|
Name |
Accession |
Description |
Interval |
E-value |
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-237 |
1.05e-138 |
|
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: 388.19 E-value: 1.05e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 3 EPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGI 82
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 83 AQAPEGRRIFPDMSVEENLLMGTIPVGNQHA-AEDMQSMFDLFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLL 161
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAEvRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953848 162 DEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEVRKAYLGG 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 |
1.12e-119 |
|
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: 339.80 E-value: 1.12e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAQA 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 86 PEGRRIFPDMSVEENLLMGTIPVGNQHAAEDMQSMFDLFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515953848 166 LGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKD 227
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-237 |
9.50e-101 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 292.55 E-value: 9.50e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATG 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 81 GIAQAPEGRRIFPDMSVEENLLMGTIPVGNQHAAEDMQSMFDLFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLL 160
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515953848 161 LDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEVRKAYLGG 237
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLGG 237
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-233 |
6.45e-80 |
|
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: 239.35 E-value: 6.45e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAQA 85
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 86 PEGRRIFPDMSVEENLLMG--TIPVGNQHAAEDMqsmFDLFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGlaALPRRSRKIPDEI---YELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953848 164 PSLGLAPIVVKQIFQTLRELA-RNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEAlLKDPEVRKA 233
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRaEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDE-LDEDKVRRY 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-237 |
2.13e-63 |
|
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: 197.95 E-value: 2.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 2 SEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGG 81
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 IA---QAPegrRIFPDMSVEENLLMGtipVGNQHAAEDMQSMFDLFPR-------------------LKERRNQRAMTLS 139
Cdd:COG0411 81 IArtfQNP---RLFPELTVLENVLVA---AHARLGRGLLAALLRLPRArreereareraeellervgLADRADEPAGNLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 140 GGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEqnaHH---ALKLSDRGYVMVNGQI 215
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIE---HDmdlVMGLADRIVVLDFGRV 231
|
250 260
....*....|....*....|..
gi 515953848 216 RLSGSGEALLKDPEVRKAYLGG 237
Cdd:COG0411 232 IAEGTPAEVRADPRVIEAYLGE 253
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-230 |
9.33e-58 |
|
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: 183.02 E-value: 9.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIA-- 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 -QAPegrRIFPDMSVEENLLMGTIPVGNQH------------AAEDMQSMFDLFpRLKERRNQRAMTLSGGEQQMLAIAR 150
Cdd:cd03219 81 fQIP---RLFPELTVLENVMVAAQARTGSGlllararreereARERAEELLERV-GLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEV 230
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-236 |
1.75e-56 |
|
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: 179.66 E-value: 1.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 14 FYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAQAPEGRRIFP 93
Cdd:cd03218 9 RYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLPQEASIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 94 DMSVEENLL--MGTIPVGNQHAAEDMQSMFDLFpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:cd03218 89 KLTVEENILavLEIRGLSKKEREEKLEELLEEF-HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515953848 172 VVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEVRKAYLG 236
Cdd:cd03218 168 AVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-236 |
3.07e-53 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 171.75 E-value: 3.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 3 EPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGI 82
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 83 ---AQAPEgrrIFPDMSVEENLL--MGTIPVGNQHAAEDMQSMFDLFpRLKERRNQRAMTLSGGEQQMLAIARALMSRPK 157
Cdd:COG1137 81 gylPQEAS---IFRKLTVEDNILavLELRKLSKKEREERLEELLEEF-GITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515953848 158 LLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEVRKAYLG 236
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLG 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-226 |
4.99e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 171.01 E-value: 4.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATggIAQA 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR--IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 86 PEGRRIFPDMSVEENL-LMGTI-PVGNQHAAEDMQSMFDLFpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:COG1131 79 PQEPALYPDLTVRENLrFFARLyGLPRKEARERIDELLELF-GLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515953848 164 PSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLK 226
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
15-236 |
6.55e-49 |
|
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: 160.52 E-value: 6.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAQAPEGRRIFPD 94
Cdd:TIGR04406 11 YKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYLPQEASIFRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 95 MSVEENLLMGTIPVGNQHAAEDMQSMFDLFPRL--KERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIV 172
Cdd:TIGR04406 91 LTVEENIMAVLEIRKDLDRAEREERLEALLEEFqiSHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515953848 173 VKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEVRKAYLG 236
Cdd:TIGR04406 171 VGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLG 234
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-234 |
8.23e-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: 8.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTH--YVA 78
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 79 tggiaQAPEGRRIFPdMSVEENLLMGTIPVGNqhaaedmqsmfdLFPRLKERRNQRAM-----------------TLSGG 141
Cdd:COG1121 82 -----QRAEVDWDFP-ITVRDVVLMGRYGRRG------------LFRRPSRADREAVDealervgledladrpigELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 142 EQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRgYVMVNGQIRLSGSG 221
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDR-VLLLNRGLVAHGPP 222
|
250
....*....|...
gi 515953848 222 EALLKDPEVRKAY 234
Cdd:COG1121 223 EEVLTPENLSRAY 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-215 |
8.65e-44 |
|
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: 145.23 E-value: 8.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVatGGIAQA 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK--RRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 86 PEGRRIFPDMSVEENLlmgtipvgnqhaaedmqsmfdlfprlkerrnqramTLSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:cd03230 79 PEEPSLYENLTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515953848 166 LGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-233 |
2.16e-43 |
|
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: 145.94 E-value: 2.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVAtggiaq 84
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 85 apegRRI-----FPD-----MSVEENLLMGtiPVGNQHAAEDMQ-------SMFDlfprLKERRNQRAMTLSGGEQQMLA 147
Cdd:COG1122 75 ----RKVglvfqNPDdqlfaPTVEEDVAFG--PENLGLPREEIRerveealELVG----LEHLADRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 148 IARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKD 227
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSD 224
|
....*.
gi 515953848 228 PEVRKA 233
Cdd:COG1122 225 YELLEE 230
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-229 |
4.50e-43 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 145.52 E-value: 4.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHyvatggIAQ 84
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKD------INK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 85 ApegRR----------IFPDMSVEENLLMGTIPVGNQHAAEDMQSMFDLFPR--LKERRNQRAMTLSGGEQQMLAIARAL 152
Cdd:COG1126 75 L---RRkvgmvfqqfnLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERvgLADKADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515953848 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPE 229
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQ 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-235 |
1.02e-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: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVAtgGIAQ 84
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARR--QIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 85 APEGRRIFPDMSVEENL-----LMGTIPVGNQHAAEDMQSMFDLFprlkERRNQRAMTLSGGEQQMLAIARALMSRPKLL 159
Cdd:COG4555 79 LPDERGLYDRLTVRENIryfaeLYGLFDEELKKRIEELIELLGLE----EFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515953848 160 LLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLK---DPEVRKAYL 235
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREeigEENLEDAFV 233
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-214 |
3.20e-42 |
|
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: 142.61 E-value: 3.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 7 QFQDVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVA--TGGI 82
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 83 AQAPEGRRIFPdmSVEENLLMGtiPVGNQHAAEDMQ----SMFDLFpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKL 158
Cdd:cd03225 81 FQNPDDQFFGP--TVEEEVAFG--LENLGLPEEEIEerveEALELV-GLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515953848 159 LLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQ 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 |
2.43e-41 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 140.78 E-value: 2.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLL-----MSVFGQPRIRNGQILFCGEDISHKSTHYVA-- 78
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLrllnrLNDLIPGAPDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 79 --TGGIAQAPEgrrIFPdMSVEENLLMGTIPVG---NQHAAEDMQ---SMFDLFPRLKerRNQRAMTLSGGEQQMLAIAR 150
Cdd:cd03260 81 rrVGMVFQKPN---PFP-GSIYDNVAYGLRLHGiklKEELDERVEealRKAALWDEVK--DRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515953848 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNgMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-224 |
3.69e-41 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 140.96 E-value: 3.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 4 PMLQFQDVDV-FYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSThyvatggi 82
Cdd:COG3638 1 PMLELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 83 AQAPEGRR----IF------PDMSVEENLLMGTIPvgnQHAAedMQSMFDLFPR--------------LKERRNQRAMTL 138
Cdd:COG3638 73 RALRRLRRrigmIFqqfnlvPRLSVLTNVLAGRLG---RTST--WRSLLGLFPPedreralealervgLADKAYQRADQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 139 SGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELAR-NGMTIfLVeqNAHH---ALKLSDRGYVMVNGQ 214
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITV-VV--NLHQvdlARRYADRIIGLRDGR 224
|
250
....*....|
gi 515953848 215 IRLSGSGEAL 224
Cdd:COG3638 225 VVFDGPPAEL 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-234 |
1.33e-40 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 139.41 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVAT--GGI 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARriAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 83 AQAPEGRrifPDMSVEENLLMGTIPVGN---QHAAED----MQSMFDLfpRLKERRNQRAMTLSGGEQQMLAIARALMSR 155
Cdd:COG1120 81 PQEPPAP---FGLTVRELVALGRYPHLGlfgRPSAEDreavEEALERT--GLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 156 PKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVeqnAH---HALKLSDRGYVMVNGQIRLSGSGEALLKDPEVR 231
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMV---LHdlnLAARYADRLVLLKDGRIVAQGPPEEVLTPELLE 232
|
...
gi 515953848 232 KAY 234
Cdd:COG1120 233 EVY 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-205 |
2.56e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 137.88 E-value: 2.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVatggia 83
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREI------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 qaPEGRR----IF------PDMSVEENLLMGTIPVGNQHA--AEDMQSMFDLFpRLKERRNQRAMTLSGGEQQMLAIARA 151
Cdd:COG2884 75 --PYLRRrigvVFqdfrllPDRTVYENVALPLRVTGKSRKeiRRRVREVLDLV-GLSDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953848 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIF-------LVEQNAHHALKLSD 205
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLiathdleLVDRMPKRVLELED 212
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-215 |
2.88e-40 |
|
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: 137.62 E-value: 2.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYG----VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHyvatgg 81
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEK------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 iAQAPEGRR----IF------PDMSVEENLLMGTIPVG--NQHAAEDMQSMFDLFpRLKERRNQRAMTLSGGEQQMLAIA 149
Cdd:cd03255 75 -ELAAFRRRhigfVFqsfnllPDLTALENVELPLLLAGvpKKERRERAEELLERV-GLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515953848 150 RALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNaHHALKLSDRGYVMVNGQI 215
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-214 |
4.13e-40 |
|
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: 135.45 E-value: 4.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 7 QFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSthyvatggiaqap 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 87 egrrifpdmsveenllmgtipvgnqhaaedmqsmfdlfprLKERRNQRAMT--LSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:cd00267 68 ----------------------------------------LEELRRRIGYVpqLSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515953848 165 SLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQ 214
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-219 |
4.17e-40 |
|
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: 137.28 E-value: 4.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 7 QFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTH--YVAtggiaQ 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigYVP-----Q 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 85 APEGRRIFPdMSVEENLLMGTIPVGNQH------------AAEDMQSMFDLfprlkerRNQRAMTLSGGEQQMLAIARAL 152
Cdd:cd03235 76 RRSIDRDFP-ISVRDVVLMGLYGHKGLFrrlskadkakvdEALERVGLSEL-------ADRQIGELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515953848 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRgYVMVNGQIRLSG 219
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-215 |
6.29e-40 |
|
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: 136.51 E-value: 6.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSThyvatggiaQA 85
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKK---------NI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 86 PEGRR----------IFPDMSVEENLLMGTIPVGNQHAAEDMQSMFDLFPR--LKERRNQRAMTLSGGEQQMLAIARALM 153
Cdd:cd03262 72 NELRQkvgmvfqqfnLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKvgLADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515953848 154 SRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-236 |
7.21e-40 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 137.81 E-value: 7.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATG 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 81 GIAQAPEGRRIFPDMSVEENLLMG--------------TIPVGNQHAAEDMQSMFDLFPR--LKERRNQRAMTLSGGEQQ 144
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLVAqhqqlktglfsgllKTPAFRRAESEALDRAATWLERvgLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 145 MLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEA 223
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
250
....*....|...
gi 515953848 224 LLKDPEVRKAYLG 236
Cdd:PRK11300 241 IRNNPDVIKAYLG 253
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-164 |
1.44e-39 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 133.54 E-value: 1.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVaTGGIAQAPEGRRIFPDMSVEEN 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL-RKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515953848 101 LLMGTIPVGNQHAAEDMQ-----SMFDLFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARaeealEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-215 |
2.57e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 141.69 E-value: 2.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 2 SEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGG 81
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 IA---QAPEgrrIFPDMSVEENLLMGTIPVG---------NQHAAEDMQSM-FDLFPRlkerrnQRAMTLSGGEQQMLAI 148
Cdd:COG1129 81 IAiihQELN---LVPNLSVAENIFLGREPRRgglidwramRRRARELLARLgLDIDPD------TPVGDLSVAQQQLVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVeqnAHH---ALKLSDRGYVMVNGQI 215
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYI---SHRldeVFEIADRVTVLRDGRL 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-215 |
2.87e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 135.17 E-value: 2.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 3 EPMLQFQDVDVFYGV----IQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKS----T 74
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 75 HYvatggiaqapegRR-----IF------PDMSVEENLLMGTIPVGNQHA-----AEDMQSMFDLfprlKERRNQRAMTL 138
Cdd:COG1136 82 RL------------RRrhigfVFqffnllPELTALENVALPLLLAGVSRKerrerARELLERVGL----GDRLDHRPSQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 139 SGGEQQMLAIARALMSRPKLLLLDEP--SL----GlapivvKQIFQTLRELARN-GMTIFLV---EQNAHHAlklsDRGY 208
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPtgNLdsktG------EEVLELLRELNRElGTTIVMVthdPELAARA----DRVI 215
|
....*..
gi 515953848 209 VMVNGQI 215
Cdd:COG1136 216 RLRDGRI 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-215 |
3.50e-39 |
|
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: 135.33 E-value: 3.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFY----GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATG 80
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 81 G-----IAQAPeGRRIFPDMSVEENLLMGTIPVGNQHAAEDMQ----SMFDLFPRLKERRNQRAMTLSGGEQQMLAIARA 151
Cdd:cd03257 81 RkeiqmVFQDP-MSSLNPRMTIGEQIAEPLRIHGKLSKKEARKeavlLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515953848 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARNGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-234 |
4.53e-39 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 135.39 E-value: 4.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYG-VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVA-----T 79
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 80 GGIAQAPegrRIFPDMSVEENLLMGTIpvgNQHAAedMQSMFDLFPR--------------LKERRNQRAMTLSGGEQQM 145
Cdd:cd03256 81 GMIFQQF---NLIERLSVLENVLSGRL---GRRST--WRSLFGLFPKeekqralaalervgLLDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLveqNAHH---ALKLSDRGYVMVNGQIRLSGSG 221
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIV---SLHQvdlAREYADRIVGLKDGRIVFDGPP 229
|
250
....*....|...
gi 515953848 222 EAlLKDPEVRKAY 234
Cdd:cd03256 230 AE-LTDEVLDEIY 241
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-215 |
5.45e-39 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 134.18 E-value: 5.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHyvaTGGIAQA 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE---RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 86 PEGRRIFPDMSVEEN----LLMGTIPVGNQHA-AEDMQSMFDLFPRLKERRNQramtLSGGEQQMLAIARALMSRPKLLL 160
Cdd:cd03259 78 FQDYALFPHLTVAENiafgLKLRGVPKAEIRArVRELLELVGLEGLLNRYPHE----LSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515953848 161 LDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-228 |
2.32e-38 |
|
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: 139.27 E-value: 2.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYGV-----IQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSth 75
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVrgkggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLS-- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 76 yvatgGIAQAPEGRRI-----------FPDMSVEENL-----LMGTIPVGNQHA-AEDMQSMFDLFPRLKERRnqrAMTL 138
Cdd:COG1123 334 -----RRSLRELRRRVqmvfqdpysslNPRMTVGDIIaeplrLHGLLSRAERRErVAELLERVGLPPDLADRY---PHEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 139 SGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVeqnAHH---ALKLSDRGYVMVNGQ 214
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFI---SHDlavVRYIADRVAVMYDGR 482
|
250
....*....|....
gi 515953848 215 IRLSGSGEALLKDP 228
Cdd:COG1123 483 IVEDGPTEEVFANP 496
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-229 |
4.07e-38 |
|
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: 138.50 E-value: 4.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 3 EPMLQFQDVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFG---QPRIRNGQILFCGEDISHKSTHYV 77
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 78 AT--GGIAQAPE----GRRIFPDmsVEENLLMGTIPvgNQHAAEDMQSMFDLFpRLKERRNQRAMTLSGGEQQMLAIARA 151
Cdd:COG1123 82 GRriGMVFQDPMtqlnPVTVGDQ--IAEALENLGLS--RAEARARVLELLEAV-GLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515953848 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPE 229
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-234 |
1.03e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 133.31 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLmsvfgqpRIRN-------GQILFCGEDISHKSTH-- 75
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTI-------RIILgilapdsGEVLWDGEPLDPEDRRri 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 76 -YVatggiaqaPEGRRIFPDMSVEENLL-------MGtipvgnqhAAEDMQSMFDLFPR--LKERRNQRAMTLSGGEQQM 145
Cdd:COG4152 74 gYL--------PEERGLYPKMKVGEQLVylarlkgLS--------KAEAKRRADEWLERlgLGDRANKKVEELSKGNQQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEall 225
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD--- 214
|
....*....
gi 515953848 226 kdpEVRKAY 234
Cdd:COG4152 215 ---EIRRQF 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-214 |
2.06e-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: 129.23 E-value: 2.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDIshksthyvATGGIAQA 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL--------TDLEDELP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 86 PEGRRI---------FPDMSVEENLLMGtipvgnqhaaedmqsmfdlfprlkerrnqramtLSGGEQQMLAIARALMSRP 156
Cdd:cd03229 73 PLRRRIgmvfqdfalFPHLTVLENIALG---------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515953848 157 KLLLLDEPSLGLAPIVVKQIFQTLREL-ARNGMTIFLVEQNAHHALKLSDRGYVMVNGQ 214
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-228 |
2.31e-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: 133.68 E-value: 2.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHksthyvatg 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 81 giaQAPEGRRI---------FPDMSVEEN----LLMGTIPVGNQHA-AEDMQSMFdlfpRLKERRNQRAMTLSGGEQQML 146
Cdd:COG3842 72 ---LPPEKRNVgmvfqdyalFPHLTVAENvafgLRMRGVPKAEIRArVAELLELV----GLEGLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 147 AIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARNGMTIFLVeqnAHH---ALKLSDRGYVMVNGQIRLSGSGE 222
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYV---THDqeeALALADRIAVMNDGRIEQVGTPE 221
|
....*.
gi 515953848 223 ALLKDP 228
Cdd:COG3842 222 EIYERP 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-219 |
2.32e-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: 130.03 E-value: 2.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAQA 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 86 PEgrrIFPDMSVEENL-----LMGtIPVGNQHAAEDMQSmfdlfprLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLL 160
Cdd:cd03268 81 PG---FYPNLTARENLrllarLLG-IRKKRIDEVLDVVG-------LKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515953848 161 LDEPSLGLAPIVVKQIFQTLRELARNGMTIFLveqnAHHAL----KLSDRGYVMVNGQIRLSG 219
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGITVLI----SSHLLseiqKVADRIGIINKGKLIEEG 208
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-215 |
4.00e-37 |
|
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: 128.32 E-value: 4.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 3 EPMLQFQDVdvfyGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGI 82
Cdd:cd03215 2 EPVLEVRGL----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 83 AQAPEGRR---IFPDMSVEENLLMGTIpvgnqhaaedmqsmfdlfprlkerrnqramtLSGGEQQMLAIARALMSRPKLL 159
Cdd:cd03215 78 AYVPEDRKregLVLDLSVAENIALSSL-------------------------------LSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515953848 160 LLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-231 |
4.41e-37 |
|
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: 130.10 E-value: 4.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHyvatg 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 81 giAQAPEGRRI---------FPDMSVEENLlmgtipvgnqhaaedmqsMFDL--FPRLKER-RNQRAMT----------- 137
Cdd:COG1127 76 --ELYELRRRIgmlfqggalFDSLTVFENV------------------AFPLreHTDLSEAeIRELVLEklelvglpgaa 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 138 ------LSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVM 210
Cdd:COG1127 136 dkmpseLSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVL 215
|
250 260
....*....|....*....|...
gi 515953848 211 VNGQIRLSGSGEALLK--DPEVR 231
Cdd:COG1127 216 ADGKIIAEGTPEELLAsdDPWVR 238
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-228 |
4.62e-37 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 130.21 E-value: 4.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDIshksthyvaTGGIAQ 84
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV---------NDPKVD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 85 APEGRR----------IFPDMSVEENLLMGTIPVGNQHAAEDMQSMFDLFPR--LKERRNQRAMTLSGGEQQMLAIARAL 152
Cdd:PRK09493 72 ERLIRQeagmvfqqfyLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKvgLAERAHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953848 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDP 228
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-220 |
4.69e-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: 126.85 E-value: 4.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDIshKSTHYVATGGIAQAPEGRRIFPDMSVEE 99
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQSLGYCPQFDALFDELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 100 NL-LMGTIP-VGNQHAAEDMQSMFDLFpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIF 177
Cdd:cd03263 95 HLrFYARLKgLPKSEIKEEVELLLRVL-GLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIW 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515953848 178 QTLRELARNgMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGS 220
Cdd:cd03263 174 DLILEVRKG-RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGS 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-219 |
1.05e-35 |
|
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: 125.86 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGE--DISHKSThyvatggIA 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKplDIAARNR-------IG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 QAPEGRRIFPDMSVEENL-----LMGtipVGNQHAAEDMQSMFDLFpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKL 158
Cdd:cd03269 74 YLPEERGLYPKMKVIDQLvylaqLKG---LKKEEARRRIDEWLERL-ELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953848 159 LLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSG 219
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-215 |
1.66e-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: 1.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAqa 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 86 pegrrifpdmsveenllmgTIPvgnqhaaedmqsmfdlfprlkerrnQramtLSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:cd03216 79 -------------------MVY-------------------------Q----LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515953848 166 LGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-231 |
1.84e-35 |
|
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: 125.69 E-value: 1.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSthyvatgGIAQA 85
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLS-------EAELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 86 PEGRRI---------FPDMSVEENllmgtipVG---NQHAAEDMQSMFDL------FPRLKERRNQRAMTLSGGEQQMLA 147
Cdd:cd03261 74 RLRRRMgmlfqsgalFDSLTVFEN-------VAfplREHTRLSEEEIREIvlekleAVGLRGAEDLYPAELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 148 IARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELAR-NGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLK 226
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
....*..
gi 515953848 227 --DPEVR 231
Cdd:cd03261 227 sdDPLVR 233
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-229 |
3.23e-35 |
|
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: 125.30 E-value: 3.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGV----IQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKST--HYVA 78
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkaFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 79 TGGIAQAPEG-----RRIfpDMSVEENLLMGTIPVGNQHAAEDMQSMfDLFPRLKERR-NQramtLSGGEQQMLAIARAL 152
Cdd:COG1124 81 VQMVFQDPYAslhprHTV--DRILAEPLRIHGLPDREERIAELLEQV-GLPPSFLDRYpHQ----LSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515953848 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPE 229
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-215 |
3.48e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.52 E-value: 3.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 3 EPMLQFQDVdvfyGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGI 82
Cdd:COG1129 254 EVVLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 83 AQAPEGRR---IFPDMSVEENLLMGTIP-------VGNQHAAEDMQSMFDLFpRLK-ERRNQRAMTLSGGEQQMLAIARA 151
Cdd:COG1129 330 AYVPEDRKgegLVLDLSIRENITLASLDrlsrgglLDRRRERALAEEYIKRL-RIKtPSPEQPVGNLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515953848 152 LMSRPKLLLLDEPSLGlapIVV---KQIFQTLRELARNGMTIFLV-----EqnahhALKLSDRGYVMVNGQI 215
Cdd:COG1129 409 LATDPKVLILDEPTRG---IDVgakAEIYRLIRELAAEGKAVIVIsselpE-----LLGLSDRILVMREGRI 472
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-236 |
4.26e-35 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 125.01 E-value: 4.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAQAPEGRRIFPDMSVE 98
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEASIFRRLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 99 ENLlMGTIPVGNQHAAEDMQ----SMFDLFpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVK 174
Cdd:PRK10895 97 DNL-MAVLQIRDDLSAEQREdranELMEEF-HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515953848 175 QIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEVRKAYLG 236
Cdd:PRK10895 175 DIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLG 236
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-229 |
4.60e-35 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 125.27 E-value: 4.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSV--FGQ--PRIR-NGQILFCGEDISHKSTH 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDlnPEVTiTGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 76 YV----ATGGIAQAPEGrriFPdMSVEENLLMGTIPVGNQ------HAAEDMQSMFDLFPRLKERRNQRAMTLSGGEQQM 145
Cdd:PRK14239 81 TVdlrkEIGMVFQQPNP---FP-MSIYENVVYGLRLKGIKdkqvldEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELaRNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALL 225
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
....
gi 515953848 226 KDPE 229
Cdd:PRK14239 236 MNPK 239
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-214 |
5.31e-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: 122.49 E-value: 5.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYG--VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYV--ATGG 81
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 IAQAPEgrrIFpDMSVEENLLmgtipvgnqhaaedmqsmfdlfprlkerrnqramtlSGGEQQMLAIARALMSRPKLLLL 161
Cdd:cd03228 81 VPQDPF---LF-SGTIRENIL------------------------------------SGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515953848 162 DEPSLGLAPIVVKQIFQTLRELARnGMTIFLVeqnAH--HALKLSDRGYVMVNGQ 214
Cdd:cd03228 121 DEATSALDPETEALILEALRALAK-GKTVIVI---AHrlSTIRDADRIIVLDDGR 171
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-226 |
1.27e-33 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 126.80 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 2 SEPMLQFQDVDVFYGV-IQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVAT- 79
Cdd:COG4988 333 GPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRq 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 80 -GGIAQAPegrRIFPDmSVEENLLMGTIPVGN---QHAAE--DMQSMFDLFPR-LKERRNQRAMTLSGGEQQMLAIARAL 152
Cdd:COG4988 413 iAWVPQNP---YLFAG-TIRENLRLGRPDASDeelEAALEaaGLDEFVAALPDgLDTPLGEGGRGLSGGQAQRLALARAL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953848 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARnGMTIFLVeqnAH--HALKLSDRGYVMVNGQIRLSGSGEALLK 226
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILI---THrlALLAQADRILVLDDGRIVEQGTHEELLA 560
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-222 |
1.40e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 121.73 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVD-VFY-GVI---QALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTH---- 75
Cdd:COG1101 1 MLELKNLSkTFNpGTVnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYkrak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 76 YVAtggiaqapegrRIF--------PDMSVEENLLMG---------TIPVGNQHAAE--DMQSMFDLfpRLKERRNQRAM 136
Cdd:COG1101 81 YIG-----------RVFqdpmmgtaPSMTIEENLALAyrrgkrrglRRGLTKKRRELfrELLATLGL--GLENRLDTKVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 137 TLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARNGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
....*..
gi 515953848 216 RLSGSGE 222
Cdd:COG1101 228 ILDVSGE 234
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-229 |
1.83e-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: 126.42 E-value: 1.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 2 SEPMLQFQDVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYV-- 77
Cdd:COG4987 330 GGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLrr 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 78 ATGGIAQAPEgrrIFpDMSVEENLLMGtipvgNQHAAED-MQSMF------DLFPRLKERRN----QRAMTLSGGEQQML 146
Cdd:COG4987 410 RIAVVPQRPH---LF-DTTLRENLRLA-----RPDATDEeLWAALervglgDWLAALPDGLDtwlgEGGRRLSGGERRRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 147 AIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARnGMTIFLVeqnAHH--ALKLSDRGYVMVNGQIRLSGSGEAL 224
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLI---THRlaGLERMDRILVLEDGRIVEQGTHEEL 556
|
....*
gi 515953848 225 LKDPE 229
Cdd:COG4987 557 LAQNG 561
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-215 |
1.86e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 121.30 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 2 SEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLL-----MSVFgQPRIR-NGQILFCGEDISHKSTH 75
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnrMNDL-IPGARvEGEILLDGEDIYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 76 YVA----TGGIAQAPegrRIFPdMSVEENL-----LMGTIPVGN---------QHAAedmqsmfdLFPRLKERRNQRAMT 137
Cdd:COG1117 87 VVElrrrVGMVFQKP---NPFP-KSIYDNVayglrLHGIKSKSEldeiveeslRKAA--------LWDEVKDRLKKSALG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515953848 138 LSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNgMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
15-224 |
2.13e-33 |
|
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: 120.17 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAqaPEGRRIFPD 94
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIV--FQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 95 MSVEENLLM-GTI-PVGNQHAAEDMQSMFDLFpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIV 172
Cdd:cd03265 88 LTGWENLYIhARLyGVPGAERRERIDELLDFV-GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515953848 173 VKQIFQTLREL-ARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEAL 224
Cdd:cd03265 167 RAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-219 |
2.38e-33 |
|
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: 118.69 E-value: 2.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 9 QDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVAtggiaqapeg 88
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 89 RRIfpdmsveenllmGTIPvgnqhaaedmQSM--FDLFPrLKERRnqrAMTLSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:cd03214 73 RKI------------AYVP----------QALelLGLAH-LADRP---FNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515953848 167 GLAPIVVKQIFQTLRELAR-NGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSG 219
Cdd:cd03214 127 HLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-200 |
2.88e-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: 120.57 E-value: 2.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 3 EPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLL--------------MSVFGQPRirngqilfCGED 68
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLslitgdlpptygndVRLFGERR--------GGED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 69 ISHKSTHYvatgGIAQAPEGRRIFPDMSVEENLLMG---TIPVGNQHAAEDMQ---SMFDLFpRLKERRNQRAMTLSGGE 142
Cdd:COG1119 73 VWELRKRI----GLVSPALQLRFPRDETVLDVVLSGffdSIGLYREPTDEQRErarELLELL-GLAHLADRPFGTLSQGE 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515953848 143 QQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNG-MTIFLVeqnAHHA 200
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLV---THHV 203
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-205 |
7.98e-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: 118.50 E-value: 7.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVAT--GG 81
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLlrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 IAQAPEGRRIFPDMSVEENLLMGTIPVGN-----QHAAEDMQSMFDLfprlKERRNQRAMTLSGGEQQMLAIARALMSRP 156
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKkereiQRRVGAALRQVGL----EHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515953848 157 KLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIF-------LVEQNAHHALKLSD 205
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIvathdlsLVDRVAHRVIILDD 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-231 |
9.39e-33 |
|
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: 118.49 E-value: 9.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAQA 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 86 pegRRIFPDMSVEENLLMG--TIPVGNQHAAEDMQSMFDLFpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:cd03300 81 ---YALFPHLTVFENIAFGlrLKKLPKAEIKERVAEALDLV-QLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515953848 164 PSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEVR 231
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANR 225
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-215 |
2.98e-32 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 117.81 E-value: 2.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLL--MSVFGQPRirNGQILFCGEDIShksthYVATGGIA 83
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLrvLNLLETPD--SGQLNIAGHQFD-----FSQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 QAPEGRR----------IFPDMSVEENLLMGTIPVGNQHAAEDMQSMFDLFPRLK--ERRNQRAMTLSGGEQQMLAIARA 151
Cdd:COG4161 76 AIRLLRQkvgmvfqqynLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRltDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515953848 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-215 |
3.07e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 116.45 E-value: 3.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTH-------YVA 78
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPewrrqvaYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 79 tggiaQAPegrRIFPDmSVEENLLMgtiPVGNQHAAEDMQSMFDLFPRL---KERRNQRAMTLSGGEQQMLAIARALMSR 155
Cdd:COG4619 81 -----QEP---ALWGG-TVRDNLPF---PFQLRERKFDRERALELLERLglpPDILDKPVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953848 156 PKLLLLDEPSLGLAPIVVKQIFQTLREL-ARNGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-205 |
5.05e-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: 5.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 4 PMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDI-SHKSTHYVATGGI 82
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIrDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 83 AQAPEgrrIFPDMSVEENLLMGTIPVGNQHAAEDMQSMFDLFpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLD 162
Cdd:COG4133 81 GHADG---LKPELTVRENLRFWAALYGLRADREAIDEALEAV-GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515953848 163 EPSLGLAPIVVKQIFQTLRELARNGMTIFLVeqnAHHALKLSD 205
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLARGGAVLLT---THQPLELAA 196
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-210 |
5.39e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 117.50 E-value: 5.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFY----GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHy 76
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 77 vaTGGIAQAPegrRIFPDMSVEENLLMG--TIPVGNQHAAEDMQSMFDLFpRLKERRNQRAMTLSGGEQQMLAIARALMS 154
Cdd:COG1116 82 --RGVVFQEP---ALLPWLTVLDNVALGleLRGVPKAERRERARELLELV-GLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515953848 155 RPKLLLLDEPslglapivvkqiF-----QT--------LRELARNGMTIFLVEQNAHHALKLSDRGYVM 210
Cdd:COG1116 156 DPEVLLMDEP------------FgaldaLTrerlqdelLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-210 |
5.80e-32 |
|
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: 116.42 E-value: 5.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYG----VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHyvaTGG 81
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 IAQAPegrRIFPDMSVEENLLMG--TIPVGNQHAAEDMQSMFDLFpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLL 159
Cdd:cd03293 78 VFQQD---ALLPWLTVLDNVALGleLQGVPKAEARERAEELLELV-GLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515953848 160 LLDEPSLGLAPIVVKQIFQTLREL-ARNGMTIFLVEQNAHHALKLSDRGYVM 210
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-215 |
8.61e-32 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 116.27 E-value: 8.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSepmLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLL--MSVFGQPRirNGQIlfcgeDISHKSTHYVA 78
Cdd:PRK11124 1 MS---IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLrvLNLLEMPR--SGTL-----NIAGNHFDFSK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 79 TGGIAQAPEGRR----------IFPDMSVEENLLMGTIPVGNQHAAEDMQSMFDLFPRLkeRRNQRA----MTLSGGEQQ 144
Cdd:PRK11124 71 TPSDKAIRELRRnvgmvfqqynLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERL--RLKPYAdrfpLHLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953848 145 MLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-226 |
2.13e-31 |
|
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: 121.09 E-value: 2.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVAtGGIAQAPEGRRIFPDmSVEE 99
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLR-RQIGVVLQDVFLFSG-TIRE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 100 NLLMGTIPVGNQH---------AAEDMQSM---FDLfpRLKERrnqrAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:COG2274 568 NITLGDPDATDEEiieaarlagLHDFIEALpmgYDT--VVGEG----GSNLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953848 168 LAPIVVKQIFQTLRELARnGMTIFLVeqnAH--HALKLSDRGYVMVNGQIRLSGSGEALLK 226
Cdd:COG2274 642 LDAETEAIILENLRRLLK-GRTVIII---AHrlSTIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-236 |
4.69e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.08 E-value: 4.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGviQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHksthyvatggiaQ 84
Cdd:COG3840 1 MLRLDDLTYRYG--DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA------------L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 85 APEGRRI---------FPDMSVEENLLMGtipvgnqhaaedmqsmfdLFPRLKERRNQRAM------------------- 136
Cdd:COG3840 67 PPAERPVsmlfqennlFPHLTVAQNIGLG------------------LRPGLKLTAEQRAQveqalervglaglldrlpg 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 137 TLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVeqnAHH---ALKLSDRGYVMVN 212
Cdd:COG3840 129 QLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMV---THDpedAARIADRVLLVAD 205
|
250 260
....*....|....*....|....*.
gi 515953848 213 GQIRLSGSGEALL--KDPEVRKAYLG 236
Cdd:COG3840 206 GRIAADGPTAALLdgEPPPALAAYLG 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-225 |
1.42e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 114.90 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATG 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 81 GIAqaPEGRRIFPDMSVEENLLMGTIPVG-NQHAAEDMQSMFDLFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLL 159
Cdd:PRK13537 83 GVV--PQFDNLDPDFTVRENLLVFGRYFGlSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953848 160 LLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALL 225
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-229 |
1.91e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 115.24 E-value: 1.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSepmLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDIShksthyvatg 80
Cdd:COG1118 1 MS---IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 81 gIAQAPEGRRI---------FPDMSVEENLLMGtIPVGNQHAAE------DMQSMFDLfPRLKERR-NQramtLSGGEQQ 144
Cdd:COG1118 68 -TNLPPRERRVgfvfqhyalFPHMTVAENIAFG-LRVRPPSKAEirarveELLELVQL-EGLADRYpSQ----LSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 145 MLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLREL--ARNGMTIF----LVEqnahhALKLSDRGYVMVNGQIRLS 218
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhdELGGTTVFvthdQEE-----ALELADRVVVMNQGRIEQV 215
|
250
....*....|.
gi 515953848 219 GSGEALLKDPE 229
Cdd:COG1118 216 GTPDEVYDRPA 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-215 |
3.21e-30 |
|
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: 111.19 E-value: 3.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 14 FYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKsTHYVATGGIAQAPeGRRIFP 93
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK-ERRKSIGYVMQDV-DYQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 94 DmSVEENLLMGT--IPVGNQHAAEDMQSMfDLFpRLKERRnqrAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:cd03226 87 D-SVREELLLGLkeLDAGNEQAETVLKDL-DLY-ALKERH---PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515953848 172 VVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:cd03226 161 NMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-235 |
3.50e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 113.25 E-value: 3.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVA---TGGIA-QAPEGRRIFPd 94
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEvrkTVGIVfQNPDDQLFAP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 95 mSVEENLLMGTIPVGNQHaaEDMQSmfdlfpRLKERRNQRAMT---------LSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:PRK13639 95 -TVEEDVAFGPLNLGLSK--EEVEK------RVKEALKAVGMEgfenkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953848 166 LGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPE-VRKAYL 235
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIEtIRKANL 236
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-228 |
1.21e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 113.50 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHksthyvatg 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 81 giaQAPEGRRI---------FPDMSVEEN----LLMGTIPvgNQHAAE---DMQSMFdlfpRLKERRNQRAMTLSGGEQQ 144
Cdd:PRK09452 81 ---VPAENRHVntvfqsyalFPHMTVFENvafgLRMQKTP--AAEITPrvmEALRMV----QLEEFAQRKPHQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 145 MLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEA 223
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
....*
gi 515953848 224 LLKDP 228
Cdd:PRK09452 232 IYEEP 236
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
16-219 |
1.96e-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: 109.76 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 16 GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHyvATGGIAQAPEGRRIFPDM 95
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE--ARRRLGFVSDSTGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 96 SVEENLL-MGTIPVGNQHAAED-MQSMFDLFpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVV 173
Cdd:cd03266 94 TARENLEyFAGLYGLKGDELTArLEELADRL-GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515953848 174 KQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSG 219
Cdd:cd03266 173 RALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-215 |
2.23e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 114.74 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 3 EPMLQFQDVDVF--YGVIqALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATG 80
Cdd:COG3845 255 EVVLEVENLSVRddRGVP-ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 81 GIAQAPEGRR---IFPDMSVEENLLMGTI---PVGN---------QHAAEDMQSMFDLFPRlkeRRNQRAMTLSGGEQQM 145
Cdd:COG3845 334 GVAYIPEDRLgrgLVPDMSVAENLILGRYrrpPFSRggfldrkaiRAFAEELIEEFDVRTP---GPDTPARSLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-228 |
2.27e-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: 110.12 E-value: 2.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAQA 85
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 86 pegRRIFPDMSVEENLLMG--TIPVGNQHAAEDMQ----SMFDLFpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLL 159
Cdd:cd03296 83 ---YALFRHMTVFDNVAFGlrVKPRSERPPEAEIRakvhELLKLV-QLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 160 LLDEPSLGLAPIVVKQIFQTLRELA-RNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDP 228
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-215 |
4.41e-29 |
|
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: 109.06 E-value: 4.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFY----GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHY 76
Cdd:COG4181 4 SSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 77 VATGgiaqapEGRRI------F---PDMSVEENLLMgtiP---VGNQHAAEDMQSMFDlfpR--LKERRNQRAMTLSGGE 142
Cdd:COG4181 84 RARL------RARHVgfvfqsFqllPTLTALENVML---PlelAGRRDARARARALLE---RvgLGHRLDHYPAQLSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515953848 143 QQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELAR-NGMTIFLVEqnahHALKL---SDRGYVMVNGQI 215
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVT----HDPALaarCDRVLRLRAGRL 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-228 |
7.86e-29 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 108.58 E-value: 7.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHyvaTGGIAQAPEGRRIFPDMSVEEN 100
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE---KRDISYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 101 LLMGTIPVGNQHAaEDMQSMFDLFPRLKERR--NQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQ 178
Cdd:cd03299 92 IAYGLKKRKVDKK-EIERKVLEIAEMLGIDHllNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515953848 179 TLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDP 228
Cdd:cd03299 171 ELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-228 |
8.77e-29 |
|
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: 110.14 E-value: 8.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFY----GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFG---QPRIRNGQILFCGEDISHKSthyv 77
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKLS---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 78 atggiaqaPEGRR---------IFPD-MSVeenlLMGTIPVGNQ-------H-------AAEDMQSMFDL--FPRLKERR 131
Cdd:COG0444 77 --------EKELRkirgreiqmIFQDpMTS----LNPVMTVGDQiaeplriHgglskaeARERAIELLERvgLPDPERRL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 132 NQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVeqnAHH---ALKLSDRG 207
Cdd:COG0444 145 DRYPHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFI---THDlgvVAEIADRV 221
|
250 260
....*....|....*....|.
gi 515953848 208 YVMVNGQIRLSGSGEALLKDP 228
Cdd:COG0444 222 AVMYAGRIVEEGPVEELFENP 242
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-228 |
1.02e-28 |
|
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: 108.54 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQ-ALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDIS-------HKSTHYV 77
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReqdpvelRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 78 atggIAQAPegrrIFPDMSVEENLlmGTIPVGN-------QHAAEDMQSMFDLFPrlKERRNQRAMTLSGGEQQMLAIAR 150
Cdd:cd03295 81 ----IQQIG----LFPHMTVEENI--ALVPKLLkwpkekiRERADELLALVGLDP--AEFADRYPHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515953848 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDP 228
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-222 |
2.38e-28 |
|
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: 106.46 E-value: 2.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQP--RIRNGQILFCGEDIShksthyvatggia 83
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDIT------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 qapegrrifpDMSVEENLLMGtIPVGNQHAAEdmqsmfdlFPRLKERRNQRAM--TLSGGEQQMLAIARALMSRPKLLLL 161
Cdd:cd03217 68 ----------DLPPEERARLG-IFLAFQYPPE--------IPGVKNADFLRYVneGFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515953848 162 DEPSLGLAPIVVKQIFQTLRELARNGMTIFLVeqnAHHA--LKL--SDRGYVMVNGQIRLSGSGE 222
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREEGKSVLII---THYQrlLDYikPDRVHVLYDGRIVKSGDKE 190
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-214 |
3.52e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.27 E-value: 3.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTlLMSV-FG--QPriRNGQILFCGEDISHKSTHYV 77
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKST-LMKIlYGlyQP--DSGEILIDGKPVRIRSPRDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 78 ATGGIA---QAPegrRIFPDMSVEENLLMGTIPVGN-----QHAAEDMQSMFDLFPrLKERRNQRAMTLSGGEQQMLAIA 149
Cdd:COG3845 78 IALGIGmvhQHF---MLVPNLTVAENIVLGLEPTKGgrldrKAARARIRELSERYG-LDVDPDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515953848 150 RALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVeqnAHH---ALKLSDRGYVMVNGQ 214
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFI---THKlreVMAIADRVTVLRRGK 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-219 |
5.13e-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: 105.84 E-value: 5.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 23 QVSLEVNkGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGedishksTHYVATG-GIAQAPEGRRI---------F 92
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG-------TVLFDSRkKINLPPQQRKIglvfqqyalF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 93 PDMSVEENLLMGTIPVGNQHAAEDMQSMFDLFpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIV 172
Cdd:cd03297 88 PHLNVRENLAFGLKRKRNREDRISVDELLDLL-GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515953848 173 VKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSG 219
Cdd:cd03297 167 RLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-234 |
1.47e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.58 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATggiaq 84
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELAR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 85 apegRRI---------FPdMSVEENLLMGTIPVG-----NQHAAEDMQSMFDLfPRLKERRNQramTLSGGEQQMLAIAR 150
Cdd:COG4559 76 ----RRAvlpqhsslaFP-FTVEEVVALGRAPHGssaaqDRQIVREALALVGL-AHLAGRSYQ---TLSGGEQQRVQLAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 151 AL-------MSRPKLLLLDEP--SLGLAPivVKQIFQTLRELARNGMTIFLVeqnaHHALKL----SDRGYVMVNGQIRL 217
Cdd:COG4559 147 VLaqlwepvDGGPRWLFLDEPtsALDLAH--QHAVLRLARQLARRGGGVVAV----LHDLNLaaqyADRILLLHQGRLVA 220
|
250
....*....|....*..
gi 515953848 218 SGSGEALLKDPEVRKAY 234
Cdd:COG4559 221 QGTPEEVLTDELLERVY 237
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-234 |
5.98e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 106.85 E-value: 5.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 4 PMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHyVATGGIA 83
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR-AASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 QAPEGRRIFPDMSVEENLLMGTIPvgnqHaaedmQSMFDLFPRLKERRNQRAM--------------TLSGGEQQMLAIA 149
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTP----H-----RSRFDTWTETDRAAVERAMertgvaqfadrpvtSLSGGERQRVLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 150 RALMSRPKLLLLDEPSlglAPIVVKQIFQTL---RELARNGMTIFLveqnAHHALKLSDRgY-----VMVNGQIRLSGSG 221
Cdd:PRK09536 152 RALAQATPVLLLDEPT---ASLDINHQVRTLelvRRLVDDGKTAVA----AIHDLDLAAR-YcdelvLLADGRVRAAGPP 223
|
250
....*....|...
gi 515953848 222 EALLKDPEVRKAY 234
Cdd:PRK09536 224 ADVLTADTLRAAF 236
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-222 |
1.80e-26 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 106.63 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAQAPEGRR---IFPDMSV 97
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 98 EENL----------LMGTIpvgnQHAAEDM--QSMFDLFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:PRK10762 348 KENMsltalryfsrAGGSL----KHADEQQavSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515953848 166 LGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIrlsgSGE 222
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI----SGE 476
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-226 |
1.88e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 106.79 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTL--LMSVFGQPRirNGQILFCGEDISHKSTHYV--ATG 80
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLvnLLLRFYDPT--SGRILIDGVDIRDLTLESLrrQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 81 GIAQAPEgrrIFpDMSVEENLLMGTIPVGNQ---HAAEDMQSMfDLFPRLKERRN----QRAMTLSGGEQQMLAIARALM 153
Cdd:COG1132 418 VVPQDTF---LF-SGTIRENIRYGRPDATDEeveEAAKAAQAH-EFIEALPDGYDtvvgERGVNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515953848 154 SRPKLLLLDEPSLGLAPIVVKQIFQTLRELARnGMTIFLVeqnAH--HALKLSDRGYVMVNGQIRLSGSGEALLK 226
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVI---AHrlSTIRNADRILVLDDGRIVEQGTHEELLA 563
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-234 |
4.34e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.77 E-value: 4.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 4 PMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATggia 83
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 qapegRR---------IFPdMSVEENLLMGTIPVGNQHAAED------MQSMfDLFPrLKERRNQramTLSGGEQQMLAI 148
Cdd:PRK13548 77 -----RRavlpqhsslSFP-FTVEEVVAMGRAPHGLSRAEDDalvaaaLAQV-DLAH-LAGRDYP---QLSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 149 ARALM------SRPKLLLLDEP--SLGLApivvKQ--IFQTLRELARngmtiflvEQNAH-----HALKL----SDRGYV 209
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEPtsALDLA----HQhhVLRLARQLAH--------ERGLAvivvlHDLNLaaryADRIVL 213
|
250 260
....*....|....*....|....*
gi 515953848 210 MVNGQIRLSGSGEALLKDPEVRKAY 234
Cdd:PRK13548 214 LHQGRLVADGTPAEVLTPETLRRVY 238
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-227 |
4.62e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 105.52 E-value: 4.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 4 PMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIA 83
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 QAPEGRRIFPDMSVEENLLMGTipvgnQHAAEDMQSMFDLFPRLKERRN--QRAMTLSGGEQQMLAIARALMSRPKLLLL 161
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFGL-----PKRQASMQKMKQLLAALGCQLDldSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953848 162 DEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKD 227
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-227 |
6.49e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 102.99 E-value: 6.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSThyVATG 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR--LARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 81 GIAQAPEGRRIFPDMSVEENLL-------MGTipvgnQHAAEDMQSMFDlFPRLKERRNQRAMTLSGGEQQMLAIARALM 153
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLLvfgryfgMST-----REIEAVIPSLLE-FARLESKADARVSDLSGGMKRRLTLARALI 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515953848 154 SRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKD 227
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-231 |
1.16e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.99 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 4 PMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIA 83
Cdd:PRK11607 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 QApegRRIFPDMSVEENLLMG----TIPVGnqHAAEDMQSMFDLFpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLL 159
Cdd:PRK11607 98 QS---YALFPHMTVEQNIAFGlkqdKLPKA--EIASRVNEMLGLV-HMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515953848 160 LLDEPSLGLAPIVVKQI-FQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEVR 231
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-219 |
1.31e-25 |
|
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: 99.57 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETvALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATggIAQA 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR--IGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 86 PEGRRIFPDMSVEENL----LMGTIPVGNQHAAEDMqsMFDLFpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLL 161
Cdd:cd03264 78 PQEFGVYPNFTVREFLdyiaWLKGIPSKEVKARVDE--VLELV-NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515953848 162 DEPSLGLAP---IVVKQIfqtLRELARNGMTIF---LVEQNAHHALKLSdrgyVMVNGQIRLSG 219
Cdd:cd03264 155 DEPTAGLDPeerIRFRNL---LSELGEDRIVILsthIVEDVESLCNQVA----VLNKGKLVFEG 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-205 |
1.48e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 100.63 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 2 SEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLmSVFGQ-----PRIR-NGQILFCGEDISHKSTH 75
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTIL-RCFNRlndliPGFRvEGKVTFHGKNLYAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 76 YVAT----GGIAQAPEGrriFPDmSVEENLLMGTIPVGNQhaaEDMQSMFD-------LFPRLKERRNQRAMTLSGGEQQ 144
Cdd:PRK14243 86 PVEVrrriGMVFQKPNP---FPK-SIYDNIAYGARINGYK---GDMDELVErslrqaaLWDEVKDKLKQSGLSLSGGQQQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953848 145 MLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNgMTIFLVEQNAHHALKLSD 205
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-228 |
2.93e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 101.30 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKsthyvatggiaq 84
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDL------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 85 APEGRRI---------FPDMSVEENL-----LMGTIPVGNQHAAEDMQSMFDLFPRLkerrNQRAMTLSGGEQQMLAIAR 150
Cdd:COG3839 71 PPKDRNIamvfqsyalYPHMTVYENIafplkLRKVPKAEIDRRVREAAELLGLEDLL----DRKPKQLSGGQRQRVALGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 151 ALMSRPKLLLLDEPslgLAPIVVK---QIFQTLREL-ARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLK 226
Cdd:COG3839 147 ALVREPKVFLLDEP---LSNLDAKlrvEMRAEIKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYD 223
|
..
gi 515953848 227 DP 228
Cdd:COG3839 224 RP 225
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-225 |
4.24e-25 |
|
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: 98.84 E-value: 4.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGgIAQAPEGRRIFPDmSVE 98
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRA-IGVVPQDTVLFND-TIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 99 ENLLMGTIPVGNQH---AAEDMQsMFDLFPRLKERRN----QRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:cd03253 93 YNIRYGRPDATDEEvieAAKAAQ-IHDKIMRFPDGYDtivgERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTH 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515953848 172 VVKQIFQTLRELARNGMTIFLveqnAH--HALKLSDRGYVMVNGQIRLSGSGEALL 225
Cdd:cd03253 172 TEREIQAALRDVSKGRTTIVI----AHrlSTIVNADKIIVLKDGRIVERGTHEELL 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-206 |
6.36e-25 |
|
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: 97.86 E-value: 6.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISH---KSTHYVATGg 81
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgRAIPYLRRK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 IAQAPEGRRIFPDMSVEEN--LLMGTIPVGNQHAAEDMQSMFDLFPrLKERRNQRAMTLSGGEQQMLAIARALMSRPKLL 159
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENvaFALEVTGVPPREIRKRVPAALELVG-LSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515953848 160 LLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLveqnAHHALKLSDR 206
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVV----ATHAKELVDT 201
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
19-229 |
6.57e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 98.67 E-value: 6.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSV--FGQP---RIRNGQILF-CGEDISHKSTHYVA----TGGIAQapeG 88
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlLEQPeagTIRVGDITIdTARSLSQQKGLIRQlrqhVGFVFQ---N 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 89 RRIFPDMSVEENLLMGTIPVGNQHAAEDMQSMFDLFPR--LKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:PRK11264 94 FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKvgLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515953848 167 GLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPE 229
Cdd:PRK11264 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-219 |
8.47e-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: 96.23 E-value: 8.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYG--VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDIShksthyvatggia 83
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 qapegrrifpdmsVEENLLMGTIPVGNQHAaedmqSMFDlfprlKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:cd03247 68 -------------DLEKALSSLISVLNQRP-----YLFD-----TTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515953848 164 PSLGLAPIVVKQIFQTLRELARNGMTIFLveqnAHH--ALKLSDRGYVMVNGQIRLSG 219
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLKDKTLIWI----THHltGIEHMDKILFLENGKIIMQG 178
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-228 |
8.99e-25 |
|
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: 100.19 E-value: 8.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 24 VSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEdishksTHYVATGGIAQAPEGRRI---------FPD 94
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR------TLFDSRKGIFLPPEKRRIgyvfqearlFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 95 MSVEENLLMG---TIPVGNQHAAEDMQSMFDLFPRLKERRNqramTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:TIGR02142 90 LSVRGNLRYGmkrARPSERRISFERVIELLGIGHLLGRLPG----RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515953848 172 VVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDP 228
Cdd:TIGR02142 166 RKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-205 |
9.05e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.57 E-value: 9.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 4 PMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVF------GQPRIRnGQILFCGEDISHKSTHY- 76
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmneleSEVRVE-GRVEFFNQNIYERRVNLn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 77 VATGGIAQAPEGRRIFPdMSVEENLLMGTIPVGNQHAAE---DMQSMF---DLFPRLKERRNQRAMTLSGGEQQMLAIAR 150
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEiddIVESALkdaDLWDEIKHKIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515953848 151 ALMSRPKLLLLDEPSLGLAPIV---VKQIFQTLRelARNGMTIFLVEQNAHHALKLSD 205
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIAsmkVESLIQSLR--LRSELTMVIVSHNLHQVSRLSD 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-206 |
9.09e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 97.96 E-value: 9.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVAT------GGIAQApegRRIFPD 94
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnqklGFIYQF---HHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 95 MSVEENLLMGTIpVGNQHAAEDMQSMFDLFPR--LKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIV 172
Cdd:PRK11629 102 FTALENVAMPLL-IGKKKPAEINSRALEMLAAvgLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190
....*....|....*....|....*....|....
gi 515953848 173 VKQIFQTLRELARNGMTIFLVeqnAHHALKLSDR 206
Cdd:PRK11629 181 ADSIFQLLGELNRLQGTAFLV---VTHDLQLAKR 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-216 |
1.40e-24 |
|
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: 96.94 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKsthYVATGGIAQA 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL---PPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 86 PEGRRIFPDMSVEENLLMG---------TIPVGNQHAAEDMQsmfdlfprLKERRNQRAMTLSGGEQQMLAIARALMSRP 156
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGlklrkvpkdEIDERVREVAELLQ--------IEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953848 157 KLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIR 216
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-226 |
1.40e-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: 97.23 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 18 IQALKQVSLEVNKGETVALIGANGAGKSTL--LMSVFGQPRirNGQILFCGEDISHKSTHYVAT--GGIAQAPEgrrIFp 93
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVvsLLERFYDPT--SGEILLDGVDIRDLNLRWLRSqiGLVSQEPV---LF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 94 DMSVEENLLMGTipvGNQHAAEDMQ--------SMFDLFP-RLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:cd03249 90 DGTIAENIRYGK---PDATDEEVEEaakkanihDFIMSLPdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515953848 165 SLGLAPIVVKQIFQTLRELARNGMTIFLveqnAH--HALKLSDRGYVMVNGQIRLSGSGEALLK 226
Cdd:cd03249 167 TSALDAESEKLVQEALDRAMKGRTTIVI----AHrlSTIRNADLIAVLQNGQVVEQGTHDELMA 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-226 |
2.53e-24 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 96.53 E-value: 2.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 7 QFQDVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTL--LMSVFGQPRirNGQILFCGEDIsHKSTHYVATGGIA 83
Cdd:cd03254 4 EFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLinLLMRFYDPQ--KGQILIDGIDI-RDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 QAPEGRRIFPDmSVEENLLMGTipvgNQHAAEDMQSM-----FDLFPR-----LKERRNQRAMTLSGGEQQMLAIARALM 153
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLGR----PNATDEEVIEAakeagAHDFIMklpngYDTVLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515953848 154 SRPKLLLLDEPSLGLAPIVVKQIFQTLRELaRNGMTIFLVeqnAHH--ALKLSDRGYVMVNGQIRLSGSGEALLK 226
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIII---AHRlsTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-229 |
4.70e-24 |
|
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: 99.76 E-value: 4.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYG----VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFG----QPRIRNGQILFCGEDISHk 72
Cdd:COG4172 2 MSMPLLSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRllpdPAAHPSGSILFDGQDLLG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 73 sthyvatggiaqAPE-------GRRI---FPDMSVEENLLMgtiPVGNQ-------H----AAEDMQSMFDLF-----PR 126
Cdd:COG4172 81 ------------LSErelrrirGNRIamiFQEPMTSLNPLH---TIGKQiaevlrlHrglsGAAARARALELLervgiPD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 127 LKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARNGMTIFLVEqnahHAL---- 201
Cdd:COG4172 146 PERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLIT----HDLgvvr 221
|
250 260
....*....|....*....|....*...
gi 515953848 202 KLSDRGYVMVNGQIRLSGSGEALLKDPE 229
Cdd:COG4172 222 RFADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-234 |
4.78e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 99.74 E-value: 4.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 22 KQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAQAPEGRR---IFPDMSVE 98
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQssgLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 99 EN---LLMGTIPVGNQHAAEdmQSMFDLFPR---LK-ERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:PRK15439 360 WNvcaLTHNRRGFWIKPARE--NAVLERYRRalnIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515953848 172 VVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEVRKAY 234
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMRLAF 500
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
6-234 |
6.52e-24 |
|
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: 95.79 E-value: 6.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQP--RIRNGQILFCGEDISHKSTHYVATGGI- 82
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPsyEVTSGTILFKGQDLLELEPDERARAGLf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 83 --AQAPEGrriFPDMSVEEnLLMGTIPVGNQHAAEDMQSMFDLFPRLKERRNQRAMT-----------LSGGEQQMLAIA 149
Cdd:TIGR01978 81 laFQYPEE---IPGVSNLE-FLRSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDeeflnrsvnegFSGGEKKRNEIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 150 RALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVeqnAHHA--LKL--SDRGYVMVNGQIRLSGsGEALL 225
Cdd:TIGR01978 157 QMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLII---THYQrlLNYikPDYVHVLLDGRIVKSG-DVELA 232
|
....*....
gi 515953848 226 KDPEvRKAY 234
Cdd:TIGR01978 233 KELE-AKGY 240
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-231 |
6.60e-24 |
|
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: 97.86 E-value: 6.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 23 QVSLEVNKGETVALIGANGAGKSTLLMSVFG--QP---RIR-NGQILFcgeDishksthyvATGGIAQAPEGRRI----- 91
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGleRPdsgRIRlGGEVLQ---D---------SARGIFLPPHRRRIgyvfq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 92 ----FPDMSVEENLLMGTIPVGNQHAAEDMQSMFDLF---PRLkerrNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:COG4148 85 earlFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLgigHLL----DRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953848 165 --SLGLApivVKQ-IFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEVR 231
Cdd:COG4148 161 laALDLA---RKAeILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLL 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-215 |
6.67e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 99.22 E-value: 6.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 24 VSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAQAPEGRR---IFPDMSVEEN 100
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 101 LLMG----TIPVGN--------QHAAEDMQSMfdlfpRLKER-RNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:PRK11288 352 INISarrhHLRAGClinnrweaENADRFIRSL-----NIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515953848 168 LAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:PRK11288 427 IDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-229 |
7.69e-24 |
|
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: 95.34 E-value: 7.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYG----VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDIShksthyvATG 80
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLT-------LLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 81 GIAQAPEGRRI---------FPDMSVEENLlmgTIP--VGNQHAAEDMQSMFDL--FPRLKERRNQRAMTLSGGEQQMLA 147
Cdd:cd03258 74 GKELRKARRRIgmifqhfnlLSSRTVFENV---ALPleIAGVPKAEIEERVLELleLVGLEDKADAYPAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 148 IARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLK 226
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
...
gi 515953848 227 DPE 229
Cdd:cd03258 231 NPQ 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-213 |
7.97e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 99.09 E-value: 7.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATG 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 81 GIAQAPEGRRIFPDMSVEENLLMGTIPVG-----NQHAAEDMQ---SMFDLFPRLKERRNQRAMTLSGGEQQMLAIARAL 152
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLYIGRHLTKkvcgvNIIDWREMRvraAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953848 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNG 213
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-219 |
8.38e-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: 94.87 E-value: 8.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 25 SLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSthyVATGGIAQAPEGRRIFPDMSVEENLLMG 104
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP---PADRPVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 105 TIPvGNQHAAEDMQSMFDLFPR--LKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRE 182
Cdd:cd03298 95 LSP-GLKLTAEDRQAIEVALARvgLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 515953848 183 LARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSG 219
Cdd:cd03298 174 LHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-189 |
9.19e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.85 E-value: 9.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTlLMSV------FGQpriRNGQILFCGEDISHKST 74
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKST-LMKVlsgvypHGT---YEGEIIFEGEELQASNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 75 HYVATGGIAQAPEGRRIFPDMSVEENLLMGTIPV--GNQHAAEDMQSMFDLFPRLKERRN--QRAMTLSGGEQQMLAIAR 150
Cdd:PRK13549 77 RDTERAGIAIIHQELALVKELSVLENIFLGNEITpgGIMDYDAMYLRAQKLLAQLKLDINpaTPVGNLGLGQQQLVEIAK 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 515953848 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMT 189
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIA 195
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-229 |
1.67e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.50 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYV----ATGGIAQAPEgRRIFPDm 95
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSdirkKVGLVFQYPE-YQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 96 SVEENLLMGTIPVG------NQHAAEDMQSMFDLFPRLKERRnqrAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:PRK13637 100 TIEKDIAFGPINLGlseeeiENRVKRAMNIVGLDYEDYKDKS---PFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953848 170 PIVVKQIFQTLREL-ARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPE 229
Cdd:PRK13637 177 PKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVE 237
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-236 |
2.10e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.05 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTH---YVATGGIAQAPEGRriFPDMS 96
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLqgiRKLVGIVFQNPETQ--FVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 97 VEENLLMG----TIPVGNQHAAEDMqSMFDLfpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIV 172
Cdd:PRK13644 95 VEEDLAFGpenlCLPPIEIRKRVDR-ALAEI--GLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515953848 173 VKQIFQTLRELARNGMTIFLVEQNAHHaLKLSDRGYVMVNGQIRLSGSGEALLKDPEVRkaYLG 236
Cdd:PRK13644 172 GIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ--TLG 232
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-226 |
2.81e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.98 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQP--RIRNGQILFCGEDISHKSTHYVATGGIA---QAPEgrRIfPDM 95
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERARAGIFlafQYPV--EI-PGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 96 SVEeNLLMGTIpvgNQHAAEDMqSMFDLFPRLKERRNQRAMT-----------LSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:COG0396 93 SVS-NFLRTAL---NARRGEEL-SAREFLKLLKEKMKELGLDedfldryvnegFSGGEKKRNEILQMLLLEPKLAILDET 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953848 165 SLGLAPIVVKQIFQTLRELARNGMTIFLVeqnAHHA--LKL--SDRGYVMVNGQIRLSGSGEALLK 226
Cdd:COG0396 168 DSGLDIDALRIVAEGVNKLRSPDRGILII---THYQriLDYikPDFVHVLVDGRIVKSGGKELALE 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-231 |
3.18e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 95.92 E-value: 3.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 14 FYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAQApegRRIFP 93
Cdd:PRK10851 11 SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH---YALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 94 DMSVEENLLMG-TI------PVGNQHAAEDMQ--SMFDLfPRLKERRNQRamtLSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:PRK10851 88 HMTVFDNIAFGlTVlprrerPNAAAIKAKVTQllEMVQL-AHLADRYPAQ---LSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515953848 165 SLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEVR 231
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATR 231
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-220 |
3.89e-23 |
|
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: 93.33 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVAT--GG 81
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSriSI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 IAQAPEgrrIFPDmSVEENLlmgtIPVGnQHAAEDMQSMFDLFpRLKERRNQRAMTL-----------SGGEQQMLAIAR 150
Cdd:cd03244 83 IPQDPV---LFSG-TIRSNL----DPFG-EYSDEELWQALERV-GLKEFVESLPGGLdtvveeggenlSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515953848 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRElARNGMTIFLVeqnAH--HALKLSDRGYVMVNGQIRLSGS 220
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTI---AHrlDTIIDSDRILVLDKGRVVEFDS 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-214 |
5.92e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.52 E-value: 5.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 2 SEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGG 81
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 IAQAPEGRRIFPDMSVEENLLMGTIP---------VGNQHAAEDMQSM-FDLFPRLKERRnqramtLSGGEQQMLAIARA 151
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGQLPhkggivnrrLLNYEAREQLEHLgVDIDPDTPLKY------LSIGQRQMVEIAKA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515953848 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQ 214
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-190 |
6.49e-23 |
|
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: 92.88 E-value: 6.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 17 VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFC--GEDIShksthyvatggIAQAPEGR----- 89
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVD-----------LAQASPREilalr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 90 -----------RIFPDMS----VEENLL-MGtipVGNQHAAEDMQSMFDLFpRLKERRNQRA-MTLSGGEQQMLAIARAL 152
Cdd:COG4778 92 rrtigyvsqflRVIPRVSaldvVAEPLLeRG---VDREEARARARELLARL-NLPERLWDLPpATFSGGEQQRVNIARGF 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515953848 153 MSRPKLLLLDEPSLGLAP---IVVKQIfqtLRELARNGMTI 190
Cdd:COG4778 168 IADPPLLLLDEPTASLDAanrAVVVEL---IEEAKARGTAI 205
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-230 |
9.43e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.33 E-value: 9.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVA--TGG 81
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRkfVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 IAQAPEGRRIFPdmSVEENLLMGTIPVG-----NQHAAEDMQSMFDLfprlKERRNQRAMTLSGGEQQMLAIARALMSRP 156
Cdd:PRK13652 83 VFQNPDDQIFSP--TVEQDIAFGPINLGldeetVAHRVSSALHMLGL----EELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515953848 157 KLLLLDEPSLGLAPIVVKQIFQTLRELA-RNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEV 230
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPeTYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-229 |
1.17e-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: 95.91 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 3 EPMLQFQDVDVFY-----------GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFG-QPRirNGQILFCGEDIS 70
Cdd:COG4172 273 PPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRlIPS--EGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 71 HKSTHyvatggiAQAPEGRRI---F--------PDMSVEEnllmgTIpvgnqhaAEDMQSmfdLFPRL--KERRNQ--RA 135
Cdd:COG4172 351 GLSRR-------ALRPLRRRMqvvFqdpfgslsPRMTVGQ-----II-------AEGLRV---HGPGLsaAERRARvaEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 136 MT---------------LSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARNGMT-IFLveqnaH 198
Cdd:COG4172 409 LEevgldpaarhrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAyLFI-----S 483
|
250 260 270
....*....|....*....|....*....|....*
gi 515953848 199 HALK----LSDRGYVMVNGQIRLSGSGEALLKDPE 229
Cdd:COG4172 484 HDLAvvraLAHRVMVMKDGKVVEQGPTEQVFDAPQ 518
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-227 |
1.41e-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: 91.91 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYG--VIQALKQVSLEVNKGETVALIGANGAGKSTL--LMSVFGQPriRNGQILFCGEDISHKSTHYVATgG 81
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLvnLIPRFYDV--DSGRILIDGHDVRDYTLASLRR-Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 IAQAPEGRRIFPDmSVEENLLMGTIPVGNQ---HAAEDMQSMfDLFPRLKE----RRNQRAMTLSGGEQQMLAIARALMS 154
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIAYGRPGATREeveEAARAANAH-EFIMELPEgydtVIGERGVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515953848 155 RPKLLLLDEPSLGLAPIVVKQIFQTLRELARNgMTIFLVeqnAHH--ALKLSDRGYVMVNGQIRLSGSGEALLKD 227
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKN-RTTFVI---AHRlsTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-237 |
2.08e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 91.90 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLL------MSVFGQPRIRnGQILFCGEDISHKSTHYVA- 78
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrlIELYPEARVS-GEVYLDGQDIFKMDVIELRr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 79 -TGGIAQAPEGrriFPDMSVEENLLMG-----------TIPVGNQHAAEDMQsmfdLFPRLKERRNQRAMTLSGGEQQML 146
Cdd:PRK14247 83 rVQMVFQIPNP---IPNLSIFENVALGlklnrlvkskkELQERVRWALEKAQ----LWDEVKDRLDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 147 AIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNgMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLK 226
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
250
....*....|...
gi 515953848 227 DP--EVRKAYLGG 237
Cdd:PRK14247 235 NPrhELTEKYVTG 247
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
19-224 |
2.41e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 92.00 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 19 QALKQVSLEVNKGETVALIGANGAGKSTLL----------------MSVFGQPRIRNGQIlfcGEDISHKSTHyvaTGGI 82
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsglitgdksagshIELLGRTVQREGRL---ARDIRKSRAN---TGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 83 AQApegRRIFPDMSVEENLLMGTIpvgnqHAAEDMQSMFDLFPRLKERR--------------NQRAMTLSGGEQQMLAI 148
Cdd:PRK09984 92 FQQ---FNLVNRLSVLENVLIGAL-----GSTPFWRTCFSWFTREQKQRalqaltrvgmvhfaHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515953848 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEAL 224
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-226 |
2.88e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 92.84 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLL-M--------SvfgqprirnGQILFCGEDISHKSTHYVatggiaqa 85
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIkMltgilvptS---------GEVRVLGYVPFKRRKEFA-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 86 pegRRI----------FPDMSVEENL-LMGTI-PVGNQHAAEDMQSMFDLFpRLKERRNQRAMTLSGGeQQMLA-IARAL 152
Cdd:COG4586 95 ---RRIgvvfgqrsqlWWDLPAIDSFrLLKAIyRIPDAEYKKRLDELVELL-DLGELLDTPVRQLSLG-QRMRCeLAAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARNGMTIFL-------VEQnahhalkLSDRGYVMVNGQIRLSGSGEAL 224
Cdd:COG4586 170 LHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLtshdmddIEA-------LCDRVIVIDHGRIIYDGSLEEL 242
|
..
gi 515953848 225 LK 226
Cdd:COG4586 243 KE 244
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-164 |
4.38e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 90.23 E-value: 4.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQ--PRIR-NGQILFCGEDISHKsthyvatgg 81
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSaSGEVLLNGRRLTAL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 iaqAPEGRRI---------FPDMSVEENLLMG---TIPVGN-QHAAED------MQSMFDLFPrlkerrnqraMTLSGGE 142
Cdd:COG4136 72 ---PAEQRRIgilfqddllFPHLSVGENLAFAlppTIGRAQrRARVEQaleeagLAGFADRDP----------ATLSGGQ 138
|
170 180
....*....|....*....|..
gi 515953848 143 QQMLAIARALMSRPKLLLLDEP 164
Cdd:COG4136 139 RARVALLRALLAEPRALLLDEP 160
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-196 |
4.71e-22 |
|
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: 89.98 E-value: 4.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 9 QDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSThyvatggiAQAPEG 88
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNS--------KKASKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 89 RR-----IFPDM------SVEENLLMGTIPVgNQHAAEDMQSMFDLFPR--LKERRNQRAMTLSGGEQQMLAIARALMSR 155
Cdd:TIGR03608 74 RReklgyLFQNFalieneTVEENLDLGLKYK-KLSKKEKREKKKEALEKvgLNLKLKQKIYELSGGEQQRVALARAILKP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515953848 156 PKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQN 196
Cdd:TIGR03608 153 PPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHD 193
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-215 |
8.62e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 93.31 E-value: 8.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 22 KQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAQAPEGRR---IFPDMSVE 98
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 99 ENL-------------LMGTI-PVGNQHAAEDMQSMFDlfprLK-ERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:PRK09700 360 QNMaisrslkdggykgAMGLFhEVDEQRTAENQRELLA----LKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515953848 164 PSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-200 |
1.17e-21 |
|
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: 92.73 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 4 PMLQFQDVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHyVATGGI 82
Cdd:TIGR02857 320 SSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD-SWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 83 AQAPEGRRIFPDmSVEENLLMGTiPVGNQHAAEDMQSMFDLFPRLKERRN-------QRAMTLSGGEQQMLAIARALMSR 155
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRLAR-PDASDAEIREALERAGLDEFVAALPQgldtpigEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515953848 156 PKLLLLDEPSLGLAPIVVKQIFQTLRELARnGMTIFLVEQNAHHA 200
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALA 520
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-214 |
1.30e-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: 92.58 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFG-QPR-IRNGQILFCGEDISHKSTHYVATGGI 82
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvYPHgTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 83 AQAPEGRRIFPDMSVEENLLMG---TIPVGNQHAAEDMQSMFDLFPRLK---ERRNQRAMTLSGGEQQMLAIARALMSRP 156
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGneiTLPGGRMAYNAMYLRAKNLLRELQldaDNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515953848 157 KLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQ 214
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-219 |
1.36e-21 |
|
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: 89.25 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGqpRIRN-----GQILFCGEDISHKSTHYVatggIAQAPEGRRIFP 93
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG--RVEGggttsGQILFNGQPRKPDQFQKC----VAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 94 DMSVEENLLMGTIPVGNQHAAEDMQSMFDLFPRLKE-----RRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:cd03234 95 GLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDlaltrIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515953848 169 APIVVKQIFQTLRELARNGMTIFL-VEQNAHHALKLSDRGYVMVNGQIRLSG 219
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-214 |
2.25e-21 |
|
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: 87.91 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGedishkSTHYVAtggiaQAPegrRIFPDmSVEE 99
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------SIAYVS-----QEP---WIQNG-TIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 100 NLLMGTiPVGNQ------HAA---EDmqsmFDLFPRLKERR-NQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:cd03250 85 NILFGK-PFDEEryekviKACalePD----LEILPDGDLTEiGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515953848 170 PIVVKQIFQT-LRELARNGMTIFLVEQNAHHaLKLSDRGYVMVNGQ 214
Cdd:cd03250 160 AHVGRHIFENcILGLLLNNKTRILVTHQLQL-LPHADQIVVLDNGR 204
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-213 |
2.63e-21 |
|
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: 88.68 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDIShksthyvatggiAQAPEGRRIF------PD 94
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT------------EPGPDRMVVFqnysllPW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 95 MSVEENLLMGTIPVGNQHAAEDMQSMFD---LFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:TIGR01184 69 LTVRENIALAVDRVLPDLSKSERRAIVEehiALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515953848 172 VVKQIFQTLRELAR-NGMTIFLVEQNAHHALKLSDRGYVMVNG 213
Cdd:TIGR01184 149 TRGNLQEELMQIWEeHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
24-228 |
2.85e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.55 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 24 VSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSthyVATGGIAQAPEGRRIFPDMSVEENLLM 103
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS---IQQRDICMVFQSYALFPHMSLGENVGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 104 GTipvgnqhaaeDMQSmfdlfpRLKERRNQR---AMTL--------------SGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:PRK11432 102 GL----------KMLG------VPKEERKQRvkeALELvdlagfedryvdqiSGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515953848 167 GLAPIVVKQIFQTLREL-ARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDP 228
Cdd:PRK11432 166 NLDANLRRSMREKIRELqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-229 |
3.05e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 88.87 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDIS---------- 70
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 71 --HKSTHYVATGGIAQAPEGRRIFPDMSVEENLLMGTIPV---GNQHAAEDMQSMFDLFPRLKERRNQRAMTLSGGEQQM 145
Cdd:PRK10619 81 vaDKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVlglSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALL 225
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
....
gi 515953848 226 KDPE 229
Cdd:PRK10619 241 GNPQ 244
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-219 |
3.08e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.39 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVA--TGG 81
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 IAQAPEGRRIFPDMSVEENLLMGTIPVGNqhAAEDMQ----SMFDLFPRLKERRNqRAMTLSGGEQQMLAIARALMSRPK 157
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGA--SGDDIRrrvsAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515953848 158 LLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVeqnAHHALKLSDRGY-VMVNGQIRLSG 219
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMA---THDIGLISRRSYrMLTLSDGHLHG 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-225 |
3.22e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.81 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 2 SEPMLQFQDVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTLLmsvfgQPRIRN-----GQILFCGEDIS--HK 72
Cdd:PRK11160 335 DQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL-----QLLTRAwdpqqGEILLNGQPIAdySE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 73 STHYVATGGIAQAPEgrrIFPDmSVEENLLMGtIP-------------VGNQHAAEDMQSMfDLFprLKERRNQramtLS 139
Cdd:PRK11160 410 AALRQAISVVSQRVH---LFSA-TLRDNLLLA-APnasdealievlqqVGLEKLLEDDKGL-NAW--LGEGGRQ----LS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 140 GGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLveqnAH--HALKLSDRGYVMVNGQIRL 217
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMI----THrlTGLEQFDRICVMDNGQIIE 553
|
....*...
gi 515953848 218 SGSGEALL 225
Cdd:PRK11160 554 QGTHQELL 561
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-235 |
4.25e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.91 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVA----TG 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlrqqVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 81 GIAQAPEGRRIFPDMSVEENLLMGTIPVGNQHAAEDMQSMFDLFPRlKERRNQRAMTLSGGEQQMLAIARALMSRPKLLL 160
Cdd:PRK13638 81 TVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDA-QHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953848 161 LDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGS-GEALLKDPEVRKAYL 235
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGApGEVFACTEAMEQAGL 235
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
4.39e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.14 E-value: 4.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYG-VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGE--DISHKSTHYV 77
Cdd:PRK13636 1 MEDYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 78 --ATGGIAQAPEgRRIFpDMSVEENLLMGtiPVGNQHAAEDMQSMFDlfpRLKER------RNQRAMTLSGGEQQMLAIA 149
Cdd:PRK13636 81 reSVGMVFQDPD-NQLF-SASVYQDVSFG--AVNLKLPEDEVRKRVD---NALKRtgiehlKDKPTHCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 150 RALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDP 228
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
....*...
gi 515953848 229 EV-RKAYL 235
Cdd:PRK13636 234 EMlRKVNL 241
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-216 |
5.78e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 90.76 E-value: 5.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 24 VSLEVNKGETVALIGANGAGKSTLLMSVFGQ-PRIRNGQILFCGEDISHKSTHYVATGGIAQAPEGRR---IFPDMSVEE 99
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKrdgIVPVMGVGK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 100 NLlmgTIPVGNQ--------HAAEdMQSMFDLFPRLKERRN---QRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:PRK13549 361 NI---TLAALDRftggsridDAAE-LKTILESIQRLKVKTAspeLAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515953848 169 APIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIR 216
Cdd:PRK13549 437 DVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-238 |
8.36e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 87.59 E-value: 8.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSV-----FGQPRIRNGQILFCGEDISHKSTHYV--- 77
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIevr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 78 -ATGGIAQAPEGrriFPDMSVEENLLMGTIPVGNQHAAEDMQSMFD-------LFPRLKERRNQRAMTLSGGEQQMLAIA 149
Cdd:PRK14267 85 rEVGMVFQYPNP---FPHLTIYDNVAIGVKLNGLVKSKKELDERVEwalkkaaLWDEVKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 150 RALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELaRNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDP- 228
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPe 240
|
250
....*....|.
gi 515953848 229 -EVRKAYLGGV 238
Cdd:PRK14267 241 hELTEKYVTGA 251
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-227 |
1.02e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.22 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 17 VIQALKQVSLEVNKGETVALIGANGAGKSTLL--MSVFGQPRIRNGQILFCGEDISHKSTHY--VATGGIAQAPEGRRI- 91
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIehLNALLLPDTGTIEWIFKDEKNKKKTKEKekVLEKLVIQKTRFKKIk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 92 --------------FPDM-----SVEENLLMGTIPVG--NQHAAEDMQSMFDLFPrLKERRNQRA-MTLSGGEQQMLAIA 149
Cdd:PRK13651 99 kikeirrrvgvvfqFAEYqlfeqTIEKDIIFGPVSMGvsKEEAKKRAAKYIELVG-LDESYLQRSpFELSGGQKRRVALA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515953848 150 RALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKD 227
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-199 |
1.13e-20 |
|
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: 90.11 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 3 EPMLQFQDVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVAT-- 79
Cdd:TIGR02868 332 KPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRrv 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 80 GGIAQAPEgrrIFpDMSVEENLLMGTiPVGNQHAAEDMQSMFDLFPRLKERRN-------QRAMTLSGGEQQMLAIARAL 152
Cdd:TIGR02868 412 SVCAQDAH---LF-DTTVRENLRLAR-PDATDEELWAALERVGLADWLRALPDgldtvlgEGGARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515953848 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLRElARNGMTIFLVeqnAHH 199
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLI---THH 529
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-214 |
1.13e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 90.06 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 3 EPMLQFQDVD-VFYGViQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGG 81
Cdd:PRK10762 2 QALLQLKGIDkAFPGV-KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 IAQAPEGRRIFPDMSVEENLLMGTIPVgNQHAAEDMQSMFD----LFPRLKERRNQRAM--TLSGGEQQMLAIARALMSR 155
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLGREFV-NRFGRIDWKKMYAeadkLLARLNLRFSSDKLvgELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515953848 156 PKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEqnahHALK----LSDRGYVMVNGQ 214
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYIS----HRLKeifeICDDVTVFRDGQ 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
5-225 |
1.26e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 86.94 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYgviQALK-QVSLEVNKGETVALIGANGAGKSTLL--MSVFGQPRirNGQILFCGEDisHKSThyvatgG 81
Cdd:PRK10771 1 MLKLTDITWLY---HHLPmRFDLTVERGERVAILGPSGAGKSTLLnlIAGFLTPA--SGSLTLNGQD--HTTT------P 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 IAQAP-----EGRRIFPDMSVEENLLMGTIP-----VGNQHAAEDM-QSMF--DLFPRLKERrnqramtLSGGEQQMLAI 148
Cdd:PRK10771 68 PSRRPvsmlfQENNLFSHLTVAQNIGLGLNPglklnAAQREKLHAIaRQMGieDLLARLPGQ-------LSGGQRQRVAL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515953848 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALL 225
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-215 |
1.30e-20 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 86.49 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKStHYVATGGIA 83
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD-PADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 QAPEGRRIFPDmSVEENLLMGTIPVGNQH--AAEDMQSMFDLFPRLK---ERR-NQRAMTLSGGEQQMLAIARALMSRPK 157
Cdd:cd03245 82 YVPQDVTLFYG-TLRDNITLGAPLADDERilRAAELAGVTDFVNKHPnglDLQiGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 158 LLLLDEPSLGLAPIVVKQIFQTLRELARnGMTIFLVeqnAHH--ALKLSDRGYVMVNGQI 215
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIII---THRpsLLDLVDRIIVMDSGRI 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-219 |
2.08e-20 |
|
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: 86.05 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLmsvfgqpRIRNGQIL-FCGEDISHKSTHYV--ATGGIAqapegrri 91
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLL-------RLLAGIYPpDSGTVTVRGRVSSLlgLGGGFN-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 92 fPDMSVEENL-LMGTIpvgNQHAAEDMQSMFDL---FPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEpslG 167
Cdd:cd03220 97 -PELTGRENIyLNGRL---LGLSRKEIDEKIDEiieFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE---V 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515953848 168 LApiVVKQIFQ-----TLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSG 219
Cdd:cd03220 170 LA--VGDAAFQekcqrRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-229 |
2.47e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.99 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFY----GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFG---QPRIR--NGQILFCGEDISH 71
Cdd:PRK15134 1 MTQPLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRllpSPPVVypSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 72 KSthyvatggiAQAPEGRR------IF--------PDMSVEENLL--------MGTIP-----------VGNQHAAEdmq 118
Cdd:PRK15134 81 AS---------EQTLRGVRgnkiamIFqepmvslnPLHTLEKQLYevlslhrgMRREAargeilncldrVGIRQAAK--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 119 smfdlfpRLKERRNQramtLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNA 197
Cdd:PRK15134 149 -------RLTDYPHQ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNL 217
|
250 260 270
....*....|....*....|....*....|..
gi 515953848 198 HHALKLSDRGYVMVNGQIRLSGSGEALLKDPE 229
Cdd:PRK15134 218 SIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-220 |
2.75e-20 |
|
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: 88.73 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 18 IQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQ-PRIRNGQILFCGEDISHKSTHYVATGGIAQAPEGRR---IFP 93
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 94 DMSVEENLLMGTIP----VGNQHAAEDMQSMFDLFPRLKERRNQRAM---TLSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:TIGR02633 353 ILGVGKNITLSVLKsfcfKMRIDAAAELQIIGSAIQRLKVKTASPFLpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515953848 167 GLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRgyVMVNGQIRLSGS 220
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDR--VLVIGEGKLKGD 484
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-215 |
2.94e-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: 84.91 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQ--PRIRNGQILFCGEDISHKSTHYVatggIAQAPEGRRIFPDMSVE 98
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKI----IGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 99 ENLlmgtipvgnQHAAEdMQSmfdlfprlkerrnqramtLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQ 178
Cdd:cd03213 101 ETL---------MFAAK-LRG------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 515953848 179 TLRELARNGMT-IFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:cd03213 153 LLRRLADTGRTiICSIHQPSSEIFELFDKLLLLSQGRV 190
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-215 |
5.49e-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: 85.63 E-value: 5.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSthyvatggiaqaPEGRRIF------ 92
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLD------------RKQRRAFrrdvql 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 93 ----------PDMSVEENL------LMGTIPVGNQHAAEDMQSMFDLFPRLKERRNQRamtLSGGEQQMLAIARALMSRP 156
Cdd:TIGR02769 93 vfqdspsavnPRMTVRQIIgeplrhLTSLDESEQKARIAELLDMVGLRSEDADKLPRQ---LSGGQLQRINIARALAVKP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 157 KLLLLDEPSLGLAPIVVKQIFQTLREL-ARNGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:TIGR02769 170 KLIVLDEAVSNLDMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-237 |
7.78e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.10 E-value: 7.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLL------MSVFGQPRIRNGQILFCGEDISHKSTHYV--ATGGIAQAPEGrriF 92
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLkvlnrlIEIYDSKIKVDGKVLYFGKDIFQIDAIKLrkEVGMVFQQPNP---F 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 93 PDMSVEENLLMGTIPVGNQHAAEDMQSMFD------LFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSl 166
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVEEclrkvgLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT- 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515953848 167 GLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDP--EVRKAYLGG 237
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPknELTEKYVIG 254
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
6-226 |
9.71e-20 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 87.49 E-value: 9.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGV-IQALKQVSLEVNKGETVALIGANGAGKSTL--LMSVFGQPRirNGQILFCGEDISHKSTHYVaTGGI 82
Cdd:TIGR01193 474 IVINDVSYSYGYgSNILSDISLTIKMNSKTTIVGMSGSGKSTLakLLVGFFQAR--SGEILLNGFSLKDIDRHTL-RQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 83 AQAPEGRRIFpDMSVEENLLMGTIPVGNQhaaEDMQSMFDL---------FPR-LKERRNQRAMTLSGGEQQMLAIARAL 152
Cdd:TIGR01193 551 NYLPQEPYIF-SGSILENLLLGAKENVSQ---DEIWAACEIaeikddienMPLgYQTELSEEGSSISGGQKQRIALARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953848 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLRELarNGMTIFLVeqnAHH--ALKLSDRGYVMVNGQIRLSGSGEALLK 226
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDTITEKKIVNNLLNL--QDKTIIFV---AHRlsVAKQSDKIIVLDHGKIIEQGSHDELLD 697
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-228 |
1.18e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 84.59 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDishKSTHYVAT- 79
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD---GQLRDLYAl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 80 -------------GGIAQAP-EGRRifPDMSVEENL---LMGtipVGNQHAAEDMQSMFDLFPRLK---ERRNQRAMTLS 139
Cdd:PRK11701 79 seaerrrllrtewGFVHQHPrDGLR--MQVSAGGNIgerLMA---VGARHYGDIRATAGDWLERVEidaARIDDLPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 140 GGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLS 218
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
250
....*....|
gi 515953848 219 GSGEALLKDP 228
Cdd:PRK11701 234 GLTDQVLDDP 243
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-164 |
1.24e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.04 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 8 FQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLmsvfgqpRIRNGQIlfcgedishksthyVATGGIAQAPE 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLL-------KILAGEL--------------EPDSGEVSIPK 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 88 GRRI---------FPDMSVEENLLMGTIPVGNQHAA------------EDMQSMFDLFPRLKER---------------- 130
Cdd:COG0488 60 GLRIgylpqepplDDDLTVLDTVLDGDAELRALEAEleeleaklaepdEDLERLAELQEEFEALggweaearaeeilsgl 139
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515953848 131 ------RNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:COG0488 140 gfpeedLDRPVSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-215 |
1.42e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 85.62 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGV----IQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSthyvaTG 80
Cdd:PRK11153 1 MIELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALS-----EK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 81 GIAQApegRR----IFPDMsveeNLLMGTIPVGN---------QHAAEDMQSMFDLFPR--LKERRNQRAMTLSGGEQQM 145
Cdd:PRK11153 76 ELRKA---RRqigmIFQHF----NLLSSRTVFDNvalplelagTPKAEIKARVTELLELvgLSDKADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515953848 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEqnahHAL----KLSDRGYVMVNGQI 215
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLIT----HEMdvvkRICDRVAVIDAGRL 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-228 |
1.71e-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: 84.62 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 16 GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSThyvatggiAQAPEGRR----- 90
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSR--------KELRELRRkkism 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 91 ------IFPDMSVEENLLMGT----IPVGNQH--AAEDMQSMfdlfpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKL 158
Cdd:cd03294 107 vfqsfaLLPHRTVLENVAFGLevqgVPRAEREerAAEALELV-----GLEGWEHKYPDELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953848 159 LLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDP 228
Cdd:cd03294 182 LLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-220 |
1.96e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.59 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLmsvfgqprirngQILfcgedishksthyvatGGIAQAPEGR----- 89
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLL------------KLI----------------AGILEPTSGRvevng 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 90 RI---------F-PDMSVEEN-----LLMGtipvgnqHAAEDMQSMFD---LFPRLKERRNQRAMTLSGGEQQMLAIARA 151
Cdd:COG1134 88 RVsallelgagFhPELTGRENiylngRLLG-------LSRKEIDEKFDeivEFAELGDFIDQPVKTYSSGMRARLAFAVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515953848 152 LMSRPKLLLLDEpslGLApiVVKQIFQT-----LRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGS 220
Cdd:COG1134 161 TAVDPDILLVDE---VLA--VGDAAFQKkclarIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD 229
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-222 |
2.00e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.31 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 19 QALKQVSLEVN-----KGETvALIGANGAGKSTLLMSVFG-----QPRIR-NGQILFCGEdishksthyvatGGIAQAPE 87
Cdd:PRK11144 8 QQLGDLCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGltrpqKGRIVlNGRVLFDAE------------KGICLPPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 88 GRRI---------FPDMSVEENLLMGTipvgnqhaAEDMQSMFD----------LFPRLkerrnqrAMTLSGGEQQMLAI 148
Cdd:PRK11144 75 KRRIgyvfqdarlFPHYKVRGNLRYGM--------AKSMVAQFDkivallgiepLLDRY-------PGSLSGGEKQRVAI 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515953848 149 ARALMSRPKLLLLDEP--SLGLAPivVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGE 222
Cdd:PRK11144 140 GRALLTAPELLLMDEPlaSLDLPR--KRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLE 214
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-215 |
3.57e-19 |
|
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: 82.46 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYV--ATGGIAQAPegrrifpdms 96
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLrsSLTIIPQDP---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 97 veeNLLMGTIPvgNQHAAEDMQSMFDLFPRLkeRRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQI 176
Cdd:cd03369 92 ---TLFSGTIR--SNLDPFDEYSDEEIYGAL--RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515953848 177 FQTLRELArNGMTIFLVeqnAH--HALKLSDRGYVMVNGQI 215
Cdd:cd03369 165 QKTIREEF-TNSTILTI---AHrlRTIIDYDKILVMDAGEV 201
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-214 |
6.59e-19 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 84.78 E-value: 6.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 14 FYGViQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAQAPEGRRIFP 93
Cdd:PRK10982 8 FPGV-KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 94 DMSVEENLLMGTIP-----VGNQHAAEDMQSMF-----DLFPRLKerrnqrAMTLSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:PRK10982 87 QRSVMDNMWLGRYPtkgmfVDQDKMYRDTKAIFdeldiDIDPRAK------VATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515953848 164 PSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQ 214
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-190 |
6.86e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.18 E-value: 6.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 9 QDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDIShKSTHYVATGG-IAQAPE 87
Cdd:NF033858 5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA-DARHRRAVCPrIAYMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 88 --GRRIFPDMSVEENLlmgtipvgnqhaaedmqsmfDLFPRL-----KERRnQR-----------------AMTLSGGEQ 143
Cdd:NF033858 84 glGKNLYPTLSVFENL--------------------DFFGRLfgqdaAERR-RRidellratglapfadrpAGKLSGGMK 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515953848 144 QMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQ---TLRElARNGMTI 190
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWElidRIRA-ERPGMSV 191
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-226 |
7.22e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 82.76 E-value: 7.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYV- 77
Cdd:PRK13635 1 MKEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 78 -ATGGIAQAPEGRriFPDMSVEENLLMGTIPVGNQHaaEDMQsmfdlfPRLKERRNQRAMT---------LSGGEQQMLA 147
Cdd:PRK13635 81 rQVGMVFQNPDNQ--FVGATVQDDVAFGLENIGVPR--EEMV------ERVDQALRQVGMEdflnrephrLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 148 IARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGM-TIFLVEQNAHHALKlSDRGYVMVNGQIRLSG------- 219
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGtpeeifk 229
|
....*..
gi 515953848 220 SGEALLK 226
Cdd:PRK13635 230 SGHMLQE 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
6-233 |
7.30e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.16 E-value: 7.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGV---IQALKQVSLEVNKGETVALIGANGAGKST--LLMSVFGQPRirNGQILFCGEDISHKSTHYVAT- 79
Cdd:TIGR00958 479 IEFQDVSFSYPNrpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTvaALLQNLYQPT--GGQVLLDGVPLVQYDHHYLHRq 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 80 -GGIAQAPegrrIFPDMSVEENLLMG--------TIPVGNQHAAEDMQSMF--DLFPRLKERRNQramtLSGGEQQMLAI 148
Cdd:TIGR00958 557 vALVGQEP----VLFSGSVRENIAYGltdtpdeeIMAAAKAANAHDFIMEFpnGYDTEVGEKGSQ----LSGGQKQRIAI 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 149 ARALMSRPKLLLLDEPSLGLaPIVVKQIFQTLRELArnGMTIFLVE------QNAHHALklsdrgyVMVNGQIRLSGSGE 222
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSAL-DAECEQLLQESRSRA--SRTVLLIAhrlstvERADQIL-------VLKKGSVVEMGTHK 698
|
250
....*....|.
gi 515953848 223 ALLKDPEVRKA 233
Cdd:TIGR00958 699 QLMEDQGCYKH 709
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-229 |
7.48e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 83.59 E-value: 7.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFY----GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSthyvaTG 80
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALS-----ER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 81 GIAQApegRR----IFpdmsveenllmgtipvgnQHaaedmqsmFDLFPRL----------------KERRNQRAM---- 136
Cdd:COG1135 76 ELRAA---RRkigmIF------------------QH--------FNLLSSRtvaenvalpleiagvpKAEIRKRVAelle 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 137 -------------TLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALK 202
Cdd:COG1135 127 lvglsdkadaypsQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRR 206
|
250 260
....*....|....*....|....*..
gi 515953848 203 LSDRGYVMVNGQIRLSGSGEALLKDPE 229
Cdd:COG1135 207 ICDRVAVLENGRIVEQGPVLDVFANPQ 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-229 |
8.41e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.84 E-value: 8.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSV-----------FGQPRIRNGQILFCGEDISHKSTHyvaTGGIAQAPEGr 89
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvsgyrYSGDVLLGGRSIFNYRDVLEFRRR---VGMLFQRPNP- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 90 riFPdMSVEENLLMGT-----IPVGN-QHAAEDMQSMFDLFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:PRK14271 113 --FP-MSIMDNVLAGVrahklVPRKEfRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953848 164 PSLGLAPIVVKQIFQTLRELArNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPE 229
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPK 254
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-215 |
1.16e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 84.01 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAQAPEGRR---IFPDMS 96
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEERRstgIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 97 VEENLLMGTI-----PVG---NQHAAEDMQSMFDLFpRLKERRNQRAM-TLSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:PRK10982 343 IGFNSLISNIrnyknKVGlldNSRMKSDTQWVIDSM-RVKTPGHRTQIgSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515953848 168 LAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:PRK10982 422 IDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-238 |
1.85e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 81.74 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 23 QVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTH--YVATGGIAQAPEGRRIFPDMSVEEN 100
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 101 -------------------LLMGTIPVGNQHAAEDMQSmfdlfprlkerrnqramTLSGGEQQMLAIARALMSRPKLLLL 161
Cdd:PRK11831 105 vayplrehtqlpapllhstVMMKLEAVGLRGAAKLMPS-----------------ELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 162 DEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLK--DPEVRKaYLGGV 238
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAnpDPRVRQ-FLDGI 246
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-207 |
2.27e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.32 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 3 EPMLQFQDVDVF---YGVIqaLKQVSLEVNKGETVALIGANGAGKSTLLMSV-----FGQPRIR---NGQILFcgedISH 71
Cdd:COG4178 360 DGALALEDLTLRtpdGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpYGSGRIArpaGARVLF----LPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 72 KSthYVATGGIAQA---PEGRRIFPDMSVEENLLMgtipVGNQHaaedmqsmfdLFPRLKERRNqRAMTLSGGEQQMLAI 148
Cdd:COG4178 434 RP--YLPLGTLREAllyPATAEAFSDAELREALEA----VGLGH----------LAERLDEEAD-WDQVLSLGEQQRLAF 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515953848 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRElARNGMTIFLV----EQNAHHA--LKLSDRG 207
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVghrsTLAAFHDrvLELTGDG 560
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-226 |
2.59e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.17 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLlMSVFGQpRIRNGqilfcgediSHKSTHYVATGGIAQAPEGRRI--------- 91
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTL-MNALAF-RSPKG---------VKGSGSVLLNGMPIDAKEMRAIsayvqqddl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 92 -FPDMSVEENLL-MGTIPVGNQHAA-EDMQSMFDLFPRLKERRNQ--------RAMTLSGGEQQMLAIARALMSRPKLLL 160
Cdd:TIGR00955 110 fIPTLTVREHLMfQAHLRMPRRVTKkEKRERVDEVLQALGLRKCAntrigvpgRVKGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515953848 161 LDEPSLGLAPIVVKQIFQTLRELARNGMTIFL-VEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLK 226
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICtIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-215 |
3.34e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.89 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSThyvatggiAQAPEGRR----IFPD 94
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR--------AQRKAFRRdiqmVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 95 M------------SVEENL--LMGTIPVGNQHAAEDMQSMFDLFPRLKERRNQRamtLSGGEQQMLAIARALMSRPKLLL 160
Cdd:PRK10419 98 SisavnprktvreIIREPLrhLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ---LSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515953848 161 LDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVeqnAHHALKLSD----RGYVMVNGQI 215
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLF---ITHDLRLVErfcqRVMVMDNGQI 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
6-235 |
3.92e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 81.03 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGV-----IQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDI----SHKSTHY 76
Cdd:PRK13641 3 IKFENVDYIYSPgtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 77 V--ATGGIAQAPEGRrIFPDmSVEENLLMGTIPVG--NQHAAEDMQSMFDLFPRLKERRNQRAMTLSGGEQQMLAIARAL 152
Cdd:PRK13641 83 LrkKVSLVFQFPEAQ-LFEN-TVLKDVEFGPKNFGfsEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPE-VR 231
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwLK 240
|
....
gi 515953848 232 KAYL 235
Cdd:PRK13641 241 KHYL 244
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-217 |
4.31e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 80.07 E-value: 4.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAQAPEGRRIFpD 94
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWW-D 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 95 MSVEENLLMgtipvgnqhaaedMQSMFDLFP-RLKERR-------------NQRAMTLSGGEQQMLAIARALMSRPKLLL 160
Cdd:cd03267 110 LPVIDSFYL-------------LAAIYDLPPaRFKKRLdelselldleellDTPVRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515953848 161 LDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRgyVMVNGQIRL 217
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARR--VLVIDKGRL 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-233 |
4.54e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 80.90 E-value: 4.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 20 ALKQVSLEVNKGETVALIGANGAGKST-------LLMSVFGQPRIRNgqilFCGEDISHKSTHYVATGGIAQAPEGRRIf 92
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTiakhmnaLLIPSEGKVYVDG----LDTSDEENLWDIRNKAGMVFQNPDNQIV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 93 pDMSVEENLLMGTIPVGNQhaAEDMQSMFDlfPRLK-----ERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:PRK13633 100 -ATIVEEDVAFGPENLGIP--PEEIRERVD--ESLKkvgmyEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515953848 168 LAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKlSDRGYVMVNGQIRLSGSGEALLKDPEVRKA 233
Cdd:PRK13633 175 LDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMMKK 240
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-235 |
5.36e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 80.42 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 2 SEPMLQFQDVDVFYG--VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVAT 79
Cdd:PRK13632 4 KSVMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 80 --GGIAQAPEGRriFPDMSVE-------ENLL-----MGTIpVGNQHAAEDMQSMFDlfprlKERRNqramtLSGGEQQM 145
Cdd:PRK13632 84 kiGIIFQNPDNQ--FIGATVEddiafglENKKvppkkMKDI-IDDLAKKVGMEDYLD-----KEPQN-----LSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGM-TIFLVEQNAHHALkLSDRGYVMVNGQIRLSGSGEAL 224
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229
|
250
....*....|..
gi 515953848 225 LKDPE-VRKAYL 235
Cdd:PRK13632 230 LNNKEiLEKAKI 241
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-225 |
6.77e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.93 E-value: 6.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 7 QFQDVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKST---LLMSVFgQPriRNGQILFCGEDISHKST----HYVA 78
Cdd:PRK13657 336 EFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTlinLLQRVF-DP--QSGRILIDGTDIRTVTRaslrRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 79 TggIAQAPegrRIFpDMSVEENLLMGTIPVGNQH---AAEDMQSMfDLFPRLKERRN----QRAMTLSGGEQQMLAIARA 151
Cdd:PRK13657 413 V--VFQDA---GLF-NRSIEDNIRVGRPDATDEEmraAAERAQAH-DFIERKPDGYDtvvgERGRQLSGGERQRLAIARA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515953848 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELaRNGMTIFLVeqnAHhalKLS-----DRGYVMVNGQIRLSGSGEALL 225
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFII---AH---RLStvrnaDRILVFDNGRVVESGSFDELV 557
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-164 |
7.08e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.03 E-value: 7.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 4 PMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQIlfcgeDISHKsthyVATGGIA 83
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-----KLGET----VKIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 QapEGRRIFPDMSVEENLLMGTIPVGNQHAAEDMQSMfdLFPRlkERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:COG0488 385 Q--HQEELDPDKTVLDELRDGAPGGTEQEVRGYLGRF--LFSG--DDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
.
gi 515953848 164 P 164
Cdd:COG0488 459 P 459
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-230 |
1.35e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.39 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYV--ATGGIAQAPEGrRIFpDMS 96
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrsKVGLVFQDPDD-QVF-SST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 97 VEENLLMGTIPVG------NQHAAEDMQSMfdlfpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAP 170
Cdd:PRK13647 97 VWDDVAFGPVNMGldkdevERRVEEALKAV-----RMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 171 IVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIrLSGSGEALLKDPEV 230
Cdd:PRK13647 172 RGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRV-LAEGDKSLLTDEDI 230
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-210 |
1.89e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 78.75 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 4 PMLQFQDVDVFYGV----IQALKQVSLEVNKGETVALIGANGAGKSTLL--MSVFGQPRirNGQILFCGEDISHksthyv 77
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLnlIAGFLAPS--SGEITLDGVPVTG------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 78 atggiaqaPEGRR--------IFPDMSVEENLLMGT----IPVGNQHA-AEDMQSMFDLfprlKERRNQRAMTLSGGEQQ 144
Cdd:COG4525 74 --------PGADRgvvfqkdaLLPWLNVLDNVAFGLrlrgVPKAERRArAEELLALVGL----ADFARRRIWQLSGGMRQ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515953848 145 MLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARNGMTIFLVEQNAHHALKLSDRGYVM 210
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-232 |
2.05e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.79 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQprirngqilfcgedISH-KSTHYVATGGIAQAPEGRRIFpDMSVEE 99
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGE--------------LSHaETSSVVIRGSVAYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 100 NLLMGTIPVGNQHA----AEDMQSMFDLFP-RLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVK 174
Cdd:PLN03232 698 NILFGSDFESERYWraidVTALQHDLDLLPgRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515953848 175 QIFQTLRELARNGMTIFLVeQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEVRK 232
Cdd:PLN03232 778 QVFDSCMKDELKGKTRVLV-TNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFK 834
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-224 |
2.19e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.01 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGE--------DISHKsthyvaTGGIAQAPEGRriF 92
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllteenvwDIRHK------IGMVFQNPDNQ--F 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 93 PDMSVEENLLMGTIPVGNQHaaEDMQSMFDLFPRL------KERRNQRamtLSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:PRK13650 95 VGATVEDDVAFGLENKGIPH--EEMKERVNEALELvgmqdfKEREPAR---LSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515953848 167 GLAPIVVKQIFQTLREL-ARNGMTIFLVEQNAHHaLKLSDRGYVMVNGQIRLSGSGEAL 224
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIrDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPREL 227
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-229 |
2.40e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.91 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFcGEDI--SHKSTHYVAT-----GGIAQAPEgRRIF 92
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitAGKKNKKLKPlrkkvGIVFQFPE-HQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 93 PDmSVEENLLMGTIPVG--NQHAAEDMQSMFDLFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAP 170
Cdd:PRK13634 100 EE-TVEKDICFGPMNFGvsEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 171 IVVKQIFQTLRELAR-NGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPE 229
Cdd:PRK13634 179 KGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-220 |
2.51e-17 |
|
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: 80.83 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDIshKSTHYVATGGIAQAPEGRRIFPDMSVEE 99
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 100 NLLMGTIPVGN--QHAAEDMQSMFDlFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIF 177
Cdd:TIGR01257 1023 HILFYAQLKGRswEEAQLEMEAMLE-DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515953848 178 QTLRELaRNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGS 220
Cdd:TIGR01257 1102 DLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-215 |
2.73e-17 |
|
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: 76.49 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQA--LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDIS--HKSTHYVATGG 81
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 IAQapegrrifpdmsvEENLLMGTIpvgnqhaAEDMqsmfdlfprlkerrnqramtLSGGEQQMLAIARALMSRPKLLLL 161
Cdd:cd03246 81 LPQ-------------DDELFSGSI-------AENI--------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515953848 162 DEPSLGLAPIVVKQIFQTLRELARNGMTIFLVeqnAHH--ALKLSDRGYVMVNGQI 215
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAAGATRIVI---AHRpeTLASADRILVLEDGRV 173
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-201 |
4.05e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.50 E-value: 4.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGqilfcgedishkSTHYVATGGIAQAP---EGRRI 91
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG------------TVRRAGGARVAYVPqrsEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 92 FPdMSVEENLLMGTIP---VGNQHAAEDMQSMFDLFPR--LKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:NF040873 70 LP-LTVRDLVAMGRWArrgLWRRLTRDDRAAVDDALERvgLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190
....*....|....*....|....*....|....*
gi 515953848 167 GLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHAL 201
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGATVVVVTHDLELVR 183
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
15-217 |
4.91e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.41 E-value: 4.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILfcgedishksthyVATGGIAQAPEG------ 88
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-------------AGTAPLAEAREDtrlmfq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 89 -RRIFPDMSVEENLLMGTIPVGNQHAAEDMQSMfdlfpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPsLG 167
Cdd:PRK11247 89 dARLLPWKKVIDNVGLGLKGQWRDAALQALAAV-----GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP-LG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515953848 168 ----LAPIVVKQIFQTLRElaRNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRL 217
Cdd:PRK11247 163 aldaLTRIEMQDLIESLWQ--QHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGL 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-226 |
5.33e-17 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 79.41 E-value: 5.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISH-------KSTHYVAtggiaQAPEgrrIFP 93
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwdreelgRHIGYLP-----QDVE---LFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 94 DmSVEENL-LMGTIPVGNQHAAEDMQSMFDLFPRLKE----RRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:COG4618 420 G-TIAENIaRFGDADPEKVVAAAKLAGVHEMILRLPDgydtRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 169 APIVVKQIFQTLRELARNGMTIFLVeqnAH--HALKLSDRGYVMVNGQIRLSGSGEALLK 226
Cdd:COG4618 499 DDEGEAALAAAIRALKARGATVVVI---THrpSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-228 |
5.41e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 78.23 E-value: 5.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFY-----------GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDI 69
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 70 SHKSTHyvatggiAQAPEGRR---IF--------PDMSVEENL-----LMGTIPVGN-QHAAEDMQSMFDLFPrlkERRN 132
Cdd:COG4608 83 TGLSGR-------ELRPLRRRmqmVFqdpyaslnPRMTVGDIIaeplrIHGLASKAErRERVAELLELVGLRP---EHAD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 133 QRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARNGMT-IFLveqnAH------HalkLS 204
Cdd:COG4608 153 RYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLqDELGLTyLFI----SHdlsvvrH---IS 225
|
250 260
....*....|....*....|....
gi 515953848 205 DRGYVMVNGQIRLSGSGEALLKDP 228
Cdd:COG4608 226 DRVAVMYLGKIVEIAPRDELYARP 249
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
5-238 |
5.87e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.85 E-value: 5.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYG-----VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFG-----QPRIRNGQILFCGEDiSHKST 74
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSSTS-KQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 75 HYV--ATGGIAQAPEGRrIFPDmSVEENLLMG--TIPVGNQHAAEDMQSMFDLFPRLKERRNQRAMTLSGGEQQMLAIAR 150
Cdd:PRK13643 80 KPVrkKVGVVFQFPESQ-LFEE-TVLKDVAFGpqNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEV 230
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDF 237
|
....*...
gi 515953848 231 RKAYLGGV 238
Cdd:PRK13643 238 LKAHELGV 245
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-225 |
6.87e-17 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 78.99 E-value: 6.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGV--IQALKQVSLEVNKGETVALIGANGAGKSTL--LMSVFGQPRirNGQILFCGEDISHKSTHYVATGg 81
Cdd:TIGR02203 331 VEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLvnLIPRFYEPD--SGQILLDGHDLADYTLASLRRQ- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 IAQAPEGRRIFPDmSVEENLL---MGTIP---VGNQHAAEDMQSMFDLFPR-LKERRNQRAMTLSGGEQQMLAIARALMS 154
Cdd:TIGR02203 408 VALVSQDVVLFND-TIANNIAygrTEQADraeIERALAAAYAQDFVDKLPLgLDTPIGENGVLLSGGQRQRLAIARALLK 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515953848 155 RPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLveqnAHH--ALKLSDRGYVMVNGQIRLSGSGEALL 225
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERLMQGRTTLVI----AHRlsTIEKADRIVVMDDGRIVERGTHNELL 555
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
6-227 |
1.00e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.13 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFY--GV---IQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYV--- 77
Cdd:PRK13646 3 IRFDNVSYTYqkGTpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 78 ---ATGGIAQAPEGrRIFPDmSVEENLLMGtiPVGNQHAAEDMQS-MFDLFPRLKERRN---QRAMTLSGGEQQMLAIAR 150
Cdd:PRK13646 83 vrkRIGMVFQFPES-QLFED-TVEREIIFG--PKNFKMNLDEVKNyAHRLLMDLGFSRDvmsQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515953848 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELA-RNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKD 227
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-203 |
1.30e-16 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 75.97 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 3 EPMLQFQDVDVFYGV---IQALKQVSLEVNKGETVALIGANGAGKSTL--LMSVFGQPRirNGQILFCGEDIS---HKST 74
Cdd:cd03248 9 KGIVKFQNVTFAYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVvaLLENFYQPQ--GGQVLLDGKPISqyeHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 75 HYVATGgIAQAPegrrIFPDMSVEENLL--MGTIPVGNQHAAEDMQSMFDLFPRLK----ERRNQRAMTLSGGEQQMLAI 148
Cdd:cd03248 87 HSKVSL-VGQEP----VLFARSLQDNIAygLQSCSFECVKEAAQKAHAHSFISELAsgydTEVGEKGSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953848 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNgMTIFLVE------QNAHHALKL 203
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAhrlstvERADQILVL 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-200 |
1.76e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.84 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 4 PMLQFQDVDVFY----GVIQALKQVSLEVNKGETVALIGANGAGKSTLlMSVFG---QPRirNGQILFCGEDISHKSTHY 76
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTL-MNILGcldKPT--SGTYRVAGQDVATLDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 77 VAT------GGIAQApegRRIFPDMSVEENLLMGTIPVGNQHAAEdMQSMFDLFPRL--KERRNQRAMTLSGGEQQMLAI 148
Cdd:PRK10535 80 LAQlrrehfGFIFQR---YHLLSHLTAAQNVEVPAVYAGLERKQR-LLRAQELLQRLglEDRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515953848 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHA 200
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVA 207
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-204 |
2.41e-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: 74.70 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYvaTGGIAQAPEGRRIFPDMSVEE 99
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP--HENILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 100 NL-LMGTIPVGNQHAAEDMQSMFDlfprLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQ 178
Cdd:TIGR01189 93 NLhFWAAIHGGAQRTIEDALAAVG----LTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAG 168
|
170 180
....*....|....*....|....*..
gi 515953848 179 TLRE-LARNGMTIFlveqNAHHALKLS 204
Cdd:TIGR01189 169 LLRAhLARGGIVLL----TTHQDLGLV 191
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-225 |
2.56e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 77.55 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 2 SEPMLQFQDVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYV-AT 79
Cdd:COG5265 354 GGGEVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLrAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 80 GGIAqaPEGRRIFPDmSVEENllmgtIPVGNQHAAED-------MQSMFDLFPRLKE----RRNQRAMTLSGGEQQMLAI 148
Cdd:COG5265 434 IGIV--PQDTVLFND-TIAYN-----IAYGRPDASEEeveaaarAAQIHDFIESLPDgydtRVGERGLKLSGGEKQRVAI 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLveqnAHhalKLS-----DRGYVMVNGQIRLSGSGEA 223
Cdd:COG5265 506 ARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVI----AH---RLStivdaDEILVLEAGRIVERGTHAE 578
|
..
gi 515953848 224 LL 225
Cdd:COG5265 579 LL 580
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-215 |
2.94e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 77.14 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRN--GQILFCGEDISHKSTHYVATGGIAQAPEGRR----IF 92
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRNisGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKgyglNL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 93 PDmSVEENLLMGTIP------VGNQHA----AEDMQSmfdlfpRLKERR---NQRAMTLSGGEQQMLAIARALMSRPKLL 159
Cdd:NF040905 354 ID-DIKRNITLANLGkvsrrgVIDENEeikvAEEYRK------KMNIKTpsvFQKVGNLSGGNQQKVVLSKWLFTDPDVL 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515953848 160 LLDEPSLGlapIVV--K-QIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:NF040905 427 ILDEPTRG---IDVgaKyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-185 |
3.27e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 76.30 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFY----GVIQALKQVSLEVNKGETVALIGANGAGKSTL---LMSVFGQPRIRNGQILFCGEDISHKS 73
Cdd:PRK09473 8 QADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTafaLMGLLAANGRIGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 74 THYVATggiAQAPEGRRIFPD--------MSVEENL---LMGTIPVGNQHAAEDMQSMFDL--FPRLKERRNQRAMTLSG 140
Cdd:PRK09473 88 EKELNK---LRAEQISMIFQDpmtslnpyMRVGEQLmevLMLHKGMSKAEAFEESVRMLDAvkMPEARKRMKMYPHEFSG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515953848 141 GEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELAR 185
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKR 209
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-236 |
3.43e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.69 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDIsHKSTHYVAT 79
Cdd:PRK15056 2 MQQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-RQALQKNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 80 GGIAQAPEGRRIFPDMsVEENLLMGT---IPVGNQHAAEDMQSMFDLFPR--LKERRNQRAMTLSGGEQQMLAIARALMS 154
Cdd:PRK15056 81 AYVPQSEEVDWSFPVL-VEDVVMMGRyghMGWLRRAKKRDRQIVTAALARvdMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 155 RPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGyVMVNGQIRLSGSGEALLKDPEVRKAY 234
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFTAENLELAF 238
|
..
gi 515953848 235 LG 236
Cdd:PRK15056 239 SG 240
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-230 |
6.90e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 75.27 E-value: 6.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 18 IQALKQVSLEVNKGETVALIGANGAGKSTL-------LMSVFGQPRIRNgqiLFCGEDIS-HKSTHYVATGGIAQAPEGR 89
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLvthfnglIKSKYGTIQVGD---IYIGDKKNnHELITNPYSKKIKNFKELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 90 RI------FPDM-----SVEENLLMGTIPVG------NQHAAEDMQSMfdlfpRLKERRNQRA-MTLSGGEQQMLAIARA 151
Cdd:PRK13631 116 RRvsmvfqFPEYqlfkdTIEKDIMFGPVALGvkkseaKKLAKFYLNKM-----GLDDSYLERSpFGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515953848 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEV 230
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHI 269
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-235 |
1.03e-15 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 73.67 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYV--ATGGIAQApegrRIFPDMSV 97
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLrrQVGVVLQE----NVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 98 EENLLMG--TIPVGNQHAAEDMQSMFDLFPRLKERRNQ----RAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:cd03252 93 RDNIALAdpGMSMERVIEAAKLAGAHDFISELPEGYDTivgeQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953848 172 VVKQIFQTLRELARnGMTIFLVeqnAHH--ALKLSDRGYVMVNGQIRLSGSGEALLkDPEVRKAYL 235
Cdd:cd03252 173 SEHAIMRNMHDICA-GRTVIII---AHRlsTVKNADRIIVMEKGRIVEQGSHDELL-AENGLYAYL 233
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-190 |
1.31e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.60 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISH----KSTHYVatggiaqapeGRRIF--PD 94
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpdvaEACHYL----------GHRNAmkPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 95 MSVEENL-----LMGTIPVGNQHAAEDM--QSMFDLfprlkerrnqRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:PRK13539 88 LTVAENLefwaaFLGGEELDIAAALEAVglAPLAHL----------PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180
....*....|....*....|....
gi 515953848 168 LAPIVVKQIFQTLRE-LARNGMTI 190
Cdd:PRK13539 158 LDAAAVALFAELIRAhLAQGGIVI 181
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-189 |
1.34e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.21 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 14 FYGViQALKQVSLEVNKGETVALIGANGAGKSTlLMSV------FGQpriRNGQILFCGEDISHKSTHyvatggiaqAPE 87
Cdd:NF040905 11 FPGV-KALDDVNLSVREGEIHALCGENGAGKST-LMKVlsgvypHGS---YEGEILFDGEVCRFKDIR---------DSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 88 GRRI---------FPDMSVEENllmgtIPVGNQHA-------AEDMQSMFDLFPR--LKERRNQRAMTLSGGEQQMLAIA 149
Cdd:NF040905 77 ALGIviihqelalIPYLSIAEN-----IFLGNERAkrgvidwNETNRRARELLAKvgLDESPDTLVTDIGVGKQQLVEIA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515953848 150 RALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMT 189
Cdd:NF040905 152 KALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGIT 191
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
16-228 |
1.74e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 74.68 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 16 GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDI---SHKSTHYVATGGIAQAPEGRRIF 92
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakiSDAELREVRRKKIAMVFQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 93 PDMSVEENLLMGtIPVGNQHAAEDMQSMFDLFPR--LKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAP 170
Cdd:PRK10070 119 PHMTVLDNTAFG-MELAGINAEERREKALDALRQvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515953848 171 IVVKQIFQTLREL-ARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDP 228
Cdd:PRK10070 198 LIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-234 |
2.10e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.95 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 24 VSLEVNKGETVALIGANGAGKSTLLMSVFGQPRiRNGQILFCGEDISHKST-----------------------HYVATG 80
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAaelarhraylsqqqsppfampvfQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 81 GIAQAPEgrrifpdmSVEENLLMgtipvgnqHAAEDMQSMfDLFPRlkerrnqRAMTLSGGEQQMLAIARALM------- 153
Cdd:COG4138 94 QPAGASS--------EAVEQLLA--------QLAEALGLE-DKLSR-------PLTQLSGGEWQRVRLAAVLLqvwptin 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 154 SRPKLLLLDEPSLGLApiVVKQI--FQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEVR 231
Cdd:COG4138 150 PEGQLLLLDEPMNSLD--VAQQAalDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLS 227
|
...
gi 515953848 232 KAY 234
Cdd:COG4138 228 EVF 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-227 |
2.53e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 73.24 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTH------YVATGGIAQAPEGRrIFp 93
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikqiRKKVGLVFQFPESQ-LF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 94 DMSVEENLLMGTIPVG-NQHAAEDM-QSMFDLFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:PRK13649 100 EETVLKDVAFGPQNFGvSQEEAEALaREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515953848 172 VVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKD 227
Cdd:PRK13649 180 GRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-165 |
2.79e-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: 70.17 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLmsvfgqpRIRNGQILFCGEDISHKSTHYVATggIAQa 85
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLL-------KLIAGELEPDEGIVTWGSTVKIGY--FEQ- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 86 pegrrifpdmsveenllmgtipvgnqhaaedmqsmfdlfprlkerrnqramtLSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:cd03221 71 ----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-228 |
3.12e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.59 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 18 IQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSThyvatggiAQAPEGRR----IFP 93
Cdd:PRK15079 34 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKD--------DEWRAVRSdiqmIFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 94 D--MSVEENLLMGTIpvgnqhAAEDMQSMFDLFPRLKERRNQRAMTL----------------SGGEQQMLAIARALMSR 155
Cdd:PRK15079 106 DplASLNPRMTIGEI------IAEPLRTYHPKLSRQEVKDRVKAMMLkvgllpnlinryphefSGGQCQRIGIARALILE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 156 PKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMT-IFLveqnAH------HalkLSDRGYVMVNGQIRLSGSGEALLKD 227
Cdd:PRK15079 180 PKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSlIFI----AHdlavvkH---ISDRVLVMYLGHAVELGTYDEVYHN 252
|
.
gi 515953848 228 P 228
Cdd:PRK15079 253 P 253
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-227 |
4.09e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 72.35 E-value: 4.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATgGIAQ 84
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR-RLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 85 APEGRRIFPDMSVEENLLMGTIPVGN----------QHAAEDMQSMfdlfpRLKERRNQRAMTLSGGEQQMLAIARALMS 154
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSPWLSlwgrlsaednARVNQAMEQT-----RINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 155 RPKLLLLDEPS--LGLAPIVvkQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGS-----GEALLKD 227
Cdd:PRK11231 156 DTPVVLLDEPTtyLDINHQV--ELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTpeevmTPGLLRT 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-238 |
5.92e-15 |
|
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: 73.30 E-value: 5.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRN--GQILF------------------- 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPtsGRIIYhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 65 ----CGEDISHKSTHYVATGGIAQAPEGRRI----------FPDMSVEENLLMGTIPVGNQhAAEDMQSMFDLFP--RLK 128
Cdd:TIGR03269 81 pcpvCGGTLEPEEVDFWNLSDKLRRRIRKRIaimlqrtfalYGDDTVLDNVLEALEEIGYE-GKEAVGRAVDLIEmvQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 129 ERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRG 207
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEVIEDLSDKA 239
|
250 260 270
....*....|....*....|....*....|.
gi 515953848 208 YVMVNGQIRLSGSGEallkdpEVRKAYLGGV 238
Cdd:TIGR03269 240 IWLENGEIKEEGTPD------EVVAVFMEGV 264
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-215 |
6.35e-15 |
|
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: 70.75 E-value: 6.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 18 IQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIR---NGQILFCGEDIshKSTHYVATGGIAQAPEGRRIFPD 94
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY--KEFAEKYPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 95 MSVEENLlmgtipvgnqhaaedmqsMFdlfpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVK 174
Cdd:cd03233 98 LTVRETL------------------DF----ALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515953848 175 QIFQTLRELAR--NGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:cd03233 156 EILKCIRTMADvlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-164 |
7.68e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 72.57 E-value: 7.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSThyvATGGIA 83
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP---ADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 QAPEGRRIFPDMSVEENLLMG---------TIPVGNQHAAEdmqsMFDLFPRLKERRNQramtLSGGEQQMLAIARALMS 154
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMAYGlkirgmpkaEIEERVAEAAR----ILELEPLLDRKPRE----LSGGQRQRVAMGRAIVR 151
|
170
....*....|
gi 515953848 155 RPKLLLLDEP 164
Cdd:PRK11650 152 EPAVFLFDEP 161
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-234 |
7.88e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.60 E-value: 7.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQP--RIRNGQILFCGEDISHKSTHYVA 78
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 79 TGGI---AQAP----------------EGRRIF---PDMSVEE--NLLMGTIPVGNqhaaedMQSMFdlfprLKERRNQr 134
Cdd:CHL00131 83 HLGIflaFQYPieipgvsnadflrlayNSKRKFqglPELDPLEflEIINEKLKLVG------MDPSF-----LSRNVNE- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 135 amTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVeqnAHHALKLS----DRGYVM 210
Cdd:CHL00131 151 --GFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILI---THYQRLLDyikpDYVHVM 225
|
250 260
....*....|....*....|....
gi 515953848 211 VNGQIRLSGSGEaLLKDPEvRKAY 234
Cdd:CHL00131 226 QNGKIIKTGDAE-LAKELE-KKGY 247
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-220 |
1.75e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.19 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 19 QALKQVSLEVNKGETVALIGANGAGKST-------LLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAQAPEgRRI 91
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTmiqltngLIISETGQTIVGDYAIPANLKKIKEVKRLRKEIGLVFQFPE-YQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 92 FPDmSVEENLLMGTIPVG--NQHAAEDMQSMFDLFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:PRK13645 104 FQE-TIEKDIAFGPVNLGenKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515953848 170 PIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGS 220
Cdd:PRK13645 183 PKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
15-164 |
1.81e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.60 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILfcgedISHKSTHYV--ATGGIAQAPEGRRIF 92
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLF-----IGEKRMNDVppAERGVGMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 93 PDMSVEENLLMGTIPVGN---------QHAAEDMQsmfdlFPRLKERRNQramTLSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:PRK11000 88 PHLSVAENMSFGLKLAGAkkeeinqrvNQVAEVLQ-----LAHLLDRKPK---ALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
.
gi 515953848 164 P 164
Cdd:PRK11000 160 P 160
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-228 |
1.99e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.80 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 19 QALKQVSLEVNKGETVALIGANGAGKSTLL------MSVFGQPRIrNGQILfcgEDISHKS--THYVATGGIAQAPEGrr 90
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLnallgfLPYQGSLKI-NGIEL---RELDPESwrKHLSWVGQNPQLPHG-- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 91 ifpdmSVEENLLMGTIPVGNQHAAEDMQSMF--DLFPRLKERRN----QRAMTLSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:PRK11174 438 -----TLRDNVLLGNPDASDEQLQQALENAWvsEFLPLLPQGLDtpigDQAAGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515953848 165 SLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAhhALKLSDRGYVMVNGQIRLSGSGEALLKDP 228
Cdd:PRK11174 513 TASLDAHSEQLVMQALNAASRRQTTLMVTHQLE--DLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-228 |
2.22e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.09 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 16 GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQP----RIRNGQILFCGEDISHKSthyvatggiaqaPEGRR- 90
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLS------------PRERRk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 91 --------IFPDMSveeNLLMGTIPVGNQHaaedMQSMFD------LFPRLKERRnQRAMTL------------------ 138
Cdd:COG4170 86 iigreiamIFQEPS---SCLDPSAKIGDQL----IEAIPSwtfkgkWWQRFKWRK-KRAIELlhrvgikdhkdimnsyph 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 139 --SGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:COG4170 158 elTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLqGTSILLISHDLESISQWADTITVLYCGQT 237
|
250
....*....|...
gi 515953848 216 RLSGSGEALLKDP 228
Cdd:COG4170 238 VESGPTEQILKSP 250
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-230 |
2.46e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 70.11 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVAtggiaq 84
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 85 apegRRifpdMSV--EENLLMGTIPVgnqhaaEDMQSmFDLFP----RLKERRNQ---RAM--------------TLSGG 141
Cdd:COG4604 75 ----KR----LAIlrQENHINSRLTV------RELVA-FGRFPyskgRLTAEDREiidEAIayldledladryldELSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 142 EQQMLAIARALMSRPKLLLLDEP--SLGLAPIVvkQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLS 218
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPlnNLDMKHSV--QMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQ 217
|
250
....*....|..
gi 515953848 219 GSGEALLkDPEV 230
Cdd:COG4604 218 GTPEEII-TPEV 228
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-208 |
4.32e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.44 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGIAQ 84
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 85 APEGrrIFPDMSVEENLLMGTIPVGNQHAAEDMQSMFDL-----FPrlkerrnqrAMTLSGGEQQMLAIARALMSRPKLL 159
Cdd:PRK13540 81 HRSG--INPYLTLRENCLYDIHFSPGAVGITELCRLFSLehlidYP---------CGLLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515953848 160 LLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLveqNAHHALKLSDRGY 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 ... |
3-227 |
6.81e-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: 70.22 E-value: 6.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 3 EPMLQFQDVDVFY-----GVIQALKQVSLEVNKGETVALIGANGAGKSTL---LMSVF----GQPRIRNGQ----ILFCG 66
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLskiIAGVLeptsGEVNVRVGDewvdMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 67 EDISHKSTHYVatgGIAQAPEGrrIFPDMSVEENLlmgTIPVGNQHAAE--DMQSMFDL----FPRLKERR--NQRAMTL 138
Cdd:TIGR03269 357 PDGRGRAKRYI---GILHQEYD--LYPHRTVLDNL---TEAIGLELPDElaRMKAVITLkmvgFDEEKAEEilDKYPDEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 139 SGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI----VVKQIFQTLRELarnGMTIFLVEQNAHHALKLSDRGYVMVNGQ 214
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPItkvdVTHSILKAREEM---EQTFIIVSHDMDFVLDVCDRAALMRDGK 505
|
250
....*....|...
gi 515953848 215 IRLSGSGEALLKD 227
Cdd:TIGR03269 506 IVKIGDPEEIVEE 518
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-208 |
7.32e-14 |
|
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: 67.90 E-value: 7.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCG------EDISHKSTHYVatgGIAQAPEGRrifpd 94
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpldfqRDSIARGLLYL---GHAPGIKTT----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 95 MSVEENLLMgtipvgnQHAAEDMQSMFDLFPR--LKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIV 172
Cdd:cd03231 88 LSVLENLRF-------WHADHSDEQVEEALARvgLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 515953848 173 VKQIFQTLR-ELARNGMTIFlveqNAHHALKLSDRGY 208
Cdd:cd03231 161 VARFAEAMAgHCARGGMVVL----TTHQDLGLSEAGA 193
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-216 |
8.24e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 68.27 E-value: 8.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 17 VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVA------TGGIAQApegRR 90
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklrakhVGFVFQS---FM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 91 IFPDMSVEEN-----LLMGTIPVGNQHAAEDMQSMFDLFPRLKERRNQramtLSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:PRK10584 99 LIPTLNALENvelpaLLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQ----LSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515953848 166 LGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKlSDRGYVMVNGQIR 216
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAAR-CDRRLRLVNGQLQ 225
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
5-234 |
1.57e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.93 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQ---------PRIRnGQILFCGEDISHKSTH 75
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgggaprgARVT-GDVTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 76 YVATGGIAQAPEGRRIFPdMSVEENLLMGTIPVGNQHAAEDMQSMfDLFPRLKERRNQRAM------TLSGGEQQMLAIA 149
Cdd:PRK13547 80 RLARLRAVLPQAAQPAFA-FSAREIVLLGRYPHARRAGALTHRDG-EIAWQALALAGATALvgrdvtTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 150 RAL---------MSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSG 219
Cdd:PRK13547 158 RVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
250
....*....|....*
gi 515953848 220 SGEALLKDPEVRKAY 234
Cdd:PRK13547 238 APADVLTPAHIARCY 252
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-207 |
1.95e-13 |
|
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: 66.02 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLmsvfgqpriRngqilfcgedishksthyvATGGIAQAPEGRRIFPDMsveEN 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLF---------R-------------------ALAGLWPWGSGRIGMPEG---ED 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 101 LLMgtIPvgnQHAaedmqsmfdLFPR--LKErrnQRA----MTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVK 174
Cdd:cd03223 66 LLF--LP---QRP---------YLPLgtLRE---QLIypwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180 190
....*....|....*....|....*....|....*....
gi 515953848 175 QIFQTLRELarnGMTIFLV------EQNAHHALKLSDRG 207
Cdd:cd03223 129 RLYQLLKEL---GITVISVghrpslWKFHDRVLDLDGEG 164
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
2.16e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.47 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYGVIQA--LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVA 78
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 79 --TGGIAQAPEGRriFPDMSVEENLLMG----TIPVGNQHaAEDMQSMFDLfpRLKERRNQRAMTLSGGEQQMLAIARAL 152
Cdd:PRK13648 83 khIGIVFQNPDNQ--FVGSIVKYDVAFGlenhAVPYDEMH-RRVSEALKQV--DMLERADYEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515953848 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARNGMTIFLVEQNAHHALKlSDRGYVMVNGQIRLSGSGEALLKDPE 229
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-163 |
2.73e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.66 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 2 SEPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKS--THYVAT 79
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpeIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 80 GGIAQAPEgrrIFPDmSVEENLLMgtiPVGNQHAAEDMQSMFDLFPRL---KERRNQRAMTLSGGEQQMLAIARALMSRP 156
Cdd:PRK10247 84 SYCAQTPT---LFGD-TVYDNLIF---PWQIRNQQPDPAIFLDDLERFalpDTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
....*..
gi 515953848 157 KLLLLDE 163
Cdd:PRK10247 157 KVLLLDE 163
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
15-215 |
2.78e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.22 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 15 YGVIQALKQVSLEVNKGETVALIGANGAG--KSTLLMSVFGQPRIRNGQ--ILFCGEDISHKSThyvaTGGIAQAPEGRR 90
Cdd:NF000106 23 FGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWrf*TWCANRRALRRT----IG*HRPVR*GRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 91 ifPDMSVEENLLM--GTIPVGNQHAAEDMQSMFDLFpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:NF000106 99 --ESFSGRENLYMigR*LDLSRKDARARADELLERF-SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515953848 169 APIVVKQIFQTLRELARNGMTIFLVEQ------NAHHALKLSDRGYVMVNGQI 215
Cdd:NF000106 176 DPRTRNEVWDEVRSMVRDGATVLLTTQymeeaeQLAHELTVIDRGRVIADGKV 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-232 |
2.91e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 67.52 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKST---LLMSVFGQPRIRNGQILFCGEDISHKSTH 75
Cdd:PRK13640 1 MKDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 76 YV--ATGGIAQAPEGRriFPDMSVEENLLMGTipVGNQHAAEDMQSMfdlfprLKERRNQRAMT---------LSGGEQQ 144
Cdd:PRK13640 81 DIreKVGIVFQNPDNQ--FVGATVGDDVAFGL--ENRAVPRPEMIKI------VRDVLADVGMLdyidsepanLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 145 MLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELAR-NGMTIFLVEQNAHHAlKLSDRGYVMVNGQIRLSGSGEA 223
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVE 229
|
....*....
gi 515953848 224 LLKDPEVRK 232
Cdd:PRK13640 230 IFSKVEMLK 238
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
6-234 |
3.44e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVdvfyGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRiRNGQILFCGEDISHKSTHYVAT--GGIA 83
Cdd:PRK03695 1 MQLNDV----AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARhrAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 QApegRRIFPDMSVEENLLM----GTIPVGNQHAAEDMQSMFDLFPRLKERRNQramtLSGGEQQ-------MLAIARAL 152
Cdd:PRK03695 76 QQ---QTPPFAMPVFQYLTLhqpdKTRTEAVASALNEVAEALGLDDKLGRSVNQ----LSGGEWQrvrlaavVLQVWPDI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEVRK 232
Cdd:PRK03695 149 NPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQ 228
|
..
gi 515953848 233 AY 234
Cdd:PRK03695 229 VF 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-236 |
5.35e-13 |
|
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: 68.01 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 17 VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQilfcgedISHksthyvaTGGIAQAPEGRRIFPDmS 96
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGK-------IKH-------SGRISFSPQTSWIMPG-T 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 97 VEENLLMG--------TIPVGNQHAAEDMQsmfdLFP-RLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:TIGR01271 503 IKDNIIFGlsydeyryTSVIKACQLEEDIA----LFPeKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953848 168 LAPIVVKQIFQT-LRELARNGMTIFLVEQNAHhaLKLSDRGYVMVNGQIRLSGS-GEALLKDPEVRKAYLG 236
Cdd:TIGR01271 579 LDVVTEKEIFEScLCKLMSNKTRILVTSKLEH--LKKADKILLLHEGVCYFYGTfSELQAKRPDFSSLLLG 647
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
16-228 |
6.94e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 66.75 E-value: 6.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 16 GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQP----RIRNGQILFCGEDISHKST--------HYVATggIA 83
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPrerrklvgHNVSM--IF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 QAPEGRrIFPDMSVEENLlMGTIPvGNQHAAEDMQSM-------FDLFPRLKERRNQRAM-----TLSGGEQQMLAIARA 151
Cdd:PRK15093 96 QEPQSC-LDPSERVGRQL-MQNIP-GWTYKGRWWQRFgwrkrraIELLHRVGIKDHKDAMrsfpyELTEGECQKVMIAIA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515953848 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDP 228
Cdd:PRK15093 173 LANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-204 |
8.25e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 65.88 E-value: 8.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSthyvATGGIAQ 84
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG----AERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 85 APEGrrIFPDMSVEENLLMGTIPVG-----NQHAAEDMQSMFDLfprlKERRNQRAMTLSGGEQQMLAIARALMSRPKLL 159
Cdd:PRK11248 77 QNEG--LLPWRNVQDNVAFGLQLAGvekmqRLEIAHQMLKKVGL----EGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515953848 160 LLDEPSLGLAPIVVKQIfQT--LRELARNGMTIFLVEQNAHHALKLS 204
Cdd:PRK11248 151 LLDEPFGALDAFTREQM-QTllLKLWQETGKQVLLITHDIEEAVFMA 196
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-208 |
2.08e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.05 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 25 SLEVNKGETVALIGANGAGKSTLL--MSVFGQPriRNGQILFCGEDIS------HKSTHYV--ATGgiaqapegrrIFPD 94
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLriLAGLARP--DAGEVLWQGEPIRrqrdeyHQDLLYLghQPG----------IKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 95 MSVEENLLMgtipvgNQHAAE--DMQSMFDLFPR--LKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAP 170
Cdd:PRK13538 89 LTALENLRF------YQRLHGpgDDEALWEALAQvgLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 515953848 171 IVVKQIFQTLRE-LARNGMTIFlveqNAHHALKLSDRGY 208
Cdd:PRK13538 163 QGVARLEALLAQhAEQGGMVIL----TTHQDLPVASDKV 197
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-229 |
3.78e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.98 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 4 PMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQIlfcgedishKSTHYVATGGIa 83
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLRIGYV- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 qaPEGRRIFPDMSVEENLLMGTIPvGNQHAaedmqsmfDLFPRLKERR-----NQRAMTLSGGEQQMLAIARALMSRPKL 158
Cdd:PRK09544 73 --PQKLYLDTTLPLTVNRFLRLRP-GTKKE--------DILPALKRVQaghliDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515953848 159 LLLDEPSLGLApiVVKQ------IFQTLRELarnGMTIFLVEQNAHHALKLSDRgYVMVNGQIRLSGSGEALLKDPE 229
Cdd:PRK09544 142 LVLDEPTQGVD--VNGQvalydlIDQLRREL---DCAVLMVSHDLHLVMAKTDE-VLCLNHHICCSGTPEVVSLHPE 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-224 |
5.23e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 65.03 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDIshksthyvaTGGIAQAPEGRRIFPDMSVEE 99
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI---------LTNISDVHQNMGYCPQFDAID 2024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 100 NLLmgtipVGNQH----------AAEDMQSMFDLFPR---LKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:TIGR01257 2025 DLL-----TGREHlylyarlrgvPAEEIEKVANWSIQslgLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTT 2099
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515953848 167 GLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEAL 224
Cdd:TIGR01257 2100 GMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-228 |
1.06e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.79 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 24 VSLEVNKGETVALIGANGAGKSTLLMSVFG--QPRIR--NGQILFCGEDISHKSTHYVATGGIAQAPEGR----RIFPDM 95
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSLTCAAALGilPAGVRqtAGRVLLDGKPVAPCALRGRKIATIMQNPRSAfnplHTMHTH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 96 SVEENLLMGTIPVGNQHAA-------EDMQSMFDLFPrlkerrnqraMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:PRK10418 102 ARETCLALGKPADDATLTAaleavglENAARVLKLYP----------FEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953848 169 APIVVKQIFQTLRELAR-NGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDP 228
Cdd:PRK10418 172 DVVAQARILDLLESIVQkRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-164 |
1.09e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQIlFCGEDIShksthyvatggIAQAPEGRRIF-PDMSVEE 99
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCGTKLE-----------VAYFDQHRAELdPEKTVMD 402
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515953848 100 NLLMG--TIPVGNQ--HAAEDMQSMfdLFPrlkerrNQRAMT----LSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:PRK11147 403 NLAEGkqEVMVNGRprHVLGYLQDF--LFH------PKRAMTpvkaLSGGERNRLLLARLFLKPSNLLILDEP 467
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-211 |
2.02e-11 |
|
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: 61.66 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 27 EVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKsthyvatggiaqaPEgrRIFPD--MSVEEnLLMG 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYK-------------PQ--YIKADyeGTVRD-LLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 105 TIP---VGNQHAAEDMQSMfdlfpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSlglAPIVVKQIFQTLR 181
Cdd:cd03237 85 ITKdfyTHPYFKTEIAKPL-----QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPS---AYLDVEQRLMASK 156
|
170 180 190
....*....|....*....|....*....|....
gi 515953848 182 ELAR----NGMTIFLVEQNAHHALKLSDRgyVMV 211
Cdd:cd03237 157 VIRRfaenNEKTAFVVEHDIIMIDYLADR--LIV 188
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-228 |
2.04e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.11 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 18 IQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYvatggiaQAPEGRRIFPDMSV 97
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY-------RSQRIRMIFQDPST 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 98 EEN-------LLMGTIPVGNQHAAEDMQSMFDLFPR----LKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:PRK15112 99 SLNprqrisqILDFPLRLNTDLEPEQREKQIIETLRqvglLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515953848 167 GLAPIVVKQIFQTLREL-ARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDP 228
Cdd:PRK15112 179 SLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-229 |
2.25e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.95 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 18 IQALKQVSLEVNKGETVALIGANGAGKSTL---LMSVFGQP-----------RIRNGQILFCGEdISHKSTHYVATGGIA 83
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTalaLMRLLEQAgglvqcdkmllRRRSRQVIELSE-QSAAQMRHVRGADMA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 ---QAPE---------GRRIFPDMSVEENLlmgtipvGNQHAAEDMQSMFDL--FPRLKERRNQRAMTLSGGEQQMLAIA 149
Cdd:PRK10261 108 mifQEPMtslnpvftvGEQIAESIRLHQGA-------SREEAMVEAKRMLDQvrIPEAQTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 150 RALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDP 228
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAP 260
|
.
gi 515953848 229 E 229
Cdd:PRK10261 261 Q 261
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-228 |
2.31e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 62.45 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSVFG----QPRIRNGQILFCGED---ISHKSTHYVATGGIAQapegrrI 91
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlidyPGRVMAEKLEFNGQDlqrISEKERRNLVGAEVAM------I 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 92 FPDMSVEEN-------LLMGTIPV---GN-----QHAAE--------DMQSMFDLFPRlkerrnqramTLSGGEQQMLAI 148
Cdd:PRK11022 95 FQDPMTSLNpcytvgfQIMEAIKVhqgGNkktrrQRAIDllnqvgipDPASRLDVYPH----------QLSGGMSQRVMI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIF-------LVEQNAHHALklsdrgyVMVNGQIRLSGS 220
Cdd:PRK11022 165 AMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVlithdlaLVAEAAHKII-------VMYAGQVVETGK 237
|
....*...
gi 515953848 221 GEALLKDP 228
Cdd:PRK11022 238 AHDIFRAP 245
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-215 |
2.53e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.03 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 18 IQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYV--ATGGIAQAPEGRriFPDM 95
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLrrKIGMVFQNPDNQ--FVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 96 SVEENLLMGtipVGNQHAA-EDMQSMFD---LFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:PRK13642 98 TVEDDVAFG---MENQGIPrEEMIKRVDealLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515953848 172 VVKQIFQTLRELA-RNGMTIFLVEQNAHHALKlSDRGYVMVNGQI 215
Cdd:PRK13642 175 GRQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-234 |
3.01e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.54 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVA--TGGIAQapegRRIF 92
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVArrIGLLAQ----NATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 93 P-DMSVEENLLMGTIPvgnqhaaedMQSMFDLFPRLKERRNQRAM--------------TLSGGEQQMLAIARALMSRPK 157
Cdd:PRK10253 93 PgDITVQELVARGRYP---------HQPLFTRWRKEDEEAVTKAMqatgithladqsvdTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515953848 158 LLLLDEPSLGLAPIVVKQIFQTLRELAR-NGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEVRKAY 234
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELNReKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-164 |
3.30e-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: 60.81 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 18 IQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKS---THYVATGGIAQAPEGRRIFpD 94
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSfeaTRSRNRYSVAYAAQKPWLL-N 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953848 95 MSVEENLLMGTiPVGNQH-----AAEDMQSMFDLFPRLKERR-NQRAMTLSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:cd03290 93 ATVEENITFGS-PFNKQRykavtDACSLQPDIDLLPFGDQTEiGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
14-196 |
3.59e-11 |
|
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: 60.03 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 14 FYGVIQ-ALKQVSLEVNKGETVALIGANGAGKSTLLMSVFgqprirngqilfcgedishksthyvATGGIAQAPEGRRIF 92
Cdd:cd03238 3 VSGANVhNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL-------------------------YASGKARLISFLPKF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 93 PDMSveenllmgTIPVGNqhaaedMQSMFDL---FPRLkerrNQRAMTLSGGEQQMLAIARALMSRPK--LLLLDEPSLG 167
Cdd:cd03238 58 SRNK--------LIFIDQ------LQFLIDVglgYLTL----GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180
....*....|....*....|....*....
gi 515953848 168 LAPIVVKQIFQTLRELARNGMTIFLVEQN 196
Cdd:cd03238 120 LHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-195 |
3.95e-11 |
|
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: 62.62 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLmSVFGQPRIRNGQILFCGedISHKS----THYVATGGIAQapegrRIFpdms 96
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLL-SALLRLLSTEGEIQIDG--VSWNSvtlqTWRKAFGVIPQ-----KVF---- 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 97 veenLLMGTIPVG----NQHAAED---------MQSMFDLFP-RLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLD 162
Cdd:TIGR01271 1303 ----IFSGTFRKNldpyEQWSDEEiwkvaeevgLKSVIEQFPdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLD 1378
|
170 180 190
....*....|....*....|....*....|...
gi 515953848 163 EPSLGLAPIVVKQIFQTLRELARNgMTIFLVEQ 195
Cdd:TIGR01271 1379 EPSAHLDPVTLQIIRKTLKQSFSN-CTVILSEH 1410
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-227 |
4.91e-11 |
|
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: 61.02 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFgqprirngQILFCGEDISHKSTHYVATggiaQAPEGRRIFPDMSVEEN 100
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFL--------RLLNTEGDIQIDGVSWNSV----PLQKWRKAFGVIPQKVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 101 LLMGTI-----PVGnQHAAED---------MQSMFDLFP-RLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:cd03289 88 IFSGTFrknldPYG-KWSDEEiwkvaeevgLKSVIEQFPgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515953848 166 LGLAPIVVKQIFQTLRElARNGMTIFLVEQNAHHALKlSDRGYVMVNGQIRLSGSGEALLKD 227
Cdd:cd03289 167 AHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-164 |
6.53e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 61.13 E-value: 6.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 1 MSEPMLQFQDVDVFYGV----------IQALKQVSLEVNKGETVALIGANGAGKSTL--LMSVFGQPRirNGQILFCGED 68
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVkrglfkperlVKALDGVSFTLERGKTLAVVGESGCGKSTLarLLTMIETPT--GGELYYQGQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 69 ISHKSTHYVAT-----GGIAQAPEG----RRIFPDMsVEENLLMGTipvgNQHAAE------DMQSMFDLFPrlkERRNQ 133
Cdd:PRK11308 79 LLKADPEAQKLlrqkiQIVFQNPYGslnpRKKVGQI-LEEPLLINT----SLSAAErrekalAMMAKVGLRP---EHYDR 150
|
170 180 190
....*....|....*....|....*....|.
gi 515953848 134 RAMTLSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:PRK11308 151 YPHMFSGGQRQRIAIARALMLDPDVVVADEP 181
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-227 |
9.04e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.29 E-value: 9.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGqilfcgedishksTHYVATGGIAQAPEGRRIFpDMSVEEN 100
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD-------------ASVVIRGTVAYVPQVSWIF-NATVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 101 LLMGTI--PVGNQHAAE--DMQSMFDLFP--RLKERrNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVK 174
Cdd:PLN03130 699 ILFGSPfdPERYERAIDvtALQHDLDLLPggDLTEI-GERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGR 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515953848 175 QIFQTLRELARNGMTIFLVeQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKD 227
Cdd:PLN03130 778 QVFDKCIKDELRGKTRVLV-TNQLHFLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-200 |
1.04e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.80 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 3 EPMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFG-QPR-IRNGQILF-----CGEDISHKSTH 75
Cdd:PRK10938 258 EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdHPQgYSNDLTLFgrrrgSGETIWDIKKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 76 --YVATggiaQAPEGRRIfpDMSVEENLLMGTI-PVGNQHAAEDMQSM-----FDLFPRLKERRNQRAMTLSGGEQQMLA 147
Cdd:PRK10938 338 igYVSS----SLHLDYRV--STSVRNVILSGFFdSIGIYQAVSDRQQKlaqqwLDILGIDKRTADAPFHSLSWGQQRLAL 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515953848 148 IARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMT--IFLveqnAHHA 200
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqlLFV----SHHA 462
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-225 |
1.53e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.76 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDishksthyVATGGI 82
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCD--------VAKFGL 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 83 AQAPEGRRIFPDMSVeenLLMGTI-----PVGNQHAAEDMQSMFDLFPRLKERRNQRAM---------TLSGGEQQMLAI 148
Cdd:PLN03232 1306 TDLRRVLSIIPQSPV---LFSGTVrfnidPFSEHNDADLWEALERAHIKDVIDRNPFGLdaevseggeNFSVGQRQLLSL 1382
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515953848 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNgMTIFLVEQNAHHALKlSDRGYVMVNGQIRLSGSGEALL 225
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS-CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELL 1457
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-225 |
2.36e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.03 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTL--LMSVFGQprIRNGQILFCGEDIS----------- 70
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIanLLTRFYD--IDEGEILLDGHDLRdytlaslrnqv 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 71 -------HKSTHYVATgGIAQAPEGRriFPDMSVEEnllmgtipvgnqhAAEDMQSMfDLFPRLKERRN----QRAMTLS 139
Cdd:PRK11176 420 alvsqnvHLFNDTIAN-NIAYARTEQ--YSREQIEE-------------AARMAYAM-DFINKMDNGLDtvigENGVLLS 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 140 GGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLveqnAHH--ALKLSDRGYVMVNGQIRL 217
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVI----AHRlsTIEKADEILVVEDGEIVE 558
|
....*...
gi 515953848 218 SGSGEALL 225
Cdd:PRK11176 559 RGTHAELL 566
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-220 |
2.80e-10 |
|
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: 59.10 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQilfcgedISHksthyvaTGGIAQAPEGRRIFPDmSVEEN 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGK-------IKH-------SGRISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 101 LLMGTIPVGNQH----AAEDMQSMFDLFPrlkERRN----QRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIV 172
Cdd:cd03291 118 IIFGVSYDEYRYksvvKACQLEEDITKFP---EKDNtvlgEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515953848 173 VKQIFQT-LRELARNGMTIFLVEQNAHhaLKLSDRGYVMVNGQIRLSGS 220
Cdd:cd03291 195 EKEIFEScVCKLMANKTRILVTSKMEH--LKKADKILILHEGSSYFYGT 241
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-225 |
3.00e-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: 59.96 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGqilfcgedishkstHYVATGGIAQAPEGRRIFPDmSVEEN 100
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG--------------HVHMKGSVAYVPQQAWIQND-SLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 101 LLMGTiPVGNQHAAEDMQSMfDLFPRL-------KERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVV 173
Cdd:TIGR00957 719 ILFGK-ALNEKYYQQVLEAC-ALLPDLeilpsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515953848 174 KQIFQTL--RELARNGMTIFLVEQNAHHaLKLSDRGYVMVNGQIRLSGSGEALL 225
Cdd:TIGR00957 797 KHIFEHVigPEGVLKNKTRILVTHGISY-LPQVDVIIVMSGGKISEMGSYQELL 849
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-225 |
4.03e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 59.35 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKStHYVATGGIAQAPEGRRIFPDmSVEEN 100
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAMVQQDPVVLAD-TFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 101 LLMGTiPVGNQHA---------AEDMQSMFD-LFPRLKERRNqramTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAP 170
Cdd:PRK10790 435 VTLGR-DISEEQVwqaletvqlAELARSLPDgLYTPLGEQGN----NLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515953848 171 IVVKQIFQTLRELaRNGMTIFLVeqnAHHALKLSDRGYVMV--NGQIRLSGSGEALL 225
Cdd:PRK10790 510 GTEQAIQQALAAV-REHTTLVVI---AHRLSTIVEADTILVlhRGQAVEQGTHQQLL 562
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-228 |
4.77e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.96 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISH------KSTHYVatggIAQAPegrRIFP 93
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqldswRSRLAV----VSQTP---FLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 94 DmSVEENLLMGTiPVGNQHAAED---MQSMFDLFPRLKE----RRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:PRK10789 403 D-TVANNIALGR-PDATQQEIEHvarLASVHDDILRLPQgydtEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515953848 167 GLAPIVVKQIFQTLRELaRNGMTIFLveqNAHH--ALKLSDRGYVMVNGQIRLSGSGEALLKDP 228
Cdd:PRK10789 481 AVDGRTEHQILHNLRQW-GEGRTVII---SAHRlsALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
10-190 |
6.17e-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: 56.87 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 10 DVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLmSVFGQPR---IRNGQILFCGEDIshKSTHYVATGGIAQAP 86
Cdd:cd03232 12 TVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLL-DVLAGRKtagVITGEILINGRPL--DKNFQRSTGYVEQQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 87 egrrIFPDMS-VEENLLMgtipvgnqHAAedmqsmfdlfprLKErrnqramtLSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:cd03232 89 ----VHSPNLtVREALRF--------SAL------------LRG--------LSVEQRKRLTIGVELAAKPSILFLDEPT 136
|
170 180
....*....|....*....|....*
gi 515953848 166 LGLAPIVVKQIFQTLRELARNGMTI 190
Cdd:cd03232 137 SGLDSQAAYNIVRFLKKLADSGQAI 161
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-182 |
1.48e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.83 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDIShksthyvaTGGIAQAPEGRRIFPDMSVeen 100
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS--------KFGLMDLRKVLGIIPQAPV--- 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 101 LLMGTIPVG----NQHAAEDMQSMFDLfPRLKE--RRNQRAM---------TLSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:PLN03130 1324 LFSGTVRFNldpfNEHNDADLWESLER-AHLKDviRRNSLGLdaevseageNFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180
....*....|....*....|
gi 515953848 166 lglAPIVVKQ---IFQTLRE 182
Cdd:PLN03130 1403 ---AAVDVRTdalIQKTIRE 1419
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-229 |
1.74e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.17 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 2 SEPMLQFQDVDVFYGV-----------IQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDIS 70
Cdd:PRK10261 310 GEPILQVRNLVTRFPLrsgllnrvtreVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRID 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 71 HKSThyvatggiAQAPEGRR----IFPD------------MSVEENLLMGTIPVGNQhAAEDMQSMFDLFPRLKERRNQR 134
Cdd:PRK10261 390 TLSP--------GKLQALRRdiqfIFQDpyasldprqtvgDSIMEPLRVHGLLPGKA-AAARVAWLLERVGLLPEHAWRY 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 135 AMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAHHALKLSDRGYVMVNG 213
Cdd:PRK10261 461 PHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLG 540
|
250
....*....|....*.
gi 515953848 214 QIRLSGSGEALLKDPE 229
Cdd:PRK10261 541 QIVEIGPRRAVFENPQ 556
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-193 |
1.78e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.12 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDIShksthyvatggiaqapegrrIFPDMSVEEN 100
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ--------------------FGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 101 LLmgtiPVGNQHAAEDMQSM------FDLFPRLKErrnqramtLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVK 174
Cdd:COG2401 106 IG----RKGDFKDAVELLNAvglsdaVLWLRRFKE--------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170
....*....|....*....
gi 515953848 175 QIFQTLRELARNGMTIFLV 193
Cdd:COG2401 174 RVARNLQKLARRAGITLVV 192
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-164 |
1.78e-09 |
|
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: 57.25 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLmsvfgqpRIRNG-QILFCGEDISHKSthyVATGGIAQAPEgrrIFPDMSVEE 99
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLL-------RIMAGvDKDFNGEARPQPG---IKVGYLPQEPQ---LDPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 100 NLLMGTIP----------VGNQHAAED--MQSMFDLFPRLKE-----------RRNQRAM-------------TLSGGEQ 143
Cdd:TIGR03719 88 NVEEGVAEikdaldrfneISAKYAEPDadFDKLAAEQAELQEiidaadawdldSQLEIAMdalrcppwdadvtKLSGGER 167
|
170 180
....*....|....*....|.
gi 515953848 144 QMLAIARALMSRPKLLLLDEP 164
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEP 188
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-183 |
2.10e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.02 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 2 SEPMLQFQDVDVFYGVIQ-----------ALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRnGQILFCGEDIS 70
Cdd:PRK15134 272 ASPLLDVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLH 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 71 HKSTHyvatggiAQAPEGRRI---FPDMSVEENLLMGTIpvgnQHAAEDMQSMF-DLFPRLKERRNQRAMT--------- 137
Cdd:PRK15134 351 NLNRR-------QLLPVRHRIqvvFQDPNSSLNPRLNVL----QIIEEGLRVHQpTLSAAQREQQVIAVMEevgldpetr 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515953848 138 ------LSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLREL 183
Cdd:PRK15134 420 hrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSL 471
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-232 |
2.11e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.90 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQ-ALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDIShksthyvatggiAQ 84
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT------------AE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 85 APEGRR-----IFPDMSVEENLLmgtipvGNQHAAEDMQSMFDLFPRLK-----ERRNQRAMT--LSGGEQQMLAIARAL 152
Cdd:PRK10522 391 QPEDYRklfsaVFTDFHLFDQLL------GPEGKPANPALVEKWLERLKmahklELEDGRISNlkLSKGQKKRLALLLAL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFLVEQNAH---HAlklsDRGYVMVNGQIR-LSGSGEALLKD 227
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmGKTIFAISHDDHyfiHA----DRLLEMRNGQLSeLTGEERDAASR 540
|
....*
gi 515953848 228 PEVRK 232
Cdd:PRK10522 541 DAVAR 545
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-164 |
2.42e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGE------------DISHKSTHYVAtGGIAQAPEG 88
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlivarlqqdpprNVEGTVYDFVA-EGIEEQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 89 RRIFPDMSV-------EENLlmgtipvgNQHAAedMQSMFD------LFPRLKERRNQRAMT-------LSGGEQQMLAI 148
Cdd:PRK11147 98 LKRYHDISHlvetdpsEKNL--------NELAK--LQEQLDhhnlwqLENRINEVLAQLGLDpdaalssLSGGWLRKAAL 167
|
170
....*....|....*.
gi 515953848 149 ARALMSRPKLLLLDEP 164
Cdd:PRK11147 168 GRALVSNPDVLLLDEP 183
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-190 |
3.01e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.81 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 31 GETVALIGANGAGKSTLLMSVFGQPRIRN--GQILFCGEDISH---KSTHYVATGGIaqapegrrIFPDMSVEENLLMGT 105
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKqilKRTGFVTQDDI--------LYPHLTVRETLVFCS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 106 I-----PVGNQHAAEDMQSMFDLFPRLKERR----NQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQI 176
Cdd:PLN03211 166 LlrlpkSLTKQEKILVAESVISELGLTKCENtiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170
....*....|....
gi 515953848 177 FQTLRELARNGMTI 190
Cdd:PLN03211 246 VLTLGSLAQKGKTI 259
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-211 |
5.43e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 27 EVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFcGEDISHKsthyvatggiaqaPEGRRIFPDMSVEENLLMGTI 106
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-ELKISYK-------------PQYIKPDYDGTVEDLLRSITD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 107 PVGNQHAAEDMQSMFDLfPRLKERRnqrAMTLSGGEQQMLAIARALMSRPKLLLLDEPSlglAPIVVKQ---IFQTLREL 183
Cdd:PRK13409 427 DLGSSYYKSEIIKPLQL-ERLLDKN---VKDLSGGELQRVAIAACLSRDADLYLLDEPS---AHLDVEQrlaVAKAIRRI 499
|
170 180 190
....*....|....*....|....*....|...
gi 515953848 184 ARN-GMTIFLVEqnahHALK----LSDRgyVMV 211
Cdd:PRK13409 500 AEErEATALVVD----HDIYmidyISDR--LMV 526
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-163 |
9.08e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.34 E-value: 9.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATgGIA 83
Cdd:TIGR00957 1285 VEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF-KIT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 QAPEGRRIFPDmsveeNLLMGTIPVGnQHAAEDMQSMFDL---------FP-RLKERRNQRAMTLSGGEQQMLAIARALM 153
Cdd:TIGR00957 1364 IIPQDPVLFSG-----SLRMNLDPFS-QYSDEEVWWALELahlktfvsaLPdKLDHECAEGGENLSVGQRQLVCLARALL 1437
|
170
....*....|
gi 515953848 154 SRPKLLLLDE 163
Cdd:TIGR00957 1438 RKTKILVLDE 1447
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-227 |
1.40e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 25 SLEVNKGETVALIGANGAGKSTLLMSVFGQprirngQILFCGEDISHksTHYVATGGIAQ-----APEGRRIFPDM---- 95
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGE------LPLLSGERQSQ--FSHITRLSFEQlqklvSDEWQRNNTDMlspg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 96 ------SVEENLLMGtipVGNQHAAEDMQSMFDLFPRLkerrNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:PRK10938 95 eddtgrTTAEIIQDE---VKDPARCEQLAQQFGITALL----DRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515953848 170 PIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKD 227
Cdd:PRK10938 168 VASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-211 |
1.70e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.41 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 27 EVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFcGEDISHKsthyvatggiaqaPEGRRIFPDMSVEENLlmgti 106
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-DLKISYK-------------PQYISPDYDGTVEEFL----- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 107 pvgNQHAAEDMQSMF---DLFPRLKERR--NQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSlglAPIVVKQIFQT-- 179
Cdd:COG1245 423 ---RSANTDDFGSSYyktEIIKPLGLEKllDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS---AHLDVEQRLAVak 496
|
170 180 190
....*....|....*....|....*....|....*...
gi 515953848 180 -LRELARN-GMTIFLVEqnahHALKL----SDRgyVMV 211
Cdd:COG1245 497 aIRRFAENrGKTAMVVD----HDIYLidyiSDR--LMV 528
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-228 |
3.15e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILfcgediSHKSTHYVATGG-IAQAP-EGRRIFPDmsvE 98
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW------AERSIAYVPQQAwIMNATvRGNILFFD---E 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 99 ENL--LMGTIPVGNQHAaeDMQSmfdLFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQI 176
Cdd:PTZ00243 747 EDAarLADAVRVSQLEA--DLAQ---LGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERV 821
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515953848 177 FQTLRELARNGMTIFLVEQNAhHALKLSDRGYVMVNGQIRLSGSGEALLKDP 228
Cdd:PTZ00243 822 VEECFLGALAGKTRVLATHQV-HVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
21-194 |
3.16e-08 |
|
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: 52.26 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVF---GQPRIRNGQILFCGEDISHKSTHYVatggiaQAPEGrrIFPDMSV 97
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIyaeGQRRYVESLSAYARQFLGQMDKPDV------DSIEG--LSPAIAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 98 EENLL-------MGTIpvgnqhaAEDMQSMFDLFPR--LKERRNQ-------------RAMTLSGGEQQMLAIARALMSR 155
Cdd:cd03270 83 DQKTTsrnprstVGTV-------TEIYDYLRLLFARvgIRERLGFlvdvglgyltlsrSAPTLSGGEAQRIRLATQIGSG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515953848 156 PK--LLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVE 194
Cdd:cd03270 156 LTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVE 196
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-234 |
3.43e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 52.87 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATgGIAQAPEGRRIFPDMSVEEN 100
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR-KVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 101 LLMGTIP---------VGNQHAAEDMQSMFDLFP---RLKErrnqramTLSGGEQQMLAIARALMSRPKLLLLDEPS--L 166
Cdd:PRK10575 106 VAIGRYPwhgalgrfgAADREKVEEAISLVGLKPlahRLVD-------SLSGGERQRAWIAMLVAQDSRCLLLDEPTsaL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515953848 167 GLAPIV-VKQIFQTLRElaRNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEALLKDPEVRKAY 234
Cdd:PRK10575 179 DIAHQVdVLALVHRLSQ--ERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
133-224 |
4.41e-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: 53.09 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 133 QRAMTLSGGEQQMLAIARALMSR---PKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQN------AHHALKL 203
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNldviktADYIIDL 904
|
90 100
....*....|....*....|....*
gi 515953848 204 ----SDRGyvmvnGQIRLSGSGEAL 224
Cdd:TIGR00630 905 gpegGDGG-----GTVVASGTPEEV 924
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-210 |
6.21e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.91 E-value: 6.21e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515953848 137 TLSGGEQQMLAIARALMS---RPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAhHALKLSDrgYVM 210
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVAD--YVL 882
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
132-237 |
1.33e-07 |
|
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: 51.94 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 132 NQRAMTLSGGEQQMLAIARALMSRPK--LLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNaHHALKLSDR--- 206
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD-EDTIRAADYvid 561
|
90 100 110
....*....|....*....|....*....|....*
gi 515953848 207 ---GYVMVNGQIRLSGSGEALLKDPE-VRKAYLGG 237
Cdd:TIGR00630 562 igpGAGEHGGEVVASGTPEEILANPDsLTGQYLSG 596
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
21-164 |
1.48e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQIlfcgedishKSTHYVATGGIAQAPEgrrifPDMSVEEN 100
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV---------KWSENANIGYYAQDHA-----YDFENDLT 400
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953848 101 LL--MGtipvgnQHAAE--DMQSMFDLFPRL---KERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:PRK15064 401 LFdwMS------QWRQEgdDEQAVRGTLGRLlfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
94-198 |
1.64e-07 |
|
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: 50.69 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 94 DMSVEENL-LMGTIPvgnqHAAEDMQSMFDL---FPRLkerrNQRAMTLSGGEQQMLAIARALMSR---PKLLLLDEPSL 166
Cdd:cd03271 130 DMTVEEALeFFENIP----KIARKLQTLCDVglgYIKL----GQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTT 201
|
90 100 110
....*....|....*....|....*....|..
gi 515953848 167 GLAPIVVKQIFQTLRELARNGMTIFLVEQNAH 198
Cdd:cd03271 202 GLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLD 233
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-226 |
2.33e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.98 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 133 QRAM-TLSGGEQQMLAIARALMSRPK--LLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNaHHALKLSDR--- 206
Cdd:PRK00635 471 ERALaTLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRiid 549
|
90 100
....*....|....*....|...
gi 515953848 207 ---GYVMVNGQIRLSGSGEALLK 226
Cdd:PRK00635 550 igpGAGIFGGEVLFNGSPREFLA 572
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-192 |
4.37e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.12 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 20 ALKQVSLEVNKGETVALIGANGAGKST-------LL------MSVFGQPrirngqilfcgedishksthyVATGGIAQAp 86
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLpasegeAWLFGQP---------------------VDAGDIATR- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 87 egRRI---------FPDMSVEENLLMgtipvgnqHA----------AEDMQSMFDLFpRLKERRNQRAMTLSGGEQQMLA 147
Cdd:NF033858 339 --RRVgymsqafslYGELTVRQNLEL--------HArlfhlpaaeiAARVAEMLERF-DLADVADALPDSLPLGIRQRLS 407
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515953848 148 IARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARN-GMTIFL 192
Cdd:NF033858 408 LAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREdGVTIFI 453
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-215 |
6.07e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQP----RIRNGQILFCGEDISHKSTHYvaTGGIAQAPEGRRIFPD 94
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGITPEEIKKHY--RGDVVYNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 95 MSVEENLlmgtipvgnQHAA--EDMQSMFDLFPRLKERRNQRAMTL---------------------SGGEQQMLAIARA 151
Cdd:TIGR00956 153 LTVGETL---------DFAArcKTPQNRPDGVSREEYAKHIADVYMatyglshtrntkvgndfvrgvSGGERKRVSIAEA 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953848 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVE--QNAHHALKLSDRGYVMVNGQI 215
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQ 289
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-222 |
9.33e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.25 E-value: 9.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQP--RIRNGQILFCGEDISHKSTHYVATGGI 82
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 83 AQAPEGRRIFPDMSvEENLLMGTIPVGNQHAAEDMQSMFDLFPRLKERRNQRAMT-----------LSGGEQQMLAIARA 151
Cdd:PRK09580 81 FMAFQYPVEIPGVS-NQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPedlltrsvnvgFSGGEKKRNDILQM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953848 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELaRNGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGE 222
Cdd:PRK09580 160 AVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGD 229
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
6-229 |
1.43e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDIshksthyvatgGIA 83
Cdd:PTZ00243 1309 LVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI-----------GAY 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 84 QAPEGRRIFPDMSVEENLLMGTI-----PVGNQHAAEdMQSMFDLFPrLKERRNQR-----AMTLSG------GEQQMLA 147
Cdd:PTZ00243 1378 GLRELRRQFSMIPQDPVLFDGTVrqnvdPFLEASSAE-VWAALELVG-LRERVASEsegidSRVLEGgsnysvGQRQLMC 1455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 148 IARALMSR-PKLLLLDEPSLGLAPIVVKQIFQTLRElARNGMTIFLVeqnAH--HALKLSDRGYVMVNGQIRLSGSGEAL 224
Cdd:PTZ00243 1456 MARALLKKgSGFILMDEATANIDPALDRQIQATVMS-AFSAYTVITI---AHrlHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
....*
gi 515953848 225 LKDPE 229
Cdd:PTZ00243 1532 VMNRQ 1536
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-193 |
3.61e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.19 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQIlfcgeDISHKSTHYVATGGIAQAPEGRRifpdmSVE- 98
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALIAISSGLNGQLTGIE-----NIEl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 99 ENLLMGtipVGNQHAAEDMQSMFDlFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEP-SLGlAPIVVKQIF 177
Cdd:PRK13545 109 KGLMMG---LTKEKIKEIIPEIIE-FADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAlSVG-DQTFTKKCL 183
|
170
....*....|....*.
gi 515953848 178 QTLRELARNGMTIFLV 193
Cdd:PRK13545 184 DKMNEFKEQGKTIFFI 199
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-164 |
4.01e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 19 QALKQVSLEVNKGETVALIGANGAGKSTLLmsvfgqpRIRNGqiL---FCGEDISHKSthyvATGGI-AQAPEgrrIFPD 94
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLL-------RIMAG--VdkeFEGEARPAPG----IKVGYlPQEPQ---LDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 95 MSVEENLLMGtipVGNQHAA---------------EDMQSMFDLFPRLKE-----------RRNQRAM------------ 136
Cdd:PRK11819 85 KTVRENVEEG---VAEVKAAldrfneiyaayaepdADFDALAAEQGELQEiidaadawdldSQLEIAMdalrcppwdakv 161
|
170 180
....*....|....*....|....*....
gi 515953848 137 -TLSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:PRK11819 162 tKLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
137-212 |
6.25e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 6.25e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515953848 137 TLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELA-RNGMTIFLVeqnAHH--ALKLSDRGYVMVN 212
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITI---AHRiaSIKRSDKIVVFNN 1433
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-180 |
6.48e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 4 PMLQFQDVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGE-DISHKSTHYVATGG 81
Cdd:PLN03073 507 PIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvRMAVFSQHHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 IAQAP--EGRRIFPdmSVEENLL---MGTIPVGNQHAaedMQSMFdlfprlkerrnqramTLSGGEQQMLAIARALMSRP 156
Cdd:PLN03073 587 LSSNPllYMMRCFP--GVPEQKLrahLGSFGVTGNLA---LQPMY---------------TLSGGQKSRVAFAKITFKKP 646
|
170 180
....*....|....*....|....
gi 515953848 157 KLLLLDEPSLGLAPIVVKQIFQTL 180
Cdd:PLN03073 647 HILLLDEPSNHLDLDAVEALIQGL 670
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-194 |
8.97e-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: 45.93 E-value: 8.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 30 KGETVALIGANGAGKST-------LLMSVFGQP-----------------------RIRNGQIlfcgeDISHKSTHyvat 79
Cdd:COG1245 98 KGKVTGILGPNGIGKSTalkilsgELKPNLGDYdeepswdevlkrfrgtelqdyfkKLANGEI-----KVAHKPQY---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 80 ggIAQAPegrRIFpDMSVEEnLLMGTIPVGnqhAAEDMQSMFDLFPRLkerrNQRAMTLSGGEQQMLAIARALMSRPKLL 159
Cdd:COG1245 169 --VDLIP---KVF-KGTVRE-LLEKVDERG---KLDELAEKLGLENIL----DRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515953848 160 LLDEPSLGLapivvkQIFQ------TLRELARNGMTIFLVE 194
Cdd:COG1245 235 FFDEPSSYL------DIYQrlnvarLIRELAEEGKYVLVVE 269
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-163 |
1.08e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.86 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 38 GANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVATGGiaqapEGRRIFPDMSVEENLLMGTipvGNQHAAEDM 117
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIG-----HNLGLKLEMTVFENLKFWS---EIYNSAETL 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 515953848 118 QSMFDLFpRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:PRK13541 105 YAAIHYF-KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
21-192 |
1.60e-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: 44.99 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 21 LKQVSLEVNKGETVaLIGANGAGKSTLLMS---VFGQPRIRNGQI--LFCGEDISHKSTHYVAT-----GGIAQAPEGRR 90
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEAlrlLLGPSSSRKFDEedFYLGDDPDLPEIEIELTfgsllSRLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 91 IFPDMSVEENLLMGTIPVGNQHAAEDMQSMF---------DLFPRLKERRNQRAMT--------------LSGGEQQMLA 147
Cdd:COG3593 93 DKEELEEALEELNEELKEALKALNELLSEYLkelldgldlELELSLDELEDLLKSLslriedgkelpldrLGSGFQRLIL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515953848 148 IA--RALM-----SRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFL 192
Cdd:COG3593 173 LAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVII 224
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-195 |
1.68e-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: 45.51 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 17 VIQALkqvSLEVNKGETVALIGANGAGKSTL------LMSVFGqPRI---RNGQILFcgedishksthyvatggIAQAPE 87
Cdd:TIGR00954 467 LIESL---SFEVPSGNNLLICGPNGCGKSSLfrilgeLWPVYG-GRLtkpAKGKLFY-----------------VPQRPY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 88 -GRR------IFPDmSVEENLLMGtipVGNQHAaEDMQSMFDLFPRLKERRNQRAM-----TLSGGEQQMLAIARALMSR 155
Cdd:TIGR00954 526 mTLGtlrdqiIYPD-SSEDMKRRG---LSDKDL-EQILDNVQLTHILEREGGWSAVqdwmdVLSGGEKQRIAMARLFYHK 600
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515953848 156 PKLLLLDEPSLGLAPIVVKQIFQTLRELarnGMTIFLVEQ 195
Cdd:TIGR00954 601 PQFAILDECTSAVSVDVEGYMYRLCREF---GITLFSVSH 637
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-165 |
1.72e-05 |
|
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: 45.31 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFcGEDishksthyVATGGIAQA 85
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GET--------VKLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 86 PEGrrIFPDMSVEENLLMGT--IPVGNQhaaeDMQS--MFDLFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLL 161
Cdd:TIGR03719 394 RDA--LDPNKTVWEEISGGLdiIKLGKR----EIPSraYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
....
gi 515953848 162 DEPS 165
Cdd:TIGR03719 468 DEPT 471
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
18-62 |
3.45e-05 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 44.15 E-value: 3.45e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 515953848 18 IQALKQVsleVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQI 62
Cdd:PRK01889 185 LDVLAAW---LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
135-228 |
4.25e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.25 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 135 AMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAHHALKLSDRGYVMVNGQ 214
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSNRE 656
|
90
....*....|....
gi 515953848 215 IRLSGSGEALLKDP 228
Cdd:PTZ00265 657 RGSTVDVDIIGEDP 670
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
133-196 |
9.79e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.09 E-value: 9.79e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515953848 133 QRAMTLSGGEQQMLAIARALMSRPK---LLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQN 196
Cdd:COG0178 822 QPATTLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHN 888
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-165 |
1.02e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 4 PMLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQI-LFCGEDISHKSTHYVATggi 82
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEF--- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 83 aqapegrrifpdMSVEENLLMGTIPVGNQHAAEDMQSMFDLFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLD 162
Cdd:PRK10636 388 ------------LRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
...
gi 515953848 163 EPS 165
Cdd:PRK10636 456 EPT 458
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
94-196 |
1.08e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 94 DMSVEEnllmgtipvgnqhAAEdmqsMFDLFPRLKERRN-------------QRAMTLSGGEQQMLAIARALMSRPK--- 157
Cdd:PRK00349 791 DMTVEE-------------ALE----FFEAIPKIARKLQtlvdvglgyiklgQPATTLSGGEAQRVKLAKELSKRSTgkt 853
|
90 100 110
....*....|....*....|....*....|....*....
gi 515953848 158 LLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQN 196
Cdd:PRK00349 854 LYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHN 892
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
6-211 |
1.08e-04 |
|
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: 42.20 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 6 LQFQDVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGEDISHKSTHYVAT--GG 81
Cdd:cd03288 20 IKIHDLCVRYenNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSrlSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 IAQAP---EGRRIF---PDMSVEENLLMGTIPVGNqhaaedMQSMFDLFP-RLKERRNQRAMTLSGGEQQMLAIARALMS 154
Cdd:cd03288 100 ILQDPilfSGSIRFnldPECKCTDDRLWEALEIAQ------LKNMVKSLPgGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515953848 155 RPKLLLLDEPSLGLaPIVVKQIFQTLRELARNGMTIFLVEQNAHHALklsDRGYVMV 211
Cdd:cd03288 174 KSSILIMDEATASI-DMATENILQKVVMTAFADRTVVTIAHRVSTIL---DADLVLV 226
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-165 |
1.08e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 5 MLQFQDVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSVFGQPRIRNGQILFCGE---DISHKSTHYVATGG 81
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlAWVNQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 82 IAQAPEGRRIFPDMSVEenlLMGTIPVGNQHAAEDMQSMFD-------------LFPRL---KERRNQRAMTLSGGEQQM 145
Cdd:PRK10636 81 LEYVIDGDREYRQLEAQ---LHDANERNDGHAIATIHGKLDaidawtirsraasLLHGLgfsNEQLERPVSDFSGGWRMR 157
|
170 180
....*....|....*....|
gi 515953848 146 LAIARALMSRPKLLLLDEPS 165
Cdd:PRK10636 158 LNLAQALICRSDLLLLDEPT 177
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-190 |
2.45e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.02 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 19 QALKQVSLEVNKGETVALIGANGAGKSTLL--------MSVF-GQPRIRNGQILfcgeDIS-HKSTHYVATGGIAqapeg 88
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLnvlaervtTGVItGGDRLVNGRPL----DSSfQRSIGYVQQQDLH----- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 89 rriFPDMSVEENL-----LMGTIPVGNQHAAEDMQSMFDLfprLKERRNQRAMTLSGGE------QQMLAIARALMSRPK 157
Cdd:TIGR00956 848 ---LPTSTVRESLrfsayLRQPKSVSKSEKMEYVEEVIKL---LEMESYADAVVGVPGEglnveqRKRLTIGVELVAKPK 921
|
170 180 190
....*....|....*....|....*....|....
gi 515953848 158 LLL-LDEPSLGLAPIVVKQIFQTLRELARNGMTI 190
Cdd:TIGR00956 922 LLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAI 955
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-194 |
3.77e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.33 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 30 KGETVALIGANGAGKST-------LLMSVFGQP-----------------------RIRNGQIlfcgeDISHKsTHYVAt 79
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTavkilsgELIPNLGDYeeepswdevlkrfrgtelqnyfkKLYNGEI-----KVVHK-PQYVD- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 80 ggiaQAPegrRIFpDMSVEEnLLMGTIPVGnqhAAEDMQSMFDLFPRLkerrNQRAMTLSGGEQQMLAIARALMSRPKLL 159
Cdd:PRK13409 171 ----LIP---KVF-KGKVRE-LLKKVDERG---KLDEVVERLGLENIL----DRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190
....*....|....*....|....*....|....*...
gi 515953848 160 LLDEPSLGLApivVKQ---IFQTLRELARNgMTIFLVE 194
Cdd:PRK13409 235 FFDEPTSYLD---IRQrlnVARLIRELAEG-KYVLVVE 268
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-209 |
4.75e-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: 39.86 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 27 EVNKGETVALIGANGAGKSTLLmsvfgqpRIRNGQILFCGEDIShksthyvatggiaqapegrrifpdmsveenllmgti 106
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAV-------KILAGQLIPNGDNDE------------------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 107 pvgnqhaaedmqsmfdlFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSlglAPIVVKQIFQTLRELAR- 185
Cdd:cd03222 58 -----------------WDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPS---AYLDIEQRLNAARAIRRl 117
|
170 180
....*....|....*....|....*..
gi 515953848 186 ---NGMTIFLVEQNAHHALKLSDRGYV 209
Cdd:cd03222 118 seeGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
138-194 |
8.05e-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: 39.66 E-value: 8.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 138 LSGGEQQMLAIARALMSRPKLLLLDEPSLGLApivVKQIF---QTLRELARNGMTIFLVE 194
Cdd:cd03236 140 LSGGELQRVAIAAALARDADFYFFDEPSSYLD---IKQRLnaaRLIRELAEDDNYVLVVE 196
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
35-194 |
1.11e-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: 38.49 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 35 ALIGANGAGKSTLLmsvfgqprirngqilfcgedishKSTHYVATGgiAQAPEGRRifpdmsveenllmGTIPVGNQHAA 114
Cdd:cd03227 25 IITGPNGSGKSTIL-----------------------DAIGLALGG--AQSATRRR-------------SGVKAGCIVAA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 115 EDMQSMFDLfprlkerrnqraMTLSGGEQQMLAIA-----RALMSRPkLLLLDEPSLGLAPIVVKQIFQTLRELARNGMT 189
Cdd:cd03227 67 VSAELIFTR------------LQLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVKGAQ 133
|
....*
gi 515953848 190 IFLVE 194
Cdd:cd03227 134 VIVIT 138
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
129-165 |
1.22e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.84 E-value: 1.22e-03
10 20 30
....*....|....*....|....*....|....*..
gi 515953848 129 ERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPT 372
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-188 |
1.51e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 37.74 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 30 KGETVALIGANGAGKSTLLMSVFGQ-PRIRNGQILFCGEDISHKsthyvatggiaqapegrrifpdmsveenllmgtipv 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARElGPPGGGVIYIDGEDILEE------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 109 gnqhaaedmqsmfDLFPRLKERRNQRAMTLSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARNGM 188
Cdd:smart00382 45 -------------VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLL 111
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-238 |
5.95e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.50 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953848 133 QRAMTLSGGEQQMLAIARALMSRPK---LLLLDEPSLGLAPIVVKQIFQTLRELARNGMTIFLVEQNAhHALKLSD---- 205
Cdd:PRK00635 1695 QNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDP-ALLKQADylie 1773
|
90 100 110
....*....|....*....|....*....|....*.
gi 515953848 206 --RGYVMVNGQIRLSGSGEAL-LKDPEVRKAYLGGV 238
Cdd:PRK00635 1774 mgPGSGKTGGKILFSGPPKDIsASKDSLLKTYMCNL 1809
|
|
| |
