|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-222 |
1.67e-135 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 379.39 E-value: 1.67e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 1 MD-IIKTENIVKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASL 79
Cdd:COG1136 1 MSpLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 80 AAVRNRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIV 159
Cdd:COG1136 81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2418785902 160 NDPSILLADEPTGNLDSQSGGDILEIFTELH-SQGNTVIIVTHDQAIASRAERIIKIKDGKIVD 222
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-220 |
9.83e-118 |
|
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: 334.07 E-value: 9.83e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVR 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPS 163
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 164 ILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHDQAIASRAERIIKIKDGKI 220
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-222 |
1.44e-92 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 270.77 E-value: 1.44e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGKikvRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAV 82
Cdd:COG2884 1 MIRFENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RnRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDP 162
Cdd:COG2884 78 R-RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 163 SILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASRAE-RIIKIKDGKIVD 222
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPkRVLELEDGRLVR 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-222 |
2.29e-91 |
|
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: 268.15 E-value: 2.29e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAV 82
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RNRKIGFVFQSFNLLPHLNILKNVELPLMYGGMskRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDP 162
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVMLPLELAGR--RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 163 SILLADEPTGNLDSQSGGDILEIFTELHS-QGNTVIIVTHDQAIASRAERIIKIKDGKIVD 222
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-222 |
1.52e-87 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 258.05 E-value: 1.52e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAV 82
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RNRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDP 162
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 163 SILLADEPTGNLDSQSGGDILEIFTELHSQGNT-VIIVTHDQAIASRAERIIKIKDGKIVD 222
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTsFLVVTHDLELAKKLDRVLEMKDGQLFN 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
7-221 |
2.04e-84 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 263.12 E-value: 2.04e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 7 ENIVKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVRNRK 86
Cdd:PRK10535 8 KDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 87 IGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILL 166
Cdd:PRK10535 88 FGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 167 ADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASRAERIIKIKDGKIV 221
Cdd:PRK10535 168 ADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
3-220 |
8.39e-82 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 243.09 E-value: 8.39e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAV 82
Cdd:NF038007 1 MLNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RNRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDP 162
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 163 SILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASRAERIIKIKDGKI 220
Cdd:NF038007 161 ALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-221 |
9.13e-79 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 236.04 E-value: 9.13e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYilGKIKVraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSkMPKASLAAV 82
Cdd:COG1126 1 MIEIENLHKSF--GDLEV--LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RnRKIGFVFQSFNLLPHLNILKNVELPLMY-GGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVND 161
Cdd:COG1126 76 R-RKVGMVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 162 PSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIV 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-202 |
1.73e-76 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 231.13 E-value: 1.73e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 1 MDIIKTENIVKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKmpkasla 80
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 81 avRNRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVN 160
Cdd:COG1116 78 --PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2418785902 161 DPSILLADEPTGNLDSQS----GGDILEIFTElhsQGNTVIIVTHD 202
Cdd:COG1116 156 DPEVLLMDEPFGALDALTrerlQDELLRLWQE---TGKTVLFVTHD 198
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-221 |
1.20e-73 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 226.50 E-value: 1.20e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAV 82
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RnRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDP 162
Cdd:COG1135 81 R-RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2418785902 163 SILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHD----QAIASraeRIIKIKDGKIV 221
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEmdvvRRICD---RVAVLENGRIV 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
8-222 |
2.72e-73 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 222.38 E-value: 2.72e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 8 NIVKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVRNRKI 87
Cdd:PRK11629 10 NLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 88 GFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLA 167
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2418785902 168 DEPTGNLDSQSGGDILEIFTELH-SQGNTVIIVTHDQAIASRAERIIKIKDGKIVD 222
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-223 |
6.91e-73 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 221.47 E-value: 6.91e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGKikvRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAV 82
Cdd:COG3638 2 MLELRNLSKRYPGGT---PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RnRKIGFVFQSFNLLPHLNILKNV------ELPL---MYGGMSKRKRtAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVA 153
Cdd:COG3638 79 R-RRIGMIFQQFNLVPRLSVLTNVlagrlgRTSTwrsLLGLFPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2418785902 154 IARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHS-QGNTVIIVTHDQAIASR-AERIIKIKDGKIV-DG 223
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDLARRyADRIIGLRDGRVVfDG 229
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-221 |
1.77e-72 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 224.21 E-value: 1.77e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 1 MDIIKTENIVKDYilGKikVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPkasla 80
Cdd:COG3842 3 MPALELENVSKRY--GD--VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 81 aVRNRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVN 160
Cdd:COG3842 74 -PEKRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2418785902 161 DPSILLADEPTGNLDSQS----GGDILEIFTELhsqGNTVIIVTHDQAIA-SRAERIIKIKDGKIV 221
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLreemREELRRLQREL---GITFIYVTHDQEEAlALADRIAVMNDGRIE 215
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-219 |
1.55e-71 |
|
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: 217.12 E-value: 1.55e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGkikVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAV 82
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RnRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDP 162
Cdd:TIGR02673 78 R-RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 163 SILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIKDGK 219
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDlSLVDRVAHRVIILDDGR 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-221 |
1.68e-71 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 221.49 E-value: 1.68e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 1 MDIIKTENIVKDYilGKikVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPkasla 80
Cdd:COG3839 1 MASLELENVSKSY--GG--VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 81 aVRNRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVN 160
Cdd:COG3839 72 -PKDRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2418785902 161 DPSILLADEPTGNLDSQSGGDI-LEIfTELHSQ-GNTVIIVTHDQAIA-SRAERIIKIKDGKIV 221
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEMrAEI-KRLHRRlGTTTIYVTHDQVEAmTLADRIAVMNDGRIQ 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-202 |
7.61e-71 |
|
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: 215.41 E-value: 7.61e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTyylddVLVSKMPKASlaavR 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGE-----VLVDGEPVTG----P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPS 163
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2418785902 164 ILLADEPTGNLDSQS----GGDILEIfteLHSQGNTVIIVTHD 202
Cdd:cd03293 152 VLLLDEPFSALDALTreqlQEELLDI---WRETGKTVLLVTHD 191
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-221 |
9.70e-71 |
|
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: 215.08 E-value: 9.70e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYilGKikVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPkaslaaVR 83
Cdd:cd03259 1 LELKGLSKTY--GS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP------PE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPS 163
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 164 ILLADEPTGNLDSQSGGDILEIFTELH-SQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQrELGITTIYVTHDQEEALAlADRIAVMNEGRIV 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-221 |
2.90e-69 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 212.06 E-value: 2.90e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAV 82
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RnRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDP 162
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 163 SILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHD-QAIASRAERIIKIKDGKIV 221
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEmEVVKRICDRVAVMEKGEVV 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-220 |
1.32e-68 |
|
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: 209.31 E-value: 1.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYilGKIKVraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKmPKASLAAVR 83
Cdd:cd03262 1 IEIKNLHKSF--GDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 nRKIGFVFQSFNLLPHLNILKNVELPLMY-GGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDP 162
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2418785902 163 SILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKI 220
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
21-215 |
8.59e-68 |
|
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: 207.08 E-value: 8.59e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVRNRKIGFVFQSFNLLPHL 100
Cdd:TIGR03608 12 VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQNFALIENE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 NILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGG 180
Cdd:TIGR03608 92 TVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRD 171
|
170 180 190
....*....|....*....|....*....|....*
gi 2418785902 181 DILEIFTELHSQGNTVIIVTHDQAIASRAERIIKI 215
Cdd:TIGR03608 172 EVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-221 |
1.28e-65 |
|
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: 204.03 E-value: 1.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVRNRKIGFVFQSFNLLPHLN 101
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGD 181
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2418785902 182 ILEIFTELHS-QGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:cd03294 199 MQDELLRLQAeLQKTIVFITHDLDEALRlGDRIAIMKDGRLV 240
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
6-220 |
1.73e-65 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 202.32 E-value: 1.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 6 TENIVKDYIL------GKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASL 79
Cdd:PRK10584 3 AENIVEVHHLkksvgqGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 80 AAVRNRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIV 159
Cdd:PRK10584 83 AKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2418785902 160 NDPSILLADEPTGNLDSQSGGDILEIFTEL-HSQGNTVIIVTHDQAIASRAERIIKIKDGKI 220
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-221 |
2.34e-65 |
|
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: 210.14 E-value: 2.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGKIK-VRALNGIDLQIQKGEFVAIMGPSGSGKSTLM-HILGcLDSPTDGTYYLDDVLVSKMPKASLA 80
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGgVRAVDDVSLTLRRGETLGLVGESGSGKSTLArLLLG-LLRPTSGSILFDGKDLTKLSRRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 81 AVRnRKIGFVFQ----SFNllPHLNILKNVELPLM-YGGMSKRKRTAKAKEVLQNVGLGDRLKHK-PGELSGGQRQRVAI 154
Cdd:COG1123 339 ELR-RRVQMVFQdpysSLN--PRMTVGDIIAEPLRlHGLLSRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAI 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2418785902 155 ARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGN-TVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGlTYLFISHDLAVVRYiADRVAVMYDGRIV 484
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-221 |
1.53e-64 |
|
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: 200.21 E-value: 1.53e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYilGKIKVraLNGIDLQIQKGEFVAIMGPSGSGKSTLM-HILGcLDSPTDGTYYLDDVLVSKMPKASLAA 81
Cdd:COG1127 5 MIEVRNLTKSF--GDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLkLIIG-LLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 82 VRnRKIGFVFQSFNLLPHLNILKNVELPL-MYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVN 160
Cdd:COG1127 80 LR-RRIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2418785902 161 DPSILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHD-QAIASRAERIIKIKDGKIV 221
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDlDSAFAIADRVAVLADGKII 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-220 |
6.05e-64 |
|
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: 197.63 E-value: 6.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYILGkikVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVR 83
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 nRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPS 163
Cdd:cd03292 78 -RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 164 ILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASRAE-RIIKIKDGKI 220
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-221 |
1.66e-63 |
|
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: 196.96 E-value: 1.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMpKASLAAV 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKL-SRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RNRKIGFVFQ----SFNllPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLG---DRLKHKPGELSGGQRQRVAIA 155
Cdd:cd03257 80 RRKEIQMVFQdpmsSLN--PRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 156 RAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKiADRVAVMYAGKIV 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-224 |
3.79e-62 |
|
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: 193.70 E-value: 3.79e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYILGKikvRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKmpkASLAAVR 83
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK---KNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 nRKIGFVFQ-SFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDP 162
Cdd:COG1122 75 -RKVGLVFQnPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2418785902 163 SILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIKDGKIV-DGN 224
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDlDLVAELADRVIVLDDGRIVaDGT 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-226 |
6.00e-62 |
|
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: 193.55 E-value: 6.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYILGKikvRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVR 83
Cdd:cd03256 1 IEVENLSKTYPNGK---KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 nRKIGFVFQSFNLLPHLNILKNV------ELPL---MYGGMSKRKRtAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAI 154
Cdd:cd03256 78 -RQIGMIFQQFNLIERLSVLENVlsgrlgRRSTwrsLFGLFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 155 ARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHDQAIASR-AERIIKIKDGKIV-DGNSN 226
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREyADRIVGLKDGRIVfDGPPA 230
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-221 |
1.32e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 192.59 E-value: 1.32e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYilGKikVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPkaslAAVR 83
Cdd:COG1131 1 IEVRGLTKRY--GD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP----AEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 nRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPS 163
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2418785902 164 ILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIV 210
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-227 |
1.93e-61 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 192.23 E-value: 1.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYilGKIKVraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVsKMPKASLAAV 82
Cdd:PRK09493 1 MIEFKNVSKHF--GPTQV--LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-NDPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RnRKIGFVFQSFNLLPHLNILKNVEL-PLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVND 161
Cdd:PRK09493 76 R-QEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 162 PSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKI-VDGNSNS 227
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIaEDGDPQV 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-219 |
1.95e-61 |
|
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: 190.09 E-value: 1.95e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYIlgkiKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAavR 83
Cdd:cd03229 1 LELKNVSKRYG----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPP--L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NRKIGFVFQSFNLLPHLNILKNVELPLmyggmskrkrtakakevlqnvglgdrlkhkpgelSGGQRQRVAIARAIVNDPS 163
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 164 ILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHDQAIASR-AERIIKIKDGK 219
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-221 |
2.85e-60 |
|
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: 188.86 E-value: 2.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYilGKIKVraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVR 83
Cdd:cd03261 1 IELRGLTKSF--GGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 nRKIGFVFQSFNLLPHLNILKNVELPL-MYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDP 162
Cdd:cd03261 77 -RRMGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 163 SILLADEPTGNLDSQSGGDILEIFTELH-SQGNTVIIVTHD-QAIASRAERIIKIKDGKIV 221
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKkELGLTSIMVTHDlDTAFAIADRIAVLYDGKIV 216
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
22-219 |
1.09e-59 |
|
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: 186.90 E-value: 1.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAavrnRKIGFVFQSFNL-LPHL 100
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR----RKVGLVFQNPDDqFFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 NILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGG 180
Cdd:cd03225 92 TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2418785902 181 DILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGK 219
Cdd:cd03225 172 ELLELLKKLKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-221 |
3.32e-59 |
|
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: 186.29 E-value: 3.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYIlgkiKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPkaslaaVR 83
Cdd:cd03300 1 IELENVSKFYG----GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP------PH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPS 163
Cdd:cd03300 71 KRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 164 ILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHDQAIA-SRAERIIKIKDGKIV 221
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEAlTMSDRIAVMNKGKIQ 210
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-221 |
3.93e-59 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 189.59 E-value: 3.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 7 ENIVKDYilGKikVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDD-VLVSKMPkaslaaVRNR 85
Cdd:COG1118 6 RNISKRF--GS--FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrDLFTNLP------PRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 86 KIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSIL 165
Cdd:COG1118 76 RVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 166 LADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:COG1118 156 LLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALElADRVVVMNQGRIE 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-221 |
4.01e-58 |
|
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: 186.41 E-value: 4.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMH-ILGCLDSP--TDGTYYLDDVLVSKMPKASL 79
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 80 AAVRNRKIGFVFQ----SFNllPHLNILKNVELPLMY-GGMSKRKRTAKAKEVLQNVGLGD---RLKHKPGELSGGQRQR 151
Cdd:COG0444 81 RKIRGREIQMIFQdpmtSLN--PVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2418785902 152 VAIARAIVNDPSILLADEPTGNLD--SQSggDILEIFTELHSQ-GNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDvtIQA--QILNLLKDLQRElGLAILFITHDLGVVAEiADRVAVMYAGRIV 230
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-221 |
1.13e-56 |
|
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: 180.38 E-value: 1.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAavr 83
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 nRKIGFVFQ----SFNllPHLNILKNVELPLMYGGMSKRKRtaKAKEVLQNVGLGDRLKHK-PGELSGGQRQRVAIARAI 158
Cdd:COG1124 79 -RRVQMVFQdpyaSLH--PRHTVDRILAEPLRIHGLPDREE--RIAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 159 VNDPSILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHlCDRVAVMQNGRIV 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
23-220 |
1.91e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 178.47 E-value: 1.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPkasLAAVRnRKIGFVFQSFNLLPHlNI 102
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWR-RQVAYVPQEPALWGG-TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 103 LKNVELPLMYGGmsKRKRTAKAKEVLQNVGLGDRLKHKP-GELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGD 181
Cdd:COG4619 91 RDNLPFPFQLRE--RKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2418785902 182 ILEIFTEL-HSQGNTVIIVTHDQAIASR-AERIIKIKDGKI 220
Cdd:COG4619 169 VEELLREYlAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
20-221 |
1.39e-54 |
|
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: 182.03 E-value: 1.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 20 VRALNGIDLQIQKGEFVAIMGPSGSGKSTL-MHILGCLDSPTD--GTYYLDDVLVSKMPkaslAAVRNRKIGFVFQSF-- 94
Cdd:COG1123 19 VPAVDGVSLTIAPGETVALVGESGSGKSTLaLALMGLLPHGGRisGEVLLDGRDLLELS----EALRGRRIGMVFQDPmt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 95 NLLPhLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNL 174
Cdd:COG1123 95 QLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTAL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2418785902 175 DSQSGGDILEIFTELHSQ-GNTVIIVTHDQA-IASRAERIIKIKDGKIV 221
Cdd:COG1123 174 DVTTQAEILDLLRELQRErGTTVLLITHDLGvVAEIADRVVVMDDGRIV 222
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-222 |
2.14e-54 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 174.55 E-value: 2.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 1 MDIIKTENIVKDYiLGKikvRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLV--SKMPKAS 78
Cdd:PRK11264 1 MSAIEVKNLVKKF-HGQ---TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 79 LAAVRN--RKIGFVFQSFNLLPHLNILKNV-ELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIA 155
Cdd:PRK11264 77 KGLIRQlrQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 156 RAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKIVD 222
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-221 |
3.66e-54 |
|
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: 172.82 E-value: 3.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYIlgkiKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKAslaavr 83
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPS 163
Cdd:cd03301 71 DRDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 164 ILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHDQAIA-SRAERIIKIKDGKIV 221
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAmTMADRIAVMNDGQIQ 210
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-221 |
1.13e-53 |
|
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: 172.49 E-value: 1.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYILGKikvRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLaavr 83
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDR--LKHKPGELSGGQRQRVAIARAIVND 161
Cdd:cd03295 74 RRKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2418785902 162 PSILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRlADRIAIMKNGEIV 215
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-221 |
1.25e-53 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 173.41 E-value: 1.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIvkDYILGK---IKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLA 80
Cdd:TIGR04521 1 IKLKNV--SYIYQPgtpFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 81 AVRnRKIGFVFQsF--NLLPHLNILKNVelplMYG----GMSKRKRTAKAKEVLQNVGLGDRLKHK-PGELSGGQRQRVA 153
Cdd:TIGR04521 79 DLR-KKVGLVFQ-FpeHQLFEETVYKDI----AFGpknlGLSEEEAEERVKEALELVGLDEEYLERsPFELSGGQMRRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 154 IARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELH-SQGNTVIIVTHD-QAIASRAERIIKIKDGKIV 221
Cdd:TIGR04521 153 IAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSmEDVAEYADRVIVMHKGKIV 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-221 |
2.96e-53 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 174.60 E-value: 2.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVR 83
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 nRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPS 163
Cdd:PRK11153 82 -RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 164 ILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRiCDRVAVIDAGRLV 220
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-226 |
4.22e-53 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 170.94 E-value: 4.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGKikvRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAV 82
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RnRKIGFVFQSFNLLPHLNILKNVELP-LMYG-------GMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAI 154
Cdd:TIGR02315 78 R-RRIGMIFQHYNLIERLTVLENVLHGrLGYKptwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 155 ARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHDQAIASR-AERIIKIKDGKIV-DGNSN 226
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKyADRIVGLKAGEIVfDGAPS 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-220 |
5.45e-53 |
|
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: 170.60 E-value: 5.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYilGKIkvRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPkaslaaVR 83
Cdd:cd03296 3 IEVRNVSKRF--GDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NRKIGFVFQSFNLLPHLNILKNVELplmygGMSKRKRT---------AKAKEVLQNV---GLGDRLkhkPGELSGGQRQR 151
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVAF-----GLRVKPRSerppeaeirAKVHELLKLVqldWLADRY---PAQLSGGQRQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 152 VAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHDQAIASR-AERIIKIKDGKI 220
Cdd:cd03296 145 VALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEvADRVVVMNKGRI 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-221 |
6.21e-53 |
|
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: 170.99 E-value: 6.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYilGKIKVraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAav 82
Cdd:COG1120 1 MLEAENLSVGY--GGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 rnRKIGFVFQS----FNL----------LPHLNILknvelplmyGGMSKRKRtAKAKEVLQNVGLGDrLKHKP-GELSGG 147
Cdd:COG1120 75 --RRIAYVPQEppapFGLtvrelvalgrYPHLGLF---------GRPSAEDR-EAVEEALERTGLEH-LADRPvDELSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2418785902 148 QRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTEL-HSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:COG1120 142 ERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARyADRLVLLKDGRIV 217
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-206 |
1.27e-52 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 170.37 E-value: 1.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYilGKIKVraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMP-------- 75
Cdd:COG4598 9 LEVRDLHKSF--GDLEV--LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdgelvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 76 --KASLAAVRNRkIGFVFQSFNLLPHLNILKNV-ELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRV 152
Cdd:COG4598 85 adRRQLQRIRTR-LGMVFQSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2418785902 153 AIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIA 206
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFA 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
19-221 |
2.39e-52 |
|
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: 168.51 E-value: 2.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCL-----DSPTDGTYYLDDVLVSKMPKASLAaVRnRKIGFVFQS 93
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVLE-LR-RRVGMVFQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 94 FNLLPhLNILKNVELPLMYGGMSKRKRT-AKAKEVLQNVGLGDRLKHK--PGELSGGQRQRVAIARAIVNDPSILLADEP 170
Cdd:cd03260 90 PNPFP-GSIYDNVAYGLRLHGIKLKEELdERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2418785902 171 TGNLDSQSGGDILEIFTELHSQgNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:cd03260 169 TSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARvADRTAFLLNGRLV 219
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-222 |
6.68e-52 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 167.88 E-value: 6.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYilGKikVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVR 83
Cdd:COG4161 3 IQLKNINCFY--GS--HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 --NRKIGFVFQSFNLLPHLNILKN-VELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVN 160
Cdd:COG4161 79 llRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2418785902 161 DPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKIVD 222
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIE 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-223 |
2.31e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 166.42 E-value: 2.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMH-ILGcLDSPTDGTyylddVLVSKMPkaslAAVRNRKIGFVFQSFNLL 97
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILG-LLPPTSGT-----VRLFGKP----PRRARRRIGYVPQRAEVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 98 PHLNIlkNV-ELPLM--YGGMS-----KRKRTAKAKEVLQNVGLGDrLKHKP-GELSGGQRQRVAIARAIVNDPSILLAD 168
Cdd:COG1121 88 WDFPI--TVrDVVLMgrYGRRGlfrrpSRADREAVDEALERVGLED-LADRPiGELSGGQQQRVLLARALAQDPDLLLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2418785902 169 EPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIKDGKIVDG 223
Cdd:COG1121 165 EPFAGVDAATEEALYELLRELRREGKTILVVTHDlGAVREYFDRVLLLNRGLVAHG 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-221 |
7.45e-50 |
|
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: 162.72 E-value: 7.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYIlgkiKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKAslaavR 83
Cdd:COG4555 2 IEVENLSKKYG----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-----A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPS 163
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2418785902 164 ILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIKDGKIV 221
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHImQEVEALCDRVVILHKGKVV 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
22-227 |
8.69e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 162.49 E-value: 8.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGT-----YYLDdvlVSKMPKASLAAVRNRKIGFVFQSFNL 96
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTlniagNHFD---FSKTPSDKAIRELRRNVGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 97 LPHLNILKN-VELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLD 175
Cdd:PRK11124 94 WPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2418785902 176 SQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKIVDGNSNS 227
Cdd:PRK11124 174 PEITAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
26-221 |
4.27e-49 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 160.31 E-value: 4.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 26 IDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKAslaavrNRKIGFVFQSFNLLPHLNILKN 105
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA------ERPVSMLFQENNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 106 VELplmygGMSKRKR-----TAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGG 180
Cdd:COG3840 92 IGL-----GLRPGLKltaeqRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQ 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2418785902 181 DILEIFTELH-SQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:COG3840 167 EMLDLVDELCrERGLTVLMVTHDPEDAARiADRVLLVADGRIA 209
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-223 |
4.80e-49 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 160.04 E-value: 4.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGKikvRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAV 82
Cdd:PRK10908 1 MIRFEHVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RnRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSK---RKRTAKAkevLQNVGLGDRLKHKPGELSGGQRQRVAIARAIV 159
Cdd:PRK10908 78 R-RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGddiRRRVSAA---LDKVGLLDKAKNFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 160 NDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQA-IASRAERIIKIKDGKIVDG 223
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGlISRRSYRMLTLSDGHLHGG 218
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-202 |
2.78e-48 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 159.26 E-value: 2.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 1 MDIIKTENIVKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKmPKAsla 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 81 avrNRkiGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVN 160
Cdd:COG4525 77 ---DR--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2418785902 161 DPSILLADEPTGNLDSQSGGDILEIFTEL-HSQGNTVIIVTHD 202
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHS 194
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-221 |
1.39e-47 |
|
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: 155.73 E-value: 1.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 27 DLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKAslaavrNRKIGFVFQSFNLLPHLNILKNV 106
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA------DRPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 107 ELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIF 186
Cdd:cd03298 92 GLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 2418785902 187 TELHSQ-GNTVIIVTHD-QAIASRAERIIKIKDGKIV 221
Cdd:cd03298 172 LDLHAEtKMTVLMVTHQpEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-225 |
1.94e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 158.33 E-value: 1.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYILG-KIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGT------------------Y 64
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewifkdeknkkktkekeK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 65 YLDDVLVSKMPKASLAAVRN--RKIGFVFQ--SFNLLPHlNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLG-DRLKH 139
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIKEirRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDeSYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 140 KPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIKDG 218
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDlDNVLEWTKRTIFFKDG 241
|
....*...
gi 2418785902 219 KIV-DGNS 225
Cdd:PRK13651 242 KIIkDGDT 249
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-221 |
2.30e-47 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 158.81 E-value: 2.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 38 IMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKaslaavRNRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSK 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP------HLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 118 RKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDI-LEIFTELHSQGNTV 196
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMqLELKTIQEQLGITF 154
|
170 180
....*....|....*....|....*.
gi 2418785902 197 IIVTHDQAIA-SRAERIIKIKDGKIV 221
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIAIMRKGKIA 180
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-215 |
3.26e-47 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 154.95 E-value: 3.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 25 GIDLQIQKGEFVAIMGPSGSGKSTLMH-ILGCLDSP--TDGTYYLDDVLVSKMPkaslaaVRNRKIGFVFQSFNLLPHLN 101
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALP------AEQRRIGILFQDDLLFPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ILKNvelpLMYG---GMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQS 178
Cdd:COG4136 93 VGEN----LAFAlppTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 2418785902 179 GGDILE-IFTELHSQGNTVIIVTHDQAIASRAERIIKI 215
Cdd:COG4136 169 RAQFREfVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
22-221 |
7.96e-47 |
|
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: 162.63 E-value: 7.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMH-ILGCLDsPTDGTYYLDDVLVSKMPKASLAavrnRKIGFVFQSfnllPHL 100
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLAlLLRFLD-PQSGSITLGGVDLRDLDEDDLR----RRIAVVPQR----PHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 ---NILKNVelplmyggmskrkRTAK-------AKEVLQNVGLGDRLKHKP-------GE----LSGGQRQRVAIARAIV 159
Cdd:COG4987 421 fdtTLRENL-------------RLARpdatdeeLWAALERVGLGDWLAALPdgldtwlGEggrrLSGGERRRLALARALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2418785902 160 NDPSILLADEPTGNLDSQSGGDILE-IFTelHSQGNTVIIVTHDQAIASRAERIIKIKDGKIV 221
Cdd:COG4987 488 RDAPILLLDEPTEGLDAATEQALLAdLLE--ALAGRTVLLITHRLAGLERMDRILVLEDGRIV 548
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-221 |
1.05e-46 |
|
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: 153.60 E-value: 1.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQ---KGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVRNRKIGFVFQSFNLLPH 99
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 100 LNILKNVElplmYG--GMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQ 177
Cdd:cd03297 90 LNVRENLA----FGlkRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2418785902 178 SGGDILEIFTELHSQGN-TVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:cd03297 166 LRLQLLPELKQIKKNLNiPVIFVTHDLSEAEYlADRIVVMEDGRLQ 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
22-219 |
1.91e-46 |
|
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: 151.38 E-value: 1.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAavrnRKIGFVFQSFNLLpHLN 101
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLR----KNIAYVPQDPFLF-SGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ILKNVelplmyggmskrkrtakakevlqnvglgdrlkhkpgeLSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGD 181
Cdd:cd03228 92 IRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 2418785902 182 ILEIFTELhSQGNTVIIVTHDQAIASRAERIIKIKDGK 219
Cdd:cd03228 135 ILEALRAL-AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-220 |
2.55e-46 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 156.93 E-value: 2.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 1 MDIIKTENIVKDYIlGKIKVraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKM-PKasl 79
Cdd:PRK11650 1 MAGLKLQAVRKSYD-GKTQV--IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELePA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 80 aavrNRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIV 159
Cdd:PRK11650 75 ----DRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2418785902 160 NDPSILLADEPTGNLDSQSGGDI-LEIfTELHSQ-GNTVIIVTHDQAIA-SRAERIIKIKDGKI 220
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAKLRVQMrLEI-QRLHRRlKTTSLYVTHDQVEAmTLADRVVVMNGGVA 213
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
26-220 |
5.87e-46 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 156.34 E-value: 5.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 26 IDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKAslaavrNRKIGFVFQSFNLLPHLNILKN 105
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA------ERGVGMVFQSYALYPHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 106 VELPLMYGGMSK---RKRTAKAKEVLQnvgLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDS----QS 178
Cdd:PRK11000 96 MSFGLKLAGAKKeeiNQRVNQVAEVLQ---LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrvQM 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2418785902 179 GGDIleifTELHSQ-GNTVIIVTHDQAIA-SRAERIIKIKDGKI 220
Cdd:PRK11000 173 RIEI----SRLHKRlGRTMIYVTHDQVEAmTLADKIVVLDAGRV 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
22-220 |
6.72e-46 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 156.26 E-value: 6.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPkaslaaVRNRKIGFVFQSFNLLPHLN 101
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP------AENRHVNTVFQSYALFPHMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGD 181
Cdd:PRK09452 103 VFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2418785902 182 I-LEIfTELHSQ-GNTVIIVTHDQAIA-SRAERIIKIKDGKI 220
Cdd:PRK09452 183 MqNEL-KALQRKlGITFVFVTHDQEEAlTMSDRIVVMRDGRI 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
23-220 |
6.76e-46 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 152.91 E-value: 6.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGtyyldDVLVSKMPkasLAAVRNrKIGFVFQSFNLLPHLNI 102
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-----ELLAGTAP---LAEARE-DTRLMFQDARLLPWKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 103 LKNVELPLmyggmsKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDI 182
Cdd:PRK11247 99 IDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEM 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2418785902 183 LEIFTELHSQ-GNTVIIVTHD--QAIASrAERIIKIKDGKI 220
Cdd:PRK11247 173 QDLIESLWQQhGFTVLLVTHDvsEAVAM-ADRVLLIEEGKI 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-222 |
1.01e-45 |
|
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: 151.72 E-value: 1.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYilgkiKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKaslaavR 83
Cdd:cd03299 1 LKVENLSKDW-----KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP------E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPS 163
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 164 ILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHDQA-IASRAERIIKIKDGKIVD 222
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEeAWALADKVAIMLNGKLIQ 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
21-222 |
1.46e-45 |
|
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: 159.15 E-value: 1.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAavrnRKIGFVFQSfnllPHL 100
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWR----RQIAWVPQN----PYL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 -------NILknvelplmyggMSKRKRTAKA-KEVLQNVGLGDRLKHKP-------GE----LSGGQRQRVAIARAIVND 161
Cdd:COG4988 423 fagtireNLR-----------LGRPDASDEElEAALEAAGLDEFVAALPdgldtplGEggrgLSGGQAQRLALARALLRD 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 162 PSILLADEPTGNLDSQSGGDILEIFTELhSQGNTVIIVTHDQAIASRAERIIKIKDGKIVD 222
Cdd:COG4988 492 APLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQADRILVLDDGRIVE 551
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-221 |
3.03e-45 |
|
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: 150.04 E-value: 3.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYIlgkiKVRALNGIDLQIQKGEFvAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKAslaaVR 83
Cdd:cd03264 1 LQLENLTKRYG----KKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 nRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPS 163
Cdd:cd03264 72 -RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2418785902 164 ILLADEPTGNLDSQSGGDILEIFTELhSQGNTVIIVTHD-QAIASRAERIIKIKDGKIV 221
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIvEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
21-221 |
7.20e-45 |
|
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: 147.97 E-value: 7.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAavrnRKIGFVFQsfnllphl 100
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA----RKIAYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 nilknvelplmyggmskrkrtakakeVLQNVGLGDrLKHKP-GELSGGQRQRVAIARAIVNDPSILLADEPTGNLD--SQ 177
Cdd:cd03214 81 --------------------------ALELLGLAH-LADRPfNELSGGERQRVLLARALAQEPPILLLDEPTSHLDiaHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2418785902 178 SggDILEIFTEL-HSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:cd03214 134 I--ELLELLRRLaRERGKTVVMVLHDLNLAARyADRVILLKDGRIV 177
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
21-202 |
8.39e-45 |
|
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: 148.84 E-value: 8.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTLMH-ILGCLDsPTDGTYYLDDVLVSKMPKaslaavrnrKIGFVFQSFNLLPH 99
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLLK-PTSGSIRVFGKPLEKERK---------RIGYVPQRRSIDRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 100 LNIlkNV-ELPLM--YGGMS-----KRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPT 171
Cdd:cd03235 83 FPI--SVrDVVLMglYGHKGlfrrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190
....*....|....*....|....*....|.
gi 2418785902 172 GNLDSQSGGDILEIFTELHSQGNTVIIVTHD 202
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRREGMTILVVTHD 191
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-221 |
9.28e-45 |
|
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: 156.38 E-value: 9.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 16 GKIKVRALNGIDLQIQKGEFVAIMGPSGSGKS-TLMHILGCLDSP---TDGTYYLDDVLVSKMPKASLAAVRNRKIGFVF 91
Cdd:COG4172 19 GGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSERELRRIRGNRIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 92 Q----SFNllPHLNILKNVELPLM-YGGMSKRKRTAKAKEVLQNVGLGD---RLKHKPGELSGGQRQRVAIARAIVNDPS 163
Cdd:COG4172 99 QepmtSLN--PLHTIGKQIAEVLRlHRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQRVMIAMALANEPD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 164 ILLADEPTGNLDSQSGGDILEIFTEL-HSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:COG4172 177 LLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRfADRVAVMRQGEIV 236
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-213 |
3.57e-44 |
|
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: 147.97 E-value: 3.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYilGKIKvrALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPkaslAAVR 83
Cdd:cd03219 1 LEVRGLTKRF--GGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP----PHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NRK-IGFVFQSFNLLPHLNILKNVELPLMYGG----------MSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRV 152
Cdd:cd03219 73 ARLgIGRTFQIPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2418785902 153 AIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD-QAIASRAERII 213
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDmDVVMSLADRVT 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-171 |
6.78e-44 |
|
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: 144.33 E-value: 6.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLaavrNRKIGFVFQSFNLLPHLNI 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL----RKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2418785902 103 LKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGD----RLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPT 171
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-220 |
8.53e-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: 144.85 E-value: 8.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYilGKikVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLaavr 83
Cdd:cd03230 1 IEVRNLSKRY--GK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 nRKIGFVFQSFNLLPHLNILKNVELplmyggmskrkrtakakevlqnvglgdrlkhkpgelSGGQRQRVAIARAIVNDPS 163
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 164 ILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKI 220
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
22-224 |
2.07e-43 |
|
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: 154.61 E-value: 2.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAavrnRKIGFVFQSfnllPHL- 100
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLR----RQIGVVLQD----VFLf 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 ------NI-LKNVELPLmyggmskrkrtAKAKEVLQNVGLGDRLKHKP-------GE----LSGGQRQRVAIARAIVNDP 162
Cdd:COG2274 562 sgtireNItLGDPDATD-----------EEIIEAARLAGLHDFIEALPmgydtvvGEggsnLSGGQRQRLAIARALLRNP 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2418785902 163 SILLADEPTGNLDSQSGGDILEIFTELhSQGNTVIIVTHDQAIASRAERIIKIKDGKIV-DGN 224
Cdd:COG2274 631 RILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRLADRIIVLDKGRIVeDGT 692
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
19-219 |
3.96e-43 |
|
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: 142.77 E-value: 3.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAavrnRKIGFVFQsfnllp 98
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR----RRIGYVPQ------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 99 hlnilknvelplmyggmskrkrtakakevlqnvglgdrlkhkpgeLSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQS 178
Cdd:cd00267 81 ---------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAS 115
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2418785902 179 GGDILEIFTELHSQGNTVIIVTHDQAIASRA-ERIIKIKDGK 219
Cdd:cd00267 116 RERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-221 |
5.52e-43 |
|
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: 148.33 E-value: 5.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 26 IDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDD-VLVSKMPKASLAAVRnRKIGFVFQSFNLLPHLNILK 104
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGeVLQDSARGIFLPPHR-RRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 105 NvelpLMYGgmskRKRTAKAK------EVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQS 178
Cdd:COG4148 97 N----LLYG----RKRAPRAErrisfdEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2418785902 179 GGDILEIFTELHSQGNT-VIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:COG4148 169 KAEILPYLERLRDELDIpILYVSHSLDEVARlADHVVLLEQGRVV 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-220 |
5.93e-43 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 147.92 E-value: 5.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYilGKIKVraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMpkaslaAVR 83
Cdd:PRK10851 3 IEIANIKKSF--GRTQV--LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL------HAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NRKIGFVFQSFNLLPHLNILKNVELPLMYggMSKRKR------TAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARA 157
Cdd:PRK10851 73 DRKVGFVFQHYALFRHMTVFDNIAFGLTV--LPRRERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 158 IVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGN-TVIIVTHDQAIASR-AERIIKIKDGKI 220
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEvADRVVVMSQGNI 215
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-222 |
7.21e-43 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 145.27 E-value: 7.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYILGKikVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKmpKASLAAVR 83
Cdd:TIGR04520 1 IEVENVSFSYPESE--KPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD--EENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 nRKIGFVFQ---------------SF---NL-LPHLNILKNVElplmyggmskrkrtakakEVLQNVGLGDRLKHKPGEL 144
Cdd:TIGR04520 77 -KKVGMVFQnpdnqfvgatveddvAFgleNLgVPREEMRKRVD------------------EALKLVGMEDFRDREPHLL 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2418785902 145 SGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGN-TVIIVTHDQAIASRAERIIKIKDGKIVD 222
Cdd:TIGR04520 138 SGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGiTVISITHDMEEAVLADRVIVMNKGKIVA 216
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-222 |
1.32e-42 |
|
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: 143.28 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPkaslAAV 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP----AEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RnRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDP 162
Cdd:cd03266 77 R-RRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 163 SILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIKDGKIVD 222
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHImQEVERLCDRVVVLHRGRVVY 216
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-221 |
2.73e-42 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 146.40 E-value: 2.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 2 DIIKTENIVKDYilGKIKVraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKmpkaslAA 81
Cdd:PRK11432 5 NFVVLKNITKRF--GSNTV--IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 82 VRNRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNV---GLGDRLKHkpgELSGGQRQRVAIARAI 158
Cdd:PRK11432 75 IQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVdlaGFEDRYVD---QISGGQQQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 159 VNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGN-TVIIVTHDQAIA-SRAERIIKIKDGKIV 221
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNiTSLYVTHDQSEAfAVSDTVIVMNKGKIM 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-221 |
3.37e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 144.39 E-value: 3.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYL-DDVLVSKMPKASLAAVRnRKIGFVFQsF--NLL 97
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNKKLKPLR-KKVGIVFQ-FpeHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 98 PHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLG-DRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDS 176
Cdd:PRK13634 99 FEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2418785902 177 QSGGDILEIFTELHSQGN-TVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGlTTVLVTHSMEDAARyADQIVVMHKGTVF 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-221 |
1.80e-41 |
|
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: 147.52 E-value: 1.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDY-----ILGKIK--VRALNGIDLQIQKGEFVAIMGPSGSGKSTL-MHILGCLdsPTDGTYYLDDVLVSKM 74
Cdd:COG4172 275 LLEARDLKVWFpikrgLFRRTVghVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 75 PKASLAAVRnRKIGFVFQ----SFNllPHLNILKNVELPLM--YGGMSKRKRTAKAKEVLQNVGLGDRLKHK-PGELSGG 147
Cdd:COG4172 353 SRRALRPLR-RRMQVVFQdpfgSLS--PRMTVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLDPAARHRyPHEFSGG 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2418785902 148 QRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTEL-HSQGNTVIIVTHD-QAIASRAERIIKIKDGKIV 221
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDlAVVRALAHRVMVMKDGKVV 505
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
23-220 |
1.94e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 141.64 E-value: 1.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKM----------PKASLAAVRNRkIGFVFQ 92
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvaDKNQLRLLRTR-LTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 93 SFNLLPHLNILKNV-ELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHK-PGELSGGQRQRVAIARAIVNDPSILLADEP 170
Cdd:PRK10619 100 HFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 171 TGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKI 220
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKI 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
22-221 |
4.13e-41 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 143.82 E-value: 4.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKaslaavRNRKIGFVFQSFNLLPHLN 101
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP------YQRPINMMFQSYALFPHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGD 181
Cdd:PRK11607 108 VEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2418785902 182 I-LEIFTELHSQGNTVIIVTHDQAIA-SRAERIIKIKDGKIV 221
Cdd:PRK11607 188 MqLEVVDILERVGVTCVMVTHDQEEAmTMAGRIAIMNRGKFV 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
21-208 |
4.67e-41 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 140.56 E-value: 4.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTL------MH--ILGCLdspTDGTYYLDDVLVSKmPKASLAAVRnRKIGFVFQ 92
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLlrclnrMNdlIPGAR---VEGEILLDGEDIYD-PDVDVVELR-RRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 93 SFNLLPHlNILKNVELPL-MYGGMSKRKRTAKAKEVLQNVGL----GDRLKHKPGELSGGQRQRVAIARAIVNDPSILLA 167
Cdd:COG1117 100 KPNPFPK-SIYDNVAYGLrLHGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLM 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2418785902 168 DEPTGNLDSQSGGDILEIFTELHSQgNTVIIVTHDQAIASR 208
Cdd:COG1117 179 DEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAAR 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
21-202 |
5.78e-41 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 140.22 E-value: 5.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKmPKAslaavrnrKIGFVFQSFNLLPHL 100
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGA--------ERGVVFQNEGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 NILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGG 180
Cdd:PRK11248 86 NVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180
....*....|....*....|...
gi 2418785902 181 DILEIFTEL-HSQGNTVIIVTHD 202
Cdd:PRK11248 166 QMQTLLLKLwQETGKQVLLITHD 188
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-202 |
1.51e-40 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 141.02 E-value: 1.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDY-----ILGKIK--VRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMP 75
Cdd:COG4608 7 LLEVRDLKKHFpvrggLFGRTVgvVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 76 KASLAAVRnRKIGFVFQ----SFNllPHLNILKNVELPLMYGGM-SKRKRTAKAKEVLQNVGLG----DRLKHkpgELSG 146
Cdd:COG4608 87 GRELRPLR-RRMQMVFQdpyaSLN--PRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRpehaDRYPH---EFSG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 147 GQRQRVAIARAIVNDPSILLADEPTGNLD----SQsggdILEIFTELHSQ-GNTVIIVTHD 202
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQ----VLNLLEDLQDElGLTYLFISHD 217
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-221 |
1.94e-40 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 145.31 E-value: 1.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLaavRnRKIGFVFQSFNLLpHLN 101
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL---R-RQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ILKNVelplmygGMSKRKRT-AKAKEVLQNVGLGDRLKHKP-------GE----LSGGQRQRVAIARAIVNDPSILLADE 169
Cdd:COG1132 430 IRENI-------RYGRPDATdEEVEEAAKAAQAHEFIEALPdgydtvvGErgvnLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2418785902 170 PTGNLDSQSGGDILEIFTELhSQGNTVIIVTHDQAIASRAERIIKIKDGKIV 221
Cdd:COG1132 503 ATSALDTETEALIQEALERL-MKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-227 |
4.32e-40 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 137.41 E-value: 4.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 27 DLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKAslaavrNRKIGFVFQSFNLLPHLNILKNV 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS------RRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 107 ELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIF 186
Cdd:PRK10771 93 GLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2418785902 187 TEL-HSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV-DGNSNS 227
Cdd:PRK10771 173 SQVcQERQLTLLMVSHSLEDAARiAPRSLVVADGRIAwDGPTDE 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-222 |
1.86e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 136.20 E-value: 1.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 20 VRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCL-----DSPTDGTYYLDDVLVSKMPKASLaavrNRKIGFVFQSF 94
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEL----RRRVQMVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 95 NLLPHLNILKNVELPLMYGGMSKRKRT--AKAKEVLQNVGL----GDRLKHKPGELSGGQRQRVAIARAIVNDPSILLAD 168
Cdd:PRK14247 92 NPIPNLSIFENVALGLKLNRLVKSKKElqERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 169 EPTGNLDSQSGGDILEIFTELHSQgNTVIIVTHDQAIASR-AERIIKIKDGKIVD 222
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARiSDYVAFLYKGQIVE 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-222 |
1.95e-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: 1.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYiLGkikVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKM-PKASLAA 81
Cdd:COG1129 4 LLEMRGISKSF-GG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRsPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 82 vrnrKIGFVFQSFNLLPHLNILKNV---ELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAI 158
Cdd:COG1129 80 ----GIAIIHQELNLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2418785902 159 VNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTH--DQaIASRAERIIKIKDGKIVD 222
Cdd:COG1129 156 SRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHrlDE-VFEIADRVTVLRDGRLVG 220
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-222 |
3.04e-39 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 135.97 E-value: 3.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 1 MDIIKTENIVKDY----ILGKIKVRA-LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMP 75
Cdd:PRK10419 1 MTLLNVSGLSHHYahggLSGKHQHQTvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 76 KASLAAVRnRKIGFVFQ----SFNllPHLNILKNVELPLMY-GGMSKRKRTAKAKEVLQNVGLGDRLKHK-PGELSGGQR 149
Cdd:PRK10419 81 RAQRKAFR-RDIQMVFQdsisAVN--PRKTVREIIREPLRHlLSLDKAERLARASEMLRAVDLDDSVLDKrPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 150 QRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTV-IIVTHDQAIASR-AERIIKIKDGKIVD 222
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-219 |
8.09e-39 |
|
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: 134.78 E-value: 8.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 1 MDIIKTENIVKDYilGKikVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPkaslA 80
Cdd:COG0411 2 DPLLEVRGLTKRF--GG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP----P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 81 AVRNRK-IGFVFQSFNLLPHLNILKNVELPLMYGG---------------MSKRKRTAKAKEVLQNVGLGDRLKHKPGEL 144
Cdd:COG0411 74 HRIARLgIARTFQNPRLFPELTVLENVLVAAHARLgrgllaallrlprarREEREARERAEELLERVGLADRADEPAGNL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 145 SGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELH-SQGNTVIIVTHD-QAIASRAERII------KIK 216
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDmDLVMGLADRIVvldfgrVIA 233
|
...
gi 2418785902 217 DGK 219
Cdd:COG0411 234 EGT 236
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-221 |
8.95e-39 |
|
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: 133.65 E-value: 8.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYIlgkiKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKaslaAVR 83
Cdd:cd03265 1 IEVENLVKKYG----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR----EVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 nRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDrLKHKP-GELSGGQRQRVAIARAIVNDP 162
Cdd:cd03265 73 -RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLE-AADRLvKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 163 SILLADEPTGNLDSQSGGDILEIFTELH-SQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKeEFGMTILLTTHYMEEAEQlCDRVAIIDHGRII 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-221 |
1.24e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 135.18 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYILGK-IKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKmPKASLAAV 82
Cdd:PRK13637 3 IKIENLTHIYMEGTpFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RnRKIGFVFQ--SFNLLPHlNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLG-DRLKHK-PGELSGGQRQRVAIARAI 158
Cdd:PRK13637 82 R-KKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKsPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 159 VNDPSILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHD-QAIASRAERIIKIKDGKIV 221
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSmEDVAKLADRIIVMNKGKCE 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-222 |
4.79e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 133.22 E-value: 4.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYilGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKmpkASLAAV 82
Cdd:PRK13635 5 IIRVEHISFRY--PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE---ETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RnRKIGFVFQS-FNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVND 161
Cdd:PRK13635 80 R-RQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2418785902 162 PSILLADEPTGNLDSQSGGDILEIFTELHSQGN-TVIIVTHDQAIASRAERIIKIKDGKIVD 222
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-220 |
5.91e-38 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 131.14 E-value: 5.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 27 DLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKAslaavrNRKIGFVFQSFNLLPHLNILKNV 106
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY------QRPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 107 ELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIF 186
Cdd:TIGR01277 92 GLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 2418785902 187 TELHSQGN-TVIIVTHDQAIASR-AERIIKIKDGKI 220
Cdd:TIGR01277 172 KQLCSERQrTLLMVTHHLSDARAiASQIAVVSQGKI 207
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
22-223 |
1.15e-37 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 138.46 E-value: 1.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLaavrNRKIGFVFQSFNLLpHLN 101
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADL----RRNIGYVPQDPRLF-YGT 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ILKNVELplmyggmskRKRTAKAKEVLQNV---GLGDRLKHKP-------GE----LSGGQRQRVAIARAIVNDPSILLA 167
Cdd:TIGR03375 555 LRDNIAL---------GAPYADDEEILRAAelaGVTEFVRRHPdgldmqiGErgrsLSGGQRQAVALARALLRDPPILLL 625
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2418785902 168 DEPTGNLDSQSGGDILEIFTELhSQGNTVIIVTHDQAIASRAERIIKIKDGKIV-DG 223
Cdd:TIGR03375 626 DEPTSAMDNRSEERFKDRLKRW-LAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVaDG 681
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
22-213 |
1.41e-37 |
|
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: 137.03 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVlvsKMPKASLAAVRnRKIGFVFQSfnllPHL- 100
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV---PLADADADSWR-DQIAWVPQH----PFLf 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 --NILKNVELplmyggmskRKRTAKA---KEVLQNVGLGDRLKHKP-------GE----LSGGQRQRVAIARAIVNDPSI 164
Cdd:TIGR02857 409 agTIAENIRL---------ARPDASDaeiREALERAGLDEFVAALPqgldtpiGEggagLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2418785902 165 LLADEPTGNLDSQSGGDILEIFTELhSQGNTVIIVTHDQAIASRAERII 213
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAALADRIV 527
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-220 |
2.72e-37 |
|
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: 133.31 E-value: 2.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 26 IDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVRNRKIGFVFQSFNLLPHLNILKN 105
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 106 velpLMYGgMSK---RKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDI 182
Cdd:TIGR02142 96 ----LRYG-MKRarpSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2418785902 183 LEIFTELHSQGNT-VIIVTHD-QAIASRAERIIKIKDGKI 220
Cdd:TIGR02142 171 LPYLERLHAEFGIpILYVSHSlQEVLRLADRVVVLEDGRV 210
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-221 |
5.05e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 130.21 E-value: 5.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGKI-KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPkaslAA 81
Cdd:COG1101 1 MLELKNLSKTFNPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP----EY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 82 VRNRKIGFVFQsfNLL----PHLNILKNVELPLMYG-------GMSKRKRtAKAKEVLQNVGLG--DRLKHKPGELSGGQ 148
Cdd:COG1101 77 KRAKYIGRVFQ--DPMmgtaPSMTIEENLALAYRRGkrrglrrGLTKKRR-ELFRELLATLGLGleNRLDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2418785902 149 RQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGN-TVIIVTHD--QAIASrAERIIKIKDGKIV 221
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNmeQALDY-GNRLIMMHEGRII 228
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-213 |
6.98e-37 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 127.74 E-value: 6.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTyylddvlvskmpkasLAAVRNRKIGFVFQSFNL---LP 98
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT---------------VRRAGGARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 99 hLNILKNVEL-------PLMYGGMSKRKRTAKAkevLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPT 171
Cdd:NF040873 72 -LTVRDLVAMgrwarrgLWRRLTRDDRAAVDDA---LERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2418785902 172 GNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASRAERII 213
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-221 |
1.23e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 129.95 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIvkDYILG---KIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYL-DDVLVSKMPKASL 79
Cdd:PRK13641 3 IKFENV--DYIYSpgtPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIaGYHITPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 80 AAVRnRKIGFVFQ-SFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRL-KHKPGELSGGQRQRVAIARA 157
Cdd:PRK13641 81 KKLR-KKVSLVFQfPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 158 IVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIKDGKIV 221
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNmDDVAEYADDVLVLEHGKLI 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-221 |
1.41e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 129.34 E-value: 1.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYilGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKmpkASLAAVR 83
Cdd:PRK13632 8 IKVENVSFSY--PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK---ENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NrKIGFVFQS----FnllphlnILKNVELPLMYGGMSKR----KRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIA 155
Cdd:PRK13632 83 K-KIGIIFQNpdnqF-------IGATVEDDIAFGLENKKvppkKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2418785902 156 RAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGN-TVIIVTHDQAIASRAERIIKIKDGKIV 221
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-227 |
2.04e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 129.47 E-value: 2.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVRNRKIGFVFQ-SFNLLPH 99
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 100 LNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHK-PGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQS 178
Cdd:PRK13643 100 ETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKsPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2418785902 179 GGDILEIFTELHSQGNTVIIVTH-DQAIASRAERIIKIKDGKIVDGNSNS 227
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHIISCGTPS 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-221 |
2.04e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 129.09 E-value: 2.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPK-ASLAAVRnRKIGFVFQ-SFNLLP 98
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQIR-KKVGLVFQfPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 99 HLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHK-PGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQ 177
Cdd:PRK13649 100 EETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2418785902 178 SGGDILEIFTELHSQGNTVIIVTH--DQaIASRAERIIKIKDGKIV 221
Cdd:PRK13649 180 GRKELMTLFKKLHQSGMTIVLVTHlmDD-VANYADFVYVLEKGKLV 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
23-222 |
2.49e-36 |
|
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: 128.38 E-value: 2.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVRnRKIGFVFQ----SFNllP 98
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFR-RDVQLVFQdspsAVN--P 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 99 HLNILKNVELPLM-YGGMSKRKRTAKAKEVLQNVGL-GDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDS 176
Cdd:TIGR02769 104 RMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2418785902 177 QSGGDILEIFTELHSQGNTV-IIVTHDQAIASR-AERIIKIKDGKIVD 222
Cdd:TIGR02769 184 VLQAVILELLRKLQQAFGTAyLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
23-219 |
3.63e-36 |
|
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: 126.44 E-value: 3.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTyylddVLVSKMPKASLAAVRNRKIGFVFQSFNLLPHLNI 102
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGE-----VLWNGEPIRDAREDYRRRLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 103 LKNVElplMYGGMSKRKRT-AKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGD 181
Cdd:COG4133 93 RENLR---FWAALYGLRADrEAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVAL 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 2418785902 182 ILEIFTELHSQGNTVIIVTHdQAIASRAERIIKIKDGK 219
Cdd:COG4133 170 LAELIAAHLARGGAVLLTTH-QPLELAAARVLDLGDFK 206
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-202 |
3.80e-36 |
|
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: 127.20 E-value: 3.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKmPKAslaavrNRKIgfVFQSFNLLPHLNI 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGP------DRMV--VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 103 LKNVELPL--MYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGG 180
Cdd:TIGR01184 72 RENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|...
gi 2418785902 181 DILEIFTEL-HSQGNTVIIVTHD 202
Cdd:TIGR01184 152 NLQEELMQIwEEHRVTVLMVTHD 174
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
28-221 |
4.56e-36 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 130.92 E-value: 4.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 28 LQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVRNRKIGFVFQSFNLLPHLNILKNVE 107
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 108 LPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFT 187
Cdd:PRK10070 129 FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190
....*....|....*....|....*....|....*.
gi 2418785902 188 ELHSQGN-TVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:PRK10070 209 KLQAKHQrTIVFISHDLDEAMRiGDRIAIMQNGEVV 244
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-223 |
7.51e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 127.50 E-value: 7.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGkikVRALNGIDLQIQKGEFVAIMGPSGSGKSTL-MHILGCLDsPTDGTYYLDDVLVsKMPKASLAA 81
Cdd:PRK13639 1 ILETRDLKYSYPDG---TEALKGINFKAEKGEMVALLGPNGAGKSTLfLHFNGILK-PTSGEVLIKGEPI-KYDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 82 VRnRKIGFVFQ-SFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVN 160
Cdd:PRK13639 76 VR-KTVGIVFQnPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2418785902 161 DPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKIVDG 223
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKE 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-218 |
8.00e-36 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 126.01 E-value: 8.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYIL---GKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHilgCLDS---PTDGT-YYLDDVLVSKMP 75
Cdd:COG4778 4 LLEVENLSKTFTLhlqGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLK---CIYGnylPDSGSiLVRHDGGWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 76 KAS---LAAVRNRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKH-KPGELSGGQRQR 151
Cdd:COG4778 81 QASpreILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDlPPATFSGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 152 VAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDG 218
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-221 |
1.37e-35 |
|
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: 125.24 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMH-ILGCLDsPTDGTYYLDDVLVSKMPKASLAAvrnRKIGFVFQSFNLL 97
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMGLLP-PRSGSIRFDGRDITGLPPHERAR---AGIGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 98 PHLNILKNVELplmygGMSKRKRtAKAKEVLQNV-----GLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTG 172
Cdd:cd03224 88 PELTVEENLLL-----GAYARRR-AKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2418785902 173 NLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGRVV 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-223 |
2.10e-35 |
|
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: 124.62 E-value: 2.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPkaslAAVRNRKIGFVFQSfnllPHL- 100
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD----PADLRRNIGYVPQD----VTLf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 --NILKNVELplmyggmskRKRTAKAKEVLQNV---GLGDRLKHKP-------GE----LSGGQRQRVAIARAIVNDPSI 164
Cdd:cd03245 91 ygTLRDNITL---------GAPLADDERILRAAelaGVTDFVNKHPngldlqiGErgrgLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 165 LLADEPTGNLDSQSGGDILEIFTELHSqGNTVIIVTHDQAIASRAERIIKIKDGKIV-DG 223
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLLDLVDRIIVMDSGRIVaDG 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-221 |
2.83e-35 |
|
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: 123.91 E-value: 2.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 6 TENIVKDYilgKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDvlvskmpKASLAAVRNR 85
Cdd:cd03226 2 IENISFSY---KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-------KPIKAKERRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 86 KIGFVFQSFNllpHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGD-RLKHkPGELSGGQRQRVAIARAIVNDPSI 164
Cdd:cd03226 72 SIGYVMQDVD---YQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYAlKERH-PLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 165 LLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-222 |
2.88e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 125.34 E-value: 2.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCL-----DSPTDGTYYLDDVLVSKmPKASLAAVRnRKIGFVFQSFNLL 97
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYS-PDVDPIEVR-REVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 98 PHLNILKNVELPLMYGGMSKRKRT--AKAKEVLQNVGL----GDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPT 171
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2418785902 172 GNLDSQSGGDILEIFTELHSQgNTVIIVTHDQAIASR-AERIIKIKDGKIVD 222
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARvSDYVAFLYLGKLIE 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-221 |
5.48e-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: 121.77 E-value: 5.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYilGKikVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKmpkASLAAVR 83
Cdd:cd03216 1 LELRGITKRF--GG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF---ASPRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NRKIGFVFQsfnllphlnilknvelplmyggmskrkrtakakevlqnvglgdrlkhkpgeLSGGQRQRVAIARAIVNDPS 163
Cdd:cd03216 74 RAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2418785902 164 ILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIKDGKIV 221
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRlDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-221 |
7.80e-35 |
|
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: 123.49 E-value: 7.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYILGKIkvrALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLaavR 83
Cdd:cd03254 3 IEFENVNFSYDEKKP---VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NrKIGFVFQSFNLLPHlNILKNVELPLMYGGMSKRKRTAKAKEVLQNV-----GLGDRLKHKPGELSGGQRQRVAIARAI 158
Cdd:cd03254 77 S-MIGVVLQDTFLFSG-TIMENIRLGRPNATDEEVIEAAKEAGAHDFImklpnGYDTVLGENGGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2418785902 159 VNDPSILLADEPTGNLDSQSGGDILEIFTELhSQGNTVIIVTHDQAIASRAERIIKIKDGKIV 221
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKNADKILVLDDGKII 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
23-221 |
1.07e-34 |
|
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: 123.66 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYldDVLVSKMPKASLAAVRnRKIGFVFQSF--NLLPHL 100
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDV--RLFGERRGGEDVWELR-KRIGLVSPALqlRFPRDE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 NILK--------NVELPLMYGGMSKRKrtakAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTG 172
Cdd:COG1119 96 TVLDvvlsgffdSIGLYREPTDEQRER----ARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 173 NLDSQSGGDILEIFTELHSQGNTVII-VTHD-QAIASRAERIIKIKDGKIV 221
Cdd:COG1119 172 GLDLGARELLLALLDKLAAEGAPTLVlVTHHvEEIPPGITHVLLLKDGRVV 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-225 |
1.56e-34 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 123.97 E-value: 1.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYIlgkiKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLM-HILGCL--DSPTDGTYYLDDVLVSKMPKASL 79
Cdd:PRK09984 4 IIRVEKLAKTFN----QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrHLSGLItgDKSAGSHIELLGRTVQREGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 80 AAVRNR-KIGFVFQSFNLLPHLNILKNVEL------PLMYGGMS--KRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQ 150
Cdd:PRK09984 80 DIRKSRaNTGYIFQQFNLVNRLSVLENVLIgalgstPFWRTCFSwfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 151 RVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELH-SQGNTVIIVTHDQAIASR-AERIIKIKDGKIV-DGNS 225
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqNDGITVVVTLHQVDYALRyCERIVALRQGHVFyDGSS 237
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-202 |
2.11e-34 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 125.08 E-value: 2.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 20 VRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVRnRKIGFVFQsfNLLPH 99
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLR-QKIQIVFQ--NPYGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 100 LNILKNV----ELPLMYG-GMSKRKRTAKAKEVLQNVGLgdRLKHK---PGELSGGQRQRVAIARAIVNDPSILLADEPT 171
Cdd:PRK11308 105 LNPRKKVgqilEEPLLINtSLSAAERREKALAMMAKVGL--RPEHYdryPHMFSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170 180 190
....*....|....*....|....*....|...
gi 2418785902 172 GNLDSQSGGDILEIFTELHSQGNT--VIIvTHD 202
Cdd:PRK11308 183 SALDVSVQAQVLNLMMDLQQELGLsyVFI-SHD 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
3.36e-34 |
|
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: 121.84 E-value: 3.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYilGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDV-LVSKMPKASlaav 82
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsIRTDRKAAR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 rnRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDP 162
Cdd:cd03263 75 --QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 163 SILLADEPTGNLDSQSGGDILEIFTELhSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
23-220 |
4.25e-34 |
|
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: 120.01 E-value: 4.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKmpkASLAAVRnRKIGFVFQSFNLLPhlni 102
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ---WDPNELG-DHVGYLPQDDELFS---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 103 lknvelplmyggmskrkrtakaKEVLQNVglgdrlkhkpgeLSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDI 182
Cdd:cd03246 90 ----------------------GSIAENI------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 2418785902 183 LEIFTELHSQGNTVIIVTHDQAIASRAERIIKIKDGKI 220
Cdd:cd03246 136 NQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
20-206 |
6.55e-34 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 120.22 E-value: 6.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 20 VRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVsKMPKASLAAVRnRKIGFVFQSF-NLLP 98
Cdd:TIGR01166 5 PEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKGLLERR-QRVGLVFQDPdDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 99 HLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQS 178
Cdd:TIGR01166 83 AADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
|
170 180
....*....|....*....|....*...
gi 2418785902 179 GGDILEIFTELHSQGNTVIIVTHDQAIA 206
Cdd:TIGR01166 163 REQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
23-221 |
6.76e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 121.80 E-value: 6.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHIL-GCLdSPTDGTYYLDDVLVSKMPKASLAAVRnrkiGFVFQSFNLLPHLN 101
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGEL-SPDSGEVRLNGRPLADWSPAELARRR----AVLPQHSSLSFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ILKNVELPLMYGGMSKRKRTAKAKEVLQNVG---LGDRLKHkpgELSGGQRQRVAIARAIV------NDPSILLADEPTG 172
Cdd:PRK13548 93 VEEVVAMGRAPHGLSRAEDDALVAAALAQVDlahLAGRDYP---QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 173 NLDSQSGGDILEIFTEL-HSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:PRK13548 170 ALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARyADRIVLLHQGRLV 220
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-222 |
1.03e-33 |
|
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: 120.01 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYilGKIkvRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKAslaavr 83
Cdd:cd03268 1 LKTNDLTKTY--GKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NRKIGFVFQSFNLLPHLNILKNvelpLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPS 163
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTAREN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 164 ILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQA-IASRAERIIKIKDGKIVD 222
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSeIQKVADRIGIINKGKLIE 206
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-209 |
4.49e-33 |
|
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: 119.32 E-value: 4.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMH-ILGcLDSPTDGTYYLDDVLVSKMPKASLAAvrnRKIGFVFQSFNLL 97
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISG-LLPPRSGSIRFDGEDITGLPPHRIAR---LGIGYVPEGRRIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 98 PHLNILKNVELplmygGMSKRKRTAKAKEVLQNVG-----LGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTg 172
Cdd:COG0410 91 PSLTVEENLLL-----GAYARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS- 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2418785902 173 nldsqSG------GDILEIFTELHSQGNTVIIVthDQ------AIASRA 209
Cdd:COG0410 165 -----LGlaplivEEIFEIIRRLNREGVTILLV--EQnarfalEIADRA 206
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-221 |
4.86e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 120.19 E-value: 4.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 2 DIIKTENIVKDYILGKIKVR--ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMpkASL 79
Cdd:PRK13633 3 EMIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDE--ENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 80 AAVRNrKIGFVFQSfnllPHLNILKN-VELPLMYG----GMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAI 154
Cdd:PRK13633 81 WDIRN-KAGMVFQN----PDNQIVATiVEEDVAFGpenlGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 155 ARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHDQAIASRAERIIKIKDGKIV 221
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-222 |
7.69e-33 |
|
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: 118.80 E-value: 7.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 20 VRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMpkaSLAAVRnRKIGFVFQSfnllPH 99
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDL---NLRWLR-SQIGLVSQE----PV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 100 L---NILKNVELPLMYGGMSKRKRTAKAKEVLQNV-GLGDRLKHKPGE----LSGGQRQRVAIARAIVNDPSILLADEPT 171
Cdd:cd03249 88 LfdgTIAENIRYGKPDATDEEVEEAAKKANIHDFImSLPDGYDTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 172 GNLDSQSGGDILEIFTELhSQGNTVIIVTHDQAIASRAERIIKIKDGKIVD 222
Cdd:cd03249 168 SALDAESEKLVQEALDRA-MKGRTTIVIAHRLSTIRNADLIAVLQNGQVVE 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-222 |
8.76e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 123.60 E-value: 8.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYilGKikVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVS-KMPKASLAA 81
Cdd:COG3845 5 ALELRGITKRF--GG--VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 82 vrnrKIGFVFQSFNLLPHLNILKNVEL---PLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAI 158
Cdd:COG3845 81 ----GIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 159 VNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD----QAIasrAERIIKIKDGKIVD 222
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKlrevMAI---ADRVTVLRRGKVVG 221
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
21-202 |
1.12e-32 |
|
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: 123.62 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVrnrkIGFVFQSfnllPHL 100
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR----VSVCAQD----AHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 ---NILKNveLPLMYGGMSKrkrtAKAKEVLQNVGLGDRLKHKP-------GE----LSGGQRQRVAIARAIVNDPSILL 166
Cdd:TIGR02868 421 fdtTVREN--LRLARPDATD----EELWAALERVGLADWLRALPdgldtvlGEggarLSGGERQRLALARALLADAPILL 494
|
170 180 190
....*....|....*....|....*....|....*..
gi 2418785902 167 ADEPTGNLDSQSGGDILE-IFTELhsQGNTVIIVTHD 202
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEdLLAAL--SGRTVVLITHH 529
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
22-221 |
1.80e-32 |
|
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: 117.72 E-value: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLaavrNRKIGFVFQSFNLLpHLN 101
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL----RRQIGLVSQDVFLF-NDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ILKNVelplMYG--GMSKRK-----RTAKAKEVLQNV--GLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTG 172
Cdd:cd03251 92 VAENI----AYGrpGATREEveeaaRAANAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2418785902 173 NLDSQSGGDILEIFTELhSQGNTVIIVTHDQAIASRAERIIKIKDGKIV 221
Cdd:cd03251 168 ALDTESERLVQAALERL-MKNRTTFVIAHRLSTIENADRIVVLEDGKIV 215
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-221 |
2.23e-32 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 117.91 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIvkDYILGKIKVraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHIL-GCLdSPTDGTYYLDDVLVSKMPKASLAAV 82
Cdd:COG4559 2 LEAENL--SVRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGEL-TPSSGEVRLNGRPLAAWSPWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 R-----NRKIGFVFQSFNLlphlnilknVELPLMYGGMSKRKRTAKAKEVLQNVG---LGDRLKHkpgELSGGQRQRVAI 154
Cdd:COG4559 77 RavlpqHSSLAFPFTVEEV---------VALGRAPHGSSAAQDRQIVREALALVGlahLAGRSYQ---TLSGGEQQRVQL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2418785902 155 ARAIV-------NDPSILLADEPTGNLD--SQSggDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:COG4559 145 ARVLAqlwepvdGGPRWLFLDEPTSALDlaHQH--AVLRLARQLARRGGGVVAVLHDLNLAAQyADRILLLHQGRLV 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-222 |
3.06e-32 |
|
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: 122.22 E-value: 3.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 2 DIIKTENIVKDYI-LGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYL---DDVLVSKMPKA 77
Cdd:TIGR03269 278 PIIKVRNVSKRYIsVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgDEWVDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 78 SLAAVRNRKIGFVFQSFNLLPHLNILKN------VELPLMYGGMskrkrtaKAKEVLQNVGLGDR-----LKHKPGELSG 146
Cdd:TIGR03269 358 DGRGRAKRYIGILHQEYDLYPHRTVLDNlteaigLELPDELARM-------KAVITLKMVGFDEEkaeeiLDKYPDELSE 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 147 GQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILE-IFTELHSQGNTVIIVTHDQA-IASRAERIIKIKDGKIVD 222
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDfVLDVCDRAALMRDGKIVK 508
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
23-221 |
6.59e-32 |
|
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: 116.18 E-value: 6.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLaavrNRKIGFVFQSfNLLPHLNI 102
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL----RRAIGVVPQD-TVLFNDTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 103 LKNVElplmYGGMS-------KRKRTAKAKEVLQNvgLGDRLKHKPGE----LSGGQRQRVAIARAIVNDPSILLADEPT 171
Cdd:cd03253 92 GYNIR----YGRPDatdeeviEAAKAAQIHDKIMR--FPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2418785902 172 GNLDSQSGGDILEIFTELhSQGNTVIIVTHDQAIASRAERIIKIKDGKIV 221
Cdd:cd03253 166 SALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVNADKIIVLKDGRIV 214
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
21-221 |
7.49e-32 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 121.99 E-value: 7.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMpkaSLAAVRnRKIGFVFQSFNLLP-- 98
Cdd:TIGR03797 467 LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL---DVQAVR-RQLGVVLQNGRLMSgs 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 99 -HLNILKNVELPLmyggmskrkrtAKAKEVLQNVGLGDRLKHKP-----------GELSGGQRQRVAIARAIVNDPSILL 166
Cdd:TIGR03797 543 iFENIAGGAPLTL-----------DEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRKPRILL 611
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2418785902 167 ADEPTGNLDSQSGgdilEIFTE-LHSQGNTVIIVTHDQAIASRAERIIKIKDGKIV 221
Cdd:TIGR03797 612 FDEATSALDNRTQ----AIVSEsLERLKVTRIVIAHRLSTIRNADRIYVLDAGRVV 663
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-226 |
8.39e-32 |
|
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: 115.72 E-value: 8.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYilGKIKVraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMP---KASLA 80
Cdd:cd03218 1 LRAENLSKRY--GKRKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmhkRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 81 avrnrkIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLgDRLKHKPG-ELSGGQRQRVAIARAIV 159
Cdd:cd03218 77 ------IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHI-THLRKSKAsSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2418785902 160 NDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIKDGKIV-DGNSN 226
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNvRETLSITDRAYIIYEGKVLaEGTPE 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-222 |
8.47e-32 |
|
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: 116.05 E-value: 8.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLaavrNRKIGFVFQSfNLLPHLN 101
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL----RRQVGVVLQE-NVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ILKNVELplMYGGMSKRK-----RTAKAKEVLQNV--GLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNL 174
Cdd:cd03252 92 IRDNIAL--ADPGMSMERvieaaKLAGAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2418785902 175 DSQSGGDILEIFTELhSQGNTVIIVTHDQAIASRAERIIKIKDGKIVD 222
Cdd:cd03252 170 DYESEHAIMRNMHDI-CAGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-201 |
1.29e-31 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 121.31 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPtdGTYYLDDVLVSKMPkasLAAVRNRKI-GFVFQSFNLLPHLN 101
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLLNGMP---IDAKEMRAIsAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ilknVELPLMYGGM-------SKRKRTAKAKEVLQNVGLGDRLKHKPGE------LSGGQRQRVAIARAIVNDPSILLAD 168
Cdd:TIGR00955 116 ----VREHLMFQAHlrmprrvTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190
....*....|....*....|....*....|...
gi 2418785902 169 EPTGNLDSQSGGDILEIFTELHSQGNTVIIVTH 201
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-221 |
1.42e-31 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 116.09 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 1 MDIIKTENIVKDY-----ILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMP 75
Cdd:COG4167 2 SALLEVRNLSKTFkyrtgLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 76 kaslAAVRNRKIGFVFQ----SFNllPHLNILKNVELPLMYG-GMSKRKRTAKAKEVLQNVGL-GDRLKHKPGELSGGQR 149
Cdd:COG4167 82 ----YKYRCKHIRMIFQdpntSLN--PRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2418785902 150 QRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELH-SQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQeKLGISYIYVSQHLGIVKHiSDKVLVMHQGEVV 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-226 |
1.56e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 115.91 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLD-DVLVSKMPKASLAAVRNRK-IGFVFQSFNLLPHL 100
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgKVLYFGKDIFQIDAIKLRKeVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 NILKNVELPLMYGGMSKRKRTAK-AKEVLQNVGLG----DRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLD 175
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIKKiVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2418785902 176 SQSGGDILEIFTELHSQGNTVIIVTHDQAIASRAERIIKIKDGKIVD-GNSN 226
Cdd:PRK14246 186 IVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEwGSSN 237
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-201 |
1.76e-31 |
|
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: 113.80 E-value: 1.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 14 ILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLdspTDGTYYLDDVLVSKMPKaSLAAVRnRKIGFVFQS 93
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGR---RTGLGVSGEVLINGRPL-DKRSFR-KIIGYVPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 94 FNLLPHLNILKNvelpLMYggmskrkrTAKakevLQNvglgdrlkhkpgeLSGGQRQRVAIARAIVNDPSILLADEPTGN 173
Cdd:cd03213 91 DILHPTLTVRET----LMF--------AAK----LRG-------------LSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
170 180
....*....|....*....|....*...
gi 2418785902 174 LDSQSGGDILEIFTELHSQGNTVIIVTH 201
Cdd:cd03213 142 LDSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-222 |
2.49e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 116.03 E-value: 2.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLV-SKMPKASLAAVRnRKIGFVFQsfnlLPHL 100
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRPVR-KRIGMVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 NILK-NVELPLMYG----GMSKRKRTAKAKEVLQNVGLG-DRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNL 174
Cdd:PRK13646 97 QLFEdTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2418785902 175 DSQSGGDILEIFTELH-SQGNTVIIVTHD-QAIASRAERIIKIKDGKIVD 222
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQtDENKTIILVSHDmNEVARYADEVIVMKEGSIVS 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-221 |
4.11e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 114.41 E-value: 4.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYilGKIKVraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAavr 83
Cdd:COG4604 2 IEIKNVSKRY--GGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 nRKIGFVFQSfnllPHLNILKNVELPLMYGGM--SKRKRTAKAKEV----LQNVGLGDrLKHKP-GELSGGQRQRVAIAR 156
Cdd:COG4604 75 -KRLAILRQE----NHINSRLTVRELVAFGRFpySKGRLTAEDREIideaIAYLDLED-LADRYlDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2418785902 157 AIVNDPSILLADEPTGNLDSQSGGDILEIFTEL-HSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDINFASCyADHIVAMKDGRVV 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-221 |
9.22e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 114.06 E-value: 9.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYilgKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYlddVLVSKMPKASLAAV 82
Cdd:PRK13647 4 IIEVEDLHFRY---KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVK---VMGREVNAENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RNrKIGFVFQSfnllPHLNILK-NVELPLMYG----GMSKRKRTAKAKEVLQNVGLGDrLKHK-PGELSGGQRQRVAIAR 156
Cdd:PRK13647 78 RS-KVGLVFQD----PDDQVFSsTVWDDVAFGpvnmGLDKDEVERRVEEALKAVRMWD-FRDKpPYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2418785902 157 AIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVL 217
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
23-222 |
2.60e-30 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 117.92 E-value: 2.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLaavrNRKIGFVFQSfNLLPHLNI 102
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWL----RRQMGVVLQE-NVLFSRSI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 103 LKNVEL--PlmygGMSKRK-----RTAKAKEVLQNV--GLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGN 173
Cdd:TIGR01846 548 RDNIALcnP----GAPFEHvihaaKLAGAHDFISELpqGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSA 623
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2418785902 174 LDSQSGGDILEIFTELhSQGNTVIIVTHDQAIASRAERIIKIKDGKIVD 222
Cdd:TIGR01846 624 LDYESEALIMRNMREI-CRGRTVIIIAHRLSTVRACDRIIVLEKGQIAE 671
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
22-221 |
5.13e-30 |
|
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: 109.71 E-value: 5.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMH-ILGCLDsPTDGTYYLDDVLVSKMPKAslaavRNRKIGFVFQSfnllPHL 100
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQlLTGDLK-PQQGEITLDGVPVSDLEKA-----LSSLISVLNQR----PYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 NilknvelplmyggmskrkrtakAKEVLQNVGLgdrlkhkpgELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGG 180
Cdd:cd03247 87 F----------------------DTTLRNNLGR---------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2418785902 181 DILEIFTElHSQGNTVIIVTHDQAIASRAERIIKIKDGKIV 221
Cdd:cd03247 136 QLLSLIFE-VLKDKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-221 |
8.42e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 111.62 E-value: 8.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGkikVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTyylddVLVSKMPKASLAAV 82
Cdd:PRK13644 1 MIRLENVSYSYPDG---TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGK-----VLVSGIDTGDFSKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RN-RKI-GFVFQSfnllPHLNIL-KNVELPLMYGG-------MSKRKRTAKAkevLQNVGLGDRLKHKPGELSGGQRQRV 152
Cdd:PRK13644 73 QGiRKLvGIVFQN----PETQFVgRTVEEDLAFGPenlclppIEIRKRVDRA---LAEIGLEKYRHRSPKTLSGGQGQCV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2418785902 153 AIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASRAERIIKIKDGKIV 221
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-221 |
1.07e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 115.69 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLaavRNRkIGFVFQSFNLLPHlN 101
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---RQA-ISVVSQRVHLFSA-T 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ILKNVELPlmyggmSKRKRTAKAKEVLQNVGLGDRLKHKPG----------ELSGGQRQRVAIARAIVNDPSILLADEPT 171
Cdd:PRK11160 430 LRDNLLLA------APNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 172 GNLDSQSGGDILEIFTElHSQGNTVIIVTHD-QAIASrAERIIKIKDGKIV 221
Cdd:PRK11160 504 EGLDAETERQILELLAE-HAQNKTVLMITHRlTGLEQ-FDRICVMDNGQII 552
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
26-202 |
1.61e-29 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 111.01 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 26 IDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVRnRKIGFVFQSFNLLPHLNILKN 105
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 106 VELPLmyggmskRKRTAKAKEVLQN--------VGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQ 177
Cdd:PRK11831 105 VAYPL-------REHTQLPAPLLHStvmmkleaVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPI 177
|
170 180
....*....|....*....|....*.
gi 2418785902 178 SGGDILEIFTEL-HSQGNTVIIVTHD 202
Cdd:PRK11831 178 TMGVLVKLISELnSALGVTCVVVSHD 203
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-221 |
1.85e-29 |
|
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: 109.29 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYIlgkiKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTyylddVLVSKMPKAslAAVR 83
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGE-----VLFDGKPLD--IAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NRkIGFVFQSFNLLPHLNILKNvelpLMY----GGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIV 159
Cdd:cd03269 70 NR-IGYLPEERGLYPKMKVIDQ----LVYlaqlKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2418785902 160 NDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
28-223 |
3.42e-29 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 108.78 E-value: 3.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 28 LQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTyylddVLVSKMPKASlaavRNRKIGFVFQSFNLLPHLNIlkNVE 107
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGT-----VKVAGASPGK----GWRHIGYVPQRHEFAWDFPI--SVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 108 LPLMYG-----GMSKRKRTAKAKEV---LQNVGLGDrLKHKP-GELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQS 178
Cdd:TIGR03771 70 HTVMSGrtghiGWLRRPCVADFAAVrdaLRRVGLTE-LADRPvGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2418785902 179 GGDILEIFTELHSQGNTVIIVTHD--QAIASrAERIIKIKDGKIVDG 223
Cdd:TIGR03771 149 QELLTELFIELAGAGTAILMTTHDlaQAMAT-CDRVVLLNGRVIADG 194
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-221 |
3.98e-29 |
|
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: 113.74 E-value: 3.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYIlgkiKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDS--PTDG------------------- 62
Cdd:TIGR03269 1 IEVKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGriiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 63 -----------TYYLDDVLVSKMPKASLAAVRnRKIGFVFQ-SFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQN 130
Cdd:TIGR03269 77 kvgepcpvcggTLEPEEVDFWNLSDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 131 VGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTEL-HSQGNTVIIVTH-DQAIASR 208
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHwPEVIEDL 235
|
250
....*....|...
gi 2418785902 209 AERIIKIKDGKIV 221
Cdd:TIGR03269 236 SDKAIWLENGEIK 248
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-223 |
4.16e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 110.67 E-value: 4.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYilGKIKVraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDvlvskMPKASLAAV 82
Cdd:PRK13537 7 PIDFRNVEKRY--GDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-----EPVPSRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RNRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDP 162
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2418785902 163 SILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDG-KIVDG 223
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEGrKIAEG 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
23-224 |
1.01e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.47 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTyylddvlVSKMPKAslaavrnrKIGFVFQSFNLLPHLNI 102
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGE-------VSIPKGL--------RIGYLPQEPPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 103 LKNV------------ELPLMYGGMSKRKRT--------------------AKAKEVLQNVGLGDRLKHKP-GELSGGQR 149
Cdd:COG0488 79 LDTVldgdaelraleaELEELEAKLAEPDEDlerlaelqeefealggweaeARAEEILSGLGFPEEDLDRPvSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 150 QRVAIARAIVNDPSILLADEPTGNLDSQSggdI--LEIFteLHSQGNTVIIVTHDqaiasR------AERIIKIKDGKIV 221
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLES---IewLEEF--LKNYPGTVLVVSHD-----RyfldrvATRILELDRGKLT 228
|
....*
gi 2418785902 222 --DGN 224
Cdd:COG0488 229 lyPGN 233
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
23-221 |
1.70e-28 |
|
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: 112.15 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHIL-GCLdSPTDGTYYLDDVLVSKMPKASLAavrnRKIGFVFQSFNLLP--- 98
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvGVW-PPTAGSVRLDGADLSQWDREELG----RHIGYLPQDVELFDgti 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 99 ------------------------HLNILKnveLPLMY------GGMSkrkrtakakevlqnvglgdrlkhkpgeLSGGQ 148
Cdd:COG4618 423 aeniarfgdadpekvvaaaklagvHEMILR---LPDGYdtrigeGGAR---------------------------LSGGQ 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2418785902 149 RQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASRAERIIKIKDGKIV 221
Cdd:COG4618 473 RQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-222 |
2.15e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 111.72 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKST----LMHILgcldsPTDGTYYLDDVLVSKMPKASLAAVRnRKIGFVFQSFN-- 95
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVR-HRIQVVFQDPNss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 96 LLPHLNILKNVE--LPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHK-PGELSGGQRQRVAIARAIVNDPSILLADEPTG 172
Cdd:PRK15134 375 LNPRLNVLQIIEegLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2418785902 173 NLDSQSGGDILEIFTELHSQGN-TVIIVTHD-QAIASRAERIIKIKDGKIVD 222
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQlAYLFISHDlHVVRALCHQVIVLRQGEVVE 506
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
20-222 |
3.12e-28 |
|
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: 111.35 E-value: 3.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 20 VRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMpkaSLAAVRnRKIGFVFQSFNLLPH 99
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY---TLASLR-RQVALVSQDVVLFND 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 100 lNILKNVELPLMYGGMSKRKRTAKAKEVLQNV------GLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGN 173
Cdd:TIGR02203 421 -TIANNIAYGRTEQADRAEIERALAAAYAQDFvdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSA 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2418785902 174 LDSQSGGDILEIFTELHsQGNTVIIVTHDQAIASRAERIIKIKDGKIVD 222
Cdd:TIGR02203 500 LDNESERLVQAALERLM-QGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-221 |
4.64e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 108.01 E-value: 4.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDV-----------LVSKMPKASLAAVRNRK- 86
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyigdkknnhelITNPYSKKIKNFKELRRr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 87 IGFVFQsfnlLPHLNILKN-VELPLMYG----GMSKRKRTAKAKEVLQNVGLGDR-LKHKPGELSGGQRQRVAIARAIVN 160
Cdd:PRK13631 118 VSMVFQ----FPEYQLFKDtIEKDIMFGpvalGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2418785902 161 DPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIKDGKIV 221
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTmEHVLEVADEVIVMDKGKIL 255
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-225 |
5.26e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 107.40 E-value: 5.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTLMHIL-GCLDSPTDGTYYLDDVLVSKMPKASLAAVRNRKIGFVFQsfnlLPH 99
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTnGLIISETGQTIVGDYAIPANLKKIKEVKRLRKEIGLVFQ----FPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 100 LNILKN-VELPLMYG----GMSKRKRTAKAKEVLQNVGLG-DRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGN 173
Cdd:PRK13645 101 YQLFQEtIEKDIAFGpvnlGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 174 LDSQSGGDILEIFTELH-SQGNTVIIVTH--DQAIASrAERIIKIKDGKIVDGNS 225
Cdd:PRK13645 181 LDPKGEEDFINLFERLNkEYKKRIIMVTHnmDQVLRI-ADEVIVMHEGKVISIGS 234
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-224 |
7.94e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 107.12 E-value: 7.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYilGKikVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMH-ILGCLDsPTDGTYYLDDVLVSkmpkaslAA 81
Cdd:COG4152 1 MLELKGLTKRF--GD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRiILGILA-PDSGEVLWDGEPLD-------PE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 82 VRNRkIGFvfqsfnlLP----------------HLNILKnvelplmygGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELS 145
Cdd:COG4152 69 DRRR-IGY-------LPeerglypkmkvgeqlvYLARLK---------GLSKAEAKRRADEWLERLGLGDRANKKVEELS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 146 GGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV-DG 223
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVlSG 211
|
.
gi 2418785902 224 N 224
Cdd:COG4152 212 S 212
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-201 |
9.20e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 105.50 E-value: 9.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 1 MDIIKTENIVKDYilGKIKVraLNGIDLQIQKGEFVAIMGPSGSGKSTL--MhILGcLDSPTDGTYYLDDVLVSKMPkas 78
Cdd:COG1137 1 MMTLEAENLVKSY--GKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTfyM-IVG-LVKPDSGRIFLDGEDITHLP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 79 lAAVRNRK-IGF------VFQsfnllpHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQR 151
Cdd:COG1137 72 -MHKRARLgIGYlpqeasIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2418785902 152 VAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTH 201
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDH 194
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-220 |
2.34e-27 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 108.97 E-value: 2.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDdvlvskmpkasLAAVRN-------RKIGFVF 91
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLD-----------GADLKQwdretfgKHIGYLP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 92 QSFNLLPHL---NILK---NVELPLMYGGmskrKRTAKAKEVLQNV------GLGDRlkhkPGELSGGQRQRVAIARAIV 159
Cdd:TIGR01842 399 QDVELFPGTvaeNIARfgeNADPEKIIEA----AKLAGVHELILRLpdgydtVIGPG----GATLSGGQRQRIALARALY 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 160 NDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASRAERIIKIKDGKI 220
Cdd:TIGR01842 471 GDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-221 |
2.57e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 104.71 E-value: 2.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYilGKIKVraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAav 82
Cdd:PRK11231 2 TLRTENLTVGY--GTKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 rnRKIGFVFQ--------------SFNLLPHLNilknvelplMYGGMSK--RKRTAKAKEVLQNVGLGDRLKhkpGELSG 146
Cdd:PRK11231 76 --RRLALLPQhhltpegitvrelvAYGRSPWLS---------LWGRLSAedNARVNQAMEQTRINHLADRRL---TDLSG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2418785902 147 GQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:PRK11231 142 GQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVM 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-225 |
3.75e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 108.25 E-value: 3.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKS-TLMHILGCLDSPTdGTYYLDDVL-----VSKMPKASLAAVRNRKIGFVFQSf 94
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPP-VVYPSGDIRfhgesLLHASEQTLRGVRGNKIAMIFQE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 95 nLLPHLNILKNVELPL-----MYGGMSKRKRTAKAKEVLQNVGL---GDRLKHKPGELSGGQRQRVAIARAIVNDPSILL 166
Cdd:PRK15134 101 -PMVSLNPLHTLEKQLyevlsLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 167 ADEPTGNLDSQSGGDILEIFTELHSQGN-TVIIVTHDQAIASR-AERIIKIKDGKIVDGNS 225
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQELNmGLLFITHNLSIVRKlADRVAVMQNGRCVEQNR 240
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-223 |
4.77e-27 |
|
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: 103.57 E-value: 4.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDY--------ILGKIK---------VRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYL 66
Cdd:cd03267 1 IEVSNLSKSYrvyskepgLIGSLKslfkrkyreVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 67 DDVLVSKMPKASLaavrnRKIGFVF-------------QSFNLLPHLNILKNVELplmyggmskRKRTAKAKEVLQnvgL 133
Cdd:cd03267 81 AGLVPWKRRKKFL-----RRIGVVFgqktqlwwdlpviDSFYLLAAIYDLPPARF---------KKRLDELSELLD---L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 134 GDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHD-QAIASRAER 211
Cdd:cd03267 144 EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYmKDIEALARR 223
|
250
....*....|...
gi 2418785902 212 IIKIKDGKIV-DG 223
Cdd:cd03267 224 VLVIDKGRLLyDG 236
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
26-221 |
7.27e-27 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 105.34 E-value: 7.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 26 IDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDD-VLVSKMPKASLAAVRnRKIGFVFQSFNLLPHLNILK 104
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrVLFDAEKGICLPPEK-RRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 105 NvelpLMYGgMsKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILE 184
Cdd:PRK11144 96 N----LRYG-M-AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 2418785902 185 IFTELHSQGNTVII-VTHD-QAIASRAERIIKIKDGKIV 221
Cdd:PRK11144 170 YLERLAREINIPILyVSHSlDEILRLADRVVVLEQGKVK 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-223 |
1.22e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 104.53 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYiLGKIKVralNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTyylddVLVSKMPKASLAAVR 83
Cdd:PRK13536 42 IDLAGVSKSY-GDKAVV---NGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGK-----ITVLGVPVPARARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NRKIGFVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPS 163
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2418785902 164 ILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDG-KIVDG 223
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERlCDRLCVLEAGrKIAEG 254
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
21-222 |
1.61e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 104.05 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKS-TLMHILGCLDSPtdGTYYLDDVLVSKMPKASLAAVRNRKI-----GFVFQsf 94
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKLEFNGQDLQRISEKERRNLvgaevAMIFQ-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 95 NLLPHLNILKNVELPLM-----YGGMSKRKRTAKAKEVLQNVGLGD---RLKHKPGELSGGQRQRVAIARAIVNDPSILL 166
Cdd:PRK11022 97 DPMTSLNPCYTVGFQIMeaikvHQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 167 ADEPTGNLDSQSGGDILEIFTELHSQGN-TVIIVTHDQA-IASRAERIIKIKDGKIVD 222
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDLAlVAEAAHKIIVMYAGQVVE 234
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-221 |
2.36e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 102.37 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 15 LGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAavrnRKIGFVFQSF 94
Cdd:PRK10253 15 LGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 95 NLLPHLNILKNV------ELPLMyggMSKRKRTAKA-KEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLA 167
Cdd:PRK10253 91 TTPGDITVQELVargrypHQPLF---TRWRKEDEEAvTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2418785902 168 DEPTGNLDSQSGGDILEIFTELH-SQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQACRyASHLIALREGKIV 223
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
22-171 |
3.20e-26 |
|
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: 101.06 E-value: 3.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAvrnRKIGFVFQSFNLLPHLN 101
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAR---AGIAYVPQGREIFPRLT 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2418785902 102 ILKNVELPLMYGGMSKRKRTAKAKE---VLQnvglgDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPT 171
Cdd:TIGR03410 92 VEENLLTGLAALPRRSRKIPDEIYElfpVLK-----EMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
20-202 |
5.24e-26 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 102.88 E-value: 5.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 20 VRALNGIDLQIQKGEFVAIMGPSGSGKS-TLMHILGCLDSP--TDGTYYLDDVLVSKMPKASLAAVRNRKIGFVFQ---- 92
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEKELNKLRAEQISMIFQdpmt 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 93 SFNllPHLNILKNV-ELPLMYGGMSKRKRTAKAKEVLQNVGLGD---RLKHKPGELSGGQRQRVAIARAIVNDPSILLAD 168
Cdd:PRK09473 109 SLN--PYMRVGEQLmEVLMLHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190
....*....|....*....|....*....|....*
gi 2418785902 169 EPTGNLDSQSGGDILEIFTELHSQGNTVII-VTHD 202
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREFNTAIImITHD 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
19-225 |
7.11e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 101.42 E-value: 7.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVRNrKIGFVFQS-FNLL 97
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIRE-KVGIVFQNpDNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 98 PHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQ 177
Cdd:PRK13640 98 VGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2418785902 178 SGGDILEIFTELHSQGN-TVIIVTHDQAIASRAERIIKIKDGKIVDGNS 225
Cdd:PRK13640 178 GKEQILKLIRKLKKKNNlTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-220 |
7.55e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 101.37 E-value: 7.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLaavrnRK-IGFVFQSFNLLPHL 100
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL-----RKhIGIVFQNPDNQFVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 NILK-NVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSG 179
Cdd:PRK13648 99 SIVKyDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2418785902 180 GDILEIFTELHSQGN-TVIIVTHDQAIASRAERIIKIKDGKI 220
Cdd:PRK13648 179 QNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
6-225 |
7.73e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.62 E-value: 7.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 6 TENI--VKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLD------SPTDGTYYLDDVLVSkmPKA 77
Cdd:PRK14239 2 TEPIlqVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpevTITGSIVYNGHNIYS--PRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 78 SLAAVRnRKIGFVFQSFNLLPhLNILKNVELPLMYGGMSKRKRTAKAKE-VLQNVGL----GDRLKHKPGELSGGQRQRV 152
Cdd:PRK14239 80 DTVDLR-KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEkSLKGASIwdevKDRLHDSALGLSGGQQQRV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2418785902 153 AIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQgNTVIIVTHDQAIASR-AERIIKIKDGKIVDGNS 225
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRiSDRTGFFLDGDLIEYND 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-221 |
1.43e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.55 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYiLGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDvlvSKMPKASLAAV 82
Cdd:PRK13642 4 ILEVENLVFKY-EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RnRKIGFVFQS-FNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVND 161
Cdd:PRK13642 80 R-RKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 162 PSILLADEPTGNLDSQSGGDILEIFTELHSQGN-TVIIVTHDQAIASRAERIIKIKDGKIV 221
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASSDRILVMKAGEII 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
10-222 |
2.23e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 102.23 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 10 VKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTyylddVLVSKMPKASL-AAVRNRKIG 88
Cdd:PRK09536 6 VSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGT-----VLVAGDDVEALsARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 89 FVFQ----SFNL----------LPHLNilknvelplMYGGMSKRKRTAkAKEVLQNVGLgDRLKHKP-GELSGGQRQRVA 153
Cdd:PRK09536 81 SVPQdtslSFEFdvrqvvemgrTPHRS---------RFDTWTETDRAA-VERAMERTGV-AQFADRPvTSLSGGERQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 154 IARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKIVD 222
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRA 219
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-223 |
2.83e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 103.26 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLaavrNRKIGFVFQSfNLLP 98
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVGQE-PVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 99 HLNILKNVELPLMYGGMSKRKRTAKAKEVLQNV-----GLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGN 173
Cdd:TIGR00958 568 SGSVRENIAYGLTDTPDEEIMAAAKAANAHDFImefpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 174 LDSQSGgdilEIFTELHSQGN-TVIIVTHDQAIASRAERIIKIKDGKIVDG 223
Cdd:TIGR00958 648 LDAECE----QLLQESRSRASrTVLLIAHRLSTVERADQILVLKKGSVVEM 694
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-221 |
2.94e-25 |
|
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: 102.98 E-value: 2.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVrnrkIGFVFQS---FNLLPH 99
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA----IGIVPQDtvlFNDTIA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 100 LNILknvelplmYG--GMSKrkrtAKAKEVLQNVGLGDRLKHKP-------GE----LSGGQRQRVAIARAIVNDPSILL 166
Cdd:COG5265 450 YNIA--------YGrpDASE----EEVEAAARAAQIHDFIESLPdgydtrvGErglkLSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 167 ADEPTGNLDSQSGGDILEIFTELhSQGNTVIIVTHDQAIASRAERIIKIKDGKIV 221
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREV-ARGRTTLVIAHRLSTIVDADEILVLEAGRIV 571
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-221 |
3.21e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.92 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGkikVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAV 82
Cdd:PRK13636 5 ILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RNrkIGFVFQS-FNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLgDRLKHKPGE-LSGGQRQRVAIARAIVN 160
Cdd:PRK13636 82 ES--VGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2418785902 161 DPSILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHD-QAIASRAERIIKIKDGKIV 221
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDiDIVPLYCDNVFVMKEGRVI 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-201 |
3.40e-25 |
|
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: 98.50 E-value: 3.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYylDDVLVSKMPKaSLAAVRNRkIGFVFQSFNLLP 98
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTS--GQILFNGQPR-KPDQFQKC-VAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 99 HLNilknVELPLMYGGMSK---RKRTAKAKEVLQNVGLGD----RLKHK--PGeLSGGQRQRVAIARAIVNDPSILLADE 169
Cdd:cd03234 95 GLT----VRETLTYTAILRlprKSSDAIRKKRVEDVLLRDlaltRIGGNlvKG-ISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190
....*....|....*....|....*....|..
gi 2418785902 170 PTGNLDSQSGGDILEIFTELHSQGNTVIIVTH 201
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
25-222 |
3.57e-25 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 99.00 E-value: 3.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 25 GIDLQIQKGEFVAIMGPSGSGKS-TLMHILGCLdsP-----TDGTYYLDDVLVSkmpkasLAAVRNRKIGFVFQ----SF 94
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSlTCAAALGIL--PagvrqTAGRVLLDGKPVA------PCALRGRKIATIMQnprsAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 95 NllPHLNILKNVELPLMYGGmsKRKRTAKAKEVLQNVGLGDR---LKHKPGELSGGQRQRVAIARAIVNDPSILLADEPT 171
Cdd:PRK10418 93 N--PLHTMHTHARETCLALG--KPADDATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2418785902 172 GNLDSQSGGDILEIFTEL-HSQGNTVIIVTHDQAIASR-AERIIKIKDGKIVD 222
Cdd:PRK10418 169 TDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVE 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
23-220 |
7.07e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 98.65 E-value: 7.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKmpkASLAAVRnRKIGFVFQS-FNLLPHLN 101
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE---ENVWDIR-HKIGMVFQNpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGD 181
Cdd:PRK13650 99 VEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2418785902 182 ILEIFTELHSQGN-TVIIVTHDQAIASRAERIIKIKDGKI 220
Cdd:PRK13650 179 LIKTIKGIRDDYQmTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-219 |
7.44e-25 |
|
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: 96.77 E-value: 7.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTL-MHILGCLDsPTDGTYYLddvlvskmpkaslaavrNRKIGFVFQSfnllPHL 100
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLlSALLGELE-KLSGSVSV-----------------PGSIAYVSQE----PWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 -------NILknvelplmyggMSKRKRTAKAKEVLQNVGLGDRLKHKP-------GE----LSGGQRQRVAIARAIVNDP 162
Cdd:cd03250 78 qngtireNIL-----------FGKPFDEERYEKVIKACALEPDLEILPdgdlteiGEkginLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2418785902 163 SILLADEPTGNLDSQSGGDILE--IFTELhSQGNTVIIVTHDQAIASRAERIIKIKDGK 219
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRHIFEncILGLL-LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-221 |
1.60e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 96.45 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 15 LGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTyylddVLVSKMPKASLAAvrnrKIGFvfqsf 94
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGT-----VTVRGRVSSLLGL----GGGF----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 95 nlLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTgnl 174
Cdd:cd03220 96 --NPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVL--- 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2418785902 175 dsqSGGDI------LEIFTELHSQGNTVIIVTHDQ-AIASRAERIIKIKDGKIV 221
Cdd:cd03220 171 ---AVGDAafqekcQRRLRELLKQGKTVILVSHDPsSIKRLCDRALVLEKGKIR 221
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-224 |
2.52e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 96.69 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 2 DIIKTENIVKDYILGKIK------------------VRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGT 63
Cdd:COG1134 3 SMIEVENVSKSYRLYHEPsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 64 yylddVLVsKMPKASLAAVrnrkiGFVFQsfnllPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGE 143
Cdd:COG1134 83 -----VEV-NGRVSALLEL-----GAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 144 LSGGQRQRVAIARAIVNDPSILLADEPTgnldsqSGGDI------LEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIK 216
Cdd:COG1134 147 YSSGMRARLAFAVATAVDPDILLVDEVL------AVGDAafqkkcLARIRELRESGRTVIFVSHSmGAVRRLCDRAIWLE 220
|
....*....
gi 2418785902 217 DGKIV-DGN 224
Cdd:COG1134 221 KGRLVmDGD 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
4.69e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.41 E-value: 4.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 1 MDIIKTENIVKDYilgKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGtyyldDVLVSKMP--KAS 78
Cdd:PRK13652 1 MHLIETRDLCYSY---SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSG-----SVLIRGEPitKEN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 79 LAAVRnRKIGFVFQSfnllPHLNILK-NVELPLMYG----GMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVA 153
Cdd:PRK13652 73 IREVR-KFVGLVFQN----PDDQIFSpTVEQDIAFGpinlGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 154 IARAIVNDPSILLADEPTGNLDSQSGGDILEIFTEL-HSQGNTVIIVTHD-QAIASRAERIIKIKDGKIV 221
Cdd:PRK13652 148 IAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQlDLVPEMADYIYVMDKGRIV 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-219 |
5.49e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 99.23 E-value: 5.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 8 NIVKDYIlgkiKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILgCLDSPTdGTYYLDDVLVSKMPKASLAAVRNRK- 86
Cdd:PRK13549 10 NITKTFG----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL-SGVYPH-GTYEGEIIFEGEELQASNIRDTERAg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 87 IGFVFQSFNLLPHLNILKNVEL---PLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPS 163
Cdd:PRK13549 84 IAIIHQELALVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2418785902 164 ILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIKDGK 219
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKlNEVKAISDTICVIRDGR 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-224 |
7.84e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 96.69 E-value: 7.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDY--------ILGKIK---------VRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHIL-GCLdSPTDGTy 64
Cdd:COG4586 1 IIEVENLSKTYrvyekepgLKGALKglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtGIL-VPTSGE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 65 ylddVLVSKM-P---KASLAavrnRKIGFVF-------------QSFNLLPHlnilknvelplMYgGMSK---RKRTAKA 124
Cdd:COG4586 79 ----VRVLGYvPfkrRKEFA----RRIGVVFgqrsqlwwdlpaiDSFRLLKA-----------IY-RIPDaeyKKRLDEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 125 KEVLqnvGLGDrLKHKP-GELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELH-SQGNTVIIVTHD 202
Cdd:COG4586 139 VELL---DLGE-LLDTPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNrERGTTILLTSHD 214
|
250 260
....*....|....*....|....
gi 2418785902 203 QA-IASRAERIIKIKDGKIV-DGN 224
Cdd:COG4586 215 MDdIEALCDRVIVIDHGRIIyDGS 238
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
21-221 |
1.56e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 94.61 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTLmhiLGCLDS---PTDGT--YYLDDVLVSKMpkASLAAVRNRKI-----GFV 90
Cdd:PRK11701 20 KGCRDVSFDLYPGEVLGIVGESGSGKTTL---LNALSArlaPDAGEvhYRMRDGQLRDL--YALSEAERRRLlrtewGFV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 91 FQsfN----LLPHLNILKNVELPLM------YGgmskRKRtAKAKEVLQNVGLG-DRLKHKPGELSGGQRQRVAIARAIV 159
Cdd:PRK11701 95 HQ--HprdgLRMQVSAGGNIGERLMavgarhYG----DIR-ATAGDWLERVEIDaARIDDLPTTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 160 NDPSILLADEPTGNLDSQSGGDILEIFTEL-HSQGNTVIIVTHDQAIAsR--AERIIKIKDGKIV 221
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVA-RllAHRLLVMKQGRVV 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-222 |
1.61e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 97.67 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 20 VRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVS-KMPKASLAAvrnrKIGFVFQSFNLLP 98
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAA----GVAIIYQELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 99 HLNILKNV---ELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLD 175
Cdd:PRK11288 93 EMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2418785902 176 SQSGGDILEIFTELHSQGNTVIIVTHdqaiasRAERIIKI-------KDGKIVD 222
Cdd:PRK11288 173 AREIEQLFRVIRELRAEGRVILYVSH------RMEEIFALcdaitvfKDGRYVA 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-208 |
1.68e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.85 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTlmhILGCLDSPTD---------GTYYLDDVLVSkmPKASLAAVRnRKIGFVFQ 92
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKST---ILRCFNRLNDlipgfrvegKVTFHGKNLYA--PDVDPVEVR-RRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 93 SFNLLP---HLNILKNVELPLMYGGMSKRKRTAKAKEVLQNvGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADE 169
Cdd:PRK14243 99 KPNPFPksiYDNIAYGARINGYKGDMDELVERSLRQAALWD-EVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 2418785902 170 PTGNLDSQSGGDILEIFTELHSQgNTVIIVTHDQAIASR 208
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAAR 215
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
37-222 |
3.54e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.39 E-value: 3.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 37 AIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVRN--RKIGFVFQSFNLLPhLNILKNVELPLMYGG 114
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEfrRRVGMLFQRPNPFP-MSIMDNVLAGVRAHK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 115 MSKRKR-TAKAKEVLQNVGL----GDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTEL 189
Cdd:PRK14271 130 LVPRKEfRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL 209
|
170 180 190
....*....|....*....|....*....|....
gi 2418785902 190 HSQgNTVIIVTHDQAIASR-AERIIKIKDGKIVD 222
Cdd:PRK14271 210 ADR-LTVIIVTHNLAQAARiSDRAALFFDGRLVE 242
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
23-221 |
4.97e-23 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 96.55 E-value: 4.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAvrnrKIGFVFQSFNLLPHlNI 102
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLAN----SVAMVDQDIFLFEG-TV 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 103 LKNveLPLMYGGMSKRK--RTAKAKEVLQNV-----GLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLD 175
Cdd:TIGR03796 570 RDN--LTLWDPTIPDADlvRACKDAAIHDVItsrpgGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALD 647
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2418785902 176 SQSGGDILEiftELHSQGNTVIIVTHDQAIASRAERIIKIKDGKIV 221
Cdd:TIGR03796 648 PETEKIIDD---NLRRRGCTCIIVAHRLSTIRDCDEIIVLERGKVV 690
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
22-221 |
5.11e-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: 92.56 E-value: 5.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPkasLAAVRNRkIGFVFQS-------- 93
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSR-ISIIPQDpvlfsgti 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 94 -FNLLPH--------LNILKNVELplmyggmskrkrtakaKEVLQNV--GLGDRLKHKPGELSGGQRQRVAIARAIVNDP 162
Cdd:cd03244 95 rSNLDPFgeysdeelWQALERVGL----------------KEFVESLpgGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 163 SILLADEPTGNLDSQSGGDILE-IFTELHsqGNTVIIVTHD-QAIASrAERIIKIKDGKIV 221
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKtIREAFK--DCTVLTIAHRlDTIID-SDRILVLDKGRVV 216
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-221 |
5.17e-23 |
|
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: 91.82 E-value: 5.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMH-ILGCLD-SPTDGTYYLDDVLVSKMPkaslAAVRNRK-IGFVFQSfnllph 99
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKtIMGHPKyEVTEGEILFKGEDITDLP----PEERARLgIFLAFQY------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 100 lnilknvelPLMYGGMskrkrtaKAKEVLQNVGLGdrlkhkpgeLSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSG 179
Cdd:cd03217 86 ---------PPEIPGV-------KNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2418785902 180 GDILEIFTELHSQGNTVIIVTHDQAIAS--RAERIIKIKDGKIV 221
Cdd:cd03217 141 RLVAEVINKLREEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIV 184
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-221 |
7.57e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 96.07 E-value: 7.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 26 IDLQIQKGEFVAIMGPSGSGKSTLMH-ILGCLdsPTDGTYYLDDVLVSKMPKASLaavrNRKIGFVFQsfN-LLPHLNIL 103
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIELRELDPESW----RKHLSWVGQ--NpQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 104 KNVELplmyGG--MSKRK-----RTAKAKEVLQNVGLGdrLKHKPGE----LSGGQRQRVAIARAIVNDPSILLADEPTG 172
Cdd:PRK11174 441 DNVLL----GNpdASDEQlqqalENAWVSEFLPLLPQG--LDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2418785902 173 NLDSQSGGDILEIFTELhSQGNTVIIVTHDQAIASRAERIIKIKDGKIV 221
Cdd:PRK11174 515 SLDAHSEQLVMQALNAA-SRRQTTLMVTHQLEDLAQWDQIWVMQDGQIV 562
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-223 |
1.23e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.36 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAavrnRKiGFV--FQSFNLLPH 99
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA----RM-GVVrtFQHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 100 LNILKN--------VELPLMYGGM-------SKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSI 164
Cdd:PRK11300 95 MTVIENllvaqhqqLKTGLFSGLLktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2418785902 165 LLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHDQA-IASRAERIIKIKDGK-IVDG 223
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKlVMGISDRIYVVNQGTpLANG 236
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
22-225 |
1.25e-22 |
|
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: 95.58 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAavrnrkigfvfQSFNLLPhln 101
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR-----------QFINYLP--- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ilknvELPLMYGG------MSKRKRTAKAKEVLQNV--------------GLGDRLKHKPGELSGGQRQRVAIARAIVND 161
Cdd:TIGR01193 555 -----QEPYIFSGsilenlLLGAKENVSQDEIWAACeiaeikddienmplGYQTELSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2418785902 162 PSILLADEPTGNLDSQSGGDILEIFTELhsQGNTVIIVTHDQAIASRAERIIKIKDGKIVDGNS 225
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNL--QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGS 691
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-222 |
2.25e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 94.64 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLaavrNRKIGFVFQS---FN 95
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----RRNIAVVFQDaglFN 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 96 LLPHLNIL------KNVElplmyggMSKRKRTAKAKEVL--QNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLA 167
Cdd:PRK13657 423 RSIEDNIRvgrpdaTDEE-------MRAAAERAQAHDFIerKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 168 DEPTGNLDSQSGGDILEIFTELhSQGNTVIIVTHDQAIASRAERIIKIKDGKIVD 222
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-222 |
3.97e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 3.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 2 DIIKTENIVKDYilGKIKVraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDvlvskmpkaslaa 81
Cdd:COG0488 314 KVLELEGLSKSY--GDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE------------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 82 vrNRKIGFVFQSFNLL-PHLNILKNVElplmygGMSKRKRTAKAKEVLQNVGL-GDRLKHKPGELSGGQRQRVAIARAIV 159
Cdd:COG0488 377 --TVKIGYFDQHQEELdPDKTVLDELR------DGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2418785902 160 NDPSILLADEPTGNLDSQSggdiLEIFTEL--HSQGnTVIIVTHDQAIASR-AERIIKIKDGKIVD 222
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIET----LEALEEAldDFPG-TVLLVSHDRYFLDRvATRILEFEDGGVRE 509
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-221 |
4.14e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 93.70 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYIlgkiKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKAsLAAvr 83
Cdd:PRK09700 6 ISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NRKIGFVFQSFNLLPHLNILKNvelpLMYGGMSKRK-----------RTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRV 152
Cdd:PRK09700 79 QLGIGIIYQELSVIDELTVLEN----LYIGRHLTKKvcgvniidwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 153 AIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQA-IASRAERIIKIKDGKIV 221
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAeIRRICDRYTVMKDGSSV 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
23-213 |
4.34e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 90.16 E-value: 4.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLaavrNRKIGFVFQSfnllPHL-- 100
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY----RQQVSYCAQT----PTLfg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 -NILKNVELPlmYGGMSKRKRTAKAKEVLQNVGLGDRLKHKP-GELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQS 178
Cdd:PRK10247 95 dTVYDNLIFP--WQIRNQQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 2418785902 179 GGDILEIFTELHSQGN-TVIIVTHDQAIASRAERII 213
Cdd:PRK10247 173 KHNVNEIIHRYVREQNiAVLWVTHDKDEINHADKVI 208
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
23-220 |
6.38e-22 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 89.84 E-value: 6.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLaavrNRKIGFVFQSFNLLPHlNI 102
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL----HSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 103 LKNVELPLMYGGMSKRKRTAKAKEVLQNV-----GLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQ 177
Cdd:cd03248 105 QDNIAYGLQSCSFECVKEAAQKAHAHSFIselasGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2418785902 178 SGGDILEIFTELHsQGNTVIIVTHDQAIASRAERIIKIKDGKI 220
Cdd:cd03248 185 SEQQVQQALYDWP-ERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-221 |
7.27e-22 |
|
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: 92.97 E-value: 7.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYIlgkiKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILgCLDSPTdGTYYLDDVLVSKMPKASLAAV 82
Cdd:TIGR02633 1 LLEMKGIVKTFG----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKIL-SGVYPH-GTWDGEIYWSGSPLKASNIRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 RNRK-IGFVFQSFNLLPHLNILKNV----ELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKP-GELSGGQRQRVAIAR 156
Cdd:TIGR02633 75 TERAgIVIIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2418785902 157 AIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIKDGKIV 221
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKlNEVKAVCDTICVIRDGQHV 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-219 |
8.78e-22 |
|
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: 87.12 E-value: 8.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYILGKIkvraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLvskmpkaslaavr 83
Cdd:cd03221 1 IELENLSKTYGGKLL----LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 nrKIGFVFQsfnllphlnilknvelplmyggmskrkrtakakevlqnvglgdrlkhkpgeLSGGQRQRVAIARAIVNDPS 163
Cdd:cd03221 64 --KIGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2418785902 164 ILLADEPTGNLDSQSgGDILEIFteLHSQGNTVIIVTHDQAIASR-AERIIKIKDGK 219
Cdd:cd03221 91 LLLLDEPTNHLDLES-IEALEEA--LKEYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-212 |
2.23e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 90.35 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMH-ILGCLDSPTDGT---YYLDDVLVSKMPKASLAAVRNRKIGFVFQ-- 92
Cdd:COG4170 19 RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKDNWHVTadrFRWNGIDLLKLSPRERRKIIGREIAMIFQep 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 93 SFNLLPHLNILKNVE--LP-LMYGGM---SKRKRTAKAKEVLQNVGLGDrlkHK------PGELSGGQRQRVAIARAIVN 160
Cdd:COG4170 99 SSCLDPSAKIGDQLIeaIPsWTFKGKwwqRFKWRKKRAIELLHRVGIKD---HKdimnsyPHELTEGECQKVMIAMAIAN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2418785902 161 DPSILLADEPTGNLDSQSGGDILEIFTELH-SQGNTVIIVTHD-QAIASRAERI 212
Cdd:COG4170 176 QPRLLIADEPTNAMESTTQAQIFRLLARLNqLQGTSILLISHDlESISQWADTI 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-202 |
2.26e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.80 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 1 MDIIKTENIVKDYiLGKikvRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPkasLA 80
Cdd:PRK10895 1 MATLTAKNLAKAY-KGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP---LH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 81 AVRNRKIGFVFQSFNLLPHLNILKNVELPL-MYGGMSKRKRTAKAKEVLQNVGLgDRLKHKPGE-LSGGQRQRVAIARAI 158
Cdd:PRK10895 74 ARARRGIGYLPQEASIFRRLSVYDNLMAVLqIRDDLSAEQREDRANELMEEFHI-EHLRDSMGQsLSGGERRRVEIARAL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2418785902 159 VNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD 202
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHN 196
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-221 |
2.99e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 88.20 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDS--PTDGTYYLDDVLVSKMPkaslAAVRNRK-IGFVFQS------ 93
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELS----PDERARAgIFLAFQYpveipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 94 ---FNLLphLNILKNVELPLmyggMSKRKRTAKAKEVLQNVGLGDRLKHKP--GELSGGQRQRVAIARAIVNDPSILLAD 168
Cdd:COG0396 92 vsvSNFL--RTALNARRGEE----LSAREFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 169 EPtgnlDsqSGGDI------LEIFTELHSQGNTVIIVTHDQAI--ASRAERIIKIKDGKIV 221
Cdd:COG0396 166 ET----D--SGLDIdalrivAEGVNKLRSPDRGILIITHYQRIldYIKPDFVHVLVDGRIV 220
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-220 |
3.19e-21 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 86.72 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDvlvSKMPKASLAAVRNRKIGFV---FQSFNLL 97
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG---KPVTRRSPRDAIRAGIAYVpedRKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 98 PHLNILKNVELPLMyggmskrkrtakakevlqnvglgdrlkhkpgeLSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQ 177
Cdd:cd03215 91 LDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2418785902 178 SGGDILEIFTELHSQGNTVIIVTHDQA-IASRAERIIKIKDGKI 220
Cdd:cd03215 139 AKAEIYRLIRELADAGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
23-201 |
3.27e-21 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 91.48 E-value: 3.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLmhiLGCLDSPTDGTYYLDDVLVS--KMPKASLaavrnRKIGFVFQSFNLLPHL 100
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTL---LNALAGRIQGNNFTGTILANnrKPTKQIL-----KRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 NI---LKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGE-----LSGGQRQRVAIARAIVNDPSILLADEPTG 172
Cdd:PLN03211 156 TVretLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180
....*....|....*....|....*....
gi 2418785902 173 NLDSQSGGDILEIFTELHSQGNTVIIVTH 201
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-227 |
5.96e-21 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 90.63 E-value: 5.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 26 IDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSkmpKASLAAVRNRkigF--VFQSFNLLPHLNIL 103
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAYRQL---FsaVFSDFHLFDRLLGL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 104 KNVELPlmyggmskrkrtAKAKEVLQNVGLGDRLKHKPG-----ELSGGQRQRVAIARAIVNDPSILLADE------PTg 172
Cdd:COG4615 425 DGEADP------------ARARELLERLELDHKVSVEDGrfsttDLSQGQRKRLALLVALLEDRPILVFDEwaadqdPE- 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 173 nldsqsggdILEIFT-----ELHSQGNTVIIVTHDQAIASRAERIIKIKDGKIVDGNSNS 227
Cdd:COG4615 492 ---------FRRVFYtellpELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPA 542
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-218 |
7.84e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 90.25 E-value: 7.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYL---DDVLV----SKMPKASLAAVrnrkigfvfqsfn 95
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpagARVLFlpqrPYLPLGTLREA------------- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 96 llphlnilknvelpLMYGGMSKRKRTAKAKEVLQNVGLGDrLKHKPGE-------LSGGQRQRVAIARAIVNDPSILLAD 168
Cdd:COG4178 446 --------------LLYPATAEAFSDAELREALEAVGLGH-LAERLDEeadwdqvLSLGEQQRLAFARLLLHKPDWLFLD 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2418785902 169 EPTGNLDSQSGGDILEIFTElHSQGNTVIIVTHDQAIASRAERIIKIKDG 218
Cdd:COG4178 511 EATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-220 |
9.22e-21 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 90.03 E-value: 9.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSkmpKASLAAVRnRKIGFVFQSFNLLPHLn 101
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYR-KLFSAVFTDFHLFDQL- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ilknvelplmYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGE-----LSGGQRQRVAIARAIVNDPSILLADEPTGNLDS 176
Cdd:PRK10522 413 ----------LGPEGKPANPALVEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2418785902 177 QSGGDI-LEIFTELHSQGNTVIIVTHDQAIASRAERIIKIKDGKI 220
Cdd:PRK10522 483 HFRREFyQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-217 |
1.08e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 89.68 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 20 VRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGT-YYLDDVLVSKMPKASLAAvrnrKIGFVFQSFNLLP 98
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSiLYLGKEVTFNGPKSSQEA----GIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 99 HLNILKNV----ELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNL 174
Cdd:PRK10762 93 QLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2418785902 175 DSQSGGDILEIFTELHSQGNTVIIVTHdqaiasRAERIIKIKD 217
Cdd:PRK10762 173 TDTETESLFRVIRELKSQGRGIVYISH------RLKEIFEICD 209
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-222 |
4.37e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.99 E-value: 4.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDY-----ILGKIK--VRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMP 75
Cdd:PRK10261 313 ILQVRNLVTRFplrsgLLNRVTreVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 76 KASLAAVRnRKIGFVFQS--FNLLPHLNILKNVELPLMYGGMSKRKRTAK-AKEVLQNVGLgdRLKHK---PGELSGGQR 149
Cdd:PRK10261 393 PGKLQALR-RDIQFIFQDpyASLDPRQTVGDSIMEPLRVHGLLPGKAAAArVAWLLERVGL--LPEHAwryPHEFSGGQR 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 150 QRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHDQAIASR-AERIIKIKDGKIVD 222
Cdd:PRK10261 470 QRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVE 544
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-225 |
6.78e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.60 E-value: 6.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLV----------SKMPKASLAAVRNRKIG 88
Cdd:PRK10261 28 KIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrsrqvielSEQSAAQMRHVRGADMA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 89 FVFQS--FNLLPHLNILKNV-ELPLMYGGMSKRKRTAKAKEVLQNVGLGDR---LKHKPGELSGGQRQRVAIARAIVNDP 162
Cdd:PRK10261 108 MIFQEpmTSLNPVFTVGEQIaESIRLHQGASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 163 SILLADEPTGNLDSQSGGDILEIFTELHSQGNT-VIIVTHDQA-IASRAERIIKIKDGKIVDGNS 225
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGvVAEIADRVLVMYQGEAVETGS 252
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-222 |
8.14e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.38 E-value: 8.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMpkaSLAAVRNrKIGFVFQSFNLLpHLN 101
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDY---TLASLRN-QVALVSQNVHLF-NDT 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ILKNVELPlmYGGMSKRKRTAKAKEVLQNVGLGDRLKHK----PGE----LSGGQRQRVAIARAIVNDPSILLADEPTGN 173
Cdd:PRK11176 433 IANNIAYA--RTEQYSREQIEEAARMAYAMDFINKMDNGldtvIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSA 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2418785902 174 LDSQSGGDILEIFTELhsQGN-TVIIVTHDQAIASRAERIIKIKDGKIVD 222
Cdd:PRK11176 511 LDTESERAIQAALDEL--QKNrTSLVIAHRLSTIEKADEILVVEDGEIVE 558
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-215 |
8.34e-20 |
|
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: 83.56 E-value: 8.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTyylddVLVSKMPKASLAAVRNRKIGFVFQSFNLLPHL 100
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGE-----VRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 NILKNVELPLMYGGMSKRKrtakAKEVLQNVGLGDrLKHKP-GELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSG 179
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRT----IEDALAAVGLTG-FEDLPaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 2418785902 180 GDILEIFTELHSQGNTVIIVTHdQAIASRAERIIKI 215
Cdd:TIGR01189 164 ALLAGLLRAHLARGGIVLLTTH-QDLGLVEARELRL 198
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-221 |
1.47e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 83.74 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLdSPTDGTYYLDDVLVSKMPKASLAAVR-----NRKIGF---VFQSF 94
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRaylsqQQSPPFampVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 95 NL-LPHLNILKNVELPLMYggmskrkrtakakeVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVN-DPSI------LL 166
Cdd:COG4138 91 ALhQPAGASSEAVEQLLAQ--------------LAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvWPTInpegqlLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2418785902 167 ADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRhADRVWLLKQGKLV 212
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-205 |
2.04e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 84.76 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMH-ILGcLDSPTDG--TYYLDDVLvsKMPKASLAAVRNrKIGFVFQ--- 92
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARaIIG-LVKATDGevAWLGKDLL--GMKDDEWRAVRS-DIQMIFQdpl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 93 -SFNllPHLNILKNVELPL--MYGGMSKRKRTAKAKEVLQNVGLGDRLKHK-PGELSGGQRQRVAIARAIVNDPSILLAD 168
Cdd:PRK15079 109 aSLN--PRMTIGEIIAEPLrtYHPKLSRQEVKDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 2418785902 169 EPTGNLDSQSGGDILEIFTELHSQ-GNTVIIVTHDQAI 205
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAV 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-216 |
2.30e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.54 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 25 GIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKAslaavrnrkigfvFQSfNLL--PHLNI 102
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-------------YHQ-DLLylGHQPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 103 LKNVELPL----MYGGMSKRKRTAKAKEVLQNVGLGDRLkHKP-GELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQ 177
Cdd:PRK13538 85 IKTELTALenlrFYQRLHGPGDDEALWEALAQVGLAGFE-DVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 2418785902 178 SGGDILEIFTELHSQGNTVIIVTHdQAIASRAERIIKIK 216
Cdd:PRK13538 164 GVARLEALLAQHAEQGGMVILTTH-QDLPVASDKVRKLR 201
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-222 |
1.03e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.14 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 20 VRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSkmpkASLAAVRNRKIGFVFQ--SFNLL 97
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH----FGDYSYRSQRIRMIFQdpSTSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 98 PHLNILKNVELPL-MYGGMSKRKRTAKAKEVLQNVGL-GDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLD 175
Cdd:PRK15112 102 PRQRISQILDFPLrLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2418785902 176 SQSGGDILEIFTELH-SQGNTVIIVT-HDQAIASRAERIIKIKDGKIVD 222
Cdd:PRK15112 182 MSMRSQLINLMLELQeKQGISYIYVTqHLGMMKHISDQVLVMHQGEVVE 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-201 |
1.42e-18 |
|
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: 80.23 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGtyyldDVLVSKMPKASLAAVRNRKIGFVFQSFNLLPHLNI 102
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAG-----RVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 103 LKNVELPLMYGGmskrkrTAKAKEVLQNVGLGDrLKHKP-GELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGD 181
Cdd:cd03231 91 LENLRFWHADHS------DEQVEEALARVGLNG-FEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|
gi 2418785902 182 ILEIFTELHSQGNTVIIVTH 201
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTH 183
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-221 |
1.63e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 83.46 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILG---CLDsptDGTY-YLDDVLVSKM----PKASLAAVrnrkigFVFQSF 94
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLD---DGRIiYEQDLIVARLqqdpPRNVEGTV------YDFVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 95 NLLPHLNILKNVE--LPLMYGGMSKR--KRTAKAKEVLQNVG---LGDRLKH-----------KPGELSGGQRQRVAIAR 156
Cdd:PRK11147 90 GIEEQAEYLKRYHdiSHLVETDPSEKnlNELAKLQEQLDHHNlwqLENRINEvlaqlgldpdaALSSLSGGWLRKAALGR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2418785902 157 AIVNDPSILLADEPTGNLDSQSgGDILEIFteLHSQGNTVIIVTHDQA-IASRAERIIKIKDGKIV 221
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIET-IEWLEGF--LKTFQGSIIFISHDRSfIRNMATRIVDLDRGKLV 232
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-222 |
1.66e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 83.30 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 20 VRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILgcldS---PTdGTY-----YLDDVLVSKMPKASLAavrnRKIGFVF 91
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVL----SgvyPH-GSYegeilFDGEVCRFKDIRDSEA----LGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 92 QSFNLLPHLNILKNVEL---PLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLAD 168
Cdd:NF040905 85 QELALIPYLSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 169 EPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIKDGKIVD 222
Cdd:NF040905 165 EPTAALNEEDSAALLDLLLELKAQGITSIIISHKlNEIRRVADSITVLRDGRTIE 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-221 |
2.50e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.76 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSkmPKASLAAVRNRkIGFV---FQSFNLL 97
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR--IRSPRDAIRAG-IAYVpedRKGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 98 PHLNILKNVELPLM-----YGGMSKRKRTAKAKEVLqnvglgDRLKHKP-------GELSGGQRQRVAIARAIVNDPSIL 165
Cdd:COG1129 343 LDLSIRENITLASLdrlsrGGLLDRRRERALAEEYI------KRLRIKTpspeqpvGNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2418785902 166 LADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQA-IASRAERIIKIKDGKIV 221
Cdd:COG1129 417 ILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPeLLGLSDRILVMREGRIV 473
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-221 |
2.75e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.79 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 20 VRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTyylddVLVSKMPKASLAAVRNRKIG--FVFQSFNLL 97
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGT-----LEIGGNPCARLTPAKAHQLGiyLVPQEPLLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 98 PHLNILKNVELplmygGMSKRKRT-AKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDS 176
Cdd:PRK15439 99 PNLSVKENILF-----GLPKRQASmQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2418785902 177 QSGGDILEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIKDGKIV 221
Cdd:PRK15439 174 AETERLFSRIRELLAQGVGIVFISHKlPEIRQLADRISVMRDGTIA 219
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-208 |
3.76e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.47 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYILGKIkvraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDS-----PTDG-TYYLDDVLVSKmpKA 77
Cdd:PRK14258 8 IKVNNLSFYYDTQKI----LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGrVEFFNQNIYER--RV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 78 SLAAVRnRKIGFVFQSFNLLPhLNILKNVELPL-MYGGMSKRKRTAKAKEVLQNVGLGDRLKHK----PGELSGGQRQRV 152
Cdd:PRK14258 82 NLNRLR-RQVSMVHPKPNLFP-MSVYDNVAYGVkIVGWRPKLEIDDIVESALKDADLWDEIKHKihksALDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2418785902 153 AIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGN-TVIIVTHDQAIASR 208
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSR 216
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-201 |
3.78e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 25 GIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDvlvskmpkaslaavRNRKIGFVFQSFNLLPHLNILK 104
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG--------------GDIDDPDVAEACHYLGHRNAMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 105 NvELPLM---------YGGmskrkRTAKAKEVLQNVGLGDrLKHKP-GELSGGQRQRVAIARAIVNDPSILLADEPTGNL 174
Cdd:PRK13539 86 P-ALTVAenlefwaafLGG-----EELDIAAALEAVGLAP-LAHLPfGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*..
gi 2418785902 175 DSQSGGDILEIFTELHSQGNTVIIVTH 201
Cdd:PRK13539 159 DAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-202 |
7.87e-18 |
|
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: 81.52 E-value: 7.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGtyylddvlvskmpKASLAAvrNRKIGFVFQSFNLLPHLNI 102
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG-------------EARPQP--GIKVGYLPQEPQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 103 LKNVELplmygGMSKRKRT-------------------------AKAKEVLQNVGL----------GDRLKHKPGE---- 143
Cdd:TIGR03719 86 RENVEE-----GVAEIKDAldrfneisakyaepdadfdklaaeqAELQEIIDAADAwdldsqleiaMDALRCPPWDadvt 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 144 -LSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSgGDILEIFteLHSQGNTVIIVTHD 202
Cdd:TIGR03719 161 kLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES-VAWLERH--LQEYPGTVVAVTHD 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-220 |
2.41e-17 |
|
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: 80.37 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMH-ILGCLDSpTDGTYYLddvlvskmpKASLAAVrnrkigfvfqsfnllPHLN 101
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHM---------KGSVAYV---------------PQQA 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ILKNVELP--LMYGGMSKRKRTakaKEVLQNVGL---------GDR--LKHKPGELSGGQRQRVAIARAIVNDPSILLAD 168
Cdd:TIGR00957 709 WIQNDSLRenILFGKALNEKYY---QQVLEACALlpdleilpsGDRteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2418785902 169 EPTGNLDSQSGGDILE--IFTELHSQGNTVIIVTHDQAIASRAERIIKIKDGKI 220
Cdd:TIGR00957 786 DPLSAVDAHVGKHIFEhvIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-202 |
2.72e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.39 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGtyyldDVLVSKMPKASlaAVRNRKIGFVFQSFNLLPHLN 101
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASG-----KISILGQPTRQ--ALQKNLVAYVPQSEEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ILknVELPLM---YGGM-----SKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGN 173
Cdd:PRK15056 95 VL--VEDVVMmgrYGHMgwlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180
....*....|....*....|....*....
gi 2418785902 174 LDSQSGGDILEIFTELHSQGNTVIIVTHD 202
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
29-221 |
3.34e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 77.67 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 29 QIQKGEFVAIMGPSGSGKSTLMH-ILGCLDSPtdGTYYLDDVLVSKMPKASLAAVRnrkiGFVFQSFNLLPHLNILKNVE 107
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLArMAGLLPGS--GSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 108 LPLMYGGMSKRKRTAkAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVN-DPSI------LLADEPTGNLDSQSGG 180
Cdd:PRK03695 92 LHQPDKTRTEAVASA-LNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSLDVAQQA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2418785902 181 DILEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIKDGKIV 221
Cdd:PRK03695 171 ALDRLLSELCQQGIAVVMSSHDlNHTLRHADRVWLLKQGKLL 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
23-221 |
4.90e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.52 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAavrnRKIGFVFQSfnlLPHLNI 102
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQ---LPAAEG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 103 LKNVELPLM-----YGGMSKRKRT--AKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLD 175
Cdd:PRK10575 100 MTVRELVAIgrypwHGALGRFGAAdrEKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2418785902 176 SQSGGDILEIFTEL-HSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:PRK10575 180 IAHQVDVLALVHRLsQERGLTVIAVLHDINMAARyCDYLVALRGGEMI 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-220 |
5.82e-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: 79.29 E-value: 5.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTyylddVLVS-KMPKASLAAVRnRKIGFVFQSFNLLPHL 100
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGT-----VLVGgKDIETNLDAVR-QSLGMCPQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 NILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGG 180
Cdd:TIGR01257 1019 TVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2418785902 181 DILEIFTELHSqGNTVIIVTHDQAIAS-RAERIIKIKDGKI 220
Cdd:TIGR01257 1099 SIWDLLLKYRS-GRTIIMSTHHMDEADlLGDRIAIISQGRL 1138
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-221 |
1.11e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.07 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASlaaVRNRKIGFVFQSFNLLP 98
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAK---IMREAVAIVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 99 HLNILKNVElplMYGGMSKRK----RTAKAKEVLQNvgLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNL 174
Cdd:PRK11614 94 RMTVEENLA---MGGFFAERDqfqeRIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2418785902 175 DSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:PRK11614 169 APIIIQQIFDTIEQLREQGMTIFLVEQNANQALKlADRGYVLENGHVV 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-202 |
1.86e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.81 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTyylddVLVSKMP----KASLAAVRnRKIGFVFQSFNL-L 97
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGA-----VLWQGKPldysKRGLLALR-QQVATVFQDPEQqI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 98 PHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGlGDRLKHKPGE-LSGGQRQRVAIARAIVNDPSILLADEPTGNLDS 176
Cdd:PRK13638 91 FYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180
....*....|....*....|....*.
gi 2418785902 177 QSGGDILEIFTELHSQGNTVIIVTHD 202
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQGNHVIISSHD 195
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-207 |
3.00e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.61 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 15 LGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLM-HILGcldsptdgtyylddvLVSKMPKASLAAVRNRKIGfvfqs 93
Cdd:COG2401 38 LRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLrLLAG---------------ALKGTPVAGCVDVPDNQFG----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 94 fnllPHLNILKNVelplmyggmSKRKRTAKAKEVLQNVGLGDR--LKHKPGELSGGQRQRVAIARAIVNDPSILLADEPT 171
Cdd:COG2401 98 ----REASLIDAI---------GRKGDFKDAVELLNAVGLSDAvlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 2418785902 172 GNLDSQSGGDILEIFTELHSQ-GNTVIIVTHDQAIAS 207
Cdd:COG2401 165 SHLDRQTAKRVARNLQKLARRaGITLVVATHHYDVID 201
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
21-202 |
5.58e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.38 E-value: 5.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLvskmpkaslaavrnrKIGFVFQSFNLLPhl 100
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL---------------RIGYVPQKLYLDT-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 nilknvELPLMYGGMSKRKRTAKAKEV---LQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQ 177
Cdd:PRK09544 81 ------TLPLTVNRFLRLRPGTKKEDIlpaLKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
|
170 180
....*....|....*....|....*.
gi 2418785902 178 SGGDILEIFTEL-HSQGNTVIIVTHD 202
Cdd:PRK09544 155 GQVALYDLIDQLrRELDCAVLMVSHD 180
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-212 |
1.05e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.55 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHIL-GCLDsPTDGTYYLddvlVSKMPKASLAAVRnRKIGFVFQSFNLLPHL 100
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLtGLLP-ASEGEAWL----FGQPVDAGDIATR-RRVGYMSQAFSLYGEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 NILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTgnldsqSGG 180
Cdd:NF033858 355 TVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT------SGV 428
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2418785902 181 DIL------EIFTELhS--QGNTVIIVTHDQAIASRAERI 212
Cdd:NF033858 429 DPVardmfwRLLIEL-SreDGVTIFISTHFMNEAERCDRI 467
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-222 |
1.32e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.14 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMpkaSLAAVRNrKIGFVFQSFNLLPHl 100
Cdd:PRK10790 355 LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL---SHSVLRQ-GVAMVQQDPVVLAD- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 NILKNVELplmyggmSKRKRTAKAKEVLQNVGLGDRLKHKP-------GE----LSGGQRQRVAIARAIVNDPSILLADE 169
Cdd:PRK10790 430 TFLANVTL-------GRDISEEQVWQALETVQLAELARSLPdglytplGEqgnnLSVGQKQLLALARVLVQTPQILILDE 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2418785902 170 PTGNLDSQSGGDILEIFTELHSQgNTVIIVTHDQAIASRAERIIKIKDGKIVD 222
Cdd:PRK10790 503 ATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLSTIVEADTILVLHRGQAVE 554
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-212 |
1.41e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 74.07 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 1 MDIIKTENIVKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMH-ILGCLDSP---TDGTYYLDDVLVSKMPK 76
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKaICGVTKDNwrvTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 77 ASLAAVRNRKIGFVFQSfnllPH--LNILKNVELPLM-------YGG-----MSKRKRtaKAKEVLQNVGLGDR---LKH 139
Cdd:PRK15093 81 RERRKLVGHNVSMIFQE----PQscLDPSERVGRQLMqnipgwtYKGrwwqrFGWRKR--RAIELLHRVGIKDHkdaMRS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 140 KPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVI-IVTHD-QAIASRAERI 212
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIlLISHDlQMLSQWADKI 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-220 |
3.89e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 3.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 24 NGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSkmPKASLAAVRN---------RKIGFvFQSF 94
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAVKKgmayitesrRDNGF-FPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 95 NLLPHLNILKNVELPLMYGGM-----SKRKRTAKAKEVLQNVGLGDrLKHKPGELSGGQRQRVAIARAIVNDPSILLADE 169
Cdd:PRK09700 357 SIAQNMAISRSLKDGGYKGAMglfheVDEQRTAENQRELLALKCHS-VNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2418785902 170 PTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIKDGKI 220
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGRL 487
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-222 |
1.08e-14 |
|
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: 70.13 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPkasLAAVRnRKIGFVFQSFNLLPHl 100
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLR-SSLTIIPQDPTLFSG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 NILKNVELPLMYGgmskrkrTAKAKEVLQNVGLGDrlkhkpgELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGG 180
Cdd:cd03369 97 TIRSNLDPFDEYS-------DEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2418785902 181 DILEIFTELHSqGNTVIIVTHDQAIASRAERIIKIKDGKIVD 222
Cdd:cd03369 163 LIQKTIREEFT-NSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
13-215 |
1.79e-14 |
|
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: 68.89 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 13 YILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLmhILGCLDSPtdgtyyLDDVLVSKMPKASlaavrNRKIGFVFQ 92
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYAS------GKARLISFLPKFS-----RNKLIFIDQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 93 sfnllphlniLKNvelplmyggmskrkrtakakevLQNVGLGD-RLKHKPGELSGGQRQRVAIARAIVNDP--SILLADE 169
Cdd:cd03238 68 ----------LQF----------------------LIDVGLGYlTLGQKLSTLSGGELQRVKLASELFSEPpgTLFILDE 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2418785902 170 PTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASRAERIIKI 215
Cdd:cd03238 116 PSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-220 |
1.88e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.08 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMH-ILGCLDSPTDGTYYLDDVlVSKMPKASL---AAVRNrkigfvfqsfnllp 98
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-VAYVPQVSWifnATVRD-------------- 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 99 hlNILknvelplmYGGMSKRKRTAKAKEVlqnVGLGDRLKHKPG-----------ELSGGQRQRVAIARAIVNDPSILLA 167
Cdd:PLN03130 698 --NIL--------FGSPFDPERYERAIDV---TALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 168 DEPTGNLDSQSGGDILE--IFTELhsQGNTVIIVTHDQAIASRAERIIKIKDGKI 220
Cdd:PLN03130 765 DDPLSALDAHVGRQVFDkcIKDEL--RGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-217 |
2.18e-14 |
|
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: 68.33 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 16 GKIKVRALNgidLQIQKGEFVAIMGPSGSGKSTLMHIL--------GCLDSPTD-GTYYLDDVlvSKMPKASLAAVrnrk 86
Cdd:cd03223 13 GRVLLKDLS---FEIKPGDRLLITGPSGTGKSSLFRALaglwpwgsGRIGMPEGeDLLFLPQR--PYLPLGTLREQ---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 87 igfvfqsfnllphlnilknvelpLMYGGMSkrkrtakakevlqnvglgdrlkhkpgELSGGQRQRVAIARAIVNDPSILL 166
Cdd:cd03223 84 -----------------------LIYPWDD--------------------------VLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 167 ADEPTGNLDSQSGGDILEIFTELhsqGNTVIIVTHDQAIASRAERIIKIKD 217
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKEL---GITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-218 |
2.55e-14 |
|
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: 69.28 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLM-HILGCLDSpTDGTYYLDDVLVSKmPKASLAAVRNR-KIGFVFQSFNLLPhl 100
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNKNESE-PSFEATRSRNRySVAYAAQKPWLLN-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 nilKNVELPLMYGGMSKRKRTakaKEVLQNVGLG---DRLKH----KPGE----LSGGQRQRVAIARAIVNDPSILLADE 169
Cdd:cd03290 93 ---ATVEENITFGSPFNKQRY---KAVTDACSLQpdiDLLPFgdqtEIGErginLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 170 PTGNLDSQSGGDILE--IFTELHSQGNTVIIVTHDQAIASRAERIIKIKDG 218
Cdd:cd03290 167 PFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
38-202 |
3.95e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.53 E-value: 3.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 38 IMGPSGSGKSTLMHILGCLDSPTDGtyylddvlvskmpKASLAAvrNRKIGFVFQSFNLLPHLNILKNVELplmygGMSK 117
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEG-------------EARPAP--GIKVGYLPQEPQLDPEKTVRENVEE-----GVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 118 RK-------------------------RTAKAKEVLQNVGLGDrLKHK-----------PGE-----LSGGQRQRVAIAR 156
Cdd:PRK11819 98 VKaaldrfneiyaayaepdadfdalaaEQGELQEIIDAADAWD-LDSQleiamdalrcpPWDakvtkLSGGERRRVALCR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2418785902 157 AIVNDPSILLADEPTGNLDSQSgGDILEIFteLHSQGNTVIIVTHD 202
Cdd:PRK11819 177 LLLEKPDMLLLDEPTNHLDAES-VAWLEQF--LHDYPGTVVAVTHD 219
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-222 |
4.16e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 70.69 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 7 ENIVKDYILGKIkvraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYylddvlvskmpKASlaavRNRK 86
Cdd:PRK15064 323 ENLTKGFDNGPL----FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----------KWS----ENAN 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 87 IGFVFQSfnllpHLNILKNvELPLMyGGMSKRKRTAKAKEVLQNVgLG------DRLKHKPGELSGGQRQRVAIARAIVN 160
Cdd:PRK15064 384 IGYYAQD-----HAYDFEN-DLTLF-DWMSQWRQEGDDEQAVRGT-LGrllfsqDDIKKSVKVLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2418785902 161 DPSILLADEPTGNLDSQSggdI------LEIFtelhsQGnTVIIVTHDQA-IASRAERIIKIKDGKIVD 222
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMES---IeslnmaLEKY-----EG-TLIFVSHDREfVSSLATRIIEITPDGVVD 515
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-222 |
4.32e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.44 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 20 VRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMpkaSLAAVRNRKIGFV--------- 90
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGL---SPRERRRLGVAYIpedrlgrgl 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 91 FQSFNLLPHLnILKNVELPLM--YGGMSKRKRTAKAKEVLQ--NVGLGDrLKHKPGELSGGQRQRVAIARAIVNDPSILL 166
Cdd:COG3845 348 VPDMSVAENL-ILGRYRRPPFsrGGFLDRKAIRAFAEELIEefDVRTPG-PDTPARSLSGGNQQKVILARELSRDPKLLI 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2418785902 167 ADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIKDGKIVD 222
Cdd:COG3845 426 AAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDlDEILALSDRIAVMYEGRIVG 482
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
3-201 |
5.89e-14 |
|
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: 67.65 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGclDSPTDGTYYlDDVLVSKMP-KASLAa 81
Cdd:cd03232 3 VLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAGVIT-GEILINGRPlDKNFQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 82 vrnRKIGFVFQSFNLLPHLNilknVELPLMYggmSKRKRtakakevlqnvglgdrlkhkpgELSGGQRQRVAIARAIVND 161
Cdd:cd03232 79 ---RSTGYVEQQDVHSPNLT----VREALRF---SALLR----------------------GLSVEQRKRLTIGVELAAK 126
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2418785902 162 PSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTH 201
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
19-221 |
7.83e-14 |
|
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: 68.44 E-value: 7.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDS--PTDGTYYLDDVLVSKMP--------------------- 75
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyeVTSGTILFKGQDLLELEpderaraglflafqypeeipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 76 -------KASLAAVRNRKIGFVFQSFNLLPHLNilKNVELPLMYGGMSKRKrtakakevlQNVGlgdrlkhkpgeLSGGQ 148
Cdd:TIGR01978 92 vsnleflRSALNARRSARGEEPLDLLDFEKLLK--EKLALLDMDEEFLNRS---------VNEG-----------FSGGE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 149 RQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAI--ASRAERIIKIKDGKIV 221
Cdd:TIGR01978 150 KKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLlnYIKPDYVHVLLDGRIV 224
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
18-215 |
2.91e-13 |
|
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: 66.51 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 18 IKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLM---------------------HILGCLDSP----TDG---TYYLDDV 69
Cdd:cd03270 6 AREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPdvdsIEGlspAIAIDQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 70 LVSKMPKASlaavrnrkIGFVFQSFNLLPhlnilknvelpLMYGGMSKRKRTakakEVLQNVGLGD-RLKHKPGELSGGQ 148
Cdd:cd03270 86 TTSRNPRST--------VGTVTEIYDYLR-----------LLFARVGIRERL----GFLVDVGLGYlTLSRSAPTLSGGE 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2418785902 149 RQRVAIARAIVNDPS--ILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASRAERIIKI 215
Cdd:cd03270 143 AQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
22-221 |
1.05e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 66.66 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVlvsKMPKASLAAVRNRkigfvFQSFNLLPHL- 100
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI---PLTKLQLDSWRSR-----LAVVSQTPFLf 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 --NILKNVELPLMYGGMSKRKRTAKAKEVLQNV-GLGDRLKHKPGE----LSGGQRQRVAIARAIVNDPSILLADEPTGN 173
Cdd:PRK10789 402 sdTVANNIALGRPDATQQEIEHVARLASVHDDIlRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2418785902 174 LDSQSGGDILEIFTELhSQGNTVIIVTHDQAIASRAERIIKIKDGKIV 221
Cdd:PRK10789 482 VDGRTEHQILHNLRQW-GEGRTVIISAHRLSALTEASEILVMQHGHIA 528
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-205 |
1.42e-12 |
|
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: 65.08 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 33 GEFVAIMGPSGSGKSTLMHIL--------GCLDSPTDGTYYLDDVLVSKMPKaSLAAVRNRKIGFVF--QSFNLLPHLNI 102
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILagklkpnlGKFDDPPDWDEILDEFRGSELQN-YFTKLLEGDVKVIVkpQYVDLIPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 103 LKNVELplmyggMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDI 182
Cdd:cd03236 105 GKVGEL------LKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180
....*....|....*....|...
gi 2418785902 183 LEIFTELHSQGNTVIIVTHDQAI 205
Cdd:cd03236 179 ARLIRELAEDDNYVLVVEHDLAV 201
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
26-201 |
2.04e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.10 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 26 IDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDvlvskmpKASLAAVRNRKIGFVFQSFNLLPHLNILKN 105
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG-------KTATRGDRSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 106 VELPLMYGGMSKRKRTAKAkevLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQsGGDILE- 184
Cdd:PRK13543 103 LHFLCGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE-GITLVNr 178
|
170
....*....|....*...
gi 2418785902 185 -IFTELHSQGNTvIIVTH 201
Cdd:PRK13543 179 mISAHLRGGGAA-LVTTH 195
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-220 |
2.11e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.42 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMH-ILGclDSPTDgtyYLDDVLVSKMPKASLAAVRN--RKIGFVFQSFNLLPH 99
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSlITG--DHPQG---YSNDLTLFGRRRGSGETIWDikKHIGYVSSSLHLDYR 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 100 LNI-LKNVELPL------MYGGMSKRKRtAKAKEVLQNVGLGDRLKHKP-GELSGGQRQRVAIARAIVNDPSILLADEPT 171
Cdd:PRK10938 351 VSTsVRNVILSGffdsigIYQAVSDRQQ-KLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPL 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2418785902 172 GNLDSQSGGDILEIFTELHSQGNT-VIIVTHDQAIASR--AERIIKIKDGKI 220
Cdd:PRK10938 430 QGLDPLNRQLVRRFVDVLISEGETqLLFVSHHAEDAPAciTHRLEFVPDGDI 481
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-218 |
2.28e-12 |
|
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: 65.70 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTL-MHILGCLDsPTDGtyylddvlvsKMPKASlaavrnrKIGFVFQSFNLLPHlN 101
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLlMMIMGELE-PSEG----------KIKHSG-------RISFSPQTSWIMPG-T 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ILKNVELPLMYGGMSKRKrTAKAKEVLQNVG-LGDRLKHKPGE----LSGGQRQRVAIARAIVNDPSILLADEPTGNLDS 176
Cdd:TIGR01271 503 IKDNIIFGLSYDEYRYTS-VIKACQLEEDIAlFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2418785902 177 QSGGDILE-IFTELHSQgNTVIIVTHDQAIASRAERIIKIKDG 218
Cdd:TIGR01271 582 VTEKEIFEsCLCKLMSN-KTRILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-222 |
2.57e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.52 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 20 VRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKmpKASLAAVRNrKIGFVFQSFNLLPH 99
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDF--KSSKEALEN-GISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 100 LNILKNVEL---PLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDS 176
Cdd:PRK10982 88 RSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2418785902 177 QSGGDILEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIKDGKIVD 222
Cdd:PRK10982 168 KEVNHLFTIIRKLKERGCGIVYISHKmEEIFQLCDEITILRDGQWIA 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-220 |
2.81e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 18 IKVRALNG-----IDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKM-PKASLAAvrnrkiGFVF 91
Cdd:PRK15439 269 LTVEDLTGegfrnISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALsTAQRLAR------GLVY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 92 -----QSFNLLPHLNILKNVeLPLMYGGMSKRKRTAKAKEVLQNV--GLGDRLKHKP---GELSGGQRQRVAIARAIVND 161
Cdd:PRK15439 343 lpedrQSSGLYLDAPLAWNV-CALTHNRRGFWIKPARENAVLERYrrALNIKFNHAEqaaRTLSGGNQQKVLIAKCLEAS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 162 PSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD-QAIASRAERIIKIKDGKI 220
Cdd:PRK15439 422 PQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDlEEIEQMADRVLVMHQGEI 481
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-221 |
4.16e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.69 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 21 RALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILG---CLDSPTDGTYYLDDVLVSKMPKASLAAVRNRKI---------- 87
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdlTGGGAPRGARVTGDVTLNGEPLAAIDAPRLARLravlpqaaqp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 88 GFVFQSFNLL-----PHLNilknvelplmYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVN-- 160
Cdd:PRK13547 95 AFAFSAREIVllgryPHAR----------RAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 161 -------DPSILLADEPTGNLDSQSGGDILEIFTELHSQGNT-VIIVTHDQAIASR-AERIIKIKDGKIV 221
Cdd:PRK13547 165 pphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARhADRIAMLADGAIV 234
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
10-205 |
4.35e-12 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 64.87 E-value: 4.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 10 VKDYILGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSptdGTYYLDDVLVSKMPKASLAAVRNRkiGF 89
Cdd:PLN03140 883 MKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKT---GGYIEGDIRISGFPKKQETFARIS--GY 957
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 90 VFQSFNLLPHLnilkNVELPLMYGG-------MSKRKRTAKAKEVLQNVGLgDRLKHK----PG--ELSGGQRQRVAIAR 156
Cdd:PLN03140 958 CEQNDIHSPQV----TVRESLIYSAflrlpkeVSKEEKMMFVDEVMELVEL-DNLKDAivglPGvtGLSTEQRKRLTIAV 1032
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2418785902 157 AIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAI 205
Cdd:PLN03140 1033 ELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1081
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-201 |
4.71e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.74 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGclDSPTDGTYYLDDVLVSKMPKASLAAvrnRKIGFVFQSFNLLP 98
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNGRPLDSSFQ---RSIGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 99 HLNilknVELPLMYGG-------MSKRKRTAKAKEVLQNVGL---GDRLKHKPGE-LSGGQRQRVAIARAIVNDPSILL- 166
Cdd:TIGR00956 850 TST----VRESLRFSAylrqpksVSKSEKMEYVEEVIKLLEMesyADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLf 925
|
170 180 190
....*....|....*....|....*....|....*
gi 2418785902 167 ADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTH 201
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-171 |
7.62e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.99 E-value: 7.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYyldDVLVSKMpkASlAAVRNR---KIGFVFQSF- 94
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV---EVLGGDM--AD-ARHRRAvcpRIAYMPQGLg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 95 -NLLPHLNILKNVELplmYG---GMSKRKRTAKAKEVLQNVGLgDRLKHKP-GELSGGQRQRVAIARAIVNDPSILLADE 169
Cdd:NF033858 87 kNLYPTLSVFENLDF---FGrlfGQDAAERRRRIDELLRATGL-APFADRPaGKLSGGMKQKLGLCCALIHDPDLLILDE 162
|
..
gi 2418785902 170 PT 171
Cdd:NF033858 163 PT 164
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-220 |
8.28e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.23 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMhilgcldsptdgtyyldDVLVSKMPKASLAAVRNR-KIGFVFQS---FNLLP 98
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLI-----------------SAMLGELSHAETSSVVIRgSVAYVPQVswiFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 99 HLNILknvelplmYGGMSKRKRTAKAKEVlqnVGLGDRLKHKPGE-----------LSGGQRQRVAIARAIVNDPSILLA 167
Cdd:PLN03232 696 RENIL--------FGSDFESERYWRAIDV---TALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIF 764
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2418785902 168 DEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASRAERIIKIKDGKI 220
Cdd:PLN03232 765 DDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMI 817
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
144-213 |
1.35e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.51 E-value: 1.35e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 144 LSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGN-TVIIVTHDQAIASRAERII 213
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADkTIITIAHRIASIKRSDKIV 1429
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-220 |
1.47e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 63.34 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 13 YILGKIKVRALN-GIDLQIQkgefVAIMGPSGSGKSTLMHILGCLDSPTDGTyylddvlVSKMPKASLAavrnrkigfVF 91
Cdd:PLN03073 518 YPGGPLLFKNLNfGIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGT-------VFRSAKVRMA---------VF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 92 QSFnllpHLNILKNVELPLMY-----GGMSKRKRTAKakevLQNVGLGDRLKHKPG-ELSGGQRQRVAIARAIVNDPSIL 165
Cdd:PLN03073 578 SQH----HVDGLDLSSNPLLYmmrcfPGVPEQKLRAH----LGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHIL 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 166 LADEPTGNLDSqsggDILEIFTE--LHSQGNtVIIVTHDQ-AIASRAERIIKIKDGKI 220
Cdd:PLN03073 650 LLDEPSNHLDL----DAVEALIQglVLFQGG-VLMVSHDEhLISGSVDELWVVSEGKV 702
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-205 |
2.07e-11 |
|
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: 62.88 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 31 QKGEFVAIMGPSGSGKSTLMHIL--------GCLDSPTDgtyyLDDVLvskmpkaslaavrnRKigfvFQSFNLLPHLNI 102
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILsgelkpnlGDYDEEPS----WDEVL--------------KR----FRGTELQDYFKK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 103 LKN-----------VEL-PLMYGG-----MSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSIL 165
Cdd:COG1245 155 LANgeikvahkpqyVDLiPKVFKGtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2418785902 166 LADEPTGNLdsqsggDILE------IFTELHSQGNTVIIVTHDQAI 205
Cdd:COG1245 235 FFDEPSSYL------DIYQrlnvarLIRELAEEGKYVLVVEHDLAI 274
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-218 |
2.88e-11 |
|
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: 61.41 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTL-MHILGCLDsPTDGtyylddvlvsKMPKASlaavrnrKIGFVFQSFNLLPHlN 101
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLlMLILGELE-PSEG----------KIKHSG-------RISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ILKNVELPLMYGGMsKRKRTAKAKEVLQNVG-LGDRLKHKPGE----LSGGQRQRVAIARAIVNDPSILLADEPTGNLDS 176
Cdd:cd03291 114 IKENIIFGVSYDEY-RYKSVVKACQLEEDITkFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2418785902 177 QSGGDILEIFTELHSQGNTVIIVTHDQAIASRAERIIKIKDG 218
Cdd:cd03291 193 FTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-202 |
3.87e-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: 60.88 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEF-----VAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLAAVRNRKIGFVFQs 93
Cdd:cd03237 6 MKKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTVRDLLSS- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 94 fnllphlnILKNVelplmygGMSKRKRTakakEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGN 173
Cdd:cd03237 85 --------ITKDF-------YTHPYFKT----EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAY 145
|
170 180 190
....*....|....*....|....*....|..
gi 2418785902 174 LDSQS---GGDILEIFTELHSQgnTVIIVTHD 202
Cdd:cd03237 146 LDVEQrlmASKVIRRFAENNEK--TAFVVEHD 175
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-201 |
4.26e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.83 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 22 ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTyylddvlVSKMPKASLAAVrnrkigfvfqSFNLLPHLN 101
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT-------VDIKGSAALIAI----------SSGLNGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGD 181
Cdd:PRK13545 102 GIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180
....*....|....*....|
gi 2418785902 182 ILEIFTELHSQGNTVIIVTH 201
Cdd:PRK13545 182 CLDKMNEFKEQGKTIFFISH 201
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-205 |
5.29e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 30 IQKGEFVAIMGPSGSGKSTLMHIL--------GCLDSPTDgtyyLDDVLvsKMPKAS-----LAAVRNRKIGFVF--QSF 94
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsgelipnlGDYEEEPS----WDEVL--KRFRGTelqnyFKKLYNGEIKVVHkpQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 95 NLLPHL------NILKNVElplmyggmsKRKrtaKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLAD 168
Cdd:PRK13409 170 DLIPKVfkgkvrELLKKVD---------ERG---KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2418785902 169 EPTGNLdsqsggDILEIFT------ELhSQGNTVIIVTHDQAI 205
Cdd:PRK13409 238 EPTSYL------DIRQRLNvarlirEL-AEGKYVLVVEHDLAV 273
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
23-221 |
9.83e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.20 E-value: 9.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGcldSPTDGTYYLD-DVLVSKMPKASLAAVRNRKIGFVFQSFNLLPHLN 101
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA---NRTEGNVSVEgDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ILKNVELPLmyggmskrkrTAKAKEVLQNVglgdrlkhkpgelSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGD 181
Cdd:cd03233 100 VRETLDFAL----------RCKGNEFVRGI-------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2418785902 182 ILEIFTELHSQGNTVIIVTHDQA---IASRAERIIKIKDGKIV 221
Cdd:cd03233 157 ILKCIRTMADVLKTTTFVSLYQAsdeIYDLFDKVLVLYEGRQI 199
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-210 |
1.31e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.81 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKmpkaSLAAVRnRKIGFVFQSFNLLPHLNI 102
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLCTYQ-KQLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 103 LKNVELPLMYGGMSkrkrtAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDI 182
Cdd:PRK13540 92 RENCLYDIHFSPGA-----VGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|....*...
gi 2418785902 183 LEIFTELHSQGNTVIIVTHDQAIASRAE 210
Cdd:PRK13540 167 ITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-221 |
1.63e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.18 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLmhiLGCLDSPTDgtyylddvlvskMPKASLAAvrNRKIGFVFQS---FNLLPH 99
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTL---LQSLLSQFE------------ISEGRVWA--ERSIAYVPQQawiMNATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 100 LNILKNVElplmyggmSKRKRTAKAKEVLQ---NVG-LGDRLKHKPGE----LSGGQRQRVAIARAIVNDPSILLADEPT 171
Cdd:PTZ00243 739 GNILFFDE--------EDAARLADAVRVSQleaDLAqLGGGLETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2418785902 172 GNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASRAERIIKIKDGKIV 221
Cdd:PTZ00243 811 SALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-202 |
1.91e-10 |
|
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: 59.95 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDY---ILgkikvraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLvskmpkasl 79
Cdd:TIGR03719 322 VIEAENLTKAFgdkLL-------IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV--------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 80 aavrnrKIGFVFQSF-NLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKhKPGELSGGQRQRVAIARAI 158
Cdd:TIGR03719 386 ------KLAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQK-KVGQLSGGERNRVHLAKTL 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2418785902 159 VNDPSILLADEPTGNLDS---QSGGDILEIFTelhsqGNTVIIvTHD 202
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVetlRALEEALLNFA-----GCAVVI-SHD 499
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-220 |
2.16e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.84 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMH-ILGCLDSPTDGTYYLDDVLVS-KMPKASLAAvrnrKIGFVFQS--- 93
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDiRNPAQAIRA----GIAMVPEDrkr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 94 FNLLPHLNILKNVELPLMyGGMSKRKRTAKAKEvLQNVGLG-DRLKHKP-------GELSGGQRQRVAIARAIVNDPSIL 165
Cdd:TIGR02633 348 HGIVPILGVGKNITLSVL-KSFCFKMRIDAAAE-LQIIGSAiQRLKVKTaspflpiGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2418785902 166 LADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQA-IASRAERIIKIKDGKI 220
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAeVLGLSDRVLVIGEGKL 481
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-221 |
2.70e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.54 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 17 KIKVRALNG------IDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSkmPKASLAAVR------- 83
Cdd:PRK11288 257 RLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID--IRSPRDAIRagimlcp 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 -NRKIGFVFQSFNLLPHLNIlknvelplmyggmSKRKRTAKAKEVLQN---VGLGDR----LKHKP-------GELSGGQ 148
Cdd:PRK11288 335 eDRKAEGIIPVHSVADNINI-------------SARRHHLRAGCLINNrweAENADRfirsLNIKTpsreqliMNLSGGN 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2418785902 149 RQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQA-IASRAERIIKIKDGKIV 221
Cdd:PRK11288 402 QQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPeVLGVADRIVVMREGRIA 475
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-202 |
5.55e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYilGKIKVRALNGidlQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDdVLVSKMPK----AS 78
Cdd:PRK13409 340 LVEYPDLTKKL--GDFSLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKPQyikpDY 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 79 LAAVRN--RKIGFVFQSfnllphlNILKNvelplmyggmskrkrtakakEVLQNVGLGDRLKHKPGELSGGQRQRVAIAR 156
Cdd:PRK13409 414 DGTVEDllRSITDDLGS-------SYYKS--------------------EIIKPLQLERLLDKNVKDLSGGELQRVAIAA 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2418785902 157 AIVNDPSILLADEPTGNLDSQ---SGGDILEIFTElhSQGNTVIIVTHD 202
Cdd:PRK13409 467 CLSRDADLYLLDEPSAHLDVEqrlAVAKAIRRIAE--EREATALVVDHD 513
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
19-223 |
5.79e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.21 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGK---STLMHILGClDSPTDGTYYLDDVLVSKMPKASLAAVRNRKIGFVfQSFN 95
Cdd:NF000106 25 EVKAVDGVDLDVREGTVLGVLGP*GAA**rgALPAHV*GP-DAGRRPWRF*TWCANRRALRRTIG*HRPVR*GRR-ESFS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 96 LLPHLNIL-KNVELplmyggmSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNL 174
Cdd:NF000106 103 GRENLYMIgR*LDL-------SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 175 DSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERIIKIKDGKIV-DG 223
Cdd:NF000106 176 DPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIaDG 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
26-201 |
7.65e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.50 E-value: 7.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 26 IDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDG------TYYLDDV----------LVSKMPKASLAAVRNrKIGF 89
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdiiindSHNLKDInlkwwrskigVVSQDPLLFSNSIKN-NIKY 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 90 VFQSFNLLPHLNILKNVELPLMYGGMSKRK--------------RTAKAKEVLQ------------------NVGLGDRL 137
Cdd:PTZ00265 483 SLYSLKDLEALSNYYNEDGNDSQENKNKRNscrakcagdlndmsNTTDSNELIEmrknyqtikdsevvdvskKVLIHDFV 562
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2418785902 138 KHKP-----------GELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTV-IIVTH 201
Cdd:PTZ00265 563 SALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAH 638
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
40-202 |
7.91e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 7.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 40 GPSGSGKSTLMHILGCLDSPTDGTyylddvlVSKMPKASLAAVRNRKigFVFQSFNLLPHLnILKNVEL----------- 108
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGN-------VSLDPNERLGKLRQDQ--FAFEEFTVLDTV-IMGHTELwevkqerdriy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 109 --PLM--------------YGGMSKRKRTAKAKEVLQNVGLGDRLKHKP-GELSGGQRQRVAIARAIVNDPSILLADEPT 171
Cdd:PRK15064 104 alPEMseedgmkvadlevkFAEMDGYTAEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPT 183
|
170 180 190
....*....|....*....|....*....|...
gi 2418785902 172 GNLDSQSggdI--LEifTELHSQGNTVIIVTHD 202
Cdd:PRK15064 184 NNLDINT---IrwLE--DVLNERNSTMIIISHD 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-213 |
8.21e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.87 E-value: 8.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYilGKIKVRALNGidlQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDdVLVSKMPKaslaav 82
Cdd:COG1245 341 LVEYPDLTKSY--GGFSLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISYKPQ------ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 83 rnrkigFVFQSFNLLphlnilknVELpLMYGGMSKRKRTAKAK-EVLQNVGLgDRLKHKP-GELSGGQRQRVAIARAIVN 160
Cdd:COG1245 409 ------YISPDYDGT--------VEE-FLRSANTDDFGSSYYKtEIIKPLGL-EKLLDKNvKDLSGGELQRVAIAACLSR 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2418785902 161 DPSILLADEPTGNLDSQ---SGGDILEIFTElhSQGNTVIIVTHD-QAIASRAERII 213
Cdd:COG1245 473 DADLYLLDEPSAHLDVEqrlAVAKAIRRFAE--NRGKTAMVVDHDiYLIDYISDRLM 527
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
141-225 |
8.33e-10 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 56.46 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 141 PGELSGGQRQ------RVAIARAIVNDPSILLADEPTGNLDSQS-GGDILEIFTELHSQGN-TVIIVTHDQAIASRAERI 212
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEIIEERKSQKNfQLIVITHDEELVDAADHI 192
|
90
....*....|...
gi 2418785902 213 IKIKdgKIVDGNS 225
Cdd:cd03240 193 YRVE--KDGRQKS 203
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
144-216 |
1.86e-09 |
|
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: 54.67 E-value: 1.86e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 144 LSGGQRQRVAIA-----RAIVNDPSILLaDEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASRAERIIKIK 216
Cdd:cd03227 78 LSGGEKELSALAlilalASLKPRPLYIL-DEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
10-202 |
2.99e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.59 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 10 VKDYILGKIKVR---ALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTyylddvlVSKMPKASLAAVrnrk 86
Cdd:PRK13546 24 MKDALIPKHKNKtffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK-------VDRNGEVSVIAI---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 87 igfvfqSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILL 166
Cdd:PRK13546 93 ------SAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILV 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 2418785902 167 ADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD 202
Cdd:PRK13546 167 IDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHN 202
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-220 |
4.03e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 30 IQKGEFVAIMGPSGSGKSTLMH-ILGCLDSPTDGTYYLDDVLVSKmpKASLAAVRNrKIGFVFQS---FNLLPHLNILKN 105
Cdd:PRK13549 285 LRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKI--RNPQQAIAQ-GIAMVPEDrkrDGIVPVMGVGKN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 106 VELPlMYGGMSKRKRTAKAKEVLQNVGLGDRLKHKP-------GELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQS 178
Cdd:PRK13549 362 ITLA-ALDRFTGGSRIDDAAELKTILESIQRLKVKTaspelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGA 440
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2418785902 179 GGDILEIFTELHSQGNTVIIVTHDQA-IASRAERIIKIKDGKI 220
Cdd:PRK13549 441 KYEIYKLINQLVQQGVAIIVISSELPeVLGLSDRVLVMHEGKL 483
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
4-219 |
4.21e-09 |
|
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: 54.12 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYILGKIKVRALngidlQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKaslaavr 83
Cdd:cd03222 1 QLYPDCVKRYGVFFLLVELG-----VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQ------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 nrKIgfvfqsfnllphlnilknvelplmyggmskrkrtakakevlqnvglgdrlkhkpgELSGGQRQRVAIARAIVNDPS 163
Cdd:cd03222 69 --YI-------------------------------------------------------DLSGGELQRVAIAAALLRNAT 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2418785902 164 ILLADEPTGNLDSQSGGDILEIFTELHSQGN-TVIIVTHDQAIASRAERIIKIKDGK 219
Cdd:cd03222 92 FYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
23-221 |
6.08e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.65 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDS--PTDGtyyldDVLVSKMPKASLAAVRNRKIGfVFQSFNLLPHL 100
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEG-----DILFKGESILDLEPEERAHLG-IFLAFQYPIEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 NILKNVE-LPLMYGgmSKRKRTAKA-----------KEVLQNVGLGDRLKHK---PGeLSGGQRQRVAIARAIVNDPSIL 165
Cdd:CHL00131 97 PGVSNADfLRLAYN--SKRKFQGLPeldplefleiiNEKLKLVGMDPSFLSRnvnEG-FSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2418785902 166 LADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQaiasRAERIIK------IKDGKIV 221
Cdd:CHL00131 174 ILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQ----RLLDYIKpdyvhvMQNGKII 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-214 |
8.06e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.40 E-value: 8.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 2 DIIKTENIVKDYilGKIKVRALNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGtyyldDVLVSKmpKASLAA 81
Cdd:TIGR01257 1936 DILRLNELTKVY--SGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG-----DATVAG--KSILTN 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 82 VRNrkigfVFQSFNLLPHLNILKNVELPLMYGGMSKRKRTAKAKEV-------LQNVGL---GDRLKhkpGELSGGQRQR 151
Cdd:TIGR01257 2007 ISD-----VHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIekvanwsIQSLGLslyADRLA---GTYSGGNKRK 2078
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2418785902 152 VAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHD----QAIASRAERIIK 214
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSmeecEALCTRLAIMVK 2145
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
144-218 |
8.45e-09 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 55.22 E-value: 8.45e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2418785902 144 LSGGQRQRVAIARAIVNDPS--ILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASRAERIIKIKDG 218
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPG 553
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-218 |
1.25e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 52.38 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 32 KGEFVAIMGPSGSGKSTLMH-ILGCLDSPTDGTYYLDdvlvskmpkaslaavrnrkigfvfqsfnllphlnilknvelpl 110
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYID------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 111 myggmskrkrTAKAKEVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEI----- 185
Cdd:smart00382 38 ----------GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2418785902 186 -FTELHSQGNTVIIVTHDQ------AIASRAERIIKIKDG 218
Cdd:smart00382 108 lLLLKSEKNLTVILTTNDEkdlgpaLLRRRFDRRIVLLLI 147
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-220 |
1.57e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTyylddvlvskmpkasLAAVRNRKIGFVFQSfnllpHLNI 102
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGE---------------IGLAKGIKLGYFAQH-----QLEF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 103 LKNVELPLMY-GGMSKRKRTAKAKEVLQNVGL-GDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSqsgg 180
Cdd:PRK10636 388 LRADESPLQHlARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL---- 463
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2418785902 181 DILEIFTE-LHSQGNTVIIVTHDQ-AIASRAERIIKIKDGKI 220
Cdd:PRK10636 464 DMRQALTEaLIDFEGALVVVSHDRhLLRSTTDDLYLVHDGKV 505
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
23-225 |
1.70e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 53.37 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPkasLAAVRNRkigfvfqsfnllphLNI 102
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSR--------------LSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 103 LknVELPLMYGGMSKRKRTAKAK-------EVLQNVGLGDRLKHKPGEL-----------SGGQRQRVAIARAIVNDPSI 164
Cdd:cd03288 100 I--LQDPILFSGSIRFNLDPECKctddrlwEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 165 LLADEPTGNLDsQSGGDILEIFTELHSQGNTVIIVTHDQAIASRAERIIKIKDGKIVDGNS 225
Cdd:cd03288 178 LIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDT 237
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-225 |
4.09e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 53.38 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSpTDGTYYLD-----DVLVSKMPKAslAAVRNRKIgFVFQ-SF-- 94
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDgvswnSVTLQTWRKA--FGVIPQKV-FIFSgTFrk 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 95 NLLPHlnilknvelplmyggmsKRKRTAKAKEVLQNVGLGDRLKHKPGEL-----------SGGQRQRVAIARAIVNDPS 163
Cdd:TIGR01271 1311 NLDPY-----------------EQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAK 1373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 164 ILLADEPTGNLDSQSggdiLEIF--TELHSQGN-TVIIVTHdqaiasRAERIIKIKDGKIVDGNS 225
Cdd:TIGR01271 1374 ILLLDEPSAHLDPVT----LQIIrkTLKQSFSNcTVILSEH------RVEALLECQQFLVIEGSS 1428
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-220 |
5.98e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.31 E-value: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 17 KIKVRALNG-----IDLQIQKGEFVAIMGPSGSGKSTLMHIL-GCLDSpTDGTYYLD-DVLVSKMPKASLAAvrnrkiGF 89
Cdd:PRK10762 257 RLKVDNLSGpgvndVSFTLRKGEILGVSGLMGAGRTELMKVLyGALPR-TSGYVTLDgHEVVTRSPQDGLAN------GI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 90 VFQSFN-----LLPHLNILKNVELPLMyGGMSKRKRTAKAKEVLQNVGLGDRL-------KHKP-GELSGGQRQRVAIAR 156
Cdd:PRK10762 330 VYISEDrkrdgLVLGMSVKENMSLTAL-RYFSRAGGSLKHADEQQAVSDFIRLfniktpsMEQAiGLLSGGNQQKVAIAR 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2418785902 157 AIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQA-IASRAERIIKIKDGKI 220
Cdd:PRK10762 409 GLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPeVLGMSDRILVMHEGRI 473
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-225 |
7.82e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 7.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYILGKIKVraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMpkaSLAAVR 83
Cdd:PLN03232 1235 IKFEDVHLRYRPGLPPV--LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF---GLTDLR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 nRKIGFVFQS---------FNLLP---HLNilknvelplmyGGMSKRKRTAKAKEVLQNVGLG-DRLKHKPGE-LSGGQR 149
Cdd:PLN03232 1310 -RVLSIIPQSpvlfsgtvrFNIDPfseHND-----------ADLWEALERAHIKDVIDRNPFGlDAEVSEGGEnFSVGQR 1377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2418785902 150 QRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTElHSQGNTVIIVTHDQAIASRAERIIKIKDGKIVDGNS 225
Cdd:PLN03232 1378 QLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDS 1452
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
128-218 |
8.44e-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: 52.32 E-value: 8.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 128 LQNVGLGD-RLKHKPGELSGGQRQRVAIARAIVNDPS--ILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQA 204
Cdd:TIGR00630 472 LIDVGLDYlSLSRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED 551
|
90
....*....|....
gi 2418785902 205 IASRAERIIKIKDG 218
Cdd:TIGR00630 552 TIRAADYVIDIGPG 565
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
23-220 |
2.27e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 50.24 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSpTDGTYYLDDVLVSKMP-----KAslAAVRNRKIgFVFQSfnll 97
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPlqkwrKA--FGVIPQKV-FIFSG---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 98 phlNILKNVElPlmYGGMSKRKRTAKAKEvlqnVGLGDRLKHKPGE-----------LSGGQRQRVAIARAIVNDPSILL 166
Cdd:cd03289 92 ---TFRKNLD-P--YGKWSDEEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2418785902 167 ADEPTGNLDSQSGGDILEIFTELHSqGNTVIIVTHDQAIASRAERIIKIKDGKI 220
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTLKQAFA-DCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
3-171 |
2.36e-07 |
|
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: 50.90 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 3 IIKTENIVKDYILGKIKVRALNgidLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDD----VLVSKMPKAS 78
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLS---FEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAkgklFYVPQRPYMT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 79 LAAVRNRKIgfvfqsfnllphlnilknveLPLMYGGMSKRK-RTAKAKEVLQNVGLGDRLKHKPG---------ELSGGQ 148
Cdd:TIGR00954 528 LGTLRDQII--------------------YPDSSEDMKRRGlSDKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGE 587
|
170 180
....*....|....*....|...
gi 2418785902 149 RQRVAIARAIVNDPSILLADEPT 171
Cdd:TIGR00954 588 KQRIAMARLFYHKPQFAILDECT 610
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-222 |
3.17e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 4 IKTENIVKDYILGKIKVraLNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMpkaSLAAVR 83
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPV--LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GLMDLR 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 84 NRkIGFVFQS---------FNLLPhLNILKNVELplmyggMSKRKRtAKAKEVLQNVGLG-DRLKHKPGE-LSGGQRQRV 152
Cdd:PLN03130 1313 KV-LGIIPQApvlfsgtvrFNLDP-FNEHNDADL------WESLER-AHLKDVIRRNSLGlDAEVSEAGEnFSVGQRQLL 1383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2418785902 153 AIARAIVNDPSILLADEPTGNLDsqSGGDIL---EIFTELHSqgNTVIIVTHDQAIASRAERIIKIKDGKIVD 222
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVD--VRTDALiqkTIREEFKS--CTMLIIAHRLNTIIDCDRILVLDAGRVVE 1452
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-176 |
3.76e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 19 KVRALNGIDLQIQKGEFVAIMGPSGSGKSTLmhiLGCLDSPTDGtYYLDDVLVSKMPKASLAAVRNRKIGFVF---QSFN 95
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTL---LKTIASNTDG-FHIGVEGVITYDGITPEEIKKHYRGDVVynaETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 96 LLPHLNILKNVELP-------LMYGGMSKRKRTAKAKEV-LQNVGLGDRLKHKPGE-----LSGGQRQRVAIARAIVNDP 162
Cdd:TIGR00956 149 HFPHLTVGETLDFAarcktpqNRPDGVSREEYAKHIADVyMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGA 228
|
170
....*....|....
gi 2418785902 163 SILLADEPTGNLDS 176
Cdd:TIGR00956 229 KIQCWDNATRGLDS 242
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
122-201 |
5.08e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 122 AKAKEVLQNVGLGDRLKHKPGE-LSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSggdILEIFTELHSQGNTVIIVT 200
Cdd:PLN03073 322 ARAASILAGLSFTPEMQVKATKtFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKTFIVVS 398
|
.
gi 2418785902 201 H 201
Cdd:PLN03073 399 H 399
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-204 |
7.27e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 7.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 29 QIQKGEFVAIMGPSGSGKSTLMHI-LGCLDsPTDGT----------YY------LD--------------DVLVSKmpka 77
Cdd:PRK11147 341 QVQRGDKIALIGPNGCGKTTLLKLmLGQLQ-ADSGRihcgtklevaYFdqhraeLDpektvmdnlaegkqEVMVNG---- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 78 slaavRNRKIGFVFQSFNLLPhlnilknvelplmyggmsKRKRT-AKAkevlqnvglgdrlkhkpgeLSGGQRQRVAIAR 156
Cdd:PRK11147 416 -----RPRHVLGYLQDFLFHP------------------KRAMTpVKA-------------------LSGGERNRLLLAR 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2418785902 157 AIVNDPSILLADEPTGNLDSQSggdiLEIFTELHS--QGnTVIIVTHDQA 204
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLDVET----LELLEELLDsyQG-TVLLVSHDRQ 498
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
23-205 |
7.64e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.63 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSptdgtYYLDDVLVSKMPKASLAAVRNRKIG-FVFQSFNLlphln 101
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRED-----YEVTGGTVEFKGKDLLELSPEDRAGeGIFMAFQY----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 102 ilkNVELPlmygGMSKR---------KRTAKAKEVLQNVGLGDRLKHK------PGEL---------SGGQRQRVAIARA 157
Cdd:PRK09580 87 ---PVEIP----GVSNQfflqtalnaVRSYRGQEPLDRFDFQDLMEEKiallkmPEDLltrsvnvgfSGGEKKRNDILQM 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2418785902 158 IVNDPSILLADEPTGNLDSqsggDILEIFTE----LHSQGNTVIIVTHDQAI 205
Cdd:PRK09580 160 AVLEPELCILDESDSGLDI----DALKIVADgvnsLRDGKRSFIIVTHYQRI 207
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
23-213 |
1.07e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.99 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHilgcldsptdgtyyldDVLVskmpkASLAAVRNRKIGFV--FQSFNLLPHL 100
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIN----------------DTLY-----PALARRLHLKKEQPgnHDRIEGLEHI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 101 NILKNVE----------LPLMYGGM-----------SKRKR--------TAKAK-------------------------- 125
Cdd:cd03271 70 DKVIVIDqspigrtprsNPATYTGVfdeirelfcevCKGKRynretlevRYKGKsiadvldmtveealeffenipkiark 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 126 -EVLQNVGLGD-RLKHKPGELSGGQRQRVAIARAIVN---DPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVT 200
Cdd:cd03271 150 lQTLCDVGLGYiKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIE 229
|
250
....*....|...
gi 2418785902 201 HDQAIASRAERII 213
Cdd:cd03271 230 HNLDVIKCADWII 242
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-227 |
1.24e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.79 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMpkaSLAAVRNrKIGFVFQS--------- 93
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI---GLHDLRF-KITIIPQDpvlfsgslr 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 94 FNLLP-----HLNILKNVELPLMYGGMSkrkrtakakevlqnvGLGDRLKHKPGE----LSGGQRQRVAIARAIVNDPSI 164
Cdd:TIGR00957 1378 MNLDPfsqysDEEVWWALELAHLKTFVS---------------ALPDKLDHECAEggenLSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2418785902 165 LLADEPTGNLDSQSgGDILEIFTELHSQGNTVIIVTHDQAIASRAERIIKIKDGKIVDGNSNS 227
Cdd:TIGR00957 1443 LVLDEATAAVDLET-DNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPS 1504
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
23-221 |
1.46e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.47 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMH--ILGCLDS------PTDGTY-------------YLDDVLVSKMPKASLA- 80
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtLYPALANrlngakTVPGRYtsieglehldkviHIDQSPIGRTPRSNPAt 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 81 ------AVRN--------RKIGFV---FqSFN--------------LLPHLNILKNVELP---------------LMYGG 114
Cdd:TIGR00630 704 ytgvfdEIRElfaetpeaKVRGYTpgrF-SFNvkggrceacqgdgvIKIEMHFLPDVYVPcevckgkrynretleVKYKG 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 115 --------MS---------KRKRTAKAKEVLQNVGLGD-RLKHKPGELSGGQRQRVAIARAI---VNDPSILLADEPTGN 173
Cdd:TIGR00630 783 kniadvldMTveeayeffeAVPSISRKLQTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTG 862
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2418785902 174 LDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASRAERIIKI------KDGKIV 221
Cdd:TIGR00630 863 LHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVV 916
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-218 |
4.74e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 119 KRTAKAKEVLQNVGLGD-RLKHKPGELSGGQRQRVAIARAIV---NDPSILLADEPTGNLDSQSGGDILEIFTELHSQGN 194
Cdd:PRK00635 1674 KKIQKPLQALIDNGLGYlPLGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGH 1753
|
90 100
....*....|....*....|....
gi 2418785902 195 TVIIVTHDQAIASRAERIIKIKDG 218
Cdd:PRK00635 1754 SVIYIDHDPALLKQADYLIEMGPG 1777
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
142-200 |
5.28e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 5.28e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2418785902 142 GELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVT 200
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIIS 448
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-199 |
8.77e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 8.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTL-MHILG-CLDSPTDGTYYLD--DVLVSKMPKA---SLAAV-RNRKigfvfqSF 94
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGrSYGRNISGTVFKDgkEVDVSTVSDAidaGLAYVtEDRK------GY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 95 NLLPHLNILKNVELPLMyGGMSK----------------RKRTA-KAKEVLQNVglgdrlkhkpGELSGGQRQRVAIARA 157
Cdd:NF040905 350 GLNLIDDIKRNITLANL-GKVSRrgvideneeikvaeeyRKKMNiKTPSVFQKV----------GNLSGGNQQKVVLSKW 418
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2418785902 158 IVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIV 199
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVI 460
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-215 |
3.11e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 136 RLKHKP-----GELSGGQRQRVAIARAIVN---DPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIAS 207
Cdd:PRK00635 797 GLDYLPlgrplSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK 876
|
....*...
gi 2418785902 208 RAERIIKI 215
Cdd:PRK00635 877 VADYVLEL 884
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
128-215 |
3.47e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.25 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 128 LQNVGLG----DRLKhkpGELSGGQRQRVAIARAI----VNDPSILlaDEPTGNL---DSQSggdILEIFTELHSQGNTV 196
Cdd:COG0178 469 LVDVGLDyltlDRSA---GTLSGGEAQRIRLATQIgsglVGVLYVL--DEPSIGLhqrDNDR---LIETLKRLRDLGNTV 540
|
90
....*....|....*....
gi 2418785902 197 IIVTHDQAIASRAERIIKI 215
Cdd:COG0178 541 IVVEHDEDTIRAADYIIDI 559
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
17-49 |
3.50e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.25 E-value: 3.50e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2418785902 17 KIKVR-A----LNGIDLQIQKGEFVAIMGPSGSGKSTL 49
Cdd:COG0178 5 KIRIRgArehnLKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-178 |
3.63e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.94 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 38 IMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLVSKMPKASLaavrnrkiGFVFQSFNLLPHLNILKNVElplMYGGMSK 117
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC--------TYIGHNLGLKLEMTVFENLK---FWSEIYN 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2418785902 118 RKRTAKAkeVLQNVGLGDRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQS 178
Cdd:PRK13541 100 SAETLYA--AIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN 158
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
23-53 |
4.40e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 4.40e-05
10 20 30
....*....|....*....|....*....|..
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMH-IL 53
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVNdIL 652
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-175 |
7.27e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.18 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 32 KGEFVAIMGPSGSGKSTLMHILGCLDSPTDGTYYLDDVLvskmpkaslaavrnrKIGFVFQSFNllpHLNILKNV----- 106
Cdd:PRK11819 349 PGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV---------------KLAYVDQSRD---ALDPNKTVweeis 410
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 107 -ELPLMYGGmsKRKRTAKAKEVLQNVGLGDRLKhKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLD 175
Cdd:PRK11819 411 gGLDIIKVG--NREIPSRAYVGRFNFKGGDQQK-KVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-218 |
8.14e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.23 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMhilgcldsptdgtyylddVLVSKMPKASLAAVR--NRKIGF-----VFQSFN 95
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLL------------------LTFMRMVEVCGGEIRvnGREIGAyglreLRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 96 LLPHLNIL------KNVElPLMyggmskrkrTAKAKEV---LQNVGLGDRLKHKPGEL-----------SGGQRQRVAIA 155
Cdd:PTZ00243 1388 MIPQDPVLfdgtvrQNVD-PFL---------EASSAEVwaaLELVGLRERVASESEGIdsrvleggsnySVGQRQLMCMA 1457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 156 RAIVNDPS-ILLADEPTGN----LDSQSGGDILEIFTelhsqGNTVIIVTHDQAIASRAERIIKIKDG 218
Cdd:PTZ00243 1458 RALLKKGSgFILMDEATANidpaLDRQIQATVMSAFS-----AYTVITIAHRLHTVAQYDKIIVMDHG 1520
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
144-216 |
1.74e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 144 LSGGQRQ------RVAIARAIVNDPSILLADEPTGNLDSQ---SGGDILEIFTELHSQGNTVIIVTHDQAIASRAERIIK 214
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDrrtNLKDIIEYSLKDSSDIPQVIMISHHRELLSVADVAYE 881
|
..
gi 2418785902 215 IK 216
Cdd:PRK01156 882 VK 883
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
126-201 |
1.89e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 126 EVLQNVGLGD-RLkhkpG----ELSGGQRQRVAIARAIV---NDPSILLADEPTGNLDSQsggDI---LEIFTELHSQGN 194
Cdd:COG0178 808 QTLQDVGLGYiKL----GqpatTLSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLHFH---DIrklLEVLHRLVDKGN 880
|
....*..
gi 2418785902 195 TVIIVTH 201
Cdd:COG0178 881 TVVVIEH 887
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
122-203 |
2.01e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.69 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 122 AKAKEVLQNVGLG-DRLKHKPGELSGGQRQRVAIARAIVNDPSILLADEPTGNLDSQSggdilEIFTE--LHSQGNTVII 198
Cdd:PRK10636 127 SRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA-----VIWLEkwLKSYQGTLIL 201
|
....*
gi 2418785902 199 VTHDQ 203
Cdd:PRK10636 202 ISHDR 206
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
139-212 |
2.21e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 139 HKPGELSGGQR-Q-----RVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELhSQGNTVIIVTHDQAIASRAERI 212
Cdd:COG4717 554 RPVEELSRGTReQlylalRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAEL-AKGRQVIYFTCHEELVELFQEE 632
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
18-49 |
2.32e-04 |
|
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: 41.92 E-value: 2.32e-04
10 20 30
....*....|....*....|....*....|..
gi 2418785902 18 IKVRALNGIDLQIQKGEFVAIMGPSGSGKSTL 49
Cdd:TIGR00630 7 AREHNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
23-51 |
2.41e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 2.41e-04
10 20
....*....|....*....|....*....
gi 2418785902 23 LNGIDLQIQKGEFVAIMGPSGSGKSTLMH 51
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
17-49 |
3.07e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 3.07e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2418785902 17 KIKVRA-----LNGIDLQIQKGEFVAIMGPSGSGKSTL 49
Cdd:PRK00349 5 KIIIRGarehnLKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
15-219 |
7.14e-04 |
|
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: 39.99 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 15 LGKIKV---RALNGIDLQIQKGeFVAIMGPSGSGKSTLMHILGCLDSPTDGTYY-------------------------- 65
Cdd:COG3593 3 LEKIKIknfRSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFdeedfylgddpdlpeieieltfgsll 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 66 ---LDDVLVSKMPKASLAAVR--NRKIGFVFQSFNllphlNILKNVELPLMYGGMSKRKRTAKAKEVLQ---NVGLGDRL 137
Cdd:COG3593 82 srlLRLLLKEEDKEELEEALEelNEELKEALKALN-----ELLSEYLKELLDGLDLELELSLDELEDLLkslSLRIEDGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 138 KHKPGELSGGQRQRVAIA--RAIV-----NDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASRA- 209
Cdd:COG3593 157 ELPLDRLGSGFQRLILLAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVp 236
|
250
....*....|.
gi 2418785902 210 -ERIIKIKDGK 219
Cdd:COG3593 237 lENIRRLRRDS 247
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
144-215 |
7.28e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 7.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2418785902 144 LSGGQRQ------RVAIARAIVNDPSILLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASRAERIIKI 215
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHDEELKDAADYVIRV 866
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
32-53 |
1.27e-03 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 38.64 E-value: 1.27e-03
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
144-218 |
3.17e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 37.63 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418785902 144 LSGGQRQRVAIARA------IVNDPSI----LLADEPTGNLDSQSGGDILEIFTELHSQGNTVIIVTHDQAIASR-AERI 212
Cdd:cd03279 124 LSGGETFLASLSLAlalsevLQNRGGArleaLFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERiPQRL 203
|
....*.
gi 2418785902 213 IKIKDG 218
Cdd:cd03279 204 EVIKTP 209
|
|
| |
