KYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-232 |
2.65e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 83.49 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGqprirggqilfrgeEISH-RSTHYVASGGIAQAPEGRRIFpDMTVEE 99
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG--------------ELSHaETSSVVIRGSVAYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 100 NLLMGT----IPIGNAHAAEDMQKMFDLFP-RLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVK 174
Cdd:PLN03232 698 NILFGSdfesERYWRAIDVTALQHDLDLLPgRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487090 175 QIFQTLRELARGGMTIFLVeQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEVRK 232
Cdd:PLN03232 778 QVFDSCMKDELKGKTRVLV-TNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFK 834
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-206 |
4.37e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.20 E-value: 4.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 15 YGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGeeisHRSTHYVAsggiaQAPEGRRIFPd 94
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVP-----QRSEVPDSLP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 95 MTVEENLLMGTIPIGNA---HAAEDMQKMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLA 169
Cdd:NF040873 72 LTVRDLVAMGRWARRGLwrrLTRDDRAAVDDALERvgLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 2790487090 170 PIVVKQIFQTLRELARGGMTIFLVEQNAHHALkLADR 206
Cdd:NF040873 152 AESRERIIALLAEEHARGATVVVVTHDLELVR-RADP 187
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-230 |
4.68e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.82 E-value: 4.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 15 YGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVA----SGGIAQAPEGRR 90
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlrqqVATVFQDPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 91 IFPDMTVEENLLMGTIPIGNAHAAEDMQKMFDLFPRlKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAP 170
Cdd:PRK13638 91 FYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDA-QHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 171 IVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEV 230
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEA 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-238 |
5.17e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.58 E-value: 5.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 23 QVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIS--HRSTHYVASGGIAQAPEGRRIFPDMTVEEN 100
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPamSRSRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 101 L-------------------LMGTIPIGNAHAAEDMQKmfdlfprlkerrkqramTMSGGEQQMLAIARALMSRPTLLLL 161
Cdd:PRK11831 105 VayplrehtqlpapllhstvMMKLEAVGLRGAAKLMPS-----------------ELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 162 DEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEVR-KAYLGGV 238
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRvRQFLDGI 246
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-224 |
6.71e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 80.92 E-value: 6.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFY----GAIQALKQVSLQVNQGETVALIGANGAGKSTL---LMSIFGQPRIRGGQILFRGEEISHRS 73
Cdd:PRK09473 8 QADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTafaLMGLLAANGRIGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 74 THYVASggiAQAPEGRRIFPD--------MTVEENL---LMGTIPIGNAHAAEDMQKMFDLFpRLKERRKQraMTM---- 138
Cdd:PRK09473 88 EKELNK---LRAEQISMIFQDpmtslnpyMRVGEQLmevLMLHKGMSKAEAFEESVRMLDAV-KMPEARKR--MKMyphe 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 139 -SGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQIR 216
Cdd:PRK09473 162 fSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTM 241
|
....*...
gi 2790487090 217 LSGSGEDL 224
Cdd:PRK09473 242 EYGNARDV 249
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-219 |
7.19e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.97 E-value: 7.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS- 79
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 80 ----------GGIAQAP-EGRRifpdMTVEE--NL---LMGtipIGNAH-------AAEDMQKM------FDLFPRlker 130
Cdd:PRK11701 82 errrllrtewGFVHQHPrDGLR----MQVSAggNIgerLMA---VGARHygdiratAGDWLERVeidaarIDDLPT---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 131 rkqramTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYV 209
Cdd:PRK11701 151 ------TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLV 224
|
250
....*....|
gi 2790487090 210 MVNGQIRLSG 219
Cdd:PRK11701 225 MKQGRVVESG 234
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-235 |
9.67e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.78 E-value: 9.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 19 QALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS--GGIAQAPEGrRIFpDMT 96
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSkvGLVFQDPDD-QVF-SST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 97 VEENLLMGTIPIG--------NAHAAEDMQKMFDLfprlkerRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGL 168
Cdd:PRK13647 97 VWDDVAFGPVNMGldkdeverRVEEALKAVRMWDF-------RDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 169 APIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEVRKAYL 235
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQAGL 236
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-217 |
1.11e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 78.91 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 15 YGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAQAPEGRRIFpD 94
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWW-D 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 95 MTVEE--NLLMGTIPIGNAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIV 172
Cdd:cd03267 110 LPVIDsfYLLAAIYDLPPARFKKRLDELSELL-DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2790487090 173 VKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRgyVMVNGQIRL 217
Cdd:cd03267 189 QENIRNFLKEYNRErGTTVLLTSHYMKDIEALARR--VLVIDKGRL 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-225 |
1.57e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.86 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLlMSIFGQpRIRGGqilfrgeeiSHRSTHYVASGGIAQAPEGRRI--------- 91
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTL-MNALAF-RSPKG---------VKGSGSVLLNGMPIDAKEMRAIsayvqqddl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 92 -FPDMTVEENLL-MGTIPIGNAHAA-EDMQKMFDLFPRLKERRKQ--------RAMTMSGGEQQMLAIARALMSRPTLLL 160
Cdd:TIGR00955 110 fIPTLTVREHLMfQAHLRMPRRVTKkEKRERVDEVLQALGLRKCAntrigvpgRVKGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487090 161 LDEPSLGLAPIVVKQIFQTLRELARGGMTIFL-VEQNAHHALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICtIHQPSSELFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
6-233 |
2.28e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.54 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGA---IQALKQVSLQVNQGETVALIGANGAGKST--LLMSIFGQPRirGGQILFRGEEISHRSTHYVAS- 79
Cdd:TIGR00958 479 IEFQDVSFSYPNrpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTvaALLQNLYQPT--GGQVLLDGVPLVQYDHHYLHRq 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 80 -GGIAQAPegrrIFPDMTVEENLLMG---------TIPIGNAHAAEDMQKMFDLF-PRLKERRKQramtMSGGEQQMLAI 148
Cdd:TIGR00958 557 vALVGQEP----VLFSGSVRENIAYGltdtpdeeiMAAAKAANAHDFIMEFPNGYdTEVGEKGSQ----LSGGQKQRIAI 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 149 ARALMSRPTLLLLDEPSLGLaPIVVKQIFQTLRElaRGGMTIFLVEQNAHHALKlADRGYVMVNGQIRLSGSGEDLLGNQ 228
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSAL-DAECEQLLQESRS--RASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
....*
gi 2790487090 229 EVRKA 233
Cdd:TIGR00958 705 GCYKH 709
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-164 |
2.81e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 4 PMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQIlfrgeEISHRsthyVASGGIA 83
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-----KLGET----VKIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 84 QapEGRRIFPDMTVEENLlmgtipignAHAAEDMQKM--------FdLFPRlkERRKQRAMTMSGGEQQMLAIARALMSR 155
Cdd:COG0488 385 Q--HQEELDPDKTVLDEL---------RDGAPGGTEQevrgylgrF-LFSG--DDAFKPVGVLSGGEKARLALAKLLLSP 450
|
....*....
gi 2790487090 156 PTLLLLDEP 164
Cdd:COG0488 451 PNVLLLDEP 459
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-223 |
3.18e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.81 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 15 YGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFG--QPriRGGQILFRGEeishrsthyVAS-----GGiaqape 87
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGilEP--TSGRVEVNGR---------VSAllelgAG------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 88 grriF-PDMTVEEN-----LLMGtipignaHAAEDMQKMFD---LFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTL 158
Cdd:COG1134 99 ----FhPELTGRENiylngRLLG-------LSRKEIDEKFDeivEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 159 LLLDEpslGLApiVVKQIFQT-----LRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGED 223
Cdd:COG1134 168 LLVDE---VLA--VGDAAFQKkclarIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-229 |
3.32e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 78.67 E-value: 3.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 19 QALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS------GGIAQAPEGRrIF 92
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRpvrkriGMVFQFPESQ-LF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 93 PDmTVEENLLMG----TIPIGNAHAaedmqKMFDLFPRLKERR---KQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPS 165
Cdd:PRK13646 100 ED-TVEREIIFGpknfKMNLDEVKN-----YAHRLLMDLGFSRdvmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 166 LGLAPIVVKQIFQTLRELA-RGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQE 229
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-214 |
4.15e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 79.75 E-value: 4.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYGAIQALKQV----SLQVNQGETVALIGANGAGKSTLLMSIFG---QPRIR--GGQILFRGEEISH 71
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVvndvSLQIEAGETLALVGESGSGKSVTALSILRllpSPPVVypSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 72 ---RSTHYVASGGIAQapegrrIF--------PDMTVEENLL--------MGtipiGNAHAAEdmqkMFDLFPRLKERRK 132
Cdd:PRK15134 81 aseQTLRGVRGNKIAM------IFqepmvslnPLHTLEKQLYevlslhrgMR----REAARGE----ILNCLDRVGIRQA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 133 QRAMT-----MSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADR 206
Cdd:PRK15134 147 AKRLTdyphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADR 226
|
....*...
gi 2790487090 207 GYVMVNGQ 214
Cdd:PRK15134 227 VAVMQNGR 234
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
6-225 |
4.85e-17 |
|
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: 79.78 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYG-AIQALKQVSLQVNQGETVALIGANGAGKSTL--LMSIFGQPRirGGQILFRGEEISHRSTHYVaSGGI 82
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLakLLVGFFQAR--SGEILLNGFSLKDIDRHTL-RQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 83 AQAPEGRRIFpDMTVEENLLMGTIP------IGNAHAAEDMQKMFDLFPR-LKERRKQRAMTMSGGEQQMLAIARALMSR 155
Cdd:TIGR01193 551 NYLPQEPYIF-SGSILENLLLGAKEnvsqdeIWAACEIAEIKDDIENMPLgYQTELSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487090 156 PTLLLLDEPSLGLAPIVVKQIFQTLRELARggMTIFLVEqnahHALKLA---DRGYVMVNGQIRLSGSGEDLL 225
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVA----HRLSVAkqsDKIIVLDHGKIIEQGSHDELL 696
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-229 |
5.10e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 77.85 E-value: 5.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRST----HYVasGGIAQAPEGRriFPDMT 96
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwdirHKI--GMVFQNPDNQ--FVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 97 VEENLLMGTIPIGNAHaaEDMQKMFDLFPRL------KERRKQRamtMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAP 170
Cdd:PRK13650 99 VEDDVAFGLENKGIPH--EEMKERVNEALELvgmqdfKEREPAR---LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 171 IVVKQIFQTLREL-ARGGMTIFLVEQNAHHaLKLADRGYVMVNGQIRLSGSGEDLLGNQE 229
Cdd:PRK13650 174 EGRLELIKTIKGIrDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-224 |
5.74e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 77.75 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 20 ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIS------HRSTHYVASGGIAQAPEgRRIFP 93
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKVGIVFQFPE-HQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 94 DmTVEENLLMGTIPIG--NAHAAEDMQKMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPI 171
Cdd:PRK13634 101 E-TVEKDICFGPMNFGvsEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790487090 172 VVKQIFQTLRELAR-GGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDL 224
Cdd:PRK13634 180 GRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-190 |
6.62e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 6.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 4 PMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEI---SHR-STHYVas 79
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIddpDVAeACHYL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 80 ggiaqapeGRRIF--PDMTVEENL-----LMGTIPIGNAHAAEDM--QKMFDLfprlkerrkqRAMTMSGGEQQMLAIAR 150
Cdd:PRK13539 79 --------GHRNAmkPALTVAENLefwaaFLGGEELDIAAALEAVglAPLAHL----------PFGYLSAGQKRRVALAR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2790487090 151 ALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRE-LARGGMTI 190
Cdd:PRK13539 141 LLVSNRPIWILDEPTAALDAAAVALFAELIRAhLAQGGIVI 181
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-225 |
8.51e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.80 E-value: 8.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 24 VSLQVNQGETVALIGANGAGKSTLLMSIFGQprIRG-GQILFRGEEISHRSTHYVASggiaqapegRRIF--------PD 94
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL--LPGqGEILLNGRPLSDWSAAELAR---------HRAYlsqqqsppFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 95 MTVEENLLMGtIPiGNAHAAEDMQKMFDLFPRLKERRK-QRAMT-MSGGEQQMLAIARALM-------SRPTLLLLDEPS 165
Cdd:COG4138 84 MPVFQYLALH-QP-AGASSEAVEQLLAQLAEALGLEDKlSRPLTqLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487090 166 LGLApiVVKQI--FQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:COG4138 162 NSLD--VAQQAalDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-190 |
8.80e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.01 E-value: 8.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 7 EFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIS---HRSThyvASGGIA 83
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAdarHRRA---VCPRIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 84 QAPE--GRRIFPDMTVEENLlmgtipignahaaedmqkmfDLFPRL----KERRKQR-----------------AMTMSG 140
Cdd:NF033858 80 YMPQglGKNLYPTLSVFENL--------------------DFFGRLfgqdAAERRRRidellratglapfadrpAGKLSG 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2790487090 141 GEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQ---TLRElARGGMTI 190
Cdd:NF033858 140 GMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWElidRIRA-ERPGMSV 191
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
5-238 |
9.50e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.47 E-value: 9.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYG-----AIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFG-----QPRIRGGQILFRGEEISHRST 74
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 75 HYVASGGIA-QAPEGRrIFPDmTVEENLLMG--TIPIGNAHAAEDMQKMFDLFPRLKERRKQRAMTMSGGEQQMLAIARA 151
Cdd:PRK13643 81 PVRKKVGVVfQFPESQ-LFEE-TVLKDVAFGpqNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 152 LMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEVR 231
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFL 238
|
....*..
gi 2790487090 232 KAYLGGV 238
Cdd:PRK13643 239 KAHELGV 245
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-210 |
1.06e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 76.82 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 4 PMLEFHEVDVFYG----AIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHrsthyvas 79
Cdd:COG4525 2 SMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 80 ggiaqaPEGRR--------IFPDMTVEENL-----LMGTIPIGNAHAAEDMQKMFDLfprlKERRKQRAMTMSGGEQQML 146
Cdd:COG4525 74 ------PGADRgvvfqkdaLLPWLNVLDNVafglrLRGVPKAERRARAEELLALVGL----ADFARRRIWQLSGGMRQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 147 AIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLREL-ARGGMTIFLVEQNAHHALKLADRGYVM 210
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-215 |
1.07e-16 |
|
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: 74.95 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIS--HRSTHYVASGGIAQapegrrifpdmtvE 98
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwDPNELGDHVGYLPQ-------------D 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 99 ENLLMGTIpignahaAEDMqkmfdlfprlkerrkqramtMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQ 178
Cdd:cd03246 85 DELFSGSI-------AENI--------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQ 137
|
170 180 190
....*....|....*....|....*....|....*....
gi 2790487090 179 TLRELARGGMTIFLVeqnAHH--ALKLADRGYVMVNGQI 215
Cdd:cd03246 138 AIAALKAAGATRIVI---AHRpeTLASADRILVLEDGRV 173
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-214 |
1.35e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 78.23 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 18 IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAQAPEGRRIFPDMTV 97
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 98 EENLLMGTIP-----IGNAHAAEDMQKMF-----DLFPRLKerrkqrAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLG 167
Cdd:PRK10982 91 MDNMWLGRYPtkgmfVDQDKMYRDTKAIFdeldiDIDPRAK------VATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2790487090 168 LAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQ 214
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-204 |
1.48e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 75.09 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIS------HRSTHYvas 79
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAeqrdepHENILY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 80 ggIAQAPEgrrIFPDMTVEENL-----LMGTIPIGNAHAAEDMQkmfdlfprLKERRKQRAMTMSGGEQQMLAIARALMS 154
Cdd:TIGR01189 78 --LGHLPG---LKPELSALENLhfwaaIHGGAQRTIEDALAAVG--------LTGFEDLPAAQLSAGQQRRLALARLWLS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2790487090 155 RPTLLLLDEPSLGLAPIVVKQIFQTLRE-LARGGMTIFlveqNAHHALKLA 204
Cdd:TIGR01189 145 RRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLL----TTHQDLGLV 191
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
6-235 |
1.78e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.41 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGA-----IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS- 79
Cdd:PRK13641 3 IKFENVDYIYSPgtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 80 -----GGIAQAPEGRrIFPDmTVEENLLMGTIPIG--NAHAAEDMQKMFDLFPRLKERRKQRAMTMSGGEQQMLAIARAL 152
Cdd:PRK13641 83 lrkkvSLVFQFPEAQ-LFEN-TVLKDVEFGPKNFGfsEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 153 MSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQE-VR 231
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwLK 240
|
....
gi 2790487090 232 KAYL 235
Cdd:PRK13641 241 KHYL 244
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-225 |
2.52e-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: 77.48 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISH-------RSTHYVAsggiaQAPEgrrIFP 93
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwdreelgRHIGYLP-----QDVE---LFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 94 DmTVEENL-LMGTIPIGNAHAAEDMQKMFDLFPRLKE----RRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGL 168
Cdd:COG4618 420 G-TIAENIaRFGDADPEKVVAAAKLAGVHEMILRLPDgydtRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 169 APIVVKQIFQTLRELARGGMTIFLVeqnAH--HALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:COG4618 499 DDEGEAALAAAIRALKARGATVVVI---THrpSLLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-215 |
2.71e-16 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 74.76 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 19 QALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS--GGIAQAPegrrifpdmt 96
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSslTIIPQDP---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 97 veeNLLMGTIPigNAHAAEDMQKMFDLFPRLkeRRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQI 176
Cdd:cd03369 92 ---TLFSGTIR--SNLDPFDEYSDEEIYGAL--RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2790487090 177 FQTLRELARGGmTIFLVeqnAHHALKLA--DRGYVMVNGQI 215
Cdd:cd03369 165 QKTIREEFTNS-TILTI---AHRLRTIIdyDKILVMDAGEV 201
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-227 |
2.87e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.90 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFG-QPRIRG----GQILFRGEEI-SHRSTHYVAS--GGIAQAPEGrriF 92
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRmNDKVSGyrysGDVLLGGRSIfNYRDVLEFRRrvGMLFQRPNP---F 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 93 PdMTVEENLLMGTipigNAH----------AAEDMQKMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLD 162
Cdd:PRK14271 114 P-MSIMDNVLAGV----RAHklvprkefrgVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 163 EPSLGLAPIVVKQIFQTLRELArGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGN 227
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-233 |
2.96e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.89 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 20 ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRG---EEISHRSTHYVASGGIAQAPEGRRIfpDMT 96
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQNPDNQIV--ATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 97 VEENLLMGTIPIGNAhaAEDMQKMFDlfPRLK-----ERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPI 171
Cdd:PRK13633 103 VEEDVAFGPENLGIP--PEEIRERVD--ESLKkvgmyEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487090 172 VVKQIFQTLRELARG-GMTIFLVEQNAHHALKlADRGYVMVNGQIRLSGSGEDLLGNQEVRKA 233
Cdd:PRK13633 179 GRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMMKK 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
15-217 |
5.12e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 74.71 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 15 YGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILfrgeeishrsthyVASGGIAQAPEG------ 88
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-------------AGTAPLAEAREDtrlmfq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 89 -RRIFPDMTVEENLLMGTIPIGNAHAAEDMQKMfdlfpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPsLG 167
Cdd:PRK11247 89 dARLLPWKKVIDNVGLGLKGQWRDAALQALAAV-----GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP-LG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790487090 168 ----LAPIVVKQIFQTLRElaRGGMTIFLVEQNAHHALKLADRGYVMVNGQIRL 217
Cdd:PRK11247 163 aldaLTRIEMQDLIESLWQ--QHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGL 214
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
16-164 |
5.61e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 75.54 E-value: 5.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 16 GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHyvasggiAQAPEGRR---IF 92
Cdd:COG4608 29 GVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGR-------ELRPLRRRmqmVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 93 --------PDMTVEENLlmgtipignahaAE--DMQKMFDlfprlKERRKQRAMTM------------------SGGEQQ 144
Cdd:COG4608 102 qdpyaslnPRMTVGDII------------AEplRIHGLAS-----KAERRERVAELlelvglrpehadryphefSGGQRQ 164
|
170 180
....*....|....*....|
gi 2790487090 145 MLAIARALMSRPTLLLLDEP 164
Cdd:COG4608 165 RIGIARALALNPKLIVCDEP 184
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-215 |
6.94e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 76.30 E-value: 6.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 16 GAIQALKQVSLQVNQGETVALIGANGAGKSTlLMSIFG---QPriRGGQILFRGEEISH---------RSTHYvasGGIA 83
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKST-LMNILGcldKP--TSGTYRVAGQDVATldadalaqlRREHF---GFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 84 QApegRRIFPDMTVEENLLMGTIPIGNAHAAEdMQKMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLL 161
Cdd:PRK10535 93 QR---YHLLSHLTAAQNVEVPAVYAGLERKQR-LLRAQELLQRlgLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790487090 162 DEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKlADRGYVMVNGQI 215
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-237 |
7.11e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 74.31 E-value: 7.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLL------MSIFGQPRIRGGQILFRGEEISHRSTHYVAS--GGIAQAPEGrriF 92
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLkvlnrlIEIYDSKIKVDGKVLYFGKDIFQIDAIKLRKevGMVFQQPNP---F 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 93 PDMTVEENLlmgTIPIgNAHAAEDMQKM----------FDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLD 162
Cdd:PRK14246 103 PHLSIYDNI---AYPL-KSHGIKEKREIkkiveeclrkVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 163 EPSlGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGN--QEVRKAYLGG 237
Cdd:PRK14246 179 EPT-SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSpkNELTEKYVIG 254
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-230 |
1.10e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 74.27 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 19 QALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFrGEeishrsthYVASGGIAQAPEGRRI------- 91
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GD--------YAIPANLKKIKEVKRLrkeiglv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 92 --FPDMTVEENLLMGTIPIGNAHAAEDMQKMFDLFPRL-------KERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLD 162
Cdd:PRK13645 96 fqFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELlklvqlpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 163 EPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEV 230
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQEL 244
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-203 |
1.35e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 75.23 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 2 NEPMLEFHEVDVF---YGAIqaLKQVSLQVNQGETVALIGANGAGKSTLLMSI-----FGQPRIR---GGQILFrgeeIS 70
Cdd:COG4178 359 EDGALALEDLTLRtpdGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpYGSGRIArpaGARVLF----LP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 71 HRSthYVASGGIAQA---PEGRRIFPDMTVEENLlmgtipignaHAAedmqKMFDLFPRLkERRKQRAMTMSGGEQQMLA 147
Cdd:COG4178 433 QRP--YLPLGTLREAllyPATAEAFSDAELREAL----------EAV----GLGHLAERL-DEEADWDQVLSLGEQQRLA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 148 IARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRElARGGMTIFLV----EQNAHHALKL 203
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVghrsTLAAFHDRVL 554
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-230 |
1.50e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.50 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 18 IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISH-----RSTHYVASGGIAQAPEGRRI- 91
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDkknnhELITNPYSKKIKNFKELRRRv 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 92 -----FPDM-----TVEENLLMGTIPIG----NAH--AAEDMQKMfdlfpRLKERRKQRA-MTMSGGEQQMLAIARALMS 154
Cdd:PRK13631 119 smvfqFPEYqlfkdTIEKDIMFGPVALGvkksEAKklAKFYLNKM-----GLDDSYLERSpFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487090 155 RPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEV 230
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHI 269
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-225 |
2.19e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 72.81 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISH------------- 71
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtpsrelakrlail 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 72 RSTHYVASggiaqapegrRIfpdmTVEENLLMGTIPignaHA-----AEDMQKM------FDLFPrLKERRKQramTMSG 140
Cdd:COG4604 81 RQENHINS----------RL----TVRELVAFGRFP----YSkgrltAEDREIIdeaiayLDLED-LADRYLD---ELSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 141 GEQQMLAIARALMSRPTLLLLDEP--SLGLAPIVvkQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQIRL 217
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPlnNLDMKHSV--QMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVA 216
|
....*...
gi 2790487090 218 SGSGEDLL 225
Cdd:COG4604 217 QGTPEEII 224
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-225 |
2.92e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 74.23 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 7 EFHEVDVFY-GAIQALKQVSLQVNQGETVALIGANGAGKST---LLMSIFgQPriRGGQILFRGEEIS--HRSTHYVASG 80
Cdd:PRK13657 336 EFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTlinLLQRVF-DP--QSGRILIDGTDIRtvTRASLRRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 GIAQAPegrRIFpDMTVEENLLMGTIPIGNAH---AAEDMQKMfDLFPR----LKERRKQRAMTMSGGEQQMLAIARALM 153
Cdd:PRK13657 413 VVFQDA---GLF-NRSIEDNIRVGRPDATDEEmraAAERAQAH-DFIERkpdgYDTVVGERGRQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487090 154 SRPTLLLLDEPSLGLAPIVVKQIFQTLRELaRGGMTIFLVeqnAHH--ALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFII---AHRlsTVRNADRILVFDNGRVVESGSFDELV 557
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-227 |
3.06e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 73.91 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 20 ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRG---EEISHRSTHYVASGGIAQAPEGRRIFPDMT 96
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 97 VEENLLMGtIPIGNAHAAEDMQKMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVK 174
Cdd:PRK10070 123 VLDNTAFG-MELAGINAEERREKALDALRQvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790487090 175 QIFQTLREL-ARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGN 227
Cdd:PRK10070 202 EMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-224 |
3.51e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.11 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 19 QALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGgQILFRGEEISH--RSTHYVASGGIAQAPEgrriFPDMT 96
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQG-SLKINGIELREldPESWRKHLSWVGQNPQ----LPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 97 VEENLLMGTIPIGNAHAAEDMQKMF--DLFPRLKE----RRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAP 170
Cdd:PRK11174 439 LRDNVLLGNPDASDEQLQQALENAWvsEFLPLLPQgldtPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790487090 171 IVVKQIFQTLRELARGGMTIFLVEQNAhhALKLADRGYVMVNGQIRLSGSGEDL 224
Cdd:PRK11174 519 HSEQLVMQALNAASRRQTTLMVTHQLE--DLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-215 |
3.98e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.67 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 19 QALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQP--RIRGGQILFRGEEISHRSTHYVASGGIAQAPEGRR----IF 92
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKgyglNL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 93 PDmTVEENLLMGTIP------IGNAHA----AEDMQKmfdlfpRLKERRK---QRAMTMSGGEQQMLAIARALMSRPTLL 159
Cdd:NF040905 354 ID-DIKRNITLANLGkvsrrgVIDENEeikvAEEYRK------KMNIKTPsvfQKVGNLSGGNQQKVVLSKWLFTDPDVL 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 160 LLDEPSLGlapIVV--K-QIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:NF040905 427 ILDEPTRG---IDVgaKyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-225 |
4.48e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.97 E-value: 4.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASgGIAQ 84
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR-RLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 85 APEGRRIFPDMTVEENLLMGTIPIGN----------AHAAEDMQKMfdlfpRLKERRKQRAMTMSGGEQQMLAIARALMS 154
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSPWLSlwgrlsaednARVNQAMEQT-----RINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487090 155 RPTLLLLDEPS--LGLAPIVvkQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:PRK11231 156 DTPVVLLDEPTtyLDINHQV--ELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-182 |
6.07e-15 |
|
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: 71.35 E-value: 6.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 19 QALKQVSLQVNQGETVALIGANGAGKSTL--LMSIFGQPRirGGQILFRGEEIS---HRSTHYVASGgIAQAPegrrIFP 93
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVvaLLENFYQPQ--GGQVLLDGKPISqyeHKYLHSKVSL-VGQEP----VLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 94 DMTVEENLL--MGTIPIGNAHAAEDMQKMFDLFPRLK----ERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLG 167
Cdd:cd03248 101 ARSLQDNIAygLQSCSFECVKEAAQKAHAHSFISELAsgydTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170
....*....|....*
gi 2790487090 168 LAPIVVKQIFQTLRE 182
Cdd:cd03248 181 LDAESEQQVQQALYD 195
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-208 |
7.07e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 70.60 E-value: 7.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRG------EEISHRSTHYVasgGIAQAPEGRrifpd 94
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpldfqRDSIARGLLYL---GHAPGIKTT----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 95 MTVEENL-----LMGTIPIGNAHAAEDMQKMFDLfprlkerrkqRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLA 169
Cdd:cd03231 88 LSVLENLrfwhaDHSDEQVEEALARVGLNGFEDR----------PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2790487090 170 PIVVKQIFQTLR-ELARGGMTIFlveqNAHHALKLADRGY 208
Cdd:cd03231 158 KAGVARFAEAMAgHCARGGMVVL----TTHQDLGLSEAGA 193
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-220 |
7.69e-15 |
|
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: 73.51 E-value: 7.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 20 ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIshRSTHYVASGGIAQAPEGRRIFPDMTVEE 99
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 100 NLLMGTIPIGNA--HAAEDMQKMFDlFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIF 177
Cdd:TIGR01257 1023 HILFYAQLKGRSweEAQLEMEAMLE-DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2790487090 178 QTLRELaRGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGS 220
Cdd:TIGR01257 1102 DLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-165 |
9.08e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 69.01 E-value: 9.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILF-RGEEISHrsthyvasggIAQ 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgSTVKIGY----------FEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 85 apegrrifpdmtveenllmgtipignahaaedmqkmfdlfprlkerrkqramtMSGGEQQMLAIARALMSRPTLLLLDEP 164
Cdd:cd03221 71 -----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
.
gi 2790487090 165 S 165
Cdd:cd03221 98 T 98
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-230 |
1.48e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.93 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 20 ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS------GGIAQAPEGRrIFp 93
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKqirkkvGLVFQFPESQ-LF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 94 DMTVEENLLMGTIPIG-NAHAAEDM-QKMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPI 171
Cdd:PRK13649 100 EETVLKDVAFGPQNFGvSQEEAEALaREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 172 VVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLgnQEV 230
Cdd:PRK13649 180 GRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF--QDV 236
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-236 |
2.03e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.68 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 20 ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRsthyVASGGIAQAPEGRRI---FPdMT 96
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNLVAYVPQSEEVdwsFP-VL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 97 VEENLLMGT---IPIGNAHAAEDMQKMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPI 171
Cdd:PRK15056 97 VEDVVMMGRyghMGWLRRAKKRDRQIVTAALARvdMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 172 VVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGyVMVNGQIRLSGSGEDLLGNQEVRKAYLG 236
Cdd:PRK15056 177 TEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFTAENLELAFSG 240
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
6-225 |
2.34e-14 |
|
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: 71.77 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAI-QALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYV-ASGGIA 83
Cdd:COG5265 358 VRFENVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLrAAIGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 84 qaPEGRRIFPDmTVEENLLMGTIPIGNA--HAAEDMQKMFDLFPRLKE----RRKQRAMTMSGGEQQMLAIARALMSRPT 157
Cdd:COG5265 438 --PQDTVLFND-TIAYNIAYGRPDASEEevEAAARAAQIHDFIESLPDgydtRVGERGLKLSGGEKQRVAIARTLLKNPP 514
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487090 158 LLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLveqnAHhalKL-----ADRGYVMVNGQIRLSGSGEDLL 225
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREVARGRTTLVI----AH---RLstivdADEILVLEAGRIVERGTHAELL 580
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-228 |
2.99e-14 |
|
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: 71.87 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQilfrgeeISHrsthyvaSGGIAQAPEGRRIFPDmTVEEN 100
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGK-------IKH-------SGRISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 101 LLMG--------TIPIGNAHAAEDMQKmfdlFP-RLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPI 171
Cdd:TIGR01271 507 IIFGlsydeyryTSVIKACQLEEDIAL----FPeKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 172 VVKQIFQTLRELARGGMTIFLVEQNAHHaLKLADRGYVMVNGQIRLSGSGEDLLGNQ 228
Cdd:TIGR01271 583 TEKEIFESCLCKLMSNKTRILVTSKLEH-LKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-225 |
3.04e-14 |
|
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: 69.44 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGA--IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS--GG 81
Cdd:cd03252 1 ITFEHVRFRYKPdgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRqvGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 82 IAQApegrRIFPDMTVEENLLMG--TIPIGNAHAAEDMQKMFDLFPRLKERRKQ----RAMTMSGGEQQMLAIARALMSR 155
Cdd:cd03252 81 VLQE----NVLFNRSIRDNIALAdpGMSMERVIEAAKLAGAHDFISELPEGYDTivgeQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487090 156 PTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLveqnAHH--ALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIII----AHRlsTVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
5-234 |
4.19e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.86 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQ---------PRIRGGqILFRGEEISHRSTH 75
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgggaprgARVTGD-VTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 76 YVASGGIAQAPEGRRIFPdMTVEENLLMGTIPIGNAhAAEDMQKMFDLFPRLKERRKQRAM------TMSGGEQQMLAIA 149
Cdd:PRK13547 80 RLARLRAVLPQAAQPAFA-FSAREIVLLGRYPHARR-AGALTHRDGEIAWQALALAGATALvgrdvtTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 150 RAL---------MSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQIRLSG 219
Cdd:PRK13547 158 RVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
250
....*....|....*
gi 2790487090 220 SGEDLLGNQEVRKAY 234
Cdd:PRK13547 238 APADVLTPAHIARCY 252
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-210 |
5.51e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.12 E-value: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 17 AIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSThyvasggiAQAPEGRR----IF 92
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKD--------DEWRAVRSdiqmIF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 93 --------PDMTVeenllmGTIpignahAAEDMQKMFDLFPRLKERRKQRAMTM----------------SGGEQQMLAI 148
Cdd:PRK15079 105 qdplaslnPRMTI------GEI------IAEPLRTYHPKLSRQEVKDRVKAMMLkvgllpnlinryphefSGGQCQRIGI 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 149 ARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELAR--GGMTIFLveqnAH------HalkLADRGYVM 210
Cdd:PRK15079 173 ARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFI----AHdlavvkH---ISDRVLVM 235
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-208 |
8.44e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.67 E-value: 8.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAQ 84
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 85 APEGrrIFPDMTVEENLLMGTIPIGNAHAAEDMQKMFDL-----FPrlkerrkqrAMTMSGGEQQMLAIARALMSRPTLL 159
Cdd:PRK13540 81 HRSG--INPYLTLRENCLYDIHFSPGAVGITELCRLFSLehlidYP---------CGLLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2790487090 160 LLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLveqNAHHALKLADRGY 208
Cdd:PRK13540 150 LLDEPLVALDELSLLTIITKIQEHRAKGGAVLL---TSHQDLPLNKADY 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-224 |
8.54e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 69.83 E-value: 8.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFG--QPRIRGGQILFR------------------ 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 66 -----GEEISHRSTHYVASGGIAQAPEGRRI----------FPDMTVEENLLMGTIPIGNAhAAEDMQKMFDLFP--RLK 128
Cdd:TIGR03269 81 pcpvcGGTLEPEEVDFWNLSDKLRRRIRKRIaimlqrtfalYGDDTVLDNVLEALEEIGYE-GKEAVGRAVDLIEmvQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 129 ERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRG 207
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*..
gi 2790487090 208 YVMVNGQIRLSGSGEDL 224
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEV 256
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
15-215 |
9.62e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 69.29 E-value: 9.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 15 YGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSThyvASGGIAQAPEGRRIFPD 94
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP---AERGVGMVFQSYALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 95 MTVEENLLMGTIPIGNA---------HAAEDMQkmfdlFPRLKERRKQramTMSGGEQQMLAIARALMSRPTLLLLDEPS 165
Cdd:PRK11000 90 LSVAENMSFGLKLAGAKkeeinqrvnQVAEVLQ-----LAHLLDRKPK---ALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2790487090 166 LGL-APIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:PRK11000 162 SNLdAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-208 |
1.36e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 25 SLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIS------HRSTHYV--ASGgiaqapegrrIFPDMT 96
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdeyHQDLLYLghQPG----------IKTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 97 VEENLLMgtipignAHAAEDMQKMFDLFPRL-----KERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPI 171
Cdd:PRK13538 91 ALENLRF-------YQRLHGPGDDEALWEALaqvglAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 2790487090 172 VVKQIFQTLRE-LARGGMTIFlveqNAHHALKLADRGY 208
Cdd:PRK13538 164 GVARLEALLAQhAEQGGMVIL----TTHQDLPVASDKV 197
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-226 |
2.45e-13 |
|
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: 68.68 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 3 EPMLEFHEVDVFY-----GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFR-----------G 66
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtkpG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 67 EEISHRSTHYVasgGIAQAPEGrrIFPDMTVEENLlmgTIPIGNAHAAE--DMQKMFDLFPRLKERRKQRAM------TM 138
Cdd:TIGR03269 357 PDGRGRAKRYI---GILHQEYD--LYPHRTVLDNL---TEAIGLELPDElaRMKAVITLKMVGFDEEKAEEIldkypdEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 139 SGGEQQMLAIARALMSRPTLLLLDEPSLGLAPI----VVKQIFQTLRELargGMTIFLVEQNAHHALKLADRGYVMVNGQ 214
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPItkvdVTHSILKAREEM---EQTFIIVSHDMDFVLDVCDRAALMRDGK 505
|
250
....*....|..
gi 2790487090 215 IRLSGSGEDLLG 226
Cdd:TIGR03269 506 IVKIGDPEEIVE 517
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-215 |
2.85e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 66.13 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 18 IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRG---GQILFRGEEISHRSTHYvaSGGIAQAPEGRRIFPD 94
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKY--PGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 95 MTVEENLlmgtipignahaaedmqkmfDLFPRLKERRKQRAMtmSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVK 174
Cdd:cd03233 98 LTVRETL--------------------DFALRCKGNEFVRGI--SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2790487090 175 QIFQTLRELAR--GGMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:cd03233 156 EILKCIRTMADvlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-204 |
3.07e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 67.03 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSthyvASGGIAQ 84
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG----AERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 85 APEGrrIFPDMTVEENLLMGTIPIGNA-----HAAEDMQKMFDLfprlKERRKQRAMTMSGGEQQMLAIARALMSRPTLL 159
Cdd:PRK11248 77 QNEG--LLPWRNVQDNVAFGLQLAGVEkmqrlEIAHQMLKKVGL----EGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2790487090 160 LLDEPSLGLAPIVVKQIfQT--LRELARGGMTIFLVEQNAHHALKLA 204
Cdd:PRK11248 151 LLDEPFGALDAFTREQM-QTllLKLWQETGKQVLLITHDIEEAVFMA 196
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
16-164 |
3.24e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.95 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 16 GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSThyvASGGIAQAPEGRRIFPDM 95
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP---ADRDIAMVFQNYALYPHM 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487090 96 TVEENLLMG---------TIPIGNAHAAedmqKMFDLFPRLKerRKQRAmtMSGGEQQMLAIARALMSRPTLLLLDEP 164
Cdd:PRK11650 92 SVRENMAYGlkirgmpkaEIEERVAEAA----RILELEPLLD--RKPRE--LSGGQRQRVAMGRAIVREPAVFLFDEP 161
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-234 |
3.41e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.97 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQP--RIRGGQILFRGEEISHRSTHYVA 78
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 79 SGGIAQAPEGRRIFPDMTVEENLLMgtipIGNAHAAEDMQKMFD---LFPRLKERRKQRAMT-----------MSGGEQQ 144
Cdd:CHL00131 83 HLGIFLAFQYPIEIPGVSNADFLRL----AYNSKRKFQGLPELDpleFLEIINEKLKLVGMDpsflsrnvnegFSGGEKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 145 MLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEqnahHALKL-----ADRGYVMVNGQIRLSG 219
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILIT----HYQRLldyikPDYVHVMQNGKIIKTG 234
|
250
....*....|....*
gi 2790487090 220 SGEdlLGNQEVRKAY 234
Cdd:CHL00131 235 DAE--LAKELEKKGY 247
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-224 |
5.53e-13 |
|
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: 68.12 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYGAIQ--ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEI------SHRSTHY 76
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltnisdVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 77 vasggiaqAPEGRRIFPDMTVEENLLMGT----IPignahaAEDMQKMFDLFPR---LKERRKQRAMTMSGGEQQMLAIA 149
Cdd:TIGR01257 2017 --------CPQFDAIDDLLTGREHLYLYArlrgVP------AEEIEKVANWSIQslgLSLYADRLAGTYSGGNKRKLSTA 2082
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 150 RALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDL 224
Cdd:TIGR01257 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
10-225 |
6.67e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 66.85 E-value: 6.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 10 EVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQP----RIRGGQILFRGEEISHRSthyvasggiaqa 85
Cdd:COG4170 12 EIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLS------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 PEGRR---------IF--------PDMTVEENLlMGTIPignahaAEDMQKMFdlFPRLKERRKQ--------------R 134
Cdd:COG4170 80 PRERRkiigreiamIFqepsscldPSAKIGDQL-IEAIP------SWTFKGKW--WQRFKWRKKRaiellhrvgikdhkD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 135 AMT-----MSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELAR-GGMTIFLVEQNAHHALKLADRGY 208
Cdd:COG4170 151 IMNsypheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTIT 230
|
250
....*....|....*..
gi 2790487090 209 VMVNGQIRLSGSGEDLL 225
Cdd:COG4170 231 VLYCGQTVESGPTEQIL 247
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
7.39e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 66.31 E-value: 7.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYGAIQA--LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVA 78
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 79 S--GGIAQAPEGRriFPDMTVEENLLMG----TIPIGNAH-----AAEDMQkMFDlfprlkeRRKQRAMTMSGGEQQMLA 147
Cdd:PRK13648 83 KhiGIVFQNPDNQ--FVGSIVKYDVAFGlenhAVPYDEMHrrvseALKQVD-MLE-------RADYEPNALSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 148 IARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLREL-ARGGMTIFLVEQNAHHALKlADRGYVMVNGQIRLSGSGEDLLG 226
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
...
gi 2790487090 227 NQE 229
Cdd:PRK13648 232 HAE 234
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-164 |
7.96e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 67.12 E-value: 7.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 14 FYGaIQALKQVSLQVNQGETVALIGANGAGKSTlLMSIfgqprIRG--------GQILFRGEEISHRSTHYVASGGIAQA 85
Cdd:NF040905 11 FPG-VKALDDVNLSVREGEIHALCGENGAGKST-LMKV-----LSGvyphgsyeGEILFDGEVCRFKDIRDSEALGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 PEGRRIFPDMTVEENllmgtIPIGNAHA-------AEDMQKMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRP 156
Cdd:NF040905 84 HQELALIPYLSIAEN-----IFLGNERAkrgvidwNETNRRARELLAKvgLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
....*...
gi 2790487090 157 TLLLLDEP 164
Cdd:NF040905 159 KLLILDEP 166
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-216 |
1.05e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.19 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 3 EPMLEFHEVDVFYG----AIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVA 78
Cdd:PRK10584 4 ENIVEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 79 S------GGIAQApegRRIFPDMTVEEN-----LLMGTIPIGNAHAAEDMQKMFDLFPRLKERRKQramtMSGGEQQMLA 147
Cdd:PRK10584 84 KlrakhvGFVFQS---FMLIPTLNALENvelpaLLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQ----LSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 148 IARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKlADRGYVMVNGQIR 216
Cdd:PRK10584 157 LARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAAR-CDRRLRLVNGQLQ 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-234 |
1.30e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.39 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 15 YGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS--GGIAQapegRRIF 92
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARriGLLAQ----NATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 93 P-DMTVEENLLMGTIPignahaaedMQKMFDLFPRLKERRKQRAM--------------TMSGGEQQMLAIARALMSRPT 157
Cdd:PRK10253 93 PgDITVQELVARGRYP---------HQPLFTRWRKEDEEAVTKAMqatgithladqsvdTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487090 158 LLLLDEPSLGLAPIVVKQIFQTLRELAR-GGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEVRKAY 234
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELNReKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-234 |
1.42e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.95 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 24 VSLQVNQGETVALIGANGAGKSTLLMSIFGQprIRG-GQILFRGEEISHRSTHYVA--SGGIAQApegRRIFPDMTVEEN 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL--LPGsGSIQFAGQPLEAWSAAELArhRAYLSQQ---QTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 101 LLM----GTIPIGNAHAAEDMQKMFDLFPRLkERRKQramTMSGGEQQ-------MLAIARALMSRPTLLLLDEPSLGLA 169
Cdd:PRK03695 90 LTLhqpdKTRTEAVASALNEVAEALGLDDKL-GRSVN---QLSGGEWQrvrlaavVLQVWPDINPAGQLLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 170 PIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEVRKAY 234
Cdd:PRK03695 166 VAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-227 |
1.54e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQ-PRIRGGQILFRGEeishrsthyvasggIAQAPEGRRIFpDMTVEE 99
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGElPPRSDASVVIRGT--------------VAYVPQVSWIF-NATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 100 NLLMGTiPIG-----NAHAAEDMQKMFDLFP--RLKERrKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIV 172
Cdd:PLN03130 698 NILFGS-PFDperyeRAIDVTALQHDLDLLPggDLTEI-GERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 173 VKQIFQTLRELARGGMTIFLVeQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGN 227
Cdd:PLN03130 776 GRQVFDKCIKDELRGKTRVLV-TNQLHFLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
15-215 |
2.40e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.53 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 15 YGAIQALKQVSLQVNQGETVALIGANGAG--KSTLLMSIFGQPrirGGQILFR-GEEISHRSTHYVASGGIAQAPEGRRi 91
Cdd:NF000106 23 FGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPD---AGRRPWRf*TWCANRRALRRTIG*HRPVR*GRR- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 92 fPDMTVEENLLM--GTIPIGNAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLA 169
Cdd:NF000106 99 -ESFSGRENLYMigR*LDLSRKDARARADELLERF-SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2790487090 170 PIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLA------DRGYVMVNGQI 215
Cdd:NF000106 177 PRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAheltviDRGRVIADGKV 228
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
16-225 |
2.46e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 65.21 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 16 GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFG--QPRIRGGQILFRGEEI-----SHRSTHYVASGGIA---QA 85
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtKDNWRVTADRMRFDDIdllrlSPRERRKLVGHNVSmifQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 PEGRrIFPDMTVEENLlMGTIPiGNAHAAEDMQKM-------FDLFPRLKERRKQRAM-----TMSGGEQQMLAIARALM 153
Cdd:PRK15093 98 PQSC-LDPSERVGRQL-MQNIP-GWTYKGRWWQRFgwrkrraIELLHRVGIKDHKDAMrsfpyELTEGECQKVMIAIALA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487090 154 SRPTLLLLDEPSLGLAPIVVKQIFQTLRELAR-GGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:PRK15093 175 NQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELV 247
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-163 |
2.52e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.96 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNE--PMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRS--THY 76
Cdd:PRK10247 1 MQEnsPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpeIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 77 VASGGIAQAPEgrrIFPDmTVEENLLMgtiPIGNAHAAEDMQKMFDLFPRL---KERRKQRAMTMSGGEQQMLAIARALM 153
Cdd:PRK10247 81 QQVSYCAQTPT---LFGD-TVYDNLIF---PWQIRNQQPDPAIFLDDLERFalpDTILTKNIAELSGGEKQRISLIRNLQ 153
|
170
....*....|
gi 2790487090 154 SRPTLLLLDE 163
Cdd:PRK10247 154 FMPKVLLLDE 163
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-221 |
3.05e-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: 62.56 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSI-----FGQPRI---RGGQILFrgeeishrsthyvasggIAQAPegrrIF 92
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALaglwpWGSGRIgmpEGEDLLF-----------------LPQRP----YL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 93 PDMTVEENLLmgtipignahaaedmqkmfdlFPRLKErrkqramtMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIV 172
Cdd:cd03223 76 PLGTLREQLI---------------------YPWDDV--------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2790487090 173 VKQIFQTLRELargGMTIFLVeqnAHHA--LKLADRgyvmvngQIRLSGSG 221
Cdd:cd03223 127 EDRLYQLLKEL---GITVISV---GHRPslWKFHDR-------VLDLDGEG 164
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-200 |
4.13e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.04 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 2 NEPMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLL--------------MSIFGqpRIRGGqilfrGE 67
Cdd:PRK10938 257 NEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLslitgdhpqgysndLTLFG--RRRGS-----GE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 68 EISHRSTH--YVASggiaQAPEGRRIfpDMTVEENLLMGTI-PIGNAHAAEDMQKM-----FDLFPRLKERRKQRAMTMS 139
Cdd:PRK10938 330 TIWDIKKHigYVSS----SLHLDYRV--STSVRNVILSGFFdSIGIYQAVSDRQQKlaqqwLDILGIDKRTADAPFHSLS 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487090 140 GGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMT--IFLveqnAHHA 200
Cdd:PRK10938 404 WGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqlLFV----SHHA 462
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-228 |
4.83e-12 |
|
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: 64.11 E-value: 4.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQilfrgeeISHrsthyvaSGGIAQAPEGRRIFPDmTVEEN 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGK-------IKH-------SGRISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 101 LLMGTI--------PIGNAHAAEDMQKmfdlFP-RLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPI 171
Cdd:cd03291 118 IIFGVSydeyryksVVKACQLEEDITK----FPeKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 172 VVKQIFQTLRELARGGMTIFLVEQNAHHaLKLADRGYVMVNGQIRLSGSGEDLLGNQ 228
Cdd:cd03291 194 TEKEIFESCVCKLMANKTRILVTSKMEH-LKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-232 |
8.08e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 63.28 E-value: 8.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFY--GAIQALKQVSLQVNQGETVALIGANGAGKST---LLMSIFGQPRIRGGQILFRGEEISHRSTH 75
Cdd:PRK13640 1 MKDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 76 YVAS--GGIAQAPEGRriFPDMTVEENllmgtIPIGNAHAAEDMQKMFDLFPR------LKERRKQRAMTMSGGEQQMLA 147
Cdd:PRK13640 81 DIREkvGIVFQNPDNQ--FVGATVGDD-----VAFGLENRAVPRPEMIKIVRDvladvgMLDYIDSEPANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 148 IARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELAR-GGMTIFLVEQNAHHAlKLADRGYVMVNGQIRLSGSGEDLLG 226
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFS 232
|
....*.
gi 2790487090 227 NQEVRK 232
Cdd:PRK13640 233 KVEMLK 238
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-224 |
1.40e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.41 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 24 VSLQVNQGETVALIGANGAGKSTLLMSIFG--QPRIR--GGQILFRGEEISHRSTHYVASGGIAQAPegRRIF-PDMT-- 96
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSLTCAAALGilPAGVRqtAGRVLLDGKPVAPCALRGRKIATIMQNP--RSAFnPLHTmh 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 97 --VEENLLMGTIPIGNAHAA--------EDMQKMFDLFPrlkerrkqraMTMSGGEQQMLAIARALMSRPTLLLLDEPSL 166
Cdd:PRK10418 100 thARETCLALGKPADDATLTaaleavglENAARVLKLYP----------FEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 167 GLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDL 224
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-229 |
1.82e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.42 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 18 IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS--GGIAQAPEGRriFPDM 95
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRkiGMVFQNPDNQ--FVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 96 TVEENLLMGTIPIGNAHaaEDMQKMFD---LFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIV 172
Cdd:PRK13642 98 TVEDDVAFGMENQGIPR--EEMIKRVDealLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487090 173 VKQIFQTLRELA-RGGMTIFLVEQNAHHALKlADRGYVMVNGQIRLSGSGEDLLGNQE 229
Cdd:PRK13642 176 RQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-225 |
4.17e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 61.96 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGA--IQALKQVSLQVNQGETVALIGANGAGKSTL--LMSIFGQprIRGGQILFRGEEI------SHRSTH 75
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIanLLTRFYD--IDEGEILLDGHDLrdytlaSLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 76 YVAS-----------GGIAQAPEGRriFPDMTVEENLLMgtipignAHAAEDMQKMFDLFPRLKerrKQRAMTMSGGEQQ 144
Cdd:PRK11176 420 ALVSqnvhlfndtiaNNIAYARTEQ--YSREQIEEAARM-------AYAMDFINKMDNGLDTVI---GENGVLLSGGQRQ 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 145 MLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLveqnAHH--ALKLADRGYVMVNGQIRLSGSGE 222
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVI----AHRlsTIEKADEILVVEDGEIVERGTHA 563
|
...
gi 2790487090 223 DLL 225
Cdd:PRK11176 564 ELL 566
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-164 |
5.03e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQ-----PRIRGGQILfrgeEISHRSTHYVAsggiaqapegrrIFPDM 95
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQlqadsGRIHCGTKL----EVAYFDQHRAE------------LDPEK 398
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 96 TVEENLLMG--TIPIG--NAHAAEDMQKMfdLFPrlkerrKQRAMT----MSGGEQQMLAIARALMSRPTLLLLDEP 164
Cdd:PRK11147 399 TVMDNLAEGkqEVMVNgrPRHVLGYLQDF--LFH------PKRAMTpvkaLSGGERNRLLLARLFLKPSNLLILDEP 467
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-226 |
6.11e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.57 E-value: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 25 SLQVNQGETVALIGANGAGKSTLLMSIFGQprirggQILFRGEEISH-RSTHYVASGGIAQ--APEGRRIFPDM------ 95
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGE------LPLLSGERQSQfSHITRLSFEQLQKlvSDEWQRNNTDMlspged 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 96 ----TVEENLLMGTipiGNAHAAEDMQKMFDLFPRLKERRKQramtMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPI 171
Cdd:PRK10938 97 dtgrTTAEIIQDEV---KDPARCEQLAQQFGITALLDRRFKY----LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 172 VVKQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLG 226
Cdd:PRK10938 170 SRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-164 |
6.12e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.49 E-value: 6.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLmsifgqpRIRGG-QILFRGEEishRSTHYVASGGIAQAPEgrrIFPDMTVEE 99
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLL-------RIMAGvDKDFNGEA---RPQPGIKVGYLPQEPQ---LDPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 100 NLLMGTIPIGNAHAA------------EDMQKMFDLFPRLKE-----------RRKQRAM-------------TMSGGEQ 143
Cdd:TIGR03719 88 NVEEGVAEIKDALDRfneisakyaepdADFDKLAAEQAELQEiidaadawdldSQLEIAMdalrcppwdadvtKLSGGER 167
|
170 180
....*....|....*....|.
gi 2790487090 144 QMLAIARALMSRPTLLLLDEP 164
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEP 188
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-164 |
9.30e-11 |
|
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: 59.65 E-value: 9.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 18 IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRG---EEISHRSTHYVASGGIAQAPEGRRIFpD 94
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNkneSEPSFEATRSRNRYSVAYAAQKPWLL-N 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487090 95 MTVEENLLMGTiPIGNAH-----AAEDMQKMFDLFPRLKERR-KQRAMTMSGGEQQMLAIARALMSRPTLLLLDEP 164
Cdd:cd03290 93 ATVEENITFGS-PFNKQRykavtDACSLQPDIDLLPFGDQTEiGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-164 |
9.46e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.36 E-value: 9.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 18 IQALKQVSLQVNQGETVALIGANGAGKSTL--LMSIFGQPRirGGQILFRGEEISHRSTHYVAS-----GGIAQAPEGRr 90
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLarLLTMIETPT--GGELYYQGQDLLKADPEAQKLlrqkiQIVFQNPYGS- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 91 IFPDMTV----EENLLMGTipigNAHAAEDMQKMFDLFPR--LKERRKQRAMTM-SGGEQQMLAIARALMSRPTLLLLDE 163
Cdd:PRK11308 105 LNPRKKVgqilEEPLLINT----SLSAAERREKALAMMAKvgLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVADE 180
|
.
gi 2790487090 164 P 164
Cdd:PRK11308 181 P 181
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-224 |
1.21e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.64 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 18 IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGIAQAPEGR-------R 90
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMRHvrgadmaM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 91 IF--------PDMTVEENLLMGT---IPIGNAHAAEDMQKMFDL--FPRLKERRKQRAMTMSGGEQQMLAIARALMSRPT 157
Cdd:PRK10261 109 IFqepmtslnPVFTVGEQIAESIrlhQGASREEAMVEAKRMLDQvrIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487090 158 LLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDL 224
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
10-190 |
1.26e-10 |
|
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: 58.79 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 10 EVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLmSIFGQPRIRG---GQILFRGEEIS---HRSTHYVASGGIa 83
Cdd:cd03232 12 TVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLL-DVLAGRKTAGvitGEILINGRPLDknfQRSTGYVEQQDV- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 84 qapegrrIFPDMTVEENLLMgtipignaHAAedmqkmfdlfprLKErrkqramtMSGGEQQMLAIARALMSRPTLLLLDE 163
Cdd:cd03232 90 -------HSPNLTVREALRF--------SAL------------LRG--------LSVEQRKRLTIGVELAAKPSILFLDE 134
|
170 180
....*....|....*....|....*..
gi 2790487090 164 PSLGLAPIVVKQIFQTLRELARGGMTI 190
Cdd:cd03232 135 PTSGLDSQAAYNIVRFLKKLADSGQAI 161
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-223 |
1.27e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.66 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGqpRIRG----GQILFRGEEISH---RSTHYVASGGIaqapegrrIFP 93
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAG--RIQGnnftGTILANNRKPTKqilKRTGFVTQDDI--------LYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 94 DMTVEENLLM-GTIPIGNAHAAEDMQKMFD-LFPRLKERRKQRAMT-------MSGGEQQMLAIARALMSRPTLLLLDEP 164
Cdd:PLN03211 154 HLTVRETLVFcSLLRLPKSLTKQEKILVAEsVISELGLTKCENTIIgnsfirgISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 165 SLGLAPIVVKQIFQTLRELARGGMTIFL-VEQNAHHALKLADRGYVMVNGQIRLSGSGED 223
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKGKTIVTsMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-225 |
2.20e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 60.11 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 20 ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISH------RSTHYVASggiaQAPegrRIFP 93
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqldswRSRLAVVS----QTP---FLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 94 DmTVEENLLMGTiPIGNAHAAEDMQKM---FDLFPRLKERRK----QRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSL 166
Cdd:PRK10789 403 D-TVANNIALGR-PDATQQEIEHVARLasvHDDILRLPQGYDtevgERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487090 167 GLAPIVVKQIFQTLRELARGGMTIFlveqNAHH--ALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGEGRTVII----SAHRlsALTEASEILVMQHGHIAQRGNHDQLA 537
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-183 |
2.57e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.72 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 19 QALKQVSLQVNQGETVALIGANGAGKST----LLMSIFGQprirgGQILFRGEEISHRSTHyvasggiAQAPEGRRI--- 91
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEIWFDGQPLHNLNRR-------QLLPVRHRIqvv 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 92 F--------PDMTVEENLLMGTI---PIGNAHAAED-----MQKMfDLFPrlkERRKQRAMTMSGGEQQMLAIARALMSR 155
Cdd:PRK15134 368 FqdpnsslnPRLNVLQIIEEGLRvhqPTLSAAQREQqviavMEEV-GLDP---ETRHRYPAEFSGGQRQRIAIARALILK 443
|
170 180
....*....|....*....|....*...
gi 2790487090 156 PTLLLLDEPSLGLAPIVVKQIFQTLREL 183
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSL 471
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-225 |
5.33e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.88 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 18 IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYvasggiaQAPEGRRIFPDMTV 97
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY-------RSQRIRMIFQDPST 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 98 EEN-------LLMGTIPIGNAHAAEDMQKMFDLFPRLKERRKQRAM----TMSGGEQQMLAIARALMSRPTLLLLDEPSL 166
Cdd:PRK15112 99 SLNprqrisqILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASyyphMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 167 GLAPIVVKQIFQTLREL-ARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:PRK15112 179 SLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
14-206 |
5.78e-10 |
|
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: 56.56 E-value: 5.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 14 FYGAIQ-ALKQVSLQVNQGETVALIGANGAGKSTLLMSIF---GQPRIRGGQILFrgeeishrsthyvasggiaqaPEGR 89
Cdd:cd03238 3 VSGANVhNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLyasGKARLISFLPKF---------------------SRNK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 90 RIFPD---MTVEENLlmGTIPIGnahaaedmqkmfdlfprlkerrkQRAMTMSGGEQQMLAIARALMSRP--TLLLLDEP 164
Cdd:cd03238 62 LIFIDqlqFLIDVGL--GYLTLG-----------------------QKLSTLSGGELQRVKLASELFSEPpgTLFILDEP 116
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2790487090 165 SLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAhHALKLADR 206
Cdd:cd03238 117 STGLHQQDINQLLEVIKGLIDLGNTVILIEHNL-DVLSSADW 157
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-232 |
7.94e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.44 E-value: 7.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQ-ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIShrsthyvasggiAQ 84
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT------------AE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 85 APEGRR-----IFPDMTVEENLLmgtipiGNAHAAEDMQKMFDLFPRLKERRKQRA-------MTMSGGEQQMLAIARAL 152
Cdd:PRK10522 391 QPEDYRklfsaVFTDFHLFDQLL------GPEGKPANPALVEKWLERLKMAHKLELedgrisnLKLSKGQKKRLALLLAL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 153 MSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHaLKLADRGYVMVNGQIR-LSGSGEDLLGNQEV 230
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmGKTIFAISHDDHY-FIHADRLLEMRNGQLSeLTGEERDAASRDAV 543
|
..
gi 2790487090 231 RK 232
Cdd:PRK10522 544 AR 545
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-225 |
8.10e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.42 E-value: 8.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGqprirggqilfrgeEISHRSTHYVASGGIAQAPEGRRIFPDmTVEEN 100
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLA--------------EMDKVEGHVHMKGSVAYVPQQAWIQND-SLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 101 LLMGTiPIGNAHAAEDMQKMfDLFPRLK-----ERRK--QRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVV 173
Cdd:TIGR00957 719 ILFGK-ALNEKYYQQVLEAC-ALLPDLEilpsgDRTEigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790487090 174 KQIFQTL--RELARGGMTIFLVEQNAHHaLKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:TIGR00957 797 KHIFEHVigPEGVLKNKTRILVTHGISY-LPQVDVIIVMSGGKISEMGSYQELL 849
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-224 |
8.69e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.83 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 19 QALKQVSLQVNQGETVALIGANGAGKSTLLMSIFG----QPRIRGGQILFRGEE---ISHRSTHYVASGGIAQapegrrI 91
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlidyPGRVMAEKLEFNGQDlqrISEKERRNLVGAEVAM------I 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 92 FPDMTVEEN-------LLMGTIPI---GNAhaAEDMQKMFDLF-----PRLKERRKQRAMTMSGGEQQMLAIARALMSRP 156
Cdd:PRK11022 95 FQDPMTSLNpcytvgfQIMEAIKVhqgGNK--KTRRQRAIDLLnqvgiPDPASRLDVYPHQLSGGMSQRVMIAMAIACRP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 157 TLLLLDEPSLGLAPIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDL 224
Cdd:PRK11022 173 KLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-168 |
1.02e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.05 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 4 PMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQIlfrgeeishRSTHYVASGGIA 83
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 84 QAPEGRRIFPdMTVEENLLM--GTipignahaaedmqKMFDLFPRLKerRKQRA-------MTMSGGEQQMLAIARALMS 154
Cdd:PRK09544 74 QKLYLDTTLP-LTVNRFLRLrpGT-------------KKEDILPALK--RVQAGhlidapmQKLSGGETQRVLLARALLN 137
|
170
....*....|....
gi 2790487090 155 RPTLLLLDEPSLGL 168
Cdd:PRK09544 138 RPQLLVLDEPTQGV 151
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
6-229 |
1.45e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.87 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFY--GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIshrsthyvASGGIA 83
Cdd:PTZ00243 1309 LVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI--------GAYGLR 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 84 qapEGRRIFPDMTVEENLLMGTI-----PIGNAHAAEdMQKMFDLFPrLKERRKQRA-----------MTMSGGEQQMLA 147
Cdd:PTZ00243 1381 ---ELRRQFSMIPQDPVLFDGTVrqnvdPFLEASSAE-VWAALELVG-LRERVASESegidsrvleggSNYSVGQRQLMC 1455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 148 IARALMSRPT-LLLLDEPSLGLAPIVVKQIFQTLRElARGGMTIFLVeqnAH--HALKLADRGYVMVNGQIRLSGSGEDL 224
Cdd:PTZ00243 1456 MARALLKKGSgFILMDEATANIDPALDRQIQATVMS-AFSAYTVITI---AHrlHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
....*
gi 2790487090 225 LGNQE 229
Cdd:PTZ00243 1532 VMNRQ 1536
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
94-224 |
1.85e-09 |
|
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: 57.33 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 94 DMTVEEnllmgtipignahAAEdmqkMFDLFPRLkeRRK---------------QRAMTMSGGEQQMLAIARALMSR--- 155
Cdd:TIGR00630 790 DMTVEE-------------AYE----FFEAVPSI--SRKlqtlcdvglgyirlgQPATTLSGGEAQRIKLAKELSKRstg 850
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 156 PTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAhHALKLADrgYV--------MVNGQIRLSGSGEDL 224
Cdd:TIGR00630 851 RTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL-DVIKTAD--YIidlgpeggDGGGTVVASGTPEEV 924
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-211 |
5.13e-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: 55.11 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 28 VNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRsthyvasggiaqaPEgrRIFPD--MTVEEnLLMGT 105
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYK-------------PQ--YIKADyeGTVRD-LLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 106 IPIGNAHA---AEDMQKMfdlfpRLKERRKQRAMTMSGGEQQMLAIArALMSRPT-LLLLDEPSlglAPIVVKQIFQTLR 181
Cdd:cd03237 86 TKDFYTHPyfkTEIAKPL-----QIEQILDREVPELSGGELQRVAIA-ACLSKDAdIYLLDEPS---AYLDVEQRLMASK 156
|
170 180 190
....*....|....*....|....*....|....
gi 2790487090 182 ELARGGM----TIFLVEQNAHHALKLADRgyVMV 211
Cdd:cd03237 157 VIRRFAEnnekTAFVVEHDIIMIDYLADR--LIV 188
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-225 |
5.83e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 54.86 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGgQILFRGeeishrsthyvASGGIAQAPEGRRIFPDMTVEEN 100
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG-DIQIDG-----------VSWNSVPLQKWRKAFGVIPQKVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 101 LLMGTI-----PIGNaHAAEDMQK---------MFDLFP-RLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPS 165
Cdd:cd03289 88 IFSGTFrknldPYGK-WSDEEIWKvaeevglksVIEQFPgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 166 LGLAPIVVKQIFQTLRElARGGMTIFLVEQNAHHALKlADRGYVMVNGQIRLSGSGEDLL 225
Cdd:cd03289 167 AHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLL 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-225 |
8.89e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.56 E-value: 8.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILfrgeeiSHRSTHYVasggiaqaPEGRRIFpDMTVEEN 100
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW------AERSIAYV--------PQQAWIM-NATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 101 LLMGTipignAHAAEDMQK----------MFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAP 170
Cdd:PTZ00243 741 ILFFD-----EEDAARLADavrvsqleadLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 171 IVVKQIFQTLRELARGGMTIFLVEQNAhHALKLADRGYVMVNGQIRLSGSGEDLL 225
Cdd:PTZ00243 816 HVGERVVEECFLGALAGKTRVLATHQV-HVVPRADYVVALGDGRVEFSGSSADFM 869
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
94-205 |
1.05e-08 |
|
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: 54.16 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 94 DMTVEEnllmgtipignahAAEdmqkMFDLFPRLKERRK-------------QRAMTMSGGEQQMLAIARALMSR---PT 157
Cdd:cd03271 130 DMTVEE-------------ALE----FFENIPKIARKLQtlcdvglgyiklgQPATTLSGGEAQRIKLAKELSKRstgKT 192
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2790487090 158 LLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAhHALKLAD 205
Cdd:cd03271 193 LYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL-DVIKCAD 239
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-195 |
1.17e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.92 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLmSIFGQPRIRGGQILFRGeeISHRS----THYVASGGIAQapegrRIFpdmt 96
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLL-SALLRLLSTEGEIQIDG--VSWNSvtlqTWRKAFGVIPQ-----KVF---- 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 97 veenLLMGTIPIG-NAHA----------AED--MQKMFDLFP-RLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLD 162
Cdd:TIGR01271 1303 ----IFSGTFRKNlDPYEqwsdeeiwkvAEEvgLKSVIEQFPdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLD 1378
|
170 180 190
....*....|....*....|....*....|...
gi 2790487090 163 EPSLGLAPIVVKQIFQTLRElARGGMTIFLVEQ 195
Cdd:TIGR01271 1379 EPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEH 1410
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-215 |
1.33e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 8 FHEVDVFygaiQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQP----RIRGGQILFRG---EEISHrstHYvaSG 80
Cdd:TIGR00956 68 FRDTKTF----DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGitpEEIKK---HY--RG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 GIAQAPEGRRIFPDMTVEENLLMgtipignAHAAEDMQKMFDLFPRLKERRKQRAMTM---------------------S 139
Cdd:TIGR00956 139 DVVYNAETDVHFPHLTVGETLDF-------AARCKTPQNRPDGVSREEYAKHIADVYMatyglshtrntkvgndfvrgvS 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487090 140 GGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVE--QNAHHALKLADRGYVMVNGQI 215
Cdd:TIGR00956 212 GGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQ 289
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-164 |
1.50e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTH------------YVAsGGIAQAPEG 88
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQdpprnvegtvydFVA-EGIEEQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 89 RRIFPDMTVeenlLMGTIP-------IGNAHAAEDMQKMFDLFPRLKERRKQRAMT-------MSGGEQQMLAIARALMS 154
Cdd:PRK11147 98 LKRYHDISH----LVETDPseknlneLAKLQEQLDHHNLWQLENRINEVLAQLGLDpdaalssLSGGWLRKAALGRALVS 173
|
170
....*....|
gi 2790487090 155 RPTLLLLDEP 164
Cdd:PRK11147 174 NPDVLLLDEP 183
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-224 |
1.67e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 54.34 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRStHYVASGGIAQAPEGRRIFPDmTVEEN 100
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAMVQQDPVVLAD-TFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 101 LLMGTiPIGNAHA---------AEDMQKMFD-LFPRLKERrkqrAMTMSGGEQQMLAIARALMSRPTLLLLDEPSlglAP 170
Cdd:PRK10790 435 VTLGR-DISEEQVwqaletvqlAELARSLPDgLYTPLGEQ----GNNLSVGQKQLLALARVLVQTPQILILDEAT---AN 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 171 I------VVKQIFQTLRE----------------------LARGGMtiflVEQNAHHALkLADRG--YVMVngqiRLSGS 220
Cdd:PRK10790 507 IdsgteqAIQQALAAVREhttlvviahrlstiveadtilvLHRGQA----VEQGTHQQL-LAAQGryWQMY----QLQLA 577
|
....
gi 2790487090 221 GEDL 224
Cdd:PRK10790 578 GEEL 581
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-227 |
1.79e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.45 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 133 QRAM-TMSGGEQQMLAIARALMSRPT--LLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNaHHALKLADR--- 206
Cdd:PRK00635 471 ERALaTLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRiid 549
|
90 100
....*....|....*....|....
gi 2790487090 207 ---GYVMVNGQIRLSGSGEDLLGN 227
Cdd:PRK00635 550 igpGAGIFGGEVLFNGSPREFLAK 573
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-210 |
1.81e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.45 E-value: 1.81e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487090 137 TMSGGEQQMLAIARALMS---RPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAhHALKLADrgYVM 210
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVAD--YVL 882
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-234 |
2.53e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.25 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASgGIAQAPEGRRIFPDMTVEEN 100
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR-KVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 101 LLMGTIPIGNA---HAAEDMQKMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPS--LGLAPIV- 172
Cdd:PRK10575 106 VAIGRYPWHGAlgrFGAADREKVEEAISLvgLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTsaLDIAHQVd 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487090 173 VKQIFQTLRELArgGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEVRKAY 234
Cdd:PRK10575 186 VLALVHRLSQER--GLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-237 |
2.81e-08 |
|
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: 53.86 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 134 RAMTMSGGEQQMLAIARALMSRPT--LLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNaHHALKLADR----- 206
Cdd:TIGR00630 485 AAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD-EDTIRAADYvidig 563
|
90 100 110
....*....|....*....|....*....|...
gi 2790487090 207 -GYVMVNGQIRLSGSGEDLLGNQE-VRKAYLGG 237
Cdd:TIGR00630 564 pGAGEHGGEVVASGTPEEILANPDsLTGQYLSG 596
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-193 |
3.01e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.27 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIShrsthyvasggiaqapegrrIFPDMTVEEN 100
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ--------------------FGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 101 LLmgtiPIGNAHAA---------EDMQKMFDLFPRLKERRKQRAMtmsggeqqmlaIARALMSRPTLLLLDEPSLGLAPI 171
Cdd:COG2401 106 IG----RKGDFKDAvellnavglSDAVLWLRRFKELSTGQKFRFR-----------LALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|..
gi 2790487090 172 VVKQIFQTLRELARGGMTIFLV 193
Cdd:COG2401 171 TAKRVARNLQKLARRAGITLVV 192
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-164 |
3.11e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 19 QALKQVSLQVNQGETVALIGANGAGKSTLLmsifgqpRIRGG-QILFRGEEishrsthyVASGGI-----AQAPEgrrIF 92
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLL-------RIMAGvDKEFEGEA--------RPAPGIkvgylPQEPQ---LD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 93 PDMTVEENLLMGTIPIGNAHA---------AEDMQKMFDLFPRLKE--------------RRKQRAM------------- 136
Cdd:PRK11819 83 PEKTVRENVEEGVAEVKAALDrfneiyaayAEPDADFDALAAEQGElqeiidaadawdldSQLEIAMdalrcppwdakvt 162
|
170 180
....*....|....*....|....*...
gi 2790487090 137 TMSGGEQQMLAIARALMSRPTLLLLDEP 164
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-228 |
5.36e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFY--GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEishrsthyVASGGI 82
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCD--------VAKFGL 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 83 AQAPEGRRIFPDMTVeenLLMGTIPIG----NAHAAEDMQKMF------DLFPR----LKERRKQRAMTMSGGEQQMLAI 148
Cdd:PLN03232 1306 TDLRRVLSIIPQSPV---LFSGTVRFNidpfSEHNDADLWEALerahikDVIDRnpfgLDAEVSEGGENFSVGQRQLLSL 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 149 ARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARgGMTIFLVEQNAHHALKlADRGYVMVNGQIRLSGSGEDLLGNQ 228
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFK-SCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-165 |
7.72e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 7.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 27 QVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRgEEISHRsthyvasggiaqaPEGRRIFPDMTVEENLLMGTI 106
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYK-------------PQYIKPDYDGTVEDLLRSITD 426
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487090 107 PIGNAHAAEDMQKMFDLfPRLKERRkqrAMTMSGGEQQMLAIARALMSRPTLLLLDEPS 165
Cdd:PRK13409 427 DLGSSYYKSEIIKPLQL-ERLLDKN---VKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-215 |
1.55e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 18 IQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS-----GGIAQAP----EG 88
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAlrrdiQFIFQDPyaslDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 89 RRIFPDMTVEENLLMGTIPiGNAhAAEDMQKMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGL 168
Cdd:PRK10261 417 RQTVGDSIMEPLRVHGLLP-GKA-AAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2790487090 169 APIVVKQIFQTLRELARG-GMTIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
134-206 |
2.67e-07 |
|
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: 49.56 E-value: 2.67e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 134 RAMTMSGGEQQMLAIARALMSRPT--LLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNaHHALKLADR 206
Cdd:cd03270 134 SAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADH 207
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-163 |
6.72e-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: 49.94 E-value: 6.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASgGIAQAPEGRRIFPDmtveeN 100
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF-KITIIPQDPVLFSG-----S 1375
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487090 101 LLMGTIPIGNaHAAEDMQKMFDL---------FP-RLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDE 163
Cdd:TIGR00957 1376 LRMNLDPFSQ-YSDEEVWWALELahlktfvsaLPdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDE 1447
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-229 |
1.01e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.35 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEIShrsthyvaSGGIAQAPEGRRIFPDMTVeen 100
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS--------KFGLMDLRKVLGIIPQAPV--- 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 101 LLMGTIPIG----NAHAAEDMQKMFDLfPRLKE--RRKQRAM---------TMSGGEQQMLAIARALMSRPTLLLLDEPS 165
Cdd:PLN03130 1324 LFSGTVRFNldpfNEHNDADLWESLER-AHLKDviRRNSLGLdaevseageNFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 166 lglAPIVVKQ---IFQTLRELARG-GMTIFlveqnAHHALKL--ADRGYVMVNGQIRLSGSGEDLLGNQE 229
Cdd:PLN03130 1403 ---AAVDVRTdalIQKTIREEFKScTMLII-----AHRLNTIidCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-234 |
1.67e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQP--RIRGGQILFRGEEISHRSTHYVASGGI 82
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 83 AQAPEGRRIFPDMTvEENLLMGTIPIGNAHAAEDMQKMFDLFPRLKERRKQRAMT-----------MSGGEQQMLAIARA 151
Cdd:PRK09580 81 FMAFQYPVEIPGVS-NQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPedlltrsvnvgFSGGEKKRNDILQM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 152 LMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELaRGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQEVR 231
Cdd:PRK09580 160 AVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEE 238
|
...
gi 2790487090 232 KAY 234
Cdd:PRK09580 239 QGY 241
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-215 |
1.77e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 4 PMLEFHEVDVFY-GAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQIlFRGEE--ISHRSTHYVASG 80
Cdd:PLN03073 507 PIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-FRSAKvrMAVFSQHHVDGL 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 GIAQAP--EGRRIFPDmtVEENLL---MGTIPIGNAHAaedMQKMFdlfprlkerrkqramTMSGGEQQMLAIARALMSR 155
Cdd:PLN03073 586 DLSSNPllYMMRCFPG--VPEQKLrahLGSFGVTGNLA---LQPMY---------------TLSGGQKSRVAFAKITFKK 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 156 PTLLLLDEPSLGLAPIVVKQIFQTLrELARGGmtIFLVEQNAHHALKLADRGYVMVNGQI 215
Cdd:PLN03073 646 PHILLLDEPSNHLDLDAVEALIQGL-VLFQGG--VLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-165 |
2.22e-06 |
|
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: 48.01 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 6 LEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFrGEEishrsthyVASGGIAQA 85
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GET--------VKLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 86 PEGrrIFPDMTVEENLLMGT--IPIGN------AHAAE------DMQKmfdlfprlkerrkqRAMTMSGGEQQMLAIARA 151
Cdd:TIGR03719 394 RDA--LDPNKTVWEEISGGLdiIKLGKreipsrAYVGRfnfkgsDQQK--------------KVGQLSGGERNRVHLAKT 457
|
170
....*....|....
gi 2790487090 152 LMSRPTLLLLDEPS 165
Cdd:TIGR03719 458 LKSGGNVLLLDEPT 471
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
21-229 |
3.04e-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: 46.83 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVAS--GGIAQAP---EGRRIF--- 92
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSrlSIILQDPilfSGSIRFnld 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 93 PDMTVEENLLMGTIPIGNahaaedMQKMFDLFP-RLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLaPI 171
Cdd:cd03288 117 PECKCTDDRLWEALEIAQ------LKNMVKSLPgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI-DM 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487090 172 VVKQIFQTLRELARGGMTIFLVEQNAHHALKlADRGYVMVNGQIRLSGSGEDLLGNQE 229
Cdd:cd03288 190 ATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQED 246
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-165 |
3.31e-06 |
|
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: 47.47 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 27 QVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQIlFRGEEISHRsthyvasggiaqaPEGRRIFPDMTVEEnLLMGTI 106
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-DEDLKISYK-------------PQYISPDYDGTVEE-FLRSAN 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487090 107 PI---GNAHAAEDMQKMfdlfpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPS 165
Cdd:COG1245 427 TDdfgSSYYKTEIIKPL-----GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-163 |
3.80e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.02 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 38 GANGAGKSTLLMSIFGQPRIRGGQILFRGEEISHRSTHYVASGGiaqapEGRRIFPDMTVEENLLMGTiPIGNahAAEDM 117
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIG-----HNLGLKLEMTVFENLKFWS-EIYN--SAETL 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2790487090 118 QKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDE 163
Cdd:PRK13541 105 YAAIHYF-KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-206 |
4.01e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.38 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 4 PMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEEISH-RSTHYVASGGI 82
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRgDRSRFMAYLGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 83 AQApegrrIFPDMTVEENL-----LMGTIP---IGNAHAAEDMQKMFDLFPRlkerrkqramTMSGGEQQMLAIARALMS 154
Cdd:PRK13543 90 LPG-----LKADLSTLENLhflcgLHGRRAkqmPGSALAIVGLAGYEDTLVR----------QLSAGQKKRLALARLWLS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2790487090 155 RPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAHHALKLADR 206
Cdd:PRK13543 155 PAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTR 206
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
4-82 |
5.71e-06 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 46.47 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 4 PMLEFHEVDVFYGA-IQALKQVslqVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQIlfRGEE------ISHRSTHY 76
Cdd:PRK01889 170 PGVPVLAVSALDGEgLDVLAAW---LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV--REDDskgrhtTTHRELHP 244
|
....*.
gi 2790487090 77 VASGGI 82
Cdd:PRK01889 245 LPSGGL 250
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
137-235 |
7.92e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 137 TMSGGEQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELA-RGGMTIFLVeqnAHH--ALKLADRGYVMVNG 213
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITI---AHRiaSIKRSDKIVVFNNP 1434
|
90 100
....*....|....*....|....*...
gi 2790487090 214 Q-----IRLSGSGEDLLGNQE-VRKAYL 235
Cdd:PTZ00265 1435 DrtgsfVQAHGTHEELLSVQDgVYKKYV 1462
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
21-164 |
8.66e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 8.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQIlfrgeeishRSTHYVASGGIAQAPEGRriFP-DMTVEE 99
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV---------KWSENANIGYYAQDHAYD--FEnDLTLFD 403
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487090 100 NLLMGTIPignahaAEDMQKMFDLFPRL---KERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEP 164
Cdd:PRK15064 404 WMSQWRQE------GDDEQAVRGTLGRLlfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
94-196 |
1.33e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.79 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 94 DMTVEEnllmgtipignahAAEdmqkMFDLFPRLKERRK-------------QRAMTMSGGEQQMLAIARALMSR---PT 157
Cdd:COG0178 787 DMTVEE-------------ALE----FFENIPKIARKLQtlqdvglgyiklgQPATTLSGGEAQRVKLASELSKRstgKT 849
|
90 100 110
....*....|....*....|....*....|....*....
gi 2790487090 158 LLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQN 196
Cdd:COG0178 850 LYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHN 888
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-194 |
1.38e-05 |
|
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: 45.55 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 30 QGETVALIGANGAGKSTLLmsifgqpRIRGGQI------------------LFRGEEIShrsTHY--VASGGI--AQAPE 87
Cdd:COG1245 98 KGKVTGILGPNGIGKSTAL-------KILSGELkpnlgdydeepswdevlkRFRGTELQ---DYFkkLANGEIkvAHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 88 GRRIFPDM---TVEEnLLMGTIPIGNA-HAAE--DMQKMFDlfprlkerrkQRAMTMSGGEQQMLAIARALMSRPTLLLL 161
Cdd:COG1245 168 YVDLIPKVfkgTVRE-LLEKVDERGKLdELAEklGLENILD----------RDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*....
gi 2790487090 162 DEPSLGLapivvkQIFQ------TLRELARGGMTIFLVE 194
Cdd:COG1245 237 DEPSSYL------DIYQrlnvarLIRELAEEGKYVLVVE 269
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
94-196 |
2.12e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.06 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 94 DMTVEEnllmgtipignahAAEdmqkMFDLFPRLKERRK-------------QRAMTMSGGEQQMLAIARALMSRPT--- 157
Cdd:PRK00349 791 DMTVEE-------------ALE----FFEAIPKIARKLQtlvdvglgyiklgQPATTLSGGEAQRVKLAKELSKRSTgkt 853
|
90 100 110
....*....|....*....|....*....|....*....
gi 2790487090 158 LLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQN 196
Cdd:PRK00349 854 LYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHN 892
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
2-195 |
4.82e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 43.97 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 2 NEPMLEFHEVDVFYGAIQAL-KQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGqilfrgeeishrsTHYVASG 80
Cdd:TIGR00954 448 QDNGIKFENIPLVTPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG-------------RLTKPAK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 G----IAQAPE-GRR------IFPDmTVEENLLMGtipIGNAhaaeDMQKMFD---LFPRLKERRKQRAM-----TMSGG 141
Cdd:TIGR00954 515 GklfyVPQRPYmTLGtlrdqiIYPD-SSEDMKRRG---LSDK----DLEQILDnvqLTHILEREGGWSAVqdwmdVLSGG 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790487090 142 EQQMLAIARALMSRPTLLLLDEPSLGLAPIVVKQIFQTLRELargGMTIFLVEQ 195
Cdd:TIGR00954 587 EKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF---GITLFSVSH 637
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-165 |
5.15e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 5 MLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGE---EISHRSTHYVASGG 81
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlAWVNQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 82 IAQAPEGRRIFPDMtvEENLLMGTI-----PIGNAHAAEDMQKMFDLFPRL----------KERRKQRAMTMSGGEQQML 146
Cdd:PRK10636 81 LEYVIDGDREYRQL--EAQLHDANErndghAIATIHGKLDAIDAWTIRSRAasllhglgfsNEQLERPVSDFSGGWRMRL 158
|
170
....*....|....*....
gi 2790487090 147 AIARALMSRPTLLLLDEPS 165
Cdd:PRK10636 159 NLAQALICRSDLLLLDEPT 177
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-238 |
5.20e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 133 QRAMTMSGGEQQMLAIARALM---SRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFLVEQNAhHALKLAD---- 205
Cdd:PRK00635 1695 QNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDP-ALLKQADylie 1773
|
90 100 110
....*....|....*....|....*....|....*.
gi 2790487090 206 --RGYVMVNGQIRLSGSGEDL-LGNQEVRKAYLGGV 238
Cdd:PRK00635 1774 mgPGSGKTGGKILFSGPPKDIsASKDSLLKTYMCNL 1809
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-165 |
5.34e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 4 PMLEFHEVDVFYGAIQALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQI-LFRGEEISHRSTHYVASggi 82
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEF--- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 83 aqapegrrifpdMTVEENLLMGTIPIGNAHAAEDMQKMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLD 162
Cdd:PRK10636 388 ------------LRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
...
gi 2790487090 163 EPS 165
Cdd:PRK10636 456 EPT 458
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-192 |
6.21e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 20 ALKQVSLQVNQGETVALIGANGAGKST-------LL------MSIFGQPrirggqilfrgeeishrsthyVASGGIAQAp 86
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLpasegeAWLFGQP---------------------VDAGDIATR- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 87 egRRI---------FPDMTVEENL-----LMGtipIGNAHAAEDMQKMFDLFpRLKERRKQRAMTMSGGEQQMLAIARAL 152
Cdd:NF033858 339 --RRVgymsqafslYGELTVRQNLelharLFH---LPAAEIAARVAEMLERF-DLADVADALPDSLPLGIRQRLSLAVAV 412
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2790487090 153 MSRPTLLLLDEPSLGLAPIVVKQIFQTLRELAR-GGMTIFL 192
Cdd:NF033858 413 IHKPELLILDEPTSGVDPVARDMFWRLLIELSReDGVTIFI 453
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
21-192 |
9.71e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 42.68 E-value: 9.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 21 LKQVSLQVNQGETVaLIGANGAGKSTLLMSI---FG---QPRI------RGGQILFRGEEIS-------HRSTHYVASGG 81
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALrllLGpssSRKFdeedfyLGDDPDLPEIEIEltfgsllSRLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 82 IAQAPEG--------------------RRIFPDMTVEENLLMGTipigNAHAAEDMQKMFDLfpRLKERRKQRAMTMSGG 141
Cdd:COG3593 93 DKEELEEaleelneelkealkalnellSEYLKELLDGLDLELEL----SLDELEDLLKSLSL--RIEDGKELPLDRLGSG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487090 142 EQQMLAIA--RALM-----SRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTIFL 192
Cdd:COG3593 167 FQRLILLAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVII 224
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-227 |
1.10e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.96 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 20 ALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGeeishrSTHYVAsggIAQAPEGRrifpdMTVEE 99
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALIA---ISSGLNGQ-----LTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 100 N-----LLMGtipIGNAHAAEDMQKMFDlFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEP-SLGlAPIVV 173
Cdd:PRK13545 105 NielkgLMMG---LTKEKIKEIIPEIIE-FADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAlSVG-DQTFT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790487090 174 KQIFQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGN 227
Cdd:PRK13545 180 KKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
122-209 |
1.44e-04 |
|
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: 41.40 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 122 DLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSlglAPIVVKQIFQTLRELAR----GGMTIFLVEQNA 197
Cdd:cd03222 56 DEWDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPS---AYLDIEQRLNAARAIRRlseeGKKTALVVEHDL 132
|
90
....*....|..
gi 2790487090 198 HHALKLADRGYV 209
Cdd:cd03222 133 AVLDYLSDRIHV 144
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-205 |
1.83e-04 |
|
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: 41.58 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 31 GETVALIGANGAGKSTLLMSIFGQ--PRIRGGQ-------IL--FRGEEISHRSTHyVASGGI--AQAPEGRRIFP---D 94
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKlkPNLGKFDdppdwdeILdeFRGSELQNYFTK-LLEGDVkvIVKPQYVDLIPkavK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 95 MTVEENLlmgtipignaHAAEDMQKMFDLFPRLKER--RKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGLApiv 172
Cdd:cd03236 105 GKVGELL----------KKKDERGKLDELVDQLELRhvLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD--- 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 2790487090 173 VKQIF---QTLRELARGGMTIFLVEqnahHALKLAD 205
Cdd:cd03236 172 IKQRLnaaRLIRELAEDDNYVLVVE----HDLAVLD 203
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
129-165 |
7.58e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 7.58e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2790487090 129 ERRKQRAMTMSGGEQQMLAIARALMSRPTLLLLDEPS 165
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPT 372
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
135-168 |
1.68e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.24 E-value: 1.68e-03
10 20 30
....*....|....*....|....*....|....
gi 2790487090 135 AMTMSGGEQQMLAIARALMSRPTLLLLDEPSLGL 168
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-229 |
2.06e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.26 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 1 MNEPMLEFHEVDVFYgaiqALKQVSLQVNQGETVALIGANGAGKSTLLMSIFGQPRIRGGQILFRGEeishrsthyVASG 80
Cdd:PRK13546 24 MKDALIPKHKNKTFF----ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE---------VSVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 81 GIAQAPEGRrifpdMTVEEN-----LLMGTIPignAHAAEDMQKMFDlFPRLKERRKQRAMTMSGGEQQMLAIARALMSR 155
Cdd:PRK13546 91 AISAGLSGQ-----LTGIENiefkmLCMGFKR---KEIKAMTPKIIE-FSELGEFIYQPVKKYSSGMRAKLGFSINITVN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487090 156 PTLLLLDEP-SLGLAPIVVKQIfQTLRELARGGMTIFLVEQNAHHALKLADRGYVMVNGQIRLSGSGEDLLGNQE 229
Cdd:PRK13546 162 PDILVIDEAlSVGDQTFAQKCL-DKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYE 235
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
34-184 |
2.18e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.07 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 34 VALIGANGAGKSTLLMSI----FGQPRIRGG---QILFRGE-------EISHRSTHYV--------ASGGIAQAPEGRRI 91
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIryalYGKARSRSKlrsDLINVGSeeasvelEFEHGGKRYRierrqgefAEFLEAKPSERKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 92 FpdmtveENLLmGTIPIGNAHA-----AEDMQKMFDLFPRLKERRKQR---------AMTMSGGEQQMLAIARALMsrpt 157
Cdd:COG0419 106 L------KRLL-GLEIYEELKErlkelEEALESALEELAELQKLKQEIlaqlsgldpIETLSGGERLRLALADLLS---- 174
|
170 180
....*....|....*....|....*..
gi 2790487090 158 lLLLDEPSLGlaPIVVKQIFQTLRELA 184
Cdd:COG0419 175 -LILDFGSLD--EERLERLLDALEELA 198
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
30-62 |
4.13e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 37.38 E-value: 4.13e-03
10 20 30
....*....|....*....|....*....|...
gi 2790487090 30 QGETVALIGANGAGKSTLLMSIFGQPRIRGGQI 62
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
35-194 |
8.48e-03 |
|
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: 35.80 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 35 ALIGANGAGKSTLLmsifgqprirggqilfrgeeishRSTHYVAsgGIAQAPEGRRifpdmtveenllmGTIPIGNAHAA 114
Cdd:cd03227 25 IITGPNGSGKSTIL-----------------------DAIGLAL--GGAQSATRRR-------------SGVKAGCIVAA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487090 115 EDMQKMFDLfprlkerrkqraMTMSGGEQQMLAIARAL----MSRPTLLLLDEPSLGLAPIVVKQIFQTLRELARGGMTI 190
Cdd:cd03227 67 VSAELIFTR------------LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQV 134
|
....
gi 2790487090 191 FLVE 194
Cdd:cd03227 135 IVIT 138
|
|
| |
