|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-223 |
2.10e-122 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 346.65 E-value: 2.10e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAF 84
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RNKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKP 164
Cdd:COG1136 84 RRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 165 ALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLGKIAYLDDGKL 223
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-224 |
9.82e-118 |
|
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: 334.71 E-value: 9.82e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAF 84
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RNKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKP 164
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 165 ALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLGKIAYLDDGKLA 224
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLF 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-223 |
7.55e-113 |
|
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: 322.13 E-value: 7.55e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFR 85
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPA 165
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658758220 166 LVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLGKIAYLDDGKL 223
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-223 |
1.12e-104 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 302.12 E-value: 1.12e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTE 80
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 QAAFRNKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARAL 160
Cdd:PRK11629 81 KAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658758220 161 VTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLGKIAYLDDGKL 223
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-223 |
1.31e-92 |
|
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: 271.23 E-value: 1.31e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTE 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 QAAFRNKNLGFIYQFHHLLMEFSAVENVAMPLLIKGlnAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARAL 160
Cdd:COG4181 84 RARLRARHVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658758220 161 VTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLGKIAYLDDGKL 223
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-223 |
1.96e-83 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 247.66 E-value: 1.96e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGQnqvEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAF 84
Cdd:COG2884 1 MIRFENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RnKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKP 164
Cdd:COG2884 78 R-RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 165 ALVLADEPTGNLDKQNAIKIYDLINELNKsLNTSFVVVTHDLELADKLGK-IAYLDDGKL 223
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKrVLELEDGRL 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-211 |
7.56e-69 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 211.87 E-value: 7.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRte 80
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 qaafrnkNLGFIYQfHHLLMEF-SAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARA 159
Cdd:COG1116 81 -------DRGVVFQ-EPALLPWlTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658758220 160 LVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLE----LADK 211
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeavfLADR 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-223 |
6.37e-68 |
|
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: 208.59 E-value: 6.37e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAF 84
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RnKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKP 164
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 165 ALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKL-GKIAYLDDGKL 223
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRIcDRVAVMEKGEV 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-209 |
2.22e-67 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 207.60 E-value: 2.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAF 84
Cdd:COG3638 2 MLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RnKNLGFIYQFHHLLMEFSAVENVAMPLL--------IKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAI 156
Cdd:COG3638 79 R-RRIGMIFQQFNLVPRLSVLTNVLAGRLgrtstwrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 658758220 157 ARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELA 209
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLA 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-230 |
2.93e-66 |
|
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: 204.83 E-value: 2.93e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLL-HILGtLDTATSGSAKIKNQDVAKLSRT 79
Cdd:COG1127 1 MSEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLkLIIG-LLRPDSGEILVDGQDITGLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 80 EQAAFRnKNLGFIYQFHHLLMEFSAVENVAMPLLI-KGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIAR 158
Cdd:COG1127 76 ELYELR-RRIGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 159 ALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKL-------AIKESHH 230
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIAdRVAVLADGKIiaegtpeELLASDD 234
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-223 |
2.80e-65 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 205.31 E-value: 2.80e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFR 85
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPA 165
Cdd:COG1135 82 -RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758220 166 LVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLE----LADklgKIAYLDDGKL 223
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDvvrrICD---RVAVLENGRI 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-223 |
1.39e-64 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 200.01 E-value: 1.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAF 84
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RNKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKP 164
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 165 ALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLGKIAYLDDGKL 223
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-222 |
2.30e-63 |
|
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: 196.32 E-value: 2.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAF 84
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RNKnLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKP 164
Cdd:TIGR02673 78 RRR-IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 165 ALVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKLGK-IAYLDDGK 222
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHrVIILDDGR 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-224 |
2.78e-63 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 200.71 E-value: 2.78e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSrTE 80
Cdd:COG3842 1 MAMPALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP-PE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 QaafRNknLGFIYQ----FHHLlmefSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAI 156
Cdd:COG3842 76 K---RN--VGMVFQdyalFPHL----TVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758220 157 ARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLE----LADklgKIAYLDDGKLA 224
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEealaLAD---RIAVMNDGRIE 215
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
5-224 |
8.60e-63 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 195.24 E-value: 8.60e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAF 84
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RnKNLGFIYQFHHLLMEFSAVENVAMPL-LIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTK 163
Cdd:TIGR02982 81 R-RRIGYIFQAHNLLGFLTARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658758220 164 PALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLGKIAYLDDGKLA 224
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
6-223 |
1.08e-62 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 194.94 E-value: 1.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFR 85
Cdd:NF038007 2 LNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPA 165
Cdd:NF038007 82 RELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658758220 166 LVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKLGKIAYLDDGKL 223
Cdd:NF038007 162 LLLADEPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-212 |
9.34e-62 |
|
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: 192.30 E-value: 9.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRteqaafr 85
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nkNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPA 165
Cdd:cd03293 74 --DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 658758220 166 LVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLE----LADKL 212
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDeavfLADRV 202
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
9-223 |
1.16e-61 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 203.80 E-value: 1.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 9 QNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFRNKN 88
Cdd:PRK10535 8 KDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 89 LGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVL 168
Cdd:PRK10535 88 FGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 169 ADEPTGNLDKQNAIKIYDLINELNKSLNTsFVVVTHDLELADKLGKIAYLDDGKL 223
Cdd:PRK10535 168 ADEPTGALDSHSGEEVMAILHQLRDRGHT-VIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-223 |
1.30e-60 |
|
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: 198.20 E-value: 1.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVY-QDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAA 83
Cdd:COG1123 260 LLEVRNLSKRYpVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 84 FRnKNLGFIYQ--FHHLLMEFSAVENVAMPLLI-KGLNAKEAKEQALQMLDKVGLAHRSEHK-PSALSGGERQRVAIARA 159
Cdd:COG1123 340 LR-RRVQMVFQdpYSSLNPRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 160 LVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKL-GKIAYLDDGKL 223
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIaDRVAVMYDGRI 483
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-223 |
2.23e-60 |
|
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: 189.25 E-value: 2.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAF 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RNKnLGFIYQ--FHHLLMEFSAVENVAMPLLIKGLNAKEA--KEQALQMLDKVGLAHRSEHK-PSALSGGERQRVAIARA 159
Cdd:cd03257 81 RKE-IQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEarKEAVLLLLVGVGLPEEVLNRyPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 160 LVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKL-GKIAYLDDGKL 223
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIaDRVAVMYAGKI 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-224 |
5.11e-60 |
|
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: 188.93 E-value: 5.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFR 85
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nKNLGFIYQFHHLLMEFSAVENVAMPLL--------IKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIA 157
Cdd:cd03256 78 -RQIGMIFQQFNLIERLSVLENVLSGRLgrrstwrsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658758220 158 RALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKLA 224
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYAdRIVGLKDGRIV 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-223 |
9.44e-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: 187.71 E-value: 9.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQnqveVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFR 85
Cdd:cd03261 1 IELRGLTKSFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nKNLGFIYQFHHLLMEFSAVENVAMPLLIKG-LNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKP 164
Cdd:cd03261 77 -RRMGMLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 165 ALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIAdRIAVLYDGKI 215
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-222 |
1.91e-59 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 187.12 E-value: 1.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAkLSRTEQAAF 84
Cdd:COG1126 1 MIEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RnKNLGFIYQ----FHHLlmefSAVENVAM-PLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARA 159
Cdd:COG1126 76 R-RKVGMVFQqfnlFPHL----TVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658758220 160 LVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDL----ELADklgKIAYLDDGK 222
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMgfarEVAD---RVVFMDGGR 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-224 |
7.83e-57 |
|
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: 180.22 E-value: 7.83e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEqaaFR 85
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE---LR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nKNLGFIYQF--HHLLMEfSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTK 163
Cdd:COG1122 75 -RKVGLVFQNpdDQLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758220 164 PALVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKLG-KIAYLDDGKLA 224
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELAdRVIVLDDGRIV 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-215 |
2.50e-56 |
|
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: 181.79 E-value: 2.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 9 QNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLD--TATSGSAKIKNQDVAKLSRTEQAAFR 85
Cdd:COG0444 5 RNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPppGITSGEILFDGEDLLKLSEKELRKIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKNLGFIYQfhhllmE-FSA------VEN-VAMPLLI-KGLNAKEAKEQALQMLDKVGLAHRSEHK---PSALSGGERQR 153
Cdd:COG0444 85 GREIQMIFQ------DpMTSlnpvmtVGDqIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658758220 154 VAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDL----ELADK-----LGKI 215
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLgvvaEIADRvavmyAGRI 229
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-224 |
4.67e-55 |
|
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: 175.02 E-value: 4.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 9 QNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLsrteqaAFRNKN 88
Cdd:cd03259 4 KGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV------PPERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 89 LGFIYQ----FHHLlmefSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKP 164
Cdd:cd03259 74 IGMVFQdyalFPHL----TVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658758220 165 ALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKLA 224
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALAdRIAVMNEGRIV 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-223 |
5.63e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 175.64 E-value: 5.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVaklsRTEQAAFR 85
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPA 165
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 166 LVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKL-GKIAYLDDGKL 223
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLcDRVAIIDKGRI 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-223 |
2.43e-54 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 177.57 E-value: 2.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVIscQNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSrte 80
Cdd:COG3839 1 MASLEL--ENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 qAAFRNknLGFIYQ----FHHLlmefSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAI 156
Cdd:COG3839 72 -PKDRN--IAMVFQsyalYPHM----TVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658758220 157 ARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLE----LADklgKIAYLDDGKL 223
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVeamtLAD---RIAVMNDGRI 212
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-223 |
8.51e-54 |
|
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: 171.94 E-value: 8.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYqdGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKlSRTEQAAFR 85
Cdd:cd03262 1 IEIKNLHKSF--GDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nKNLGFIYQFHHLLMEFSAVENVAM-PLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKP 164
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 165 ALVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVAdRVIFMDDGRI 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-224 |
1.05e-53 |
|
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: 173.07 E-value: 1.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVaklSRTEQAAFR 85
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV---TRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nKNLGFIYQ-----FH------HLLMEfsavenvamPLLIKGLnaKEAKEQALQMLDKVGL----AHRsehKPSALSGGE 150
Cdd:COG1124 79 -RRVQMVFQdpyasLHprhtvdRILAE---------PLRIHGL--PDREERIAELLEQVGLppsfLDR---YPHQLSGGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 151 RQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKL-GKIAYLDDGKLA 224
Cdd:COG1124 144 RQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLcDRVAVMQNGRIV 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-224 |
6.80e-53 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 170.66 E-value: 6.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYqdGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAF 84
Cdd:PRK09493 1 MIEFKNVSKHF--GPTQV--LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RNKnlGFIYQFHHLLMEFSAVENVAM-PLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTK 163
Cdd:PRK09493 77 QEA--GMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658758220 164 PALVLADEPTGNLD---KQNAIKIY-DLINElnkslNTSFVVVTHDLELADKLG-KIAYLDDGKLA 224
Cdd:PRK09493 155 PKLMLFDEPTSALDpelRHEVLKVMqDLAEE-----GMTMVIVTHEIGFAEKVAsRLIFIDKGRIA 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-223 |
8.13e-53 |
|
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: 169.51 E-value: 8.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFR 85
Cdd:cd03292 1 IEFINVTKTYP---NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKnLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPA 165
Cdd:cd03292 78 RK-IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 166 LVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKLGK-IAYLDDGKL 223
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-223 |
1.11e-52 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 173.06 E-value: 1.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAF 84
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RnKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKP 164
Cdd:PRK11153 81 R-RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658758220 165 ALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLE----LADklgKIAYLDDGKL 223
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDvvkrICD---RVAVIDAGRL 219
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-218 |
1.80e-52 |
|
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: 168.18 E-value: 1.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 9 QNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFRNKN 88
Cdd:TIGR03608 2 KNISKKFGD----KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 89 LGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVL 168
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 658758220 169 ADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKLGKIAYL 218
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-223 |
1.26e-51 |
|
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: 167.48 E-value: 1.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAF 84
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RnKNLGFIYQFHHLLMEFSAVENVAMPLL--------IKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAI 156
Cdd:TIGR02315 78 R-RRIGMIFQHYNLIERLTVLENVLHGRLgykptwrsLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658758220 157 ARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYAdRIVGLKAGEI 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-223 |
1.90e-51 |
|
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: 173.94 E-value: 1.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGQnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLD--TATSGSAKIKNQDVAKLSrteq 81
Cdd:COG1123 4 LLEVRDLSVRYPGGD--VPAVDGVSLTIAPGETVALVGESGSGKSTLALaLMGLLPhgGRISGEVLLDGRDLLELS---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 82 AAFRNKNLGFIYQ-FHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARAL 160
Cdd:COG1123 78 EALRGRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658758220 161 VTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLEL-ADKLGKIAYLDDGKL 223
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRI 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-222 |
2.21e-51 |
|
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: 165.72 E-value: 2.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 7 SCQNLSKVYQDGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEqaafRN 86
Cdd:cd03225 1 ELKNLSFSYPDGARPA--LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE----LR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 87 KNLGFIYQF--HHLLMEfSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKP 164
Cdd:cd03225 75 RKVGLVFQNpdDQFFGP-TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 165 ALVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKLG-KIAYLDDGK 222
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELAdRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-224 |
2.53e-51 |
|
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: 166.76 E-value: 2.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAaf 84
Cdd:COG1120 1 MLEAENLSVGYGG----RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 rnKNLGFIYQFHHLLMEFSAVENVAM---PLL-IKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARAL 160
Cdd:COG1120 75 --RRIAYVPQEPPAPFGLTVRELVALgryPHLgLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658758220 161 VTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELA----DklgKIAYLDDGKLA 224
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAaryaD---RLVLLKDGRIV 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-231 |
3.75e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 163.72 E-value: 3.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLdTATSGSAKIKNQDVAKlsrt 79
Cdd:COG1121 2 MMMPAIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILGLL-PPTSGTVRLFGKPPRR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 80 eqaafRNKNLGFIYQFHHLLMEF--SAVENVAMPL-----LIKGLNAKEaKEQALQMLDKVGLAHRsEHKP-SALSGGER 151
Cdd:COG1121 73 -----ARRRIGYVPQRAEVDWDFpiTVRDVVLMGRygrrgLFRRPSRAD-REAVDEALERVGLEDL-ADRPiGELSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 152 QRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKL-GKIAYLDDGKLAIKESHH 230
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYfDRVLLLNRGLVAHGPPEE 224
|
.
gi 658758220 231 V 231
Cdd:COG1121 225 V 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
6-223 |
1.36e-48 |
|
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: 160.50 E-value: 1.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVY-----------QDGQNQVEVLKG---------VDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGS 65
Cdd:cd03294 1 IKIKGLYKIFgknpqkafkllAKGKSKEEILKKtgqtvgvndVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 66 AKIKNQDVAKLSRTEQAAFRNKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSA 145
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 146 LSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGdRIAIMKDGRL 239
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-223 |
1.41e-48 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 158.88 E-value: 1.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGQnqvEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLsRTEQAAF 84
Cdd:PRK10908 1 MIRFEHVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRL-KNREVPF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RNKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKP 164
Cdd:PRK10908 77 LRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 165 ALVLADEPTGNLDKQNAIKIYDLINELNKsLNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
10-222 |
1.40e-46 |
|
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: 152.34 E-value: 1.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 10 NLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAafRNKNL 89
Cdd:cd03229 5 NVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPP--LRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 90 GFIYQFHHLLMEFSAVENVAMPLlikglnakeakeqalqmldkvglahrsehkpsalSGGERQRVAIARALVTKPALVLA 169
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 658758220 170 DEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGK 222
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLAdRVVVLRDGK 178
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-223 |
1.69e-46 |
|
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: 153.93 E-value: 1.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQnqveVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEqaafr 85
Cdd:cd03300 1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPA 165
Cdd:cd03300 72 -RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758220 166 LVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHD----LELADklgKIAYLDDGKL 223
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDqeeaLTMSD---RIAVMNKGKI 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-223 |
1.02e-45 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 152.09 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYqdGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDV---AKLSRTEQA 82
Cdd:COG4161 3 IQLKNINCFY--GSHQA--LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 83 AFRnKNLGFIYQFHHLLMEFSAVEN-VAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALV 161
Cdd:COG4161 79 LLR-QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658758220 162 TKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSfVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQ-VIVTHEVEFARKVAsQVVYMEKGRI 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-173 |
1.93e-45 |
|
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: 148.56 E-value: 1.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 25 LKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRteqaAFRNKNLGFIYQFHHLLMEFSA 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER----KSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658758220 105 VENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHK----PSALSGGERQRVAIARALVTKPALVLADEPT 173
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-223 |
4.62e-45 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 153.38 E-value: 4.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAklsrTEQAAfR 85
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF----TNLPP-R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKNLGFIYQ----FHHLlmefSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALV 161
Cdd:COG1118 74 ERRVGFVFQhyalFPHM----TVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658758220 162 TKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHD----LELADklgKIAYLDDGKL 223
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDqeeaLELAD---RVVVMNQGRI 212
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-206 |
1.19e-44 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 152.04 E-value: 1.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYQ------DGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVA 74
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPvkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 75 KLSRTEQAA--------FRN--------KNLGFIyqfhhlLMEfsavenvamPLLIK-GLNAKEAKEQALQMLDKVGLah 137
Cdd:PRK11308 81 KADPEAQKLlrqkiqivFQNpygslnprKKVGQI------LEE---------PLLINtSLSAAERREKALAMMAKVGL-- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758220 138 RSEHK---PSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDL 206
Cdd:PRK11308 144 RPEHYdryPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDL 215
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-209 |
3.93e-44 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 148.86 E-value: 3.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVIScqNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVaklsrTE 80
Cdd:COG4525 1 MSMLTVR--HVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-----TG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 QAAFRnknlGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARAL 160
Cdd:COG4525 74 PGADR----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 658758220 161 VTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELA 209
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-223 |
4.42e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.88 E-value: 4.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQnqveVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEqaaFR 85
Cdd:COG4619 1 LELEGLSFRVGGKP----ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE---WR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nKNLGFIYQfHHLLMEFSAVENVAMPLLIKGLNAKEakEQALQMLDKVGLAHRSEHKP-SALSGGERQRVAIARALVTKP 164
Cdd:COG4619 74 -RQVAYVPQ-EPALWGGTVRDNLPFPFQLRERKFDR--ERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 165 ALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVAdRVLTLEAGRL 209
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-223 |
6.53e-44 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 147.47 E-value: 6.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYqdGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQ--DVAKLSRTEQAA 83
Cdd:PRK11124 3 IQLNGINCFY--GAHQA--LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 84 FRNKNLGFIYQFHHLLMEFSAVEN-VAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVT 162
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758220 163 KPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSfVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQ-VIVTHEVEVARKTAsRVVYMENGHI 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-224 |
1.04e-43 |
|
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: 146.14 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 7 SCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLdTATSGSAKIKNQDVAKlsrteqaafR 85
Cdd:cd03235 1 EVEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLL-KPTSGSIRVFGKPLEK---------E 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKNLGFIYQFHHLLMEF--SAVENVAMPLLIK----GLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARA 159
Cdd:cd03235 67 RKRIGYVPQRRSIDRDFpiSVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658758220 160 LVTKPALVLADEPTGNLDKQNAIKIYDLINELNKsLNTSFVVVTHDLELA-DKLGKIAYLDDGKLA 224
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVlEYFDRVLLLNRTVVA 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-223 |
4.47e-43 |
|
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: 144.70 E-value: 4.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 9 QNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEqaafrnKN 88
Cdd:cd03301 4 ENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD------RD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 89 LGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVL 168
Cdd:cd03301 74 IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658758220 169 ADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMAdRIAVMNDGQI 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-228 |
6.59e-43 |
|
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: 145.00 E-value: 6.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTeqaaf 84
Cdd:COG4555 1 MIEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RNKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKP 164
Cdd:COG4555 72 ARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 165 ALVLADEPTGNLDKQNAIKIYDLINELnKSLNTSFVVVTHDLELADKL-GKIAYLDDGKLAIKES 228
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGS 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
9-223 |
1.46e-42 |
|
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: 144.02 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 9 QNLSKVYQDGQnqvevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRteqaafRNKN 88
Cdd:cd03299 4 ENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP------EKRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 89 LGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVL 168
Cdd:cd03299 73 ISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658758220 169 ADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALAdKVAIMLNGKL 208
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-212 |
2.66e-42 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 146.38 E-value: 2.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRteqaafR 85
Cdd:PRK10851 3 IEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKNLGFIYQFHHLLMEFSAVENVAMPLLI----KGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALV 161
Cdd:PRK10851 73 DRKVGFVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 162 TKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHD----LELADKL 212
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDqeeaMEVADRV 207
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-224 |
3.82e-42 |
|
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: 142.51 E-value: 3.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQaafr 85
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPA 165
Cdd:cd03265 73 -RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 166 LVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKL-GKIAYLDDGKLA 224
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLcDRVAIIDHGRII 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-212 |
6.12e-42 |
|
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: 142.19 E-value: 6.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNdLVISCQNLSKVY----QDGQnQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLdTATSGSAKIKNQ---- 71
Cdd:COG4778 1 MT-TLLEVENLSKTFtlhlQGGK-RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKcIYGNY-LPDSGSILVRHDggwv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 72 DVAKLSRTEQAAFRNKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEH-KPSALSGGE 150
Cdd:COG4778 78 DLAQASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDlPPATFSGGE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658758220 151 RQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELnKSLNTSFVVVTHDLE----LADKL 212
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEvreaVADRV 222
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
6-223 |
1.41e-41 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 141.48 E-value: 1.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQnqveVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSrteqaaFR 85
Cdd:TIGR00968 1 IEIANISKRFGSFQ----ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVH------AR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPA 165
Cdd:TIGR00968 71 DRKIGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758220 166 LVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHD----LELADklgKIAYLDDGKL 223
Cdd:TIGR00968 151 VLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDqeeaMEVAD---RIVVMSNGKI 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-223 |
2.83e-41 |
|
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: 138.72 E-value: 2.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 7 SCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAafrn 86
Cdd:cd03214 1 EVENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 87 KNLGFIyqfhhllmefsavenvampllikglnakeakeqaLQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPAL 166
Cdd:cd03214 73 RKIAYV----------------------------------PQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658758220 167 VLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYAdRVILLKDGRI 176
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-222 |
3.36e-41 |
|
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: 138.28 E-value: 3.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEqaafR 85
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES----L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKNLGFIYQFHHLlmeFSA--VENVampllikglnakeakeqalqmldkvglahrsehkpsaLSGGERQRVAIARALVTK 163
Cdd:cd03228 75 RKNIAYVPQDPFL---FSGtiRENI-------------------------------------LSGGQRQRIAIARALLRD 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 164 PALVLADEPTGNLDKQNAIKIYDLINELNKslNTSFVVVTHDLELADKLGKIAYLDDGK 222
Cdd:cd03228 115 PPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-223 |
3.89e-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: 146.75 E-value: 3.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKS-TLLHILGTLDTA---TSGSAKIKNQDVAKL 76
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 77 SRTEQAAFRNKNLGFIYQfhhllmE--------FSAVENVAMPLLI-KGLNAKEAKEQALQMLDKVGL---AHRSEHKPS 144
Cdd:COG4172 82 SERELRRIRGNRIAMIFQ------EpmtslnplHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 145 ALSGGERQRVAIARALVTKPALVLADEPTGNLD----KQnaikIYDLINELNKSLNTSFVVVTHDL----ELADklgKIA 216
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqAQ----ILDLLKDLQRELGMALLLITHDLgvvrRFAD---RVA 228
|
....*..
gi 658758220 217 YLDDGKL 223
Cdd:COG4172 229 VMRQGEI 235
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-223 |
7.75e-41 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 139.89 E-value: 7.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQdGQnqvEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQ--DVAKLSRTEQAA 83
Cdd:PRK11264 4 IEVKNLVKKFH-GQ---TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDItiDTARSLSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 84 FRN--KNLGFIYQFHHLLMEFSAVENVAM-PLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARAL 160
Cdd:PRK11264 80 IRQlrQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658758220 161 VTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTsFVVVTHDLELA-DKLGKIAYLDDGKL 223
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFArDVADRAIFMDQGRI 222
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-224 |
1.11e-40 |
|
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: 140.28 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQ-NQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAF 84
Cdd:TIGR04521 1 IKLKNVSYIYQPGTpFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RnKNLGFIYQF-HHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGL----AHRSehkPSALSGGERQRVAIARA 159
Cdd:TIGR04521 81 R-KKVGLVFQFpEHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdeeyLERS---PFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 160 LVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLE----LADklgKIAYLDDGKLA 224
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEdvaeYAD---RVIVMHKGKIV 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-223 |
1.24e-40 |
|
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: 138.41 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 9 QNLSKVYQDGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVaklsRTEQAAFRnKN 88
Cdd:cd03263 4 RNLTKTYKKGTKPA--VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKAAR-QS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 89 LGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVL 168
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658758220 169 ADEPTGNLDKQNAIKIYDLINELNKslNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCdRIAIMSDGKL 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-215 |
1.28e-40 |
|
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: 138.00 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKlsrteQAAF 84
Cdd:COG4133 2 MLEAENLSCRRGE----RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-----ARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RNKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAkeAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKP 164
Cdd:COG4133 73 YRRRLAYLGHADGLKPELTVRENLRFWAALYGLRA--DREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 658758220 165 ALVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKLGKI 215
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQPLELAAARVL 200
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-215 |
2.52e-40 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 140.64 E-value: 2.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYQDGQN----QVEVLK---GVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDV 73
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGlfgrTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 74 AKLSRTEQAAFRnKNLGFIYQ--FHHLlmefsaveN--------VAMPLLIKGL-NAKEAKEQALQMLDKVGLahRSEHK 142
Cdd:COG4608 83 TGLSGRELRPLR-RRMQMVFQdpYASL--------NprmtvgdiIAEPLRIHGLaSKAERRERVAELLELVGL--RPEHA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 143 ---PSALSGGERQRVAIARALVTKPALVLADEPTGNLDK----QnaikIYDLINELNKSLNTSFVVVTHDL----ELADK 211
Cdd:COG4608 152 dryPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVsiqaQ----VLNLLEDLQDELGLTYLFISHDLsvvrHISDR 227
|
....*....
gi 658758220 212 -----LGKI 215
Cdd:COG4608 228 vavmyLGKI 236
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
6-223 |
2.58e-40 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 141.37 E-value: 2.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQnqvevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSrTEQaafr 85
Cdd:NF040840 2 IRIENLSKDWKEFK-----LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLP-PEK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPA 165
Cdd:NF040840 72 -RGIAYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 166 LVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:NF040840 151 LLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLAdRVGIMLNGRL 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-224 |
3.24e-40 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 137.58 E-value: 3.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 29 DLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLS---RTEQAAFRNKNLgfiyqFHHLlmefSAV 105
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpaeRPVSMLFQENNL-----FPHL----TVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 106 ENVAMpllikGLNAK-----EAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLD--- 177
Cdd:COG3840 90 QNIGL-----GLRPGlkltaEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpal 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 658758220 178 KQNaikIYDLINELNKSLNTSFVVVTHDLELADKL-GKIAYLDDGKLA 224
Cdd:COG3840 165 RQE---MLDLVDELCRERGLTVLMVTHDPEDAARIaDRVLLVADGRIA 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-223 |
3.30e-40 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 137.70 E-value: 3.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTL-----DTATSGSAKIKNQDVAKLsRTE 80
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDL-DVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 QAAFRnKNLGFIYQfHHLLMEFSAVENVAMPLLIKG-LNAKEAKEQALQMLDKVGL---AHRSEHkPSALSGGERQRVAI 156
Cdd:cd03260 76 VLELR-RRVGMVFQ-KPNPFPGSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALwdeVKDRLH-ALGLSGGQQQRLCL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658758220 157 ARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKslNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVAdRTAFLLNGRL 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-230 |
4.16e-40 |
|
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: 144.52 E-value: 4.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 3 DLVISCQNLSKVYQDGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLDtATSGSAKIKNQDVAKLSRTEQ 81
Cdd:COG4987 331 GPSLELEDVSFRYPGAGRPV--LDGLSLTLPPGERVAIVGPSGSGKSTLLAlLLRFLD-PQSGSITLGGVDLRDLDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 82 AAfrnkNLGFIYQFHHLlmeFSA--VENvampLLIKGLNAKEakEQALQMLDKVGLAHRSEHKP-----------SALSG 148
Cdd:COG4987 408 RR----RIAVVPQRPHL---FDTtlREN----LRLARPDATD--EELWAALERVGLGDWLAALPdgldtwlgeggRRLSG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 149 GERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINEL--NKSLntsfVVVTHDLELADKLGKIAYLDDGKLAIK 226
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTV----LLITHRLAGLERMDRILVLEDGRIVEQ 550
|
....
gi 658758220 227 ESHH 230
Cdd:COG4987 551 GTHE 554
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-223 |
5.87e-40 |
|
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: 135.22 E-value: 5.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGqnqvEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKlsrtEQAAFR 85
Cdd:cd03230 1 IEVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK----EPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nKNLGFIYQFhhllmefsavenvamPLLIKGLNAKEakeqalqMLDkvglahrsehkpsaLSGGERQRVAIARALVTKPA 165
Cdd:cd03230 73 -RRIGYLPEE---------------PSLYENLTVRE-------NLK--------------LSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 166 LVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCdRVAILNNGRI 173
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
21-223 |
3.03e-39 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 136.25 E-value: 3.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 21 QVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVA---------KLSRTEQAAFRNKNLGF 91
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKVADKNQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 92 IYQFHHLLMEFSAVENV-AMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHK-PSALSGGERQRVAIARALVTKPALVLA 169
Cdd:PRK10619 97 VFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 170 DEPTGNLDKQNAIKIYDLINELNKSLNTsFVVVTHDLELADKLGK-IAYLDDGKL 223
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAEEGKT-MVVVTHEMGFARHVSShVIFLHQGKI 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-222 |
4.13e-39 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 132.37 E-value: 4.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 7 SCQNLSKVYQDGQnqveVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAafrn 86
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 87 KNLGFIYQfhhllmefsavenvampllikglnakeakeqalqmldkvglahrsehkpsaLSGGERQRVAIARALVTKPAL 166
Cdd:cd00267 73 RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 658758220 167 VLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKLG-KIAYLDDGK 222
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAAdRVIVLKDGK 157
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-223 |
4.43e-39 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 135.16 E-value: 4.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSrteqaaFR 85
Cdd:cd03296 3 IEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKNLGFIYQFHHLLMEFSAVENVAMPLLIK----GLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALV 161
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVAFGLRVKprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658758220 162 TKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHD----LELADklgKIAYLDDGKL 223
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDqeeaLEVAD---RVVVMNKGRI 215
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-224 |
5.65e-39 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 138.16 E-value: 5.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYqDGQnqvEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSrTE 80
Cdd:PRK09452 10 SLSPLVELRGISKSF-DGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-AE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 QaafRNKNLGFiyQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARAL 160
Cdd:PRK09452 85 N---RHVNTVF--QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658758220 161 VTKPALVLADEPTGNLD------KQNAIKiydlinELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKLA 224
Cdd:PRK09452 160 VNKPKVLLLDESLSALDyklrkqMQNELK------ALQRKLGITFVFVTHDQEEALTMSdRIVVMRDGRIE 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-224 |
1.06e-38 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 134.35 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQNQVevlKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEqaaFR 85
Cdd:cd03295 1 IEFENVTKRYGGGKKAV---NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---LR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGL--AHRSEHKPSALSGGERQRVAIARALVTK 163
Cdd:cd03295 75 -RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758220 164 PALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKLA 224
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLAdRIAIMKNGEIV 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-224 |
2.32e-38 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 133.74 E-value: 2.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSkvYQDGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHIL-GTLdTATSGSAKIKNQDVAKLSRTEQAa 83
Cdd:PRK13548 2 MLEARNLS--VRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGEL-SPDSGEVRLNGRPLADWSPAELA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 84 frnKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALV-- 161
Cdd:PRK13548 76 ---RRRAVLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658758220 162 ----TKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELA----DklgKIAYLDDGKLA 224
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAaryaD---RIVLLHQGRLV 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-224 |
6.27e-38 |
|
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: 131.16 E-value: 6.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQnqveVLKGVDLSLNQGdMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKlSRTEqaaFR 85
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQK---LR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPA 165
Cdd:cd03264 72 -RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 166 LVLADEPTGNLDKQNAIKIYDLINELnkSLNTSFVVVTHDLE-LADKLGKIAYLDDGKLA 224
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-223 |
9.22e-38 |
|
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: 132.62 E-value: 9.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDG-----QNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRT 79
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 80 EQAAFRnKNLGFIYQ--FHHLLMEFSAVENVAMPLL-IKGLNAKEAKEQALQMLDKVGLahRSEH---KPSALSGGERQR 153
Cdd:TIGR02769 82 QRRAFR-RDVQLVFQdsPSAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGL--RSEDadkLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658758220 154 VAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCqRVAVMDKGQI 229
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-224 |
1.08e-37 |
|
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: 133.77 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 40 IVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVaklsrTEQAAFRnKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNA 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV-----TNVPPHL-RHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 120 KEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSF 199
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180
....*....|....*....|....*.
gi 658758220 200 VVVTHDLELADKL-GKIAYLDDGKLA 224
Cdd:TIGR01187 155 VFVTHDQEEAMTMsDRIAIMRKGKIA 180
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-215 |
2.38e-37 |
|
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: 136.74 E-value: 2.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 21 QVEVLKGVDLSLNQGDMLAIVGSSGSGKSTL-LHILGTLDTatSGSAKIKNQDVAKLSRTEQAAFRnKNLGFIYQ--FHH 97
Cdd:COG4172 298 HVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLIPS--EGEIRFDGQDLDGLSRRALRPLR-RRMQVVFQdpFGS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 98 LLMEFSAVENVAMPLLI--KGLNAKEAKEQALQMLDKVGLAHRSEHK-PSALSGGERQRVAIARALVTKPALVLADEPTG 174
Cdd:COG4172 375 LSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPAARHRyPHEFSGGQRQRIAIARALILEPKLLVLDEPTS 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 658758220 175 NLD----KQnaikIYDLINELNKSLNTSFVVVTHDL----ELAD-----KLGKI 215
Cdd:COG4172 455 ALDvsvqAQ----ILDLLRDLQREHGLAYLFISHDLavvrALAHrvmvmKDGKV 504
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-223 |
7.84e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 130.19 E-value: 7.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDG-----QNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTE 80
Cdd:PRK10419 4 LNVSGLSHHYAHGglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 QAAFRnKNLGFIYQfhhllMEFSAV-------ENVAMPLL-IKGLNAKEAKEQALQMLDKVGLAHRSEHK-PSALSGGER 151
Cdd:PRK10419 84 RKAFR-RDIQMVFQ-----DSISAVnprktvrEIIREPLRhLLSLDKAERLARASEMLRAVDLDDSVLDKrPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658758220 152 QRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKL-GKIAYLDDGKL 223
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFcQRVMVMDNGQI 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-209 |
1.02e-36 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 129.66 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 7 SCQNLSKVYQDGQNqvevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQ-----DVAKLSRTEQ 81
Cdd:PRK11701 8 SVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 82 AAFRNKNLGFIYQfhH----LLMEFSAVENVAMPLLIKGL-NAKEAKEQALQMLDKVGL-AHRSEHKPSALSGGERQRVA 155
Cdd:PRK11701 84 RRLLRTEWGFVHQ--HprdgLRMQVSAGGNIGERLMAVGArHYGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 658758220 156 IARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELA 209
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVA 215
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-230 |
1.18e-36 |
|
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: 134.89 E-value: 1.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 2 NDLVISCQNLSKVYQDGQNqveVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEq 81
Cdd:COG4988 333 GPPSIELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 82 aafRNKNLGFIYQFHHLlmeFSAV--ENVAmpllikgLNAKEAKEQAL-QMLDKVGLAHRSEHKP-----------SALS 147
Cdd:COG4988 409 ---WRRQIAWVPQNPYL---FAGTirENLR-------LGRPDASDEELeAALEAAGLDEFVAALPdgldtplgeggRGLS 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 148 GGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTsfVVVTHDLELADKLGKIAYLDDGKLAIKE 227
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTV--ILITHRLALLAQADRILVLDDGRIVEQG 553
|
...
gi 658758220 228 SHH 230
Cdd:COG4988 554 THE 556
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-215 |
1.63e-36 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 127.60 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 19 QNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLDTA--TSGSAKIKNQDVAKLSrTEQaafrnKNLGFIYQF 95
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALP-AEQ-----RRIGILFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 96 HHLLMEFSAVENV--AMPlliKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPT 173
Cdd:COG4136 85 DLLFPHLSVGENLafALP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 658758220 174 GNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLGKI 215
Cdd:COG4136 162 SKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRV 203
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-223 |
2.17e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 128.64 E-value: 2.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 9 QNLSKVYqdGQNqvEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNqdvAKLSrteqAAFRNKN 88
Cdd:PRK11247 16 NAVSKRY--GER--TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT---APLA----EAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 89 LGFiyQFHHLLMEFSAVENVAMPLliKGlnakEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVL 168
Cdd:PRK11247 85 LMF--QDARLLPWKKVIDNVGLGL--KG----QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 169 ADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLE----LADKLGKIaylDDGKL 223
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSeavaMADRVLLI---EEGKI 212
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-230 |
2.24e-36 |
|
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: 135.35 E-value: 2.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYqdGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRteqAAFR 85
Cdd:COG2274 474 IELENVSFRY--PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDP---ASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NkNLGFIYQfHHLLMEFSAVENVAMpllikglNAKEA-KEQALQMLDKVGLAHRSEHKP-----------SALSGGERQR 153
Cdd:COG2274 549 R-QIGVVLQ-DVFLFSGTIRENITL-------GDPDAtDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658758220 154 VAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKslNTSFVVVTHDLELADKLGKIAYLDDGKLAIKESHH 230
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHE 694
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-224 |
5.01e-36 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 130.53 E-value: 5.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQ---DVAKLSRteqa 82
Cdd:PRK11000 4 VTLRNVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAER---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 83 afrnkNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVT 162
Cdd:PRK11000 76 -----GVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658758220 163 KPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHD----LELADklgKIAYLDDGKLA 224
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDqveaMTLAD---KIVVLDAGRVA 213
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-209 |
5.20e-36 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 127.82 E-value: 5.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATsgsaKIKNQDVAKLSRTEQAAF 84
Cdd:PRK09984 4 IIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGD----KSAGSHIELLGRTVQREG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 R--------NKNLGFIYQFHHLLMEFSAVENVamplLIKGLNA------------KEAKEQALQMLDKVGLAHRSEHKPS 144
Cdd:PRK09984 76 RlardirksRANTGYIFQQFNLVNRLSVLENV----LIGALGStpfwrtcfswftREQKQRALQALTRVGMVHFAHQRVS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 145 ALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELA 209
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYA 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
22-208 |
4.10e-35 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 124.47 E-value: 4.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 22 VEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAfrnknLGFIYQFHH--LL 99
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIAR-----LGIGRTFQIprLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 100 MEFSAVENVAMPLLIKGLNA----------KEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLA 169
Cdd:cd03219 88 PELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 658758220 170 DEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLEL 208
Cdd:cd03219 168 DEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDV 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-227 |
5.16e-35 |
|
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: 130.31 E-value: 5.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKI----------------- 68
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 69 ---------------KNQDVAKLSRTEQAAFRNKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKV 133
Cdd:TIGR03269 77 kvgepcpvcggtlepEEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 134 GLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLG 213
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250
....*....|....*
gi 658758220 214 KIA-YLDDGklAIKE 227
Cdd:TIGR03269 237 DKAiWLENG--EIKE 249
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-224 |
5.20e-35 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 123.94 E-value: 5.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 28 VDLSLNqGDMLAIVGSSGSGKSTLLHILGTLDTATSGsaKIKNQDVAkLSRTEQAAF---RNKNLGFIYQFHHLLMEFSA 104
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGG--TIVLNGTV-LFDSRKKINlppQQRKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 105 VENVAMPLliKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKI 184
Cdd:cd03297 93 RENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 658758220 185 YDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKLA 224
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLAdRIVVMEDGRLQ 211
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
16-206 |
1.29e-34 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 125.99 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 16 QDGQnqVEVLKGVDLSLNQGDMLAIVGSSGSGKS-TLLHILGTL--DTATSGSAKIKNQDVAKLSRTEQAAFRNKNLGFI 92
Cdd:PRK09473 25 PDGD--VTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLaaNGRIGGSATFNGREILNLPEKELNKLRAEQISMI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 93 YQ-----------FHHLLMEfsavenVAMplLIKGLNAKEAKEQALQMLDKVGLAH---RSEHKPSALSGGERQRVAIAR 158
Cdd:PRK09473 103 FQdpmtslnpymrVGEQLME------VLM--LHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAM 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 658758220 159 ALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDL 206
Cdd:PRK09473 175 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-224 |
3.95e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 122.53 E-value: 3.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSkvYQDGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHIL-GTLdTATSGSAKIKNQDVAKLSRTEQAAF 84
Cdd:COG4559 2 LEAENLS--VRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGEL-TPSSGEVRLNGRPLAAWSPWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RnknlGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALV--- 161
Cdd:COG4559 77 R----AVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlw 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658758220 162 ----TKPALVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLEL----ADklgKIAYLDDGKLA 224
Cdd:COG4559 153 epvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLaaqyAD---RILLLHQGRLV 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-223 |
6.30e-34 |
|
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: 122.07 E-value: 6.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYqDGqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLS------- 77
Cdd:COG0411 4 LLEVRGLTKRF-GG---LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPphriarl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 78 ---RTeqaafrnknlgfiYQFHHLLMEFSAVENVAMPLLIKG----LNA-----------KEAKEQALQMLDKVGLAHRS 139
Cdd:COG0411 80 giaRT-------------FQNPRLFPELTVLENVLVAAHARLgrglLAAllrlprarreeREARERAEELLERVGLADRA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 140 EHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLE----LADklgKI 215
Cdd:COG0411 147 DEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDlvmgLAD---RI 223
|
....*...
gi 658758220 216 AYLDDGKL 223
Cdd:COG0411 224 VVLDFGRV 231
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-212 |
1.21e-33 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 123.80 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLsrtEQAafr 85
Cdd:PRK11650 4 LKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL---EPA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLnAKEAKEQ----ALQMLDKVGLAHRsehKPSALSGGERQRVAIARALV 161
Cdd:PRK11650 75 DRDIAMVFQNYALYPHMSVRENMAYGLKIRGM-PKAEIEErvaeAARILELEPLLDR---KPRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 162 TKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHD-LE---LADKL 212
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDqVEamtLADRV 205
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-224 |
1.47e-33 |
|
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: 119.91 E-value: 1.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 29 DLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKL---SRTEQAAFRNKNLgfiyqFHHLLMEfsav 105
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAppaDRPVSMLFQENNL-----FAHLTVE---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 106 ENVAMPLlIKGLNAKEAKEQALQ-MLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKI 184
Cdd:cd03298 89 QNVGLGL-SPGLKLTAEDRQAIEvALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 658758220 185 YDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKLA 224
Cdd:cd03298 168 LDLVLDLHAETKMTVLMVTHQPEDAKRLAqRVVFLDNGRIA 208
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
27-223 |
1.71e-33 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 120.17 E-value: 1.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 27 GVDLSLNQGDMLAIVGSSGSGKS-TLLHILGTLD---TATSGSAKIKNQDVAKLSrteqaaFRNKNLGFIYQ-----FHH 97
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSlTCLAILGLLPpglTQTSGEILLDGRPLLPLS------IRGRHIATIMQnprtaFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 98 LL-MEFSAVENvampLLIKGLNAKEAKEQALQMLDKVGLAHRSE--HK-PSALSGGERQRVAIARALVTKPALVLADEPT 173
Cdd:TIGR02770 78 LFtMGNHAIET----LRSLGKLSKQARALILEALEAVGLPDPEEvlKKyPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 658758220 174 GNLDKQNAIKIYDLINELNKSLNTSFVVVTHDL----ELADKLgkiAYLDDGKL 223
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLgvvaRIADEV---AVMDDGRI 204
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-223 |
4.94e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 119.63 E-value: 4.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 21 QVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTL-----DTATSGSAKIKNQDVAKLSRTEQaafrNKNLGFIYQF 95
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEL----RRRVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 96 HHLLMEFSAVENVAMPLLIKGL--NAKEAKEQALQMLDKVGL----AHRSEHKPSALSGGERQRVAIARALVTKPALVLA 169
Cdd:PRK14247 91 PNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 170 DEPTGNLDKQNAIKIYDLINELNKSLntSFVVVTHDLELADKLGK-IAYLDDGKL 223
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDyVAFLYKGQI 223
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-224 |
5.37e-33 |
|
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: 119.84 E-value: 5.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKlsrteqaafr 85
Cdd:TIGR04520 1 IEVENVSFSYPESEKPA--LKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKNLGFIYQfhHLLMEF---------SAVEN-VAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVA 155
Cdd:TIGR04520 69 EENLWEIRK--KVGMVFqnpdnqfvgATVEDdVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758220 156 IARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLE---LADklgKIAYLDDGKLA 224
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEeavLAD---RVIVMNKGKIV 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-223 |
1.15e-32 |
|
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: 117.36 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 10 NLSKVYQDGQnqvEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFRNKNL 89
Cdd:cd03226 4 NISFSYKKGT---EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 90 GfiYQFhhllmeFSavENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLA 169
Cdd:cd03226 81 D--YQL------FT--DSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 170 DEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKLGKIA-YLDDGKL 223
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVlLLANGAI 204
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-212 |
1.16e-32 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 118.78 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGQNqvevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVA-----KLSRT 79
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKG----CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAelelyQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 80 EQAAFRNKNLGFIYQ--FHHLLMEFSAVENVAMPLLIKGL-NAKEAKEQALQMLDKVGL-AHRSEHKPSALSGGERQRVA 155
Cdd:TIGR02323 79 ERRRLMRTEWGFVHQnpRDGLRMRVSAGANIGERLMAIGArHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658758220 156 IARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLE----LADKL 212
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGvarlLAQRL 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
9-222 |
1.41e-32 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 121.48 E-value: 1.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 9 QNLSKVYqDGQNQVEvlkGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEqaafRNKN 88
Cdd:PRK11607 23 RNLTKSF-DGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ----RPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 89 LGFiyQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVL 168
Cdd:PRK11607 95 MMF--QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 169 ADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKL-GKIAYLDDGK 222
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMaGRIAIMNRGK 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-212 |
2.39e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 122.89 E-value: 2.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKS-TLLHILGTLDTA----TSGSAKIKNQDVAK 75
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 76 LSRTEQAAFRNKNLGFIYQ--------FHHLLMEFSAVENvamplLIKGLNAKEAKEQALQMLDKVGL---AHRSEHKPS 144
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQepmvslnpLHTLEKQLYEVLS-----LHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658758220 145 ALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKL 212
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKL 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-227 |
5.27e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 117.49 E-value: 5.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTL-LHILGTLDtATSGSAKIKNQDVaKLSRTEQAA 83
Cdd:PRK13639 1 ILETRDLKYSYPDG---TEALKGINFKAEKGEMVALLGPNGAGKSTLfLHFNGILK-PTSGEVLIKGEPI-KYDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 84 FRnKNLGFIYQF-HHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVT 162
Cdd:PRK13639 76 VR-KTVGIVFQNpDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658758220 163 KPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTsFVVVTHDLELADKLG-KIAYLDDGKLaIKE 227
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGIT-IIISTHDVDLVPVYAdKVYVMSDGKI-IKE 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-223 |
1.79e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 116.34 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 2 NDLVISCQNLSKVYQDGQNQVE--VLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRT 79
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 80 EQaaFRNKnLGFIYQFHHLLMEFSAVE-NVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIAR 158
Cdd:PRK13633 81 WD--IRNK-AGMVFQNPDNQIVATIVEeDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 159 ALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLGKIAYLDDGKL 223
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-212 |
2.12e-31 |
|
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: 114.87 E-value: 2.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 25 LKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFRNknlgfiyqfHHLLMEFSA 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQN---------YSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 105 VENVAMPL--LIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDkqnAI 182
Cdd:TIGR01184 72 RENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD---AL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 658758220 183 KIYDLINELNKSLNTS---FVVVTHDLE----LADKL 212
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHrvtVLMVTHDVDeallLSDRV 185
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-223 |
3.88e-31 |
|
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: 113.47 E-value: 3.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQnqveVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTeqaafr 85
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEqalqMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPA 165
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 166 LVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVAdRIGIINKGKL 204
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-223 |
4.26e-31 |
|
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: 112.31 E-value: 4.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQNqvEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEqaaFR 85
Cdd:cd03246 1 LEVENVSFRYPGAEP--PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE---LG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nKNLGFIYQfHHLLMEFSAVENVampllikglnakeakeqalqmldkvglahrsehkpsaLSGGERQRVAIARALVTKPA 165
Cdd:cd03246 76 -DHVGYLPQ-DDELFSGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658758220 166 LVLADEPTGNLDKQNAIKIYDLINELNKSLNTSfVVVTHDLELADKLGKIAYLDDGKL 223
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGATR-IVIAHRPETLASADRILVLEDGRV 173
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-205 |
5.01e-31 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 116.74 E-value: 5.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYqdGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSrte 80
Cdd:PRK11432 2 TQKNFVVLKNITKRF--GSNTV--IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 qaaFRNKNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQ---ALQMLDKVGLAHRSEHKpsaLSGGERQRVAIA 157
Cdd:PRK11432 75 ---IQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRvkeALELVDLAGFEDRYVDQ---ISGGQQQRVALA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 658758220 158 RALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHD 205
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHD 196
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-212 |
7.84e-31 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 114.16 E-value: 7.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLvISCQNLSKVYQD-----GQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQdvaK 75
Cdd:COG4167 1 MSAL-LEVRNLSKTFKYrtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH---K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 76 LSrTEQAAFRNKNLGFIYQ-----------FHHLLMEfsavenvamPL-LIKGLNAKEAKEQALQMLDKVGLahRSEH-- 141
Cdd:COG4167 77 LE-YGDYKYRCKHIRMIFQdpntslnprlnIGQILEE---------PLrLNTDLTAEEREERIFATLRLVGL--LPEHan 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658758220 142 -KPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLEL----ADKL 212
Cdd:COG4167 145 fYPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIvkhiSDKV 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
10-209 |
9.26e-31 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 114.03 E-value: 9.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 10 NLSKVYQDGQNQvEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSrteqaAFRnknl 89
Cdd:PRK11248 3 QISHLYADYGGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 90 GFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLA 169
Cdd:PRK11248 73 GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 658758220 170 DEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELA 209
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-223 |
1.50e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 114.41 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDG-QNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSA-------KIKNQDVAK-- 75
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeKNKKKTKEKek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 76 ------LSRTEQAAFRN-----KNLGFIYQF-HHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRS-EHK 142
Cdd:PRK13651 83 vleklvIQKTRFKKIKKikeirRRVGVVFQFaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYlQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 143 PSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTsFVVVTHDLELADKLGK-IAYLDDG 221
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKT-IILVTHDLDNVLEWTKrTIFFKDG 241
|
..
gi 658758220 222 KL 223
Cdd:PRK13651 242 KI 243
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-223 |
3.89e-30 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 115.13 E-value: 3.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 25 LKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFRNKNLGFIYQFHHLLMEFSA 104
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 105 VENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKI 184
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 658758220 185 YDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGdRIAIMQNGEV 243
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-224 |
6.22e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.42 E-value: 6.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQnqvEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSrteQAAFR 85
Cdd:COG1132 340 IEFENVSFSYPGDR---PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nKNLGFIYQfHHLLMEFSAVENVAMpllikG-LNAKEAK-EQALQMldkVGLAHRSEHKP-----------SALSGGERQ 152
Cdd:COG1132 414 -RQIGVVPQ-DTFLFSGTIRENIRY-----GrPDATDEEvEEAAKA---AQAHEFIEALPdgydtvvgergVNLSGGQRQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 153 RVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKslNTSFVVVTHDL---ELADklgKIAYLDDGKLA 224
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLstiRNAD---RILVLDDGRIV 553
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-223 |
6.75e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 111.67 E-value: 6.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 3 DLVISCQNLSKVYqdGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTL-----DTATSGSAKIKNQDVAKlS 77
Cdd:COG1117 9 EPKIEVRNLNVYY--GDKQA--LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILLDGEDIYD-P 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 78 RTEQAAFRnKNLGFIYQ----FHHllmefSAVENVAMPLLIKGLNAK----EAKEQALQmldKVGL----AHRSEHKPSA 145
Cdd:COG1117 84 DVDVVELR-RRVGMVFQkpnpFPK-----SIYDNVAYGLRLHGIKSKseldEIVEESLR---KAALwdevKDRLKKSALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 146 LSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKslNTSFVVVTHDLE----LADklgKIAYLDDG 221
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK--DYTIVIVTHNMQqaarVSD---YTAFFYLG 229
|
..
gi 658758220 222 KL 223
Cdd:COG1117 230 EL 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
6-207 |
9.32e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 112.04 E-value: 9.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQN-QVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNqdvaklsRTEQAAF 84
Cdd:PRK13634 3 ITFQKVEHRYQYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGE-------RVITAGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RNKNL-------GFIYQF-HHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHR-SEHKPSALSGGERQRVA 155
Cdd:PRK13634 76 KNKKLkplrkkvGIVFQFpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 658758220 156 IARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLE 207
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSME 207
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-223 |
9.37e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.50 E-value: 9.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 2 NDLVISCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSrTEQ 81
Cdd:COG1129 1 AEPLLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS-PRD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 82 AafRNKNLGFIYQFHHLLMEFSAVENVAMPLLIKG---LNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIAR 158
Cdd:COG1129 76 A--QAAGIAIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 159 ALVTKPALVLADEPTGNLDKQNAIKIYDLINELnKSLNTSFVVVTHDL----ELADklgKIAYLDDGKL 223
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLdevfEIAD---RVTVLRDGRL 218
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-215 |
1.58e-29 |
|
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: 115.08 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 3 DLVISCQNLSKVYQDGQNqveVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSrteqA 82
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGRRP---ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD----A 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 83 AFRNKNLGFIYQfHHLLMEFSAVENVAmpllikgLNAKEAKEQAL-QMLDKVGLAHRSEHKP-----------SALSGGE 150
Cdd:TIGR02857 392 DSWRDQIAWVPQ-HPFLFAGTIAENIR-------LARPDASDAEIrEALERAGLDEFVAALPqgldtpigeggAGLSGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 151 RQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKslNTSFVVVTHDLELADKLGKI 215
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRI 526
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-207 |
3.17e-29 |
|
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: 109.79 E-value: 3.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 3 DLVISCQNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGsakiknQDVA----KLSR 78
Cdd:COG1119 1 DPLLELRNVTVRRGG----KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG------NDVRlfgeRRGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 79 TEQAAFRnKNLGFIYQ-FHHLLMEFSAVENVamplLIKGLNA---------KEAKEQALQMLDKVGLAHRSEHKPSALSG 148
Cdd:COG1119 71 EDVWELR-KRIGLVSPaLQLRFPRDETVLDV----VLSGFFDsiglyreptDEQRERARELLELLGLAHLADRPFGTLSQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 149 GERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLE 207
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVE 204
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-230 |
6.05e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 113.77 E-value: 6.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSrteQAAFR 85
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPV--LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS---EAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NkNLGFIYQFHHLlmeFSAV--ENvampLLIKGLNAKEakEQALQMLDKVGLAHRSEHKPS----------ALSGGERQR 153
Cdd:PRK11160 414 Q-AISVVSQRVHL---FSATlrDN----LLLAAPNASD--EALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRR 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 154 VAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINEL--NKSLntsfVVVTHDLELADKLGKIAYLDDGKLAIKESHH 230
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNKTV----LMITHRLTGLEQFDRICVMDNGQIIEQGTHQ 558
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-223 |
7.83e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 108.78 E-value: 7.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYqdGQNqvEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTL-----DTATSGSAKIKNQDVakLSRTE 80
Cdd:PRK14267 5 IETVNLRVYY--GSN--HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNI--YSPDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 QAAFRNKNLGFIYQFHHLLMEFSAVENVAMPLLIKGL--NAKEAKEQALQMLDKVGL----AHRSEHKPSALSGGERQRV 154
Cdd:PRK14267 79 DPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 155 AIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLntSFVVVTHDLELADKLGK-IAYLDDGKL 223
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDyVAFLYLGKL 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
28-224 |
8.41e-29 |
|
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: 110.96 E-value: 8.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 28 VDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKN---QDVAKLSR--TEQaafRNknLGFIYQ----FHHL 98
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARGIFlpPHR---RR--IGYVFQearlFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 99 lmefSAVENvampLL-----IKGLNAKEAKEQALQMLdkvGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPT 173
Cdd:COG4148 93 ----SVRGN----LLygrkrAPRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658758220 174 GNLD---KQnaiKIYDLINELNKSLNTSFVVVTHDLE----LADKLgkiAYLDDGKLA 224
Cdd:COG4148 162 AALDlarKA---EILPYLERLRDELDIPILYVSHSLDevarLADHV---VLLEQGRVV 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-223 |
8.46e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.85 E-value: 8.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 8 CQNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQdvAKLSRTEQAAFRNK 87
Cdd:COG0488 1 LENLSKSFGG----RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG--LRIGYLPQEPPLDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 88 NL--------GF------IYQFHHLLMEFSAVENVAMPL-----LIKGLNAKEAKEQALQMLDKVGLAHRSEHKP-SALS 147
Cdd:COG0488 75 DLtvldtvldGDaelralEAELEELEAKLAEPDEDLERLaelqeEFEALGGWEAEARAEEILSGLGFPEEDLDRPvSELS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658758220 148 GGERQRVAIARALVTKPALVLADEPTGNLDkQNAIKIydLINELnKSLNTSFVVVTHDLELADKL-GKIAYLDDGKL 223
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLD-LESIEW--LEEFL-KNYPGTVLVVSHDRYFLDRVaTRILELDRGKL 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-194 |
1.40e-28 |
|
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: 107.63 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAfr 85
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRAR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nknLGFIY--QFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTK 163
Cdd:cd03218 75 ---LGIGYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190
....*....|....*....|....*....|.
gi 658758220 164 PALVLADEPTGNLDKQNAIKIYDLINELNKS 194
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDR 182
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-223 |
1.60e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.54 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 2 NDLVISCQNLSKVYQDGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQ 81
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNA--LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 82 aafrNKNLGFIYQ-----FHHLLMEfsavENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAI 156
Cdd:PRK13632 82 ----RKKIGIIFQnpdnqFIGATVE----DDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658758220 157 ARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLGKIAYLDDGKL 223
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-213 |
3.15e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 107.48 E-value: 3.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQ-NQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHIL-GTLdTATSGSAKIKNQDVAKLSrTEQaa 83
Cdd:COG1101 2 LELKNLSKTFNPGTvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIaGSL-PPDSGSILIDGKDVTKLP-EYK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 84 fRNKNLGFIYQ------FHHLLMEfsavENVAMPL-------LIKGLNAKEAKE--QALQMLDkVGLAHRSEHKPSALSG 148
Cdd:COG1101 78 -RAKYIGRVFQdpmmgtAPSMTIE----ENLALAYrrgkrrgLRRGLTKKRRELfrELLATLG-LGLENRLDTKVGLLSG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 149 GERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLG 213
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYG 216
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-224 |
1.06e-27 |
|
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: 104.76 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVaklSRTEQAAFR 85
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV---VKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NknLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPA 165
Cdd:cd03266 79 R--LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 166 LVLADEPTGNLDKQNAIKIYDLINELnKSLNTSFVVVTHDLELADKL-GKIAYLDDGKLA 224
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLcDRVVVLHRGRVV 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-212 |
1.11e-27 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 110.33 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSA-------KIKNQDVAKLS 77
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 78 RTEQAAF---RNKNLGFIYQ--FHHLLMEFSAVENVAMPL-LIKGLNAKEAKEQALQMLDKVGLAHRSE---HKPSALSG 148
Cdd:PRK10261 92 EQSAAQMrhvRGADMAMIFQepMTSLNPVFTVGEQIAESIrLHQGASREEAMVEAKRMLDQVRIPEAQTilsRYPHQLSG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658758220 149 GERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDL----ELADKL 212
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMgvvaEIADRV 239
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-223 |
2.07e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.48 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYQDGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQdvaKLSRTE 80
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATYA--LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 QAAFRNKnLGFIYQFHHLLMEFSAVEN-VAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARA 159
Cdd:PRK13635 76 VWDVRRQ-VGMVFQNPDNQFVGATVQDdVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658758220 160 LVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLGKIAYLDDGKL 223
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEI 218
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-224 |
3.64e-27 |
|
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: 103.40 E-value: 3.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 29 DLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAafrnknLGFIYQFHHLLMEFSAVENV 108
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP------VSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 109 AM---PLLikGLNAKEaKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIY 185
Cdd:TIGR01277 92 GLglhPGL--KLNAEQ-QEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 658758220 186 DLINELNKSLNTSFVVVTHDL-ELADKLGKIAYLDDGKLA 224
Cdd:TIGR01277 169 ALVKQLCSERQRTLLMVTHHLsDARAIASQIAVVSQGKIK 208
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-230 |
1.11e-26 |
|
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: 102.69 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQnqvEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSrteQAAFR 85
Cdd:cd03253 1 IEFENVTFAYDPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nKNLGFIYQ----FHHLLMEfsaveNVAMpllikG-LNAK-----EAKEQA------LQMLD----KVGlahrseHKPSA 145
Cdd:cd03253 75 -RAIGVVPQdtvlFNDTIGY-----NIRY-----GrPDATdeeviEAAKAAqihdkiMRFPDgydtIVG------ERGLK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 146 LSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTsfVVVTHDLELADKLGKIAYLDDGKLAI 225
Cdd:cd03253 138 LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTT--IVIAHRLSTIVNADKIIVLKDGRIVE 215
|
....*
gi 658758220 226 KESHH 230
Cdd:cd03253 216 RGTHE 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-208 |
1.14e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.77 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYQDGqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVaKLSRTE 80
Cdd:PRK13636 1 MEDYILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 QAAFRnKNLGFIYQF-HHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRsEHKPS-ALSGGERQRVAIAR 158
Cdd:PRK13636 77 LMKLR-ESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHL-KDKPThCLSFGQKKRVAIAG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 658758220 159 ALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLEL 208
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDI 204
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-224 |
2.49e-26 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 101.36 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYqdGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLdTATSGSAKIKNQDVAKLSrTEQAAF 84
Cdd:cd03224 1 LEVENLNAGY--GKSQI--LFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMGLL-PPRSGSIRFDGRDITGLP-PHERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RNknLGFIYQFHHLLMEFSAVENVAMPLLI-KGLNAKEAKEQALQMLDKvgLAHRSEHKPSALSGGERQRVAIARALVTK 163
Cdd:cd03224 75 AG--IGYVPEGRRIFPELTVEENLLLGAYArRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658758220 164 PALVLADEPTGNLdkQNAI--KIYDLINELNKSlNTSFVVVTHDLELADKLGKIAY-LDDGKLA 224
Cdd:cd03224 151 PKLLLLDEPSEGL--APKIveEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYvLERGRVV 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
6-225 |
2.52e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.82 E-value: 2.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQN-QVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKlsRTEQAAF 84
Cdd:PRK13637 3 IKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD--KKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RNKNLGFIYQF-HHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRS--EHKPSALSGGERQRVAIARALV 161
Cdd:PRK13637 81 IRKKVGLVFQYpEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDykDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 162 TKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKL-GKIAYLDDGKLAI 225
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLaDRIIVMNKGKCEL 225
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
26-206 |
2.65e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 103.63 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 26 KGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFRnKNLGFIYQ--FHHLLMEFS 103
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQdpLASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 104 AVENVAMPLLI--KGLNAKEAKEQALQMLDKVGL----AHRSEHKpsaLSGGERQRVAIARALVTKPALVLADEPTGNLD 177
Cdd:PRK15079 117 IGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlpnlINRYPHE---FSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180
....*....|....*....|....*....
gi 658758220 178 KQNAIKIYDLINELNKSLNTSFVVVTHDL 206
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSLIFIAHDL 222
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-209 |
3.27e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 102.01 E-value: 3.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQnqveVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAafr 85
Cdd:PRK11231 3 LRTENLTVGYGTKR----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nKNLGFIYQfHHLLMEFSAV-ENVAM---PLL-IKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARAL 160
Cdd:PRK11231 76 -RRLALLPQ-HHLTPEGITVrELVAYgrsPWLsLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 658758220 161 VTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTsFVVVTHDLELA 209
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKT-VVTVLHDLNQA 201
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-191 |
3.38e-26 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 101.58 E-value: 3.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAF 84
Cdd:TIGR04406 1 TLVAENLIKSY----KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 rnkNLGFIYQFHHLLMEFSAVENVAMPL-LIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTK 163
Cdd:TIGR04406 77 ---GIGYLPQEASIFRKLTVEENIMAVLeIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATN 153
|
170 180
....*....|....*....|....*...
gi 658758220 164 PALVLADEPTGNLDKQNAIKIYDLINEL 191
Cdd:TIGR04406 154 PKFILLDEPFAGVDPIAVGDIKKIIKHL 181
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-223 |
4.23e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.78 E-value: 4.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTL-----DTATSGSAKIKNQDVAK 75
Cdd:PRK14239 1 MTEPILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 76 lSRTEQAAFRnKNLGFIYQFHHLLmEFSAVENVAMPLLIKGLNAK----EAKEQALQ---MLDKVglAHRSEHKPSALSG 148
Cdd:PRK14239 77 -PRTDTVDLR-KEIGMVFQQPNPF-PMSIYENVVYGLRLKGIKDKqvldEAVEKSLKgasIWDEV--KDRLHDSALGLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658758220 149 GERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKslNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISdRTGFFLDGDL 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
22-223 |
5.07e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.15 E-value: 5.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 22 VEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLdTATSGSAKIKNQDVAKLSRTEQAafrnKNLGFIYQFHHLLM 100
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRaINGTL-TPTAGTVLVAGDDVEALSARAAS----RRVASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 101 EFSAVENVAM---PLLIKGLNAKEAKEQAL-QMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNL 176
Cdd:PRK09536 91 EFDVRQVVEMgrtPHRSRFDTWTETDRAAVeRAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 658758220 177 DKQNAIKIYDLINELNKSLNTSfVVVTHDLELADKL-GKIAYLDDGKL 223
Cdd:PRK09536 171 DINHQVRTLELVRRLVDDGKTA-VAAIHDLDLAARYcDELVLLADGRV 217
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
6-223 |
6.88e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 101.74 E-value: 6.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQN-QVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAF 84
Cdd:PRK13649 3 INLQNVSYTYQAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RNKNLGFIYQF-HHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHR-SEHKPSALSGGERQRVAIARALVT 162
Cdd:PRK13649 83 IRKKVGLVFQFpESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGILAM 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758220 163 KPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTsFVVVTHDL-ELADKLGKIAYLDDGKL 223
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMT-IVLVTHLMdDVANYADFVYVLEKGKL 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-224 |
1.62e-25 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 97.50 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEqaAFR 85
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD--ARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKnLGFIYQfhhllmefsavenvampllikglnakeakeqalqmldkvglahrsehkpsaLSGGERQRVAIARALVTKPA 165
Cdd:cd03216 75 AG-IAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658758220 166 LVLADEPTGNLDKQNAIKIYDLINELnKSLNTSFVVVTHDL----ELADklgKIAYLDDGKLA 224
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLdevfEIAD---RVTVLRDGRVV 161
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-207 |
1.62e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 103.63 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKST----LLHILgtldtATSGSAKIKNQDVAKLSRTEQAAFRNKnLGFIYQ--FHH 97
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 98 LLMEFSAVENVAMPLLI--KGLNAKEAKEQALQMLDKVGLAHRSEHK-PSALSGGERQRVAIARALVTKPALVLADEPTG 174
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190
....*....|....*....|....*....|...
gi 658758220 175 NLDKQNAIKIYDLINELNKSLNTSFVVVTHDLE 207
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLH 487
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-209 |
1.72e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 100.58 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 3 DLVISCQNLSKVYQDGqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKlsRTEQA 82
Cdd:PRK13647 2 DNIIEVEDLHFRYKDG---TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA--ENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 83 aFRNKnLGFIYQF-HHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALV 161
Cdd:PRK13647 77 -VRSK-VGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 658758220 162 TKPALVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELA 209
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLA 201
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-224 |
3.11e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.89 E-value: 3.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 29 DLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLS---RTEQAAFRNKNLgfiyqFHHLLMEfsav 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPpsrRPVSMLFQENNL-----FSHLTVA---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 106 ENVAM---PLLikGLNAkEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAI 182
Cdd:PRK10771 90 QNIGLglnPGL--KLNA-AQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 658758220 183 KIYDLINELNKSLNTSFVVVTHDLELADKL---------GKIAYldDGKLA 224
Cdd:PRK10771 167 EMLTLVSQVCQERQLTLLMVSHSLEDAARIaprslvvadGRIAW--DGPTD 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
9-206 |
4.35e-25 |
|
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: 102.44 E-value: 4.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 9 QNLSKVYQDGQnqvEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAfrnkN 88
Cdd:TIGR02868 338 RDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR----R 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 89 LGFIYQFHHLlmeFSAV--ENVAmpllikgLNAKEAKEQAL-QMLDKVGLAHRSEHKP-----------SALSGGERQRV 154
Cdd:TIGR02868 411 VSVCAQDAHL---FDTTvrENLR-------LARPDATDEELwAALERVGLADWLRALPdgldtvlgeggARLSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 658758220 155 AIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTsfVVVTHDL 206
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTV--VLITHHL 530
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
24-230 |
4.89e-25 |
|
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: 98.07 E-value: 4.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRteqAAFRNKnLGFIYQFHHLLmEFS 103
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISR---KSLRSM-IGVVLQDTFLF-SGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 104 AVENVAMplliKGLNAKEAKE----QALQMLDKV-----GLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTG 174
Cdd:cd03254 93 IMENIRL----GRPNATDEEVieaaKEAGAHDFImklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658758220 175 NLDKQNAIKIYDLINELNKslNTSFVVVTHDLELADKLGKIAYLDDGKLAIKESHH 230
Cdd:cd03254 169 NIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHD 222
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
10-212 |
5.11e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 100.37 E-value: 5.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 10 NLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLDTATSGSA---KIKNQDVAKLSRTEQAAFR 85
Cdd:COG4170 8 NLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKDNWHVTAdrfRWNGIDLLKLSPRERRKII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKNLGFIYQ-----------FHHLLMEfsavenvAMP-LLIKGL---NAKEAKEQALQMLDKVGLahrSEHK------PS 144
Cdd:COG4170 88 GREIAMIFQepsscldpsakIGDQLIE-------AIPsWTFKGKwwqRFKWRKKRAIELLHRVGI---KDHKdimnsyPH 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758220 145 ALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLE----LADKL 212
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLEsisqWADTI 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-172 |
5.51e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 98.18 E-value: 5.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAaf 84
Cdd:COG1137 3 TLEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 rNKNLGFIYQ----FHHLlmefSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARAL 160
Cdd:COG1137 77 -RLGIGYLPQeasiFRKL----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170
....*....|..
gi 658758220 161 VTKPALVLADEP 172
Cdd:COG1137 152 ATNPKFILLDEP 163
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-227 |
5.60e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 99.07 E-value: 5.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 16 QDGQNQVEVlKGV-----------DLSLN--QGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQA 82
Cdd:PRK11831 2 QSVANLVDM-RGVsftrgnrcifdNISLTvpRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 83 AFRnKNLGFIYQFHHLLMEFSAVENVAMPLLIKG-LNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALV 161
Cdd:PRK11831 81 TVR-KRMSMLFQSGALFTDMNVFDNVAYPLREHTqLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 162 TKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHD----LELADKlgkiAYLDDGKLAIKE 227
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDvpevLSIADH----AYIVADKKIVAH 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
5-207 |
7.33e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 99.04 E-value: 7.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGQNQVeVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQdvaKLSRTEQAAF 84
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKY-TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RNKnLGFIYQFHHLLMEFSAVEN-VAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTK 163
Cdd:PRK13650 80 RHK-IGMVFQNPDNQFVGATVEDdVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 658758220 164 PALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLE 207
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLD 202
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
28-223 |
9.26e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.04 E-value: 9.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 28 VDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFRNKNLGFIYQF-HHLLMEFSAVE 106
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFpESQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 107 NVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRS-EHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIY 185
Cdd:PRK13643 105 DVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMM 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 658758220 186 DLINELNKSLNTsFVVVTHDL-ELADKLGKIAYLDDGKL 223
Cdd:PRK13643 185 QLFESIHQSGQT-VVLVTHLMdDVADYADYVYLLEKGHI 222
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
21-224 |
1.28e-24 |
|
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: 97.36 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 21 QVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLdTATSGSAKIKNQDVAKLsRTEQAAfrNKNLGFIYQFHHLL 99
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLL-PPRSGSIRFDGEDITGL-PPHRIA--RLGIGYVPEGRRIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 100 MEFSAVENVAMpllikGLNAKEAKEQALQMLDKVG-----LAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTG 174
Cdd:COG0410 91 PSLTVEENLLL-----GAYARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 658758220 175 NLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKLGKIAY-LDDGKLA 224
Cdd:COG0410 166 GLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYvLERGRIV 215
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-223 |
1.29e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 99.15 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 2 NDLVISCQNLSKVYQDGQ-NQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIK----NQDVAKL 76
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKQeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 77 SRTEQAAFRN--------KNLGFIYQFHHLLMEFSAVENVAM--PLLIkGLNAKEAKEQALQMLDKVGLAHRS-EHKPSA 145
Cdd:PRK13631 98 ELITNPYSKKiknfkelrRRVSMVFQFPEYQLFKDTIEKDIMfgPVAL-GVKKSEAKKLAKFYLNKMGLDDSYlERSPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 146 LSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFvVVTHD----LELADklgKIAYLDDG 221
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVF-VITHTmehvLEVAD---EVIVMDKG 252
|
..
gi 658758220 222 KL 223
Cdd:PRK13631 253 KI 254
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
6-223 |
1.85e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.98 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQN-QVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAkiknqDVAKLSRTEQAAF 84
Cdd:PRK13641 3 IKFENVDYIYSPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI-----TIAGYHITPETGN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RN-----KNLGFIYQFHHL-LMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHR-SEHKPSALSGGERQRVAIA 157
Cdd:PRK13641 78 KNlkklrKKVSLVFQFPEAqLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658758220 158 RALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTsFVVVTHDL-ELADKLGKIAYLDDGKL 223
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHT-VILVTHNMdDVAEYADDVLVLEHGKL 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
24-209 |
2.37e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.38 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLLHIL-GTLdTATSGSakiknqdvakLSRTeqaafRNKNLGFIYQFHHL--LM 100
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLaGVL-RPTSGT----------VRRA-----GGARVAYVPQRSEVpdSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 101 EFSAVENVAM-------PLLIKGLNAKEAKEQALQMLDKVGLAHRSEhkpSALSGGERQRVAIARALVTKPALVLADEPT 173
Cdd:NF040873 71 PLTVRDLVAMgrwarrgLWRRLTRDDRAAVDDALERVGLADLAGRQL---GELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 658758220 174 GNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELA 209
Cdd:NF040873 148 TGLDAESRERIIALLAEEHAR-GATVVVVTHDLELV 182
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-223 |
3.58e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 97.18 E-value: 3.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYQDgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTE 80
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPD--SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 QAAFRNKnLGFIYQFHHLLMEFSAVEN-VAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARA 159
Cdd:PRK13640 79 VWDIREK-VGIVFQNPDNQFVGATVGDdVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658758220 160 LVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLGKIAYLDDGKL 223
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-208 |
4.17e-24 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 96.34 E-value: 4.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLvISCQNLSKVYqdGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKiknqdvaklsrtE 80
Cdd:PRK09544 1 MTSL-VSLENVSVSF--GQRRV--LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------------R 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 QAAFRnknLGFIYQFHHLlmefsaveNVAMPLLIKG---LNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIA 157
Cdd:PRK09544 64 NGKLR---IGYVPQKLYL--------DTTLPLTVNRflrLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLA 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 658758220 158 RALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLEL 208
Cdd:PRK09544 133 RALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
6-223 |
5.20e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.77 E-value: 5.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQN-QVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIknQDVAKLSRTEQAAF 84
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDITITHKTKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 R--NKNLGFIYQF-HHLLMEfsavENVAMPLLIK----GLNAKEAKEQALQMLDKVGLAHR-SEHKPSALSGGERQRVAI 156
Cdd:PRK13646 81 RpvRKRIGMVFQFpESQLFE----DTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRDvMSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658758220 157 ARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDL-ELADKLGKIAYLDDGKL 223
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMnEVARYADEVIVMKEGSI 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-217 |
5.82e-24 |
|
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: 94.54 E-value: 5.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 17 DGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILG--TLDTATSGSAKIKNQDVaklsrtEQAAFRnKNLGFIYQ 94
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL------DKRSFR-KIIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 95 FHHLLMEFSAVENVAMPLLIKGLnakeakeqalqmldkvglahrsehkpsalSGGERQRVAIARALVTKPALVLADEPTG 174
Cdd:cd03213 90 DDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 658758220 175 NLDKQNAIKIYDLINELNKSlNTSFVVVTH-----DLELADKL-----GKIAY 217
Cdd:cd03213 141 GLDSSSALQVMSLLRRLADT-GRTIICSIHqpsseIFELFDKLlllsqGRVIY 192
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
27-208 |
7.30e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 95.83 E-value: 7.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 27 GVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAafrnkNLGFIYQFHH--LLMEFSA 104
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA-----RMGVVRTFQHvrLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 105 VEN--VAMPL-----LIKGLNA--------KEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLA 169
Cdd:PRK11300 98 IENllVAQHQqlktgLFSGLLKtpafrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 658758220 170 DEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLEL 208
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKL 216
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
10-208 |
1.38e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 96.35 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 10 NLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKS-TLLHILGTLD---TATSGSAKIKNQDVAKLSRTEQAAFR 85
Cdd:PRK11022 8 KLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDypgRVMAEKLEFNGQDLQRISEKERRNLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKNLGFIYQ-----------FHHLLMEFSAVEnvamplliKGLNAKEAKEQALQMLDKVGL---AHRSEHKPSALSGGER 151
Cdd:PRK11022 88 GAEVAMIFQdpmtslnpcytVGFQIMEAIKVH--------QGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 658758220 152 QRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLEL 208
Cdd:PRK11022 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLAL 216
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-224 |
1.61e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 94.76 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAafr 85
Cdd:COG4604 2 IEIKNVSKRYGG----KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nKNLGFIYQFHHLLMEFSAVENVAMpllikG--------LNA--KEAKEQALQMLDKVGLAHR--SEhkpsaLSGGERQR 153
Cdd:COG4604 75 -KRLAILRQENHINSRLTVRELVAF-----GrfpyskgrLTAedREIIDEAIAYLDLEDLADRylDE-----LSGGQRQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658758220 154 VAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELAdklgkIAYLD------DGKLA 224
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFA-----SCYADhivamkDGRVV 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-212 |
2.99e-23 |
|
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: 93.11 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNqdvaklsRTEQAAFR 85
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-------KPLDIAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKnLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPA 165
Cdd:cd03269 70 NR-IGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 658758220 166 LVLADEPTGNLDKQNAIKIYDLINELnKSLNTSFVVVTHDLELADKL 212
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEEL 194
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-223 |
3.91e-23 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 93.04 E-value: 3.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 21 QVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEqaafRNKNLGFIYQFHHLlm 100
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD----LRRNIGYVPQDVTL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 101 eFSAV--ENVAMplliKGLNAKEAK-EQALQM--------LDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLA 169
Cdd:cd03245 90 -FYGTlrDNITL----GAPLADDERiLRAAELagvtdfvnKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 170 DEPTGNLDKQNAIKiydLINELNKSL-NTSFVVVTHDLELADKLGKIAYLDDGKL 223
Cdd:cd03245 165 DEPTSAMDMNSEER---LKERLRQLLgDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-224 |
4.41e-23 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 95.56 E-value: 4.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 28 VDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFRNKNLGFIYQFHHLLMEFSAVEN 107
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 108 vamplLIKGLNAKEAKEQAL---QMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKI 184
Cdd:TIGR02142 96 -----LRYGMKRARPSERRIsfeRVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 658758220 185 YDLINELNKSLNTSFVVVTHDLE----LADKLgkiAYLDDGKLA 224
Cdd:TIGR02142 171 LPYLERLHAEFGIPILYVSHSLQevlrLADRV---VVLEDGRVA 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-224 |
5.66e-23 |
|
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: 96.74 E-value: 5.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQdGQNQVeVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHIL-GTLdTATSGSAKIKNQDVAKLSRTEQAaf 84
Cdd:COG4618 331 LSVENLTVVPP-GSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvGVW-PPTAGSVRLDGADLSQWDREELG-- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 rnKNLGFIYQFHHLLmEFSAVENVA-MPllikglNAKEAK-EQALQMLDkvglAHrsE---HKP-----------SALSG 148
Cdd:COG4618 406 --RHIGYLPQDVELF-DGTIAENIArFG------DADPEKvVAAAKLAG----VH--EmilRLPdgydtrigeggARLSG 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 149 GERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELnKSLNTSFVVVTHD---LELADklgKIAYLDDGKLA 224
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRpslLAAVD---KLLVLRDGRVQ 545
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-223 |
7.08e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 93.19 E-value: 7.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 10 NLSKVYQDGQNQVeVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDV---AKLSRTEQAAFRn 86
Cdd:PRK14246 12 NISRLYLYINDKA-ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIKLR- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 87 KNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAK-EAKEQALQMLDKVGL---AHRSEHKP-SALSGGERQRVAIARALV 161
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwkeVYDRLNSPaSQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658758220 162 TKPALVLADEPTGNLDKQNAIKIYDLINELNKSLntSFVVVTHDLELADKLGK-IAYLDDGKL 223
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADyVAFLYNGEL 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-229 |
7.13e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.02 E-value: 7.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLDtATSGSAKIKNQDVAKLSRteqaa 83
Cdd:COG4152 1 MLELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRiILGILA-PDSGEVLWDGEPLDPEDR----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 84 frnKNLGF------IYQfhhllmefsavenvAMPLL--------IKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGG 149
Cdd:COG4152 71 ---RRIGYlpeergLYP--------------KMKVGeqlvylarLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 150 ERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKL---------GKIAYldD 220
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELcdriviinkGRKVL--S 210
|
250
....*....|
gi 658758220 221 GKLA-IKESH 229
Cdd:COG4152 211 GSVDeIRRQF 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-212 |
8.34e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 96.08 E-value: 8.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 21 QVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFRnKNLGFIYQ--FHHL 98
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQdpYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 99 LMEFSAVENVAMPLLIKGL-NAKEAKEQALQMLDKVGLahRSEHK---PSALSGGERQRVAIARALVTKPALVLADEPTG 174
Cdd:PRK10261 415 DPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGL--LPEHAwryPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190
....*....|....*....|....*....|....*...
gi 658758220 175 NLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKL 212
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERI 530
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-223 |
1.02e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.33 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAF 84
Cdd:PRK13652 3 LIETRDLCYSYS---GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 rnknLGFIYQFHHLLMEFSAVE-NVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTK 163
Cdd:PRK13652 80 ----VGLVFQNPDDQIFSPTVEqDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658758220 164 PALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLGKIAY-LDDGKL 223
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYvMDKGRI 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-223 |
1.12e-22 |
|
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: 95.64 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQD-GQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQ----DVAKLSRT 79
Cdd:TIGR03269 279 IIKVRNVSKRYISvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdewvDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 80 EQAAFRnKNLGFIYQFHHLLMEFSAVENVAMPLLIKgLNAKEAKEQALQMLDKVGLAHRS-----EHKPSALSGGERQRV 154
Cdd:TIGR03269 359 GRGRAK-RYIGILHQEYDLYPHRTVLDNLTEAIGLE-LPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 155 AIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELA-DKLGKIAYLDDGKL 223
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVlDVCDRAALMRDGKI 506
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
1.14e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 92.89 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYQDgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTE 80
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQS--DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 QaafrNKNLGFIYQFHHLLMEFSAVE-NVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARA 159
Cdd:PRK13648 81 L----RKHIGIVFQNPDNQFVGSIVKyDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658758220 160 LVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLGKIAYLDDGKL 223
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
24-205 |
1.33e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 91.70 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSrteQAAFRnKNLGFIYQFHHLLMEfS 103
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK---PEIYR-QQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 104 AVENVAMPLLIKGlnaKEAKEQALQM-LDKVGLAHRSEHKP-SALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNA 181
Cdd:PRK10247 97 VYDNLIFPWQIRN---QQPDPAIFLDdLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180
....*....|....*....|....
gi 658758220 182 IKIYDLINELNKSLNTSFVVVTHD 205
Cdd:PRK10247 174 HNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-223 |
2.22e-22 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 89.80 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEqaaFRNKNLGFI---YQFHHLLM 100
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD---AIRAGIAYVpedRKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 101 EFSAVENVAMPLLikglnakeakeqalqmldkvglahrsehkpsaLSGGERQRVAIARALVTKPALVLADEPTGNLD--- 177
Cdd:cd03215 92 DLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDvga 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 658758220 178 KQNaikIYDLINELNKSlNTSFVVVTHDLE----LADklgKIAYLDDGKL 223
Cdd:cd03215 140 KAE---IYRLIRELADA-GKAVLLISSELDellgLCD---RILVMYEGRI 182
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
24-184 |
3.61e-22 |
|
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: 89.86 E-value: 3.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAklsrtEQAAFRNKNLGFIYQFHHLLMEFS 103
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD-----FQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 104 AVENvampllIKGLNAKEAKEQALQMLDKVGLAHrSEHKPSA-LSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAI 182
Cdd:cd03231 90 VLEN------LRFWHADHSDEQVEEALARVGLNG-FEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
..
gi 658758220 183 KI 184
Cdd:cd03231 163 RF 164
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-223 |
4.30e-22 |
|
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: 89.29 E-value: 4.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYqDGQNQVeVLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLDtATSGSAKIKNQDVAKLsrteQAAF 84
Cdd:cd03247 1 LSINNVSFSY-PEQEQQ-VLKNLSLELKQGEKIALLGRSGSGKSTLLQlLTGDLK-PQQGEITLDGVPVSDL----EKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RNKnLGFIYQFHHLlmeFSAVenvampllikglnakeakeqalqMLDKVGLAhrsehkpsaLSGGERQRVAIARALVTKP 164
Cdd:cd03247 74 SSL-ISVLNQRPYL---FDTT-----------------------LRNNLGRR---------FSGGERQRLALARILLQDA 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 165 ALVLADEPTGNLDKQNAIKIYDLINELNKslNTSFVVVTHDLELADKLGKIAYLDDGKL 223
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
24-229 |
4.95e-22 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 90.37 E-value: 4.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSrteQAAFRNKnLGFIYQ----FHHLL 99
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLRRQ-IGLVSQdvflFNDTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 100 MEFSA--VENVAMPLLIKGLNAKEAKEQALQMLDkvGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLD 177
Cdd:cd03251 93 AENIAygRPGATREEVEEAARAANAHEFIMELPE--GYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 658758220 178 KQNAIKIYDLINELNKSlNTSFvVVTHDLELADKLGKIAYLDDGKLAIKESH 229
Cdd:cd03251 171 TESERLVQAALERLMKN-RTTF-VIAHRLSTIENADRIVVLEDGKIVERGTH 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-229 |
6.47e-22 |
|
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: 90.24 E-value: 6.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 23 EVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAklsrTEQAAFRNKNLGFIYQfHHLLMEF 102
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA----LADPAWLRRQVGVVLQ-ENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 103 SAVENVA-----MPL--LIKGLNAKEAKEQALQMldKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGN 175
Cdd:cd03252 91 SIRDNIAladpgMSMerVIEAAKLAGAHDFISEL--PEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 658758220 176 LDKQNAIKIYDLINELNKslNTSFVVVTHDLELADKLGKIAYLDDGKLAIKESH 229
Cdd:cd03252 169 LDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSH 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-212 |
6.75e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.41 E-value: 6.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYQDGQnqveVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAklSRTE 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKL----VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP--SRAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 QAAFRnknLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARAL 160
Cdd:PRK13537 77 HARQR---VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 658758220 161 VTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTsFVVVTHDLELADKL 212
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKT-ILLTTHFMEEAERL 204
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-223 |
6.88e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 90.53 E-value: 6.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 19 QNQVEVLKGVDLSLNQGDMLAIVGSSGSGKStlLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFRNKNLGFIYQ---- 94
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIATIMQnprs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 95 -FHHLL-MEFSAVENvampLLIKGLNAKEAkeQALQMLDKVGLAHRS---EHKPSALSGGERQRVAIARALVTKPALVLA 169
Cdd:PRK10418 91 aFNPLHtMHTHARET----CLALGKPADDA--TLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658758220 170 DEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDL----ELADklgKIAYLDDGKL 223
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMgvvaRLAD---DVAVMSHGRI 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-229 |
8.39e-22 |
|
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: 89.91 E-value: 8.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 21 QVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSrteqAAFRNKNLGFIYQfHHLLM 100
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN----LRWLRSQIGLVSQ-EPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 101 EFSAVENVAMpllikGLN------AKEAKEQALqmLDK--VGLAHRSE----HKPSALSGGERQRVAIARALVTKPALVL 168
Cdd:cd03249 90 DGTIAENIRY-----GKPdatdeeVEEAAKKAN--IHDfiMSLPDGYDtlvgERGSQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658758220 169 ADEPTGNLDKQNAIKIYDLINELNKSLNTsfVVVTHDLELADKLGKIAYLDDGKLAIKESH 229
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDRAMKGRTT--IVIAHRLSTIRNADLIAVLQNGQVVEQGTH 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-194 |
1.12e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.57 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQdGQNQVEvlkGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAaf 84
Cdd:PRK10895 3 TLTAKNLAKAYK-GRRVVE---DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 rNKNLGFIYQFHHLLMEFSAVENVAMPLLI-KGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTK 163
Cdd:PRK10895 77 -RRGIGYLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAAN 155
|
170 180 190
....*....|....*....|....*....|.
gi 658758220 164 PALVLADEPTGNLDKQNAIKIYDLINELNKS 194
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDS 186
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-212 |
1.40e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 89.71 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLV--ISCQNLSkVYQDGQnqvEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATS-----GSAKIKNQDV 73
Cdd:PRK14258 1 MSKLIpaIKVNNLS-FYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 74 -------AKLSRTEQAAFRNKNLgfiyqfhhllMEFSAVENVAMPLLIKGLNAK-------EAKEQALQMLDKVglAHRS 139
Cdd:PRK14258 77 yerrvnlNRLRRQVSMVHPKPNL----------FPMSVYDNVAYGVKIVGWRPKleiddivESALKDADLWDEI--KHKI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658758220 140 EHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKL 212
Cdd:PRK14258 145 HKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRL 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-223 |
1.95e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.01 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSkvyQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRteqAAF 84
Cdd:COG3845 257 VLEVENLS---VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSP---RER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RNKNLGFIYQ--FHH-LLMEFSAVENVAM-----PLLIKG--LNAKEAKEQALQMLDKVGLAHRSEHKP-SALSGGERQR 153
Cdd:COG3845 331 RRLGVAYIPEdrLGRgLVPDMSVAENLILgryrrPPFSRGgfLDRKAIRAFAEELIEEFDVRTPGPDTPaRSLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658758220 154 VAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDL----ELADklgKIAYLDDGKL 223
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLdeilALSD---RIAVMYEGRI 480
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-223 |
2.45e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 91.83 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQnqveVLKG-VDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLdtATSGSAKIKNQDvakLSRTEQAA 83
Cdd:PRK11174 350 IEAEDLEILSPDGK----TLAGpLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIE---LRELDPES 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 84 FRnKNLGFIYQFHHLLmEFSAVENVAmpllikgLNAKEAKEQAL-QMLDKV-----------GLAHRSEHKPSALSGGER 151
Cdd:PRK11174 421 WR-KHLSWVGQNPQLP-HGTLRDNVL-------LGNPDASDEQLqQALENAwvseflpllpqGLDTPIGDQAAGLSVGQA 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758220 152 QRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTsfVVVTHDLELADKLGKIAYLDDGKL 223
Cdd:PRK11174 492 QRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTT--LMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-211 |
2.56e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 91.63 E-value: 2.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVaKLSRTE 80
Cdd:COG3845 1 MMPPALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 QAafRNKNLGFIYQfHHLLME-FSAVENVAM---PLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAI 156
Cdd:COG3845 76 DA--IALGIGMVHQ-HFMLVPnLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 157 ARALVTKPALVLADEPTGNLDKQNAIKIYDLINELnKSLNTSFVVVTHDL----ELADK 211
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLrevmAIADR 210
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-221 |
3.04e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.38 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFr 85
Cdd:PRK09700 6 ISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nkNLGFIYQFHHLLMEFSAVENVAM-PLLIK---GLNA---KEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIAR 158
Cdd:PRK09700 81 --GIGIIYQELSVIDELTVLENLYIgRHLTKkvcGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658758220 159 ALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDL-ELADKLGKIAYLDDG 221
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLaEIRRICDRYTVMKDG 221
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-209 |
3.60e-21 |
|
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: 87.98 E-value: 3.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 30 LSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRteqaafrnkNLGFIYQFHHLLMEFS-AVENV 108
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWR---------HIGYVPQRHEFAWDFPiSVAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 109 AM--------PLLIKGLNAKEAKEQALqmlDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQN 180
Cdd:TIGR03771 72 VMsgrtghigWLRRPCVADFAAVRDAL---RRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPT 148
|
170 180
....*....|....*....|....*....
gi 658758220 181 AIKIYDLINELNKSlNTSFVVVTHDLELA 209
Cdd:TIGR03771 149 QELLTELFIELAGA-GTAILMTTHDLAQA 176
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
21-209 |
3.61e-21 |
|
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: 87.97 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 21 QVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAfrnKNLGFIYQ----FH 96
Cdd:TIGR03410 12 QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAR---AGIAYVPQgreiFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 97 HLLMEfsavENVAMpllikGLNAKEAKEQAL------------QMLDKVGlahrsehkpSALSGGERQRVAIARALVTKP 164
Cdd:TIGR03410 89 RLTVE----ENLLT-----GLAALPRRSRKIpdeiyelfpvlkEMLGRRG---------GDLSGGQQQQLAIARALVTRP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 658758220 165 ALVLADEPTGNLdKQNAIK-IYDLINELNKSLNTSFVVVTHDLELA 209
Cdd:TIGR03410 151 KLLLLDEPTEGI-QPSIIKdIGRVIRRLRAEGGMAILLVEQYLDFA 195
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
23-179 |
3.69e-21 |
|
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: 87.41 E-value: 3.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 23 EVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAklsrtEQAAFRNKNLGFIYQFHHLLMEF 102
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-----EQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 103 SAVENVAMpllikgLNAKEAKEQ--ALQMLDKVGLAHRsEHKPSA-LSGGERQRVAIARALVTKPALVLADEPTGNLDKQ 179
Cdd:TIGR01189 89 SALENLHF------WAAIHGGAQrtIEDALAAVGLTGF-EDLPAAqLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-179 |
3.92e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 87.17 E-value: 3.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 27 GVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLsRTEqaafrnknlgfiyqFHHLLM------ 100
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ-RDE--------------YHQDLLylghqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 101 ----EFSAVENVAMPLLIKGLNAKEAKEQALQmldKVGLAHRsEHKP-SALSGGERQRVAIARALVTKPALVLADEPTGN 175
Cdd:PRK13538 84 giktELTALENLRFYQRLHGPGDDEALWEALA---QVGLAGF-EDVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
....
gi 658758220 176 LDKQ 179
Cdd:PRK13538 160 IDKQ 163
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-223 |
3.94e-21 |
|
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: 91.61 E-value: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQD-GQNQVEVLkgvDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVaklsRTEQAAF 84
Cdd:TIGR01257 929 VCVKNLVKIFEPsGRPAVDRL---NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAV 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RnKNLGFIYQ----FHHLlmefSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARAL 160
Cdd:TIGR01257 1002 R-QSLGMCPQhnilFHHL----TVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAF 1076
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658758220 161 VTKPALVLADEPTGNLDKQNAIKIYDLIneLNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:TIGR01257 1077 VGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGdRIAIISQGRL 1138
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
24-224 |
4.48e-21 |
|
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: 91.26 E-value: 4.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIknqDVAKLSRTEQAAFrNKNLGFIYQFHHLlMEFS 103
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRL---DGADLKQWDRETF-GKHIGYLPQDVEL-FPGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 104 AVENVAMplLIKGLNAKEAKE-----QALQMLDKVGLAHRSEHKP--SALSGGERQRVAIARALVTKPALVLADEPTGNL 176
Cdd:TIGR01842 408 VAENIAR--FGENADPEKIIEaaklaGVHELILRLPDGYDTVIGPggATLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 658758220 177 DKQNAIKIYDLINELNKSLNTSfVVVTHD---LELADklgKIAYLDDGKLA 224
Cdd:TIGR01842 486 DEEGEQALANAIKALKARGITV-VVITHRpslLGCVD---KILVLQDGRIA 532
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-217 |
5.10e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 87.77 E-value: 5.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQN-----------------QVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKI 68
Cdd:cd03267 1 IEVSNLSKSYRVYSKepgligslkslfkrkyrEVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 69 KNQDVAKlsrtEQAAFRnKNLGFIY-QFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALS 147
Cdd:cd03267 81 AGLVPWK----RRKKFL-RRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658758220 148 GGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLE----LADKLGKIAY 217
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKdieaLARRVLVIDK 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
23-224 |
5.22e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.85 E-value: 5.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 23 EVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKlsRTEQAAFRN---------KNLGfiy 93
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRI--RSPRDAIRAgiayvpedrKGEG--- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 94 qfhhLLMEFSAVENVAMPLLIKG-----LNAKEAKEQALQMLDKVGLAHRSEHKP-SALSGGERQRVAIARALVTKPALV 167
Cdd:COG1129 341 ----LVLDLSIRENITLASLDRLsrgglLDRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658758220 168 LADEPTGNLD---KQnaiKIYDLINELNKSlNTSFVVVTHDLE----LADklgKIAYLDDGKLA 224
Cdd:COG1129 417 ILDEPTRGIDvgaKA---EIYRLIRELAAE-GKAVIVISSELPellgLSD---RILVMREGRIV 473
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-223 |
5.94e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 5.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 3 DLVISCQNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHIL-GTLdTATSGSAKIkNQDVaklsrteq 81
Cdd:COG0488 313 KKVLELEGLSKSYGD----KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLaGEL-EPDSGTVKL-GETV-------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 82 aafrnkNLGFIYQFHHLL-MEFSAVENvampllIKGLNAKEAKEQALQMLDKVGLAHRSEHKP-SALSGGERQRVAIARA 159
Cdd:COG0488 379 ------KIGYFDQHQEELdPDKTVLDE------LRDGAPGGTEQEVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658758220 160 LVTKPALVLADEPTGNLDkqnaIkiyDLINELNKSLNT---SFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLD----I---ETLEALEEALDDfpgTVLLVSHDRYFLDRVAtRILEFEDGGV 507
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
28-222 |
7.00e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 89.16 E-value: 7.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 28 VDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIkNQDVakLSRTEQAAF---RNKNLGFIYQFHHLLMEFSA 104
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVL-NGRV--LFDAEKGIClppEKRRIGYVFQDARLFPHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 105 VENvamplLIKGLnAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKI 184
Cdd:PRK11144 94 RGN-----LRYGM-AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 658758220 185 YDLINELNKSLNTSFVVVTHDLE----LADKLgkiAYLDDGK 222
Cdd:PRK11144 168 LPYLERLAREINIPILYVSHSLDeilrLADRV---VVLEQGK 206
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-228 |
8.12e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 87.24 E-value: 8.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVaklSRTE 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI---TDWQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 QAAFRNKNLGFIYQFHHLLMEFSAVENVAMplliKGLNAKeaKEQALQMLDKV-----GLAHRSEHKPSALSGGERQRVA 155
Cdd:PRK11614 74 TAKIMREAVAIVPEGRRVFSRMTVEENLAM----GGFFAE--RDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658758220 156 IARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVV---VTHDLELADKlGKIayLDDGKLAIKES 228
Cdd:PRK11614 148 IGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVeqnANQALKLADR-GYV--LENGHVVLEDT 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-229 |
1.04e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 90.17 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 22 VEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTeqaaFRNKNLGFIYQfHHLLME 101
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH----YLHRQVALVGQ-EPVLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 102 FSAVENVAMPLLIKGLN-----AKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNL 176
Cdd:TIGR00958 569 GSVRENIAYGLTDTPDEeimaaAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 658758220 177 DKQnaikIYDLINELNKSLNTSFVVVTHDLELADKLGKIAYLDDGKLAIKESH 229
Cdd:TIGR00958 649 DAE----CEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTH 697
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
24-210 |
1.36e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.87 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGsakiknqdvaKLSRTEQAafrnkNLGFIYQfhhllmefs 103
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG----------RIARPAGA-----RVLFLPQ--------- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 104 avenvaMPLLIKG-LnaKEA-----------KEQALQMLDKVGLAH------RSEHKPSALSGGERQRVAIARALVTKPA 165
Cdd:COG4178 434 ------RPYLPLGtL--REAllypataeafsDAELREALEAVGLGHlaerldEEADWDQVLSLGEQQRLAFARLLLHKPD 505
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 658758220 166 LVLADEPTGNLDKQNAIKIYDLINELNKslNTSFVVVTHDLELAD 210
Cdd:COG4178 506 WLFLDEATSALDEENEAALYQLLREELP--GTTVISVGHRSTLAA 548
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-222 |
1.65e-20 |
|
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: 84.04 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQnqveVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGsaKIKNQDVAKLSRTEQaafr 85
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG--IVTWGSTVKIGYFEQ---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nknlgfiyqfhhllmefsavenvampllikglnakeakeqalqmldkvglahrsehkpsaLSGGERQRVAIARALVTKPA 165
Cdd:cd03221 71 ------------------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658758220 166 LVLADEPTGNLDKQNAIKIYDLINELNKSLntsfVVVTHDLELADKLG-KIAYLDDGK 222
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKEYPGTV----ILVSHDRYFLDQVAtKIIELEDGK 144
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-223 |
2.01e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.96 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 18 GQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAafrnKNLGFIYQFHH 97
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 98 LLMEFSAVENVA------MPLLIKGlnAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADE 171
Cdd:PRK10253 92 TPGDITVQELVArgryphQPLFTRW--RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 658758220 172 PTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLGK-IAYLDDGKL 223
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYAShLIALREGKI 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-224 |
2.60e-20 |
|
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: 84.89 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 20 NQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLD-TATSGSAKIKNQDVAKLSRTEQAafrnkNLGfiyqfhh 97
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKtIMGHPKyEVTEGEILFKGEDITDLPPEERA-----RLG------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 98 LLMEF---SAVENVAMPLLIKGLNAKeakeqalqmldkvglahrsehkpsaLSGGERQRVAIARALVTKPALVLADEPTG 174
Cdd:cd03217 79 IFLAFqypPEIPGVKNADFLRYVNEG-------------------------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 658758220 175 NLDKQNAIKIYDLINELnKSLNTSFVVVTHDLELADKL--GKIAYLDDGKLA 224
Cdd:cd03217 134 GLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIV 184
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-226 |
2.76e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.58 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTL-LHILGTLdTATSGSAKIKNQDVAKLSRTEQA- 82
Cdd:PRK13644 1 MIRLENVSYSYPDG---TPALENINLVIKKGEYIGIIGKNGSGKSTLaLHLNGLL-RPQKGKVLVSGIDTGDFSKLQGIr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 83 -----AFRNKNLGFIYQFHHLLMEFSAvENVAMPLLikglnakEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIA 157
Cdd:PRK13644 77 klvgiVFQNPETQFVGRTVEEDLAFGP-ENLCLPPI-------EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 158 RALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTsFVVVTHDLELADKLGKIAYLDDGKLAIK 226
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKT-IVYITHNLEELHDADRIIVMDRGKIVLE 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-228 |
4.52e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.22 E-value: 4.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 21 QVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDV-AKLSRTEQAAFRNKNLGFIYQF-HHL 98
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKIKEVKRLRKEIGLVFQFpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 99 LMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHR-SEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLD 177
Cdd:PRK13645 103 LFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 658758220 178 KQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKLAIKES 228
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIAdEVIVMHEGKVISIGS 234
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-224 |
7.38e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 84.51 E-value: 7.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQNQ------------------VEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAK 67
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkgevgeFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 68 IKNQDVAKLsrteqaAFrnkNLGFiyqfhhlLMEFSAVENVAMPLLIKGLNAKEAKEqalqMLDKVglAHRSE-----HK 142
Cdd:cd03220 81 VRGRVSSLL------GL---GGGF-------NPELTGRENIYLNGRLLGLSRKEIDE----KIDEI--IEFSElgdfiDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 143 P-SALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKL-GKIAYLDD 220
Cdd:cd03220 139 PvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLcDRALVLEK 217
|
....
gi 658758220 221 GKLA 224
Cdd:cd03220 218 GKIR 221
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
9-206 |
9.15e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.84 E-value: 9.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 9 QNLSKV--YQDG---QNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQdvaKLSRTEQAa 83
Cdd:PRK15112 8 RNLSKTfrYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---PLHFGDYS- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 84 FRNKNLGFIYQfhhllmEFSAVEN--------VAMPL-LIKGLNAKEAKEQALQMLDKVGLahRSEHK---PSALSGGER 151
Cdd:PRK15112 84 YRSQRIRMIFQ------DPSTSLNprqrisqiLDFPLrLNTDLEPEQREKQIIETLRQVGL--LPDHAsyyPHMLAPGQK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 152 QRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDL 206
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHL 210
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
23-229 |
1.11e-19 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 87.10 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 23 EVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFRNKNLGFIYQFHHLLME- 101
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILEn 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 102 --FSAVENVAMPLLIKGLNAKEAKEQALQMldKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQ 179
Cdd:TIGR01193 568 llLGAKENVSQDEIWAACEIAEIKDDIENM--PLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 658758220 180 NAIKIydlINELNKSLNTSFVVVTHDLELADKLGKIAYLDDGKLAIKESH 229
Cdd:TIGR01193 646 TEKKI---VNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSH 692
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
9-212 |
1.18e-19 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 85.62 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 9 QNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILG-TLDT--ATSGSAKIKNQDVAKLSRTEQAAF 84
Cdd:PRK15093 7 RNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKaICGvTKDNwrVTADRMRFDDIDLLRLSPRERRKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RNKNLGFIYQFHHLLMEFSavENVAMPLL--IKGLNAKEA--------KEQALQMLDKVGLahrSEHK------PSALSG 148
Cdd:PRK15093 87 VGHNVSMIFQEPQSCLDPS--ERVGRQLMqnIPGWTYKGRwwqrfgwrKRRAIELLHRVGI---KDHKdamrsfPYELTE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658758220 149 GERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKL 212
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQW 225
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-224 |
1.59e-19 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 83.31 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEqaaFR 85
Cdd:cd03244 3 IEFKNVSLRYRPNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHD---LR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKnLGFIYQFHHLlmeFSAV--ENVAmPLlikglnaKEAKEQAL-QMLDKVGLAHRSEHKPSAL-----------SGGER 151
Cdd:cd03244 78 SR-ISIIPQDPVL---FSGTirSNLD-PF-------GEYSDEELwQALERVGLKEFVESLPGGLdtvveeggenlSVGQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658758220 152 QRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKslNTSFVVVTHDLELADKLGKIAYLDDGKLA 224
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRLDTIIDSDRILVLDKGRVV 216
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-228 |
2.27e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 84.37 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDgQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQ-----DVAKLSRT 79
Cdd:PRK13642 4 ILEVENLVFKYEK-ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaeNVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 80 EQAAFRNKNLGFIYQfhhllmefSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARA 159
Cdd:PRK13642 83 IGMVFQNPDNQFVGA--------TVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 160 LVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLGKIAYLDDGKLaIKES 228
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEI-IKEA 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-212 |
2.35e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.88 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYQDGQnqveVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILgtLDTATSGSAKIKNQDVAKLSRTE 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMI--LGMTSPDAGKITVLGVPVPARAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 QAAFRnknLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARAL 160
Cdd:PRK13536 111 LARAR---IGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARAL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 658758220 161 VTKPALVLADEPTGNLDKQNAIKIYDLINELnKSLNTSFVVVTHDLELADKL 212
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERL 238
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-204 |
4.24e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.81 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 23 EVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHIL-GTLD-TATSGSAKIKNQDVAKLSRTEQAafrnkNLGFIYQFHH--- 97
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmGHPKyEVTSGSILLDGEDILELSPDERA-----RAGIFLAFQYpve 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 98 ----LLMEF--SAVENVAmpllIKGLNAKEAKEQALQMLDKVGL----AHRSEHkpSALSGGERQRVAIARALVTKPALV 167
Cdd:COG0396 89 ipgvSVSNFlrTALNARR----GEELSAREFLKLLKEKMKELGLdedfLDRYVN--EGFSGGEKKRNEILQMLLLEPKLA 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 658758220 168 LADEPTGNLDkQNAIKI-YDLINELNKSlNTSFVVVTH 204
Cdd:COG0396 163 ILDETDSGLD-IDALRIvAEGVNKLRSP-DRGILIITH 198
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-177 |
8.09e-19 |
|
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: 81.55 E-value: 8.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 20 NQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLDT--ATSGSAKIKNQDVAKlsrteqAAFRnKNLGFIYQFH 96
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDaISGRVEGggTTSGQILFNGQPRKP------DQFQ-KCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 97 HLLMEFSAVENVA----MPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEP 172
Cdd:cd03234 91 ILLPGLTVRETLTytaiLRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
....*
gi 658758220 173 TGNLD 177
Cdd:cd03234 171 TSGLD 175
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-223 |
8.37e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.05 E-value: 8.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDlVISCQNLSKVYQDGQNQ------------------VEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTAT 62
Cdd:COG1134 1 MSS-MIEVENVSKSYRLYHEPsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 63 SGSAKIKNQDVAKLSrteqaafrnknLGFIyqFHhllMEFSAVENVAMPLLIKGLNAKEAKEqalqMLDKV----GLaHR 138
Cdd:COG1134 80 SGRVEVNGRVSALLE-----------LGAG--FH---PELTGRENIYLNGRLLGLSRKEIDE----KFDEIvefaEL-GD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 139 SEHKP-SALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKL-GKIA 216
Cdd:COG1134 139 FIDQPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLcDRAI 217
|
....*..
gi 658758220 217 YLDDGKL 223
Cdd:COG1134 218 WLEKGRL 224
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
24-212 |
3.78e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.62 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLL-HILGTL-DTATSGSAKIKNQDvaklsrteqaafrnknlgfIYQfhhllmE 101
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLrLLAGALkGTPVAGCVDVPDNQ-------------------FGR------E 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 102 FSAVENVAmpllikglnAKEAKEQALQMLDKVGLA----HRSehKPSALSGGERQRVAIARALVTKPALVLADEPTGNLD 177
Cdd:COG2401 100 ASLIDAIG---------RKGDFKDAVELLNAVGLSdavlWLR--RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190
....*....|....*....|....*....|....*
gi 658758220 178 KQNAIKIYDLINELNKSLNTSFVVVTHDLELADKL 212
Cdd:COG2401 169 RQTAKRVARNLQKLARRAGITLVVATHHYDVIDDL 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-207 |
4.22e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.27 E-value: 4.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 22 VEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTeqAAFrNKNLGFIYQFHHLLME 101
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTT--AAL-AAGVAIIYQELHLVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 102 FSAVENV---AMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALvTKPALVLA-DEPTGNLD 177
Cdd:PRK11288 94 MTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKAL-ARNARVIAfDEPTSSLS 172
|
170 180 190
....*....|....*....|....*....|
gi 658758220 178 KQNAIKIYDLINELnKSLNTSFVVVTHDLE 207
Cdd:PRK11288 173 AREIEQLFRVIREL-RAEGRVILYVSHRME 201
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-224 |
4.23e-18 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 79.38 E-value: 4.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYqdGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTeqaAFR 85
Cdd:cd03369 7 IEVENLSVRY--APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE---DLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKnLGFIYQFHHLLM-----------EFSAVEnvamplLIKGLNAKEAKEQalqmldkvglahrsehkpsaLSGGERQRV 154
Cdd:cd03369 82 SS-LTIIPQDPTLFSgtirsnldpfdEYSDEE------IYGALRVSEGGLN--------------------LSQGQRQLL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 155 AIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKslNTSFVVVTHDLELADKLGKIAYLDDGKLA 224
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDYDKILVMDAGEVK 202
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
9-223 |
5.26e-18 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 79.44 E-value: 5.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 9 QNLSKVYQDgQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIknqDVAKLSRTEQAAFRNKn 88
Cdd:cd03248 15 QNVTFAYPT-RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL---DGKPISQYEHKYLHSK- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 89 LGFIYQfHHLLMEFSAVENVAMPLLIKGLNA-KEAKEQA-----LQMLDKvGLAHRSEHKPSALSGGERQRVAIARALVT 162
Cdd:cd03248 90 VSLVGQ-EPVLFARSLQDNIAYGLQSCSFECvKEAAQKAhahsfISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658758220 163 KPALVLADEPTGNLDKQNAIKIYDLINELNKslNTSFVVVTHDLELADKLGKIAYLDDGKL 223
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-229 |
5.53e-18 |
|
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: 82.07 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRteqAAFR 85
Cdd:TIGR02203 331 VEFRNVTFRYPG--RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTL---ASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKnLGFIYQfHHLLMEFSAVENVAMPlliKGLNAKEAK-EQALQM------LDKV--GLAHRSEHKPSALSGGERQRVAI 156
Cdd:TIGR02203 406 RQ-VALVSQ-DVVLFNDTIANNIAYG---RTEQADRAEiERALAAayaqdfVDKLplGLDTPIGENGVLLSGGQRQRLAI 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658758220 157 ARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTsfVVVTHDLELADKLGKIAYLDDGKLAIKESH 229
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTT--LVIAHRLSTIEKADRIVVMDDGRIVERGTH 551
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
6-218 |
5.65e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.02 E-value: 5.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTA---TSGSAKIKNQDVAKLSRTEQA 82
Cdd:TIGR00955 22 QLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 83 AFrnknlgfIYQFHHLLMEFSAVENV---AMPLLIKGLNAKEAKEQALQMLDKVGL---AHR---SEHKPSALSGGERQR 153
Cdd:TIGR00955 102 AY-------VQQDDLFIPTLTVREHLmfqAHLRMPRRVTKKEKRERVDEVLQALGLrkcANTrigVPGRVKGLSGGERKR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 154 VAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHD-----LELADKL-----GKIAYL 218
Cdd:TIGR00955 175 LAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQpsselFELFDKIilmaeGRVAYL 248
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
25-223 |
9.20e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.55 E-value: 9.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 25 LKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRteqAAFRnKNLGFIYQfHHLLMEFSA 104
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR---ASLR-RNIAVVFQ-DAGLFNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 105 VENvampLLIKGLNAKEA-------KEQALQMLDK--VGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGN 175
Cdd:PRK13657 426 EDN----IRVGRPDATDEemraaaeRAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 658758220 176 LDKQNAIKIYDLINELNKSlNTSFvVVTHDLELADKLGKIAYLDDGKL 223
Cdd:PRK13657 502 LDVETEAKVKAALDELMKG-RTTF-IIAHRLSTVRNADRILVFDNGRV 547
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-224 |
1.31e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 79.75 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGQNQ-----------------VEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHIL-GTLdTATSGSA 66
Cdd:COG4586 1 IIEVENLSKTYRVYEKEpglkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtGIL-VPTSGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 67 KIKNQDVAKlsrtEQAAFRnKNLGFIY-QFHHLLMEFSAVENVAMPLLIKGLNAKEAKEqALQMLDKV----GLAHRSEH 141
Cdd:COG4586 80 RVLGYVPFK----RRKEFA-RRIGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKK-RLDELVELldlgELLDTPVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 142 KpsaLSGGERQRVAIARALVTKPALVLADEPTGNLD---KQnaiKIYDLINELNKSLNTSFVVVTHDL----ELADKL-- 212
Cdd:COG4586 154 Q---LSLGQRMRCELAAALLHRPKILFLDEPTIGLDvvsKE---AIREFLKEYNRERGTTILLTSHDMddieALCDRViv 227
|
250
....*....|....*
gi 658758220 213 ---GKIAYldDGKLA 224
Cdd:COG4586 228 idhGRIIY--DGSLE 240
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
5-178 |
1.87e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.61 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVyqdgQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAF 84
Cdd:PRK13539 2 MLEGEDLACV----RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 rnknLGfiyqfHHLLM--EFSAVENVAMPLLIKGlnakEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVT 162
Cdd:PRK13539 78 ----LG-----HRNAMkpALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVS 144
|
170
....*....|....*.
gi 658758220 163 KPALVLADEPTGNLDK 178
Cdd:PRK13539 145 NRPIWILDEPTAALDA 160
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-204 |
2.43e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 76.42 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSkvYQDGQNQVeVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGsakiknqdvaKLSRTEQAafr 85
Cdd:cd03223 1 IELENLS--LATPDGRV-LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG----------RIGMPEGE--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 nkNLGFIYQfhhllmefsavenvaMPLLIKG-LnakeaKEQALQMLDKVglahrsehkpsaLSGGERQRVAIARALVTKP 164
Cdd:cd03223 65 --DLLFLPQ---------------RPYLPLGtL-----REQLIYPWDDV------------LSGGEQQRLAFARLLLHKP 110
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 658758220 165 ALVLADEPTGNLDKQNAIKIYDLINElnksLNTSFVVVTH 204
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKE----LGITVISVGH 146
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
25-229 |
5.01e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.29 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 25 LKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVA--KLSR-TEQAAFRNKNLgfiyqfhHLLME 101
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASlRNQVALVSQNV-------HLFND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 102 FSAvENVAMPLliKGLNAKEAKEQALQMLDKVGLAHRSEH--------KPSALSGGERQRVAIARALVTK-PALVLaDEP 172
Cdd:PRK11176 432 TIA-NNIAYAR--TEQYSREQIEEAARMAYAMDFINKMDNgldtvigeNGVLLSGGQRQRIAIARALLRDsPILIL-DEA 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 658758220 173 TGNLDKQNAIKIYDLINELNKslNTSFVVVTHDLELADKLGKIAYLDDGKLAIKESH 229
Cdd:PRK11176 508 TSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEILVVEDGEIVERGTH 562
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-222 |
1.18e-16 |
|
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: 78.05 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDGQnqvEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKnqdvaklsrteqaaf 84
Cdd:TIGR03719 4 IYTMNRVSKVVPPKK---EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 RNKNLGFIYQFHHLLMEFSAVENVAMPL-----LIKGLNA-------------KEAKEQA-LQ-MLDKVGlAHRSEHK-- 142
Cdd:TIGR03719 66 PGIKVGYLPQEPQLDPTKTVRENVEEGVaeikdALDRFNEisakyaepdadfdKLAAEQAeLQeIIDAAD-AWDLDSQle 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 143 --------P------SALSGGERQRVAIARALVTKPALVLADEPTGNLDkqnAIKIYDLINELnKSLNTSFVVVTHDLEL 208
Cdd:TIGR03719 145 iamdalrcPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHL-QEYPGTVVAVTHDRYF 220
|
250
....*....|....*
gi 658758220 209 ADKL-GKIAYLDDGK 222
Cdd:TIGR03719 221 LDNVaGWILELDRGR 235
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-209 |
4.37e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.82 E-value: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 3 DLVISCQNLSKVYqdGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDtatsgsakiknqDVAKLSRTE-Q 81
Cdd:PRK14243 8 ETVLRTENLNVYY--GSFLA--VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLN------------DLIPGFRVEgK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 82 AAFRNKNL--------------GFIYQFHHLLMEfSAVENVAMPLLIKGL--NAKEAKEQALQ---MLDKVglAHRSEHK 142
Cdd:PRK14243 72 VTFHGKNLyapdvdpvevrrriGMVFQKPNPFPK-SIYDNIAYGARINGYkgDMDELVERSLRqaaLWDEV--KDKLKQS 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658758220 143 PSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLntSFVVVTHDLELA 209
Cdd:PRK14243 149 GLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQA 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-228 |
8.64e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 8.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYqdgqNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTeQAaf 84
Cdd:PRK15439 11 LLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KA-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 85 rnKNLGfIY---QFHHLLMEFSAVENVAMpllikGLNAKEAKEQAL-QMLDKVGLAHRSEHKPSALSGGERQRVAIARAL 160
Cdd:PRK15439 84 --HQLG-IYlvpQEPLLFPNLSVKENILF-----GLPKRQASMQKMkQLLAALGCQLDLDSSAGSLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758220 161 VTKPALVLADEPTGNLDKQNAIKIYDLINELnKSLNTSFVVVTHDL----ELADklgKIAYLDDGKLAIKES 228
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLpeirQLAD---RISVMRDGTIALSGK 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-228 |
9.53e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 9.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 22 VEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVA-KLSRTEQAAfrnkNLGFIYQFHHLLM 100
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEA----GIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 101 EFSAVENVAMPLLIK----GLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNL 176
Cdd:PRK10762 93 QLTIAENIFLGREFVnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 658758220 177 DKQNAIKIYDLINELnKSLNTSFVVVTHDL-ELADKLGKIAYLDDGKLaIKES 228
Cdd:PRK10762 173 TDTETESLFRVIREL-KSQGRGIVYISHRLkEIFEICDDVTVFRDGQF-IAER 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-209 |
1.05e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.05 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSrteqaafrnkNLGFIYQFHHLLMEFS 103
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS----------SKAFARKVAYLPQQLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 104 AVENVAMPLLIK-------------GLNAKEAKEQALQMLDKVGLAHRSehkPSALSGGERQRVAIARALVTKPALVLAD 170
Cdd:PRK10575 96 AAEGMTVRELVAigrypwhgalgrfGAADREKVEEAISLVGLKPLAHRL---VDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 658758220 171 EPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELA 209
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMA 211
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-224 |
2.48e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 74.47 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 23 EVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSrteQAAFRnKNLG--------F--- 91
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT---QASLR-AAIGivpqdtvlFndt 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 92 IYqfhhllmefsavENVAMpllikG-LNAKEAK-EQALQMldkvglAHRS---EHKPSA-----------LSGGERQRVA 155
Cdd:COG5265 448 IA------------YNIAY-----GrPDASEEEvEAAARA------AQIHdfiESLPDGydtrvgerglkLSGGEKQRVA 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758220 156 IARALVTKPALVLADEPTGNLDKQNAIKIYDLINELnkSLNTSFVVVTHDLEL---ADklgKIAYLDDGKLA 224
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALDSRTERAIQAALREV--ARGRTTLVIAHRLSTivdAD---EILVLEAGRIV 571
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-222 |
3.06e-15 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 71.35 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQNQVE-VLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLdTATSGSAKIKNqdvaKLSRTEQAA 83
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPG----SIAYVSQEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 84 F------RNkNLGFIYQFHHLLMEfSAVENVAMpllikglnakeakEQALQMLDK-----VGlahrseHKPSALSGGERQ 152
Cdd:cd03250 76 WiqngtiRE-NILFGKPFDEERYE-KVIKACAL-------------EPDLEILPDgdlteIG------EKGINLSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758220 153 RVAIARALVTKPALVLADEPTGNLDKQNAIKIYD--LINELNKslNTSFVVVTHDLELADKLGKIAYLDDGK 222
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
20-230 |
1.34e-14 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 72.23 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 20 NQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTeqaAFRNkNLGFIYQfHHLL 99
Cdd:TIGR01192 346 NSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRE---SLRK-SIATVFQ-DAGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 100 MEFSAVENVAM----PLLIKGLNAKEAKEQALQMLDKV-GLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTG 174
Cdd:TIGR01192 421 FNRSIRENIRLgregATDEEVYEAAKAAAAHDFILKRSnGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATS 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658758220 175 NLDKQNAIKIYDLINELNKSlNTSFvVVTHDLELADKLGKIAYLDDGKLAIKESHH 230
Cdd:TIGR01192 501 ALDVETEARVKNAIDALRKN-RTTF-IIAHRLSTVRNADLVLFLDQGRLIEKGSFQ 554
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
9-212 |
8.30e-14 |
|
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: 68.20 E-value: 8.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 9 QNLSKVYQDGQNQVEVLKGvdlSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFRNKN 88
Cdd:cd03237 2 TYPTMKKTLGEFTLEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 89 LGFIYQFHHLLMEFSAVEN-VAMPLLIKGLNAKEAKEqalqmldkvglahrsehkpsaLSGGERQRVAIArALVTKPA-L 166
Cdd:cd03237 79 RDLLSSITKDFYTHPYFKTeIAKPLQIEQILDREVPE---------------------LSGGELQRVAIA-ACLSKDAdI 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 658758220 167 VLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKL 212
Cdd:cd03237 137 YLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYL 182
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
19-177 |
8.51e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.95 E-value: 8.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 19 QNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFrnknlgfIYQFHHL 98
Cdd:PRK13543 21 RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAY-------LGHLPGL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 99 LMEFSAVENVAmplLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLD 177
Cdd:PRK13543 94 KADLSTLENLH---FLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-232 |
1.11e-13 |
|
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: 69.47 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 22 VEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHIL------GTLDTATSGS-AKIKNQDVaklSRTEQaafrnKNLGFIYQ 94
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILsgvyphGTWDGEIYWSgSPLKASNI---RDTER-----AGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 95 FHHLLMEFSAVENVAM--PLLIKG--LNAKEAKEQALQMLDKVGLAHRSEHKP-SALSGGERQRVAIARALVTKPALVLA 169
Cdd:TIGR02633 86 ELTLVPELSVAENIFLgnEITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658758220 170 DEPTGNLDKQNAIKIYDLINELnKSLNTSFVVVTHdleladKLGKIAYLDDGKLAIKESHHVA 232
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDL-KAHGVACVYISH------KLNEVKAVCDTICVIRDGQHVA 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-218 |
1.36e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.11 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 15 YQDGQnqveVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSA--KIKNQDVAK---LSRTEQAA--FRNK 87
Cdd:PRK13638 11 YQDEP----VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwQGKPLDYSKrglLALRQQVAtvFQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 88 NLGFIYQFHHLLMEFSavenvampllIKGLNAKEAK-----EQALQMLDkvglAHRSEHKP-SALSGGERQRVAIARALV 161
Cdd:PRK13638 87 EQQIFYTDIDSDIAFS----------LRNLGVPEAEitrrvDEALTLVD----AQHFRHQPiQCLSHGQKKRVAIAGALV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 658758220 162 TKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNtSFVVVTHDLELADKLGKIAYL 218
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYV 208
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-206 |
1.58e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.99 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYQDGQNqveVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKlsrte 80
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHT---ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 qaAFRNKNLGFIYQFHHLLMEFSA-VENVAMP--------LLIKGLNAKEAKEQALQMLDKVGLAHRsehKPSALSGGER 151
Cdd:PRK15056 74 --ALQKNLVAYVPQSEEVDWSFPVlVEDVVMMgryghmgwLRRAKKRDRQIVTAALARVDMVEFRHR---QIGELSGGQK 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 152 QRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTsFVVVTHDL 206
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKT-MLVSTHNL 202
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-177 |
1.67e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.99 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYQDGQnqvEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNqdvaklsrte 80
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPPKK---QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAP---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 qaafrNKNLGFIYQFHHLLMEFSAVENVAMPL-----LIKGLNA-------------KEAKEQA-LQ-MLDKVGlAHRSE 140
Cdd:PRK11819 69 -----GIKVGYLPQEPQLDPEKTVRENVEEGVaevkaALDRFNEiyaayaepdadfdALAAEQGeLQeIIDAAD-AWDLD 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 658758220 141 HK----------PSA------LSGGERQRVAIARALVTKPALVLADEPTGNLD 177
Cdd:PRK11819 143 SQleiamdalrcPPWdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-222 |
2.11e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.80 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHIL------GTLDtatsGSAKIKNQDV- 73
Cdd:PRK13549 1 MMEYLLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvyphGTYE----GEIIFEGEELq 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 74 -AKLSRTEQAAfrnknLGFIYQFHHLLMEFSAVENVAM---PLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGG 149
Cdd:PRK13549 73 aSNIRDTERAG-----IAIIHQELALVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658758220 150 ERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELnKSLNTSFVVVTHDL-ELADKLGKIAYLDDGK 222
Cdd:PRK13549 148 QQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLnEVKAISDTICVIRDGR 220
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-212 |
2.13e-13 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 67.39 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 35 GDMLAIVGSSGSGKSTLLHIL-GTLDTATSGSAKIKN-QDVAKlsrteqaAFRNKNLGfIYqFHHLLM-EFSAVENVA-- 109
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILaGKLKPNLGKFDDPPDwDEILD-------EFRGSELQ-NY-FTKLLEgDVKVIVKPQyv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 110 --MPLLIKG-----LNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAI 182
Cdd:cd03236 97 dlIPKAVKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190
....*....|....*....|....*....|
gi 658758220 183 KIYDLINELNKSLNtSFVVVTHDLELADKL 212
Cdd:cd03236 177 NAARLIRELAEDDN-YVLVVEHDLAVLDYL 205
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-226 |
2.21e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.36 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 1 MNDLVISCQNLskvyQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLD--TATSGSAKIKNQDVAKLSr 78
Cdd:CHL00131 3 KNKPILEIKNL----HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLE- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 79 TEQAAFRNKNLGFIYQFhhllmEFSAVENvaMPLLIKGLNAKEAKEQALQM------------LDKVGLahrsehKPSAL 146
Cdd:CHL00131 78 PEERAHLGIFLAFQYPI-----EIPGVSN--ADFLRLAYNSKRKFQGLPELdplefleiinekLKLVGM------DPSFL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 147 --------SGGERQRVAIARALVTKPALVLADEPTGNLDKqNAIK-IYDLINELnKSLNTSFVVVTHDLELADKL----- 212
Cdd:CHL00131 145 srnvnegfSGGEKKRNEILQMALLDSELAILDETDSGLDI-DALKiIAEGINKL-MTSENSIILITHYQRLLDYIkpdyv 222
|
250
....*....|....*....
gi 658758220 213 -----GKIAYLDDGKLAIK 226
Cdd:CHL00131 223 hvmqnGKIIKTGDAELAKE 241
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-223 |
3.66e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.05 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 25 LKGVDLSLNQGDMLAIVGSSGSGKSTLLHILG---TLDtatSGSAKIkNQDVaKLSRTEQAAFRNKNlGFIY-------- 93
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLD---DGRIIY-EQDL-IVARLQQDPPRNVE-GTVYdfvaegie 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 94 -------QFHHLLMEfsaVENVAMPLLIKGLnakeAKEQAL--------------QMLDKVGLAhrSEHKPSALSGGERQ 152
Cdd:PRK11147 93 eqaeylkRYHDISHL---VETDPSEKNLNEL----AKLQEQldhhnlwqlenrinEVLAQLGLD--PDAALSSLSGGWLR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758220 153 RVAIARALVTKPALVLADEPTGNLDkqnaIKIYDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMAtRIVDLDRGKL 231
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-223 |
4.24e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 66.40 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 20 NQVEV---LKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLdTATSGSAKIKNQDVAKLSRTEQAAFR------NKNLG 90
Cdd:COG4138 4 NDVAVagrLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRaylsqqQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 91 FIYQFHHLLMEFSAVENVampllikglnakEAKEQALQML-DKVGLAHRSEHKPSALSGGERQRVAIARALVT------- 162
Cdd:COG4138 83 AMPVFQYLALHQPAGASS------------EAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinp 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 163 KPALVLADEPTGNLDKQNAIKIYDLINELnKSLNTSFVVVTHDLEL----ADklgKIAYLDDGKL 223
Cdd:COG4138 151 EGQLLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHtlrhAD---RVWLLKQGKL 211
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-223 |
4.43e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.66 E-value: 4.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSG---SAKIKNQDVAKLSRTEQAAFRNKnLGFIYQFHHLLm 100
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrySGDVLLGGRSIFNYRDVLEFRRR-VGMLFQRPNPF- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 101 EFSAVENVampllIKGLNA------KEAKEQALQMLDKVGL----AHRSEHKPSALSGGERQRVAIARALVTKPALVLAD 170
Cdd:PRK14271 114 PMSIMDNV-----LAGVRAhklvprKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 658758220 171 EPTGNLDKQNAIKIYDLINELNKSLntSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISdRAALFFDGRL 240
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-193 |
5.36e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.34 E-value: 5.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 21 QVEVLKG-----VDLSLNQGDMLAIVGSSGSGKSTLLHIL-GTLdTATSGSAKIKNQDVAklSRTEQAAFRNknlGFIY- 93
Cdd:PRK10762 259 KVDNLSGpgvndVSFTLRKGEILGVSGLMGAGRTELMKVLyGAL-PRTSGYVTLDGHEVV--TRSPQDGLAN---GIVYi 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 94 ----QFHHLLMEFSAVENVAMPllikglnakeakeqALQMLDKVG--LAHRSEHK-------------PSA------LSG 148
Cdd:PRK10762 333 sedrKRDGLVLGMSVKENMSLT--------------ALRYFSRAGgsLKHADEQQavsdfirlfniktPSMeqaiglLSG 398
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 658758220 149 GERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNK 193
Cdd:PRK10762 399 GNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKA 443
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-212 |
7.80e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 67.35 E-value: 7.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQdGQNQVEVLKgVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDV-AKLSRTEQaa 83
Cdd:TIGR01257 1937 ILRLNELTKVYS-GTSSPAVDR-LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQ-- 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 84 frnkNLGFIYQFHHLLMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTK 163
Cdd:TIGR01257 2013 ----NMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 658758220 164 PALVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKL 212
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEAL 2136
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
17-203 |
7.99e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.21 E-value: 7.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 17 DGQNQVE---VLKGVDLSLNQGDMLAIVGSSGSGKSTLLHIL-GTLDTAT-SGSAKIKNQDVAK--LSRTeqaafrnknl 89
Cdd:PLN03211 73 DETRQIQertILNGVTGMASPGEILAVLGPSGSGKSTLLNALaGRIQGNNfTGTILANNRKPTKqiLKRT---------- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 90 GFIYQ----FHHLLMEFSAVeNVAMPLLIKGLNAKEAKEQALQMLDKVGLAhRSEHKP------SALSGGERQRVAIARA 159
Cdd:PLN03211 143 GFVTQddilYPHLTVRETLV-FCSLLRLPKSLTKQEKILVAESVISELGLT-KCENTIignsfiRGISGGERKRVSIAHE 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 658758220 160 LVTKPALVLADEPTGNLDKQNAikiYDLINELNKSLNTSFVVVT 203
Cdd:PLN03211 221 MLINPSLLILDEPTSGLDATAA---YRLVLTLGSLAQKGKTIVT 261
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-212 |
1.02e-12 |
|
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: 66.73 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 34 QGDMLAIVGSSGSGKSTLLHIL--------GTLDTATSGSAKIKnqdvaKLSRTE-QAAFR---NKNLGFIY--QFhhll 99
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILsgelkpnlGDYDEEPSWDEVLK-----RFRGTElQDYFKklaNGEIKVAHkpQY---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 100 mefsaVENVamPLLIKGlNAKEA------KEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPT 173
Cdd:COG1245 169 -----VDLI--PKVFKG-TVRELlekvdeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190
....*....|....*....|....*....|....*....
gi 658758220 174 GNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLELADKL 212
Cdd:COG1245 241 SYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYL 278
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
39-215 |
1.21e-12 |
|
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: 64.55 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 39 AIVGSSGSGKSTllhILGTLDTATSGSAKIKNQDVAKLsrtEQAAFRNKNLGFIYqfhhllMEFSAVENVAMPLlikgln 118
Cdd:cd03240 26 LIVGQNGAGKTT---IIEALKYALTGELPPNSKGGAHD---PKLIREGEVRAQVK------LAFENANGKKYTI------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 119 akeakEQALQMLDKVGLAHRSEHK------PSALSGGERQ------RVAIARALVTKPALVLADEPTGNLDKQN-AIKIY 185
Cdd:cd03240 88 -----TRSLAILENVIFCHQGESNwplldmRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLA 162
|
170 180 190
....*....|....*....|....*....|
gi 658758220 186 DLINELNKSLNTSFVVVTHDLELADKLGKI 215
Cdd:cd03240 163 EIIEERKSQKNFQLIVITHDEELVDAADHI 192
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-221 |
1.76e-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: 66.47 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLDTAtsgSAKIKNQdvAKLSRTEQAAFrnknlgfiyqfhhlLMEF 102
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELEPS---EGKIKHS--GRISFSPQTSW--------------IMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 103 SAVENVampllIKGLNAKEAKE----QALQMLDKVGLAHRSEHKP-----SALSGGERQRVAIARALVTKPALVLADEPT 173
Cdd:TIGR01271 502 TIKDNI-----IFGLSYDEYRYtsviKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 658758220 174 GNLDKQNAIKIYDliNELNKSL-NTSFVVVTHDLELADKLGKIAYLDDG 221
Cdd:TIGR01271 577 THLDVVTEKEIFE--SCLCKLMsNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-212 |
2.26e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 34 QGDMLAIVGSSGSGKSTLLHIL--------GTLDTATSGSAKIKnqdvaKLSRTE-QAAF---RNKNLGFIY--QFHHLL 99
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILsgelipnlGDYEEEPSWDEVLK-----RFRGTElQNYFkklYNGEIKVVHkpQYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 100 mefsavenvamPLLIKGlNAKEAKEQA------LQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPT 173
Cdd:PRK13409 173 -----------PKVFKG-KVRELLKKVdergklDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190
....*....|....*....|....*....|....*....
gi 658758220 174 GNLDKQNAIKIYDLINELNKslNTSFVVVTHDLELADKL 212
Cdd:PRK13409 241 SYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYL 277
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-223 |
2.69e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.18 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 20 NQVEV---LKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLDtaTSGSAKIKNQDVAKLSRTEQAAFRnknlGFIYQ- 94
Cdd:PRK03695 4 NDVAVstrLGPLSAEVRAGEILHLVGPNGAGKSTLLArMAGLLP--GSGSIQFAGQPLEAWSAAELARHR----AYLSQq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 95 ---------FHHLLMEFSAVENVAMPllikglnAKEAKE--QALQMLDKVglaHRSehkPSALSGGERQRVAIARAL--- 160
Cdd:PRK03695 78 qtppfampvFQYLTLHQPDKTRTEAV-------ASALNEvaEALGLDDKL---GRS---VNQLSGGEWQRVRLAAVVlqv 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 161 --VTKPA--LVLADEPTGNLD--KQNAikIYDLINELnKSLNTSFVVVTHDL-ELADKLGKIAYLDDGKL 223
Cdd:PRK03695 145 wpDINPAgqLLLLDEPMNSLDvaQQAA--LDRLLSEL-CQQGIAVVMSSHDLnHTLRHADRVWLLKQGKL 211
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-206 |
4.30e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.74 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQNqveVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSrteQAAFR 85
Cdd:PRK10790 341 IDIDNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS---HSVLR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NkNLGFIYQFHHLLMEfSAVENVAMpllikGLNAKEakEQALQMLDKVGLAHRSEHKP-----------SALSGGERQRV 154
Cdd:PRK10790 415 Q-GVAMVQQDPVVLAD-TFLANVTL-----GRDISE--EQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 155 AIARALVTKPALVLADEPTGNLD---KQNAIKIYDLINElnkslNTSFVVVTHDL 206
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDsgtEQAIQQALAAVRE-----HTTLVVIAHRL 535
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-201 |
5.35e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 62.67 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 10 NLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLL-HILGTLDTATSGSAKIKnqdvaklsrteqaaFRNKN 88
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLkALANRTEGNVSVEGDIH--------------YNGIP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 89 LGFIYQFHHLLMEFSAVENVAMPLLikglNAKEAKEQALQMldkvglahRSEHKPSALSGGERQRVAIARALVTKPALVL 168
Cdd:cd03233 74 YKEFAEKYPGEIIYVSEEDVHFPTL----TVRETLDFALRC--------KGNEFVRGISGGERKRVSIAEALVSRASVLC 141
|
170 180 190
....*....|....*....|....*....|...
gi 658758220 169 ADEPTGNLDKQNAIKIYDLINELNKSLNTSFVV 201
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTMADVLKTTTFV 174
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-224 |
1.50e-11 |
|
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: 63.43 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 25 LKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLDTaTSGSAKIKNQdVAKLSrtEQAAFRNKNLGfiyqfhhllmefs 103
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKGS-VAYVP--QQAWIQNDSLR------------- 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 104 avENVampLLIKGLNAKEAKE--QALQMLDKVGL---AHRSE--HKPSALSGGERQRVAIARALVTKPALVLADEPTGNL 176
Cdd:TIGR00957 717 --ENI---LFGKALNEKYYQQvlEACALLPDLEIlpsGDRTEigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 658758220 177 DKQNAIKIYD-LINELNKSLNTSFVVVTHDLELADKLGKIAYLDDGKLA 224
Cdd:TIGR00957 792 DAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKIS 840
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
4-191 |
1.90e-11 |
|
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: 60.72 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 4 LVISCQNLSKVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTA--TSGSAKIKNQDVAKlsrteq 81
Cdd:cd03232 2 SVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDK------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 82 aAFRnKNLGFIYQfhhllmefsavenvaMPLLIKGLNAKEAKEQalqmldkvglahrsehkpSA----LSGGERQRVAIA 157
Cdd:cd03232 76 -NFQ-RSTGYVEQ---------------QDVHSPNLTVREALRF------------------SAllrgLSVEQRKRLTIG 120
|
170 180 190
....*....|....*....|....*....|....
gi 658758220 158 RALVTKPALVLADEPTGNLDKQNAIKIYDLINEL 191
Cdd:cd03232 121 VELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
24-223 |
3.15e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.38 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLLHIL-GTL-------DTATSGSAKIKNQDVAKLSRTEQAAFRnknlGFIYQF 95
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLtgggaprGARVTGDVTLNGEPLAAIDAPRLARLR----AVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 96 HHLLMEFSAVENVAM---PLLIK-GLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARAL---------VT 162
Cdd:PRK13547 92 AQPAFAFSAREIVLLgryPHARRaGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758220 163 KPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHAdRIAMLADGAI 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
13-206 |
4.05e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.35 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 13 KVYQDGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIknQDVAKLSRTEQAAFRNKnLGFI 92
Cdd:PTZ00265 389 RFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDINLKWWRSK-IGVV 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 93 YQfHHLLMEFSAVENVAMPLL-IKGLNAKEAKEQA--------------------------LQMLDKVGLAH-RSEHK-- 142
Cdd:PTZ00265 466 SQ-DPLLFSNSIKNNIKYSLYsLKDLEALSNYYNEdgndsqenknkrnscrakcagdlndmSNTTDSNELIEmRKNYQti 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 143 --------------------------------PSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINE 190
Cdd:PTZ00265 545 kdsevvdvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINN 624
|
250
....*....|....*.
gi 658758220 191 LNKSLNTSFVVVTHDL 206
Cdd:PTZ00265 625 LKGNENRITIIIAHRL 640
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-208 |
4.63e-11 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 59.64 E-value: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 25 LKGVDLSLNQGDMLAIVGSSGSGKSTLLhilgtldtatsgSAKIKNQDVAKLSRTEQAAFRNKNLgFIYQfhhllmefsa 104
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV------------NEGLYASGKARLISFLPKFSRNKLI-FIDQ---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 105 venvampllikglnakeakeqaLQMLDKVGLAH-RSEHKPSALSGGERQRVAIARALV--TKPALVLADEPTGNLDKQna 181
Cdd:cd03238 68 ----------------------LQFLIDVGLGYlTLGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQ-- 123
|
170 180
....*....|....*....|....*....
gi 658758220 182 iKIYDLINELNK--SLNTSFVVVTHDLEL 208
Cdd:cd03238 124 -DINQLLEVIKGliDLGNTVILIEHNLDV 151
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
23-204 |
5.18e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.58 E-value: 5.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 23 EVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLD--TATSGSAKIKNQDVAKLSRTEQAAfRNKNLGFIYQfhhllM 100
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAG-EGIFMAFQYP-----V 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 101 EFSAVENvaMPLLIKGLNA-KEAKEQAlqMLDKVGLAHRSEHKPSAL---------------SGGERQRVAIARALVTKP 164
Cdd:PRK09580 89 EIPGVSN--QFFLQTALNAvRSYRGQE--PLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVLEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 658758220 165 ALVLADEPTGNLDKqNAIKIY-DLINELNKSlNTSFVVVTH 204
Cdd:PRK09580 165 ELCILDESDSGLDI-DALKIVaDGVNSLRDG-KRSFIIVTH 203
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-221 |
5.54e-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: 61.03 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLDTAtsgSAKIKNQdvAKLSRTEQAAFrnknlgfiyqfhhlLMEF 102
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELEPS---EGKIKHS--GRISFSSQFSW--------------IMPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 103 SAVENVampllIKGLNAKEAKE----QALQMLDKVGLAHRSEHKPSA-----LSGGERQRVAIARALVTKPALVLADEPT 173
Cdd:cd03291 113 TIKENI-----IFGVSYDEYRYksvvKACQLEEDITKFPEKDNTVLGeggitLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 658758220 174 GNLDKQNAIKIYDliNELNKSL-NTSFVVVTHDLELADKLGKIAYLDDG 221
Cdd:cd03291 188 GYLDVFTEKEIFE--SCVCKLMaNKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-224 |
6.64e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 21 QVEVLKG-----VDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAfrnknLGFIY-- 93
Cdd:PRK15439 270 TVEDLTGegfrnISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLA-----RGLVYlp 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 94 ---QFHHLLMEFSAVENV-AMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSA---LSGGERQRVAIARALVTKPAL 166
Cdd:PRK15439 345 edrQSSGLYLDAPLAWNVcALTHNRRGFWIKPARENAVLERYRRALNIKFNHAEQAartLSGGNQQKVLIAKCLEASPQL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758220 167 VLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDLE----LADklgKIAYLDDGKLA 224
Cdd:PRK15439 425 LIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEeieqMAD---RVLVMHQGEIS 482
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-177 |
8.30e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.10 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 3 DLVISCQNLSKVYQDGQnqveVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKnqDVAKLSRTEQa 82
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKL----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETVKLAYVDQ- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 83 aFR-----NKNlgfIYQfhhllmEFSA------VENVAMP--LLIKGLNAKEAKEQalqmlDKVGlahrsehkpsALSGG 149
Cdd:TIGR03719 393 -SRdaldpNKT---VWE------EISGgldiikLGKREIPsrAYVGRFNFKGSDQQ-----KKVG----------QLSGG 447
|
170 180
....*....|....*....|....*...
gi 658758220 150 ERQRVAIARALVTKPALVLADEPTGNLD 177
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
21-223 |
1.62e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.75 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 21 QVEVLKGVDLSLNQGDMLAIVGSSGSGKSTllhilGTLDTATSGSAKIKNQDVAKLSRTEQAAFRnKNLGFIYQFHHLLM 100
Cdd:NF000106 25 EVKAVDGVDLDVREGTVLGVLGP*GAA**R-----GALPAHV*GPDAGRRPWRF*TWCANRRALR-RTIG*HRPVR*GRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 101 E-FSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQ 179
Cdd:NF000106 99 EsFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 658758220 180 NAIKIYDLINELNKSlNTSFVVVTHDLELADKLG-KIAYLDDGKL 223
Cdd:NF000106 179 TRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAhELTVIDRGRV 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
26-224 |
2.27e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.80 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 26 KGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAklSRTEQAAFRnKNLGFIYQ-------FHHl 98
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAVK-KGMAYITEsrrdngfFPN- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 99 lmeFSAVENVAMPLLIK--------GL-NAKEAKEQALQMLDKVGL-AHRSEHKPSALSGGERQRVAIARALVTKPALVL 168
Cdd:PRK09700 356 ---FSIAQNMAISRSLKdggykgamGLfHEVDEQRTAENQRELLALkCHSVNQNITELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658758220 169 ADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLGKIAYLDDGKLA 224
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-222 |
3.56e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.03 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 22 VEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIknqdvakLSRTEQAAFRNKN----LGF--IYQF 95
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEI-------LFDGEVCRFKDIRdseaLGIviIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 96 HHLLMEFSAVENVAM--PLLIKGL-NAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEP 172
Cdd:NF040905 87 LALIPYLSIAENIFLgnERAKRGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 658758220 173 TGNLDKQNAIKIYDLINELNKSLNTSfVVVTHDL----ELADklgKIAYLDDGK 222
Cdd:NF040905 167 TAALNEEDSAALLDLLLELKAQGITS-IIISHKLneirRVAD---SITVLRDGR 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
10-210 |
1.10e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.87 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 10 NLSKVYqdGQNQVEVLKGvdlSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGS----AKI--KNQDV-AKLSRTEQA 82
Cdd:COG1245 346 DLTKSY--GGFSLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEvdedLKIsyKPQYIsPDYDGTVEE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 83 AFRNKNLGFI----YQfhhllmefsavENVAMPLLIKGLNAKEAKEqalqmldkvglahrsehkpsaLSGGERQRVAIAR 158
Cdd:COG1245 421 FLRSANTDDFgssyYK-----------TEIIKPLGLEKLLDKNVKD---------------------LSGGELQRVAIAA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 658758220 159 ALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELAD 210
Cdd:COG1245 469 CLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLID 520
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
25-223 |
5.80e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.82 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 25 LKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKiKNQDVAKLSRTeqaAFRNKNLgfiyqfhhllmefSA 104
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-RNGEVSVIAIS---AGLSGQL-------------TG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 105 VENVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKI 184
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 658758220 185 YDLINELnKSLNTSFVVVTHDLELADKL-GKIAYLDDGKL 223
Cdd:PRK13546 183 LDKIYEF-KEQNKTIFFVSHNLGQVRQFcTKIAWIEGGKL 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
28-173 |
8.17e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 28 VDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDV-AKLSRTeqaafRnKNLGFIYQFHHLLMEFSAVE 106
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdAGDIAT-----R-RRVGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658758220 107 NVAMPLLIKGLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPT 173
Cdd:NF033858 359 NLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
28-223 |
8.53e-09 |
|
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: 55.19 E-value: 8.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 28 VDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRteqAAFRNKnlgF------IYQFHHLLme 101
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNR---EAYRQL---FsavfsdFHLFDRLL-- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 102 fsavenvampllikGLNAKEAKEQALQMLDKVGLahrsEHKPS---------ALSGGERQRVAIARALVT-KPALVL--- 168
Cdd:COG4615 423 --------------GLDGEADPARARELLERLEL----DHKVSvedgrfsttDLSQGQRKRLALLVALLEdRPILVFdew 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 169 -ADEptgnlDKQNAIKIY-DLINELnKSLNTSFVVVTHD---LELADKLGKiayLDDGKL 223
Cdd:COG4615 485 aADQ-----DPEFRRVFYtELLPEL-KARGKTVIAISHDdryFDLADRVLK---MDYGKL 535
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-227 |
2.32e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.97 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 17 DGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLDTATSGSAKIKNQ--DVAKLSRTEQAAFRNkNLGFIY 93
Cdd:PLN03130 625 DSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTvaYVPQVSWIFNATVRD-NILFGS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 94 QFHHLLMEfSAVENVAMpllikglnakeakEQALQMLDKVGLAHRSEhKPSALSGGERQRVAIARALVTKPALVLADEPT 173
Cdd:PLN03130 704 PFDPERYE-RAIDVTAL-------------QHDLDLLPGGDLTEIGE-RGVNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658758220 174 GNLDKQNAIKIYD--LINELNkslNTSFVVVTHDLELADKLGKIAYLDDGKlaIKE 227
Cdd:PLN03130 769 SALDAHVGRQVFDkcIKDELR---GKTRVLVTNQLHFLSQVDRIILVHEGM--IKE 819
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-223 |
2.33e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.82 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQNQVevlKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTE----- 80
Cdd:PRK10522 323 LELRNVTFAYQDNGFSV---GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrklf 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 81 QAAFRNKNLgfiyqFHHLLMEfsavenvamplliKGLNAKEAKEQA----LQMLDKVGLahrSEHKPS--ALSGGERQRV 154
Cdd:PRK10522 400 SAVFTDFHL-----FDQLLGP-------------EGKPANPALVEKwlerLKMAHKLEL---EDGRISnlKLSKGQKKRL 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758220 155 AIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHD---LELADKLGKIaylDDGKL 223
Cdd:PRK10522 459 ALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDdhyFIHADRLLEM---RNGQL 527
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
25-221 |
2.41e-08 |
|
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: 51.59 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 25 LKGVDLSLNQGDMLAIVGSSGSGKSTLLhilgtldtatsgsakiknqdvaklsrteqaafrnKNLGFIyqfhhLLMEFSA 104
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTIL----------------------------------DAIGLA-----LGGAQSA 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 105 venvamplLIKGLNAKEAKEQALQMLDKVGLAHRsehkpsaLSGGERQRVAIARALV---TKPA-LVLADEPTGNLDKQN 180
Cdd:cd03227 52 --------TRRRSGVKAGCIVAAVSAELIFTRLQ-------LSGGEKELSALALILAlasLKPRpLYILDEIDRGLDPRD 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 658758220 181 AIKIYDLINELNKSLNTsFVVVTHDLEL---ADKLGKIAYLDDG 221
Cdd:cd03227 117 GQALAEAILEHLVKGAQ-VIVITHLPELaelADKLIHIKKVITG 159
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
10-210 |
3.27e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 10 NLSKVYqdGQNQVEVLKGvdlSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGS--AKIK----------NQD--VAK 75
Cdd:PRK13409 345 DLTKKL--GDFSLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEvdPELKisykpqyikpDYDgtVED 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 76 LSRTEQAAFRNKnlgFIYqfhhllmefsavenvamPLLIKGLNAKEakeqalqMLDKvglahrsehKPSALSGGERQRVA 155
Cdd:PRK13409 420 LLRSITDDLGSS---YYK-----------------SEIIKPLQLER-------LLDK---------NVKDLSGGELQRVA 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658758220 156 IARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELAD 210
Cdd:PRK13409 464 IAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMID 518
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-220 |
3.65e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.49 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 22 VEVLKGVDLSLNQGDMLAIVGSSGSGKSTLL------------HILGTLDTATSGSAKIKNQ-----------DVAKLSR 78
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMsllmrfydlkndHHIVFKNEHTNDMTNEQDYqgdeeqnvgmkNVNEFSL 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 79 TEQAAFRN-----KNLGFI---------YQFHHLLMEFSAVENvaMPLLIKGL---NAKEAKEQAL-------------- 127
Cdd:PTZ00265 1261 TKEGGSGEdstvfKNSGKIlldgvdicdYNLKDLRNLFSIVSQ--EPMLFNMSiyeNIKFGKEDATredvkrackfaaid 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 128 QMLDKVGLAHRSEHKP--SALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHD 205
Cdd:PTZ00265 1339 EFIESLPNKYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR 1418
|
250
....*....|....*
gi 658758220 206 LELADKLGKIAYLDD 220
Cdd:PTZ00265 1419 IASIKRSDKIVVFNN 1433
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-193 |
5.56e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 5.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 25 LKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAklSRTEQAAFRNknlGF-----------IY 93
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKIN--NHNANEAINH---GFalvteerrstgIY 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 94 QFhhLLMEF-SAVENVAMPLLIKGL-NAKEAKEQALQMLDKVGLAHRSEHKP-SALSGGERQRVAIARALVTKPALVLAD 170
Cdd:PRK10982 339 AY--LDIGFnSLISNIRNYKNKVGLlDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180
....*....|....*....|...
gi 658758220 171 EPTGNLDKQNAIKIYDLINELNK 193
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAELAK 439
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
138-222 |
5.75e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.03 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 138 RSEHKPS--ALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLGKI 215
Cdd:cd03222 62 TPVYKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDR 141
|
....*..
gi 658758220 216 AYLDDGK 222
Cdd:cd03222 142 IHVFEGE 148
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
31-210 |
6.70e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 31 SLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEQAAFRNKNLGFIY----QFHHLLMEFSAVE 106
Cdd:PRK10636 23 TINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIdgdrEYRQLEAQLHDAN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 107 NV----AMPLLIKGLNAKEA---KEQALQMLDKVGLAHRSEHKP-SALSGGERQRVAIARALVTKPALVLADEPTGNLDK 178
Cdd:PRK10636 103 ERndghAIATIHGKLDAIDAwtiRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL 182
|
170 180 190
....*....|....*....|....*....|..
gi 658758220 179 QNAIKIYDLInelnKSLNTSFVVVTHDLELAD 210
Cdd:PRK10636 183 DAVIWLEKWL----KSYQGTLILISHDRDFLD 210
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
28-213 |
9.43e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 28 VDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLDTATSGSAKIKNQDVAklSRTEQAAFRNknlGFIY-----QFHHLLME 101
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVK--IRNPQQAIAQ---GIAMvpedrKRDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 102 FSAVENVAMPLL---IKGLNAKEAKEQ--ALQMLDKVGLAHRSEHKPSA-LSGGERQRVAIARALVTKPALVLADEPTGN 175
Cdd:PRK13549 356 MGVGKNITLAALdrfTGGSRIDDAAELktILESIQRLKVKTASPELAIArLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190
....*....|....*....|....*....|....*...
gi 658758220 176 LDKQNAIKIYDLINELNKSlNTSFVVVTHdlELADKLG 213
Cdd:PRK13549 436 IDVGAKYEIYKLINQLVQQ-GVAIIVISS--ELPEVLG 470
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
25-221 |
1.34e-07 |
|
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: 50.41 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 25 LKGVDLSLNQGDMLAIVGSSGSGKSTLL-HILGTLDTaTSGSAKIKNQDVAKLSRTEQAAFRNKNLGFIYQfHHLLMEFS 103
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQ-KPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 104 AVENVAMPLLIKGLNAKEAKEQ-ALQM-LDKVGLAHRSE--HKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDkq 179
Cdd:cd03290 95 VEENITFGSPFNKQRYKAVTDAcSLQPdIDLLPFGDQTEigERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD-- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 658758220 180 naIKIYDL-----INELNKSLNTSFVVVTHDLELADKLGKIAYLDDG 221
Cdd:cd03290 173 --IHLSDHlmqegILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-179 |
1.44e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 51.25 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 19 QNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGsaKIKNQDVaKLSRTEQAAFRNKnLGFIYQFHHL 98
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG--DIRFHDI-PLTKLQLDSWRSR-LAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 99 LMEfSAVENVAmpllikgLNAKEAKEQALQMLDKVGLAH----------RSE--HKPSALSGGERQRVAIARALVTKPAL 166
Cdd:PRK10789 401 FSD-TVANNIA-------LGRPDATQQEIEHVARLASVHddilrlpqgyDTEvgERGVMLSGGQKQRISIARALLLNAEI 472
|
170
....*....|...
gi 658758220 167 VLADEPTGNLDKQ 179
Cdd:PRK10789 473 LILDDALSAVDGR 485
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-224 |
1.45e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.48 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLS----RTEQAAFRNKNLGFIYQFHHLL 99
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGlhdlRFKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 100 MEFSAV--ENVAMPLLIKGLNAKEAKEQAlqmldkvGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLD 177
Cdd:TIGR00957 1381 DPFSQYsdEEVWWALELAHLKTFVSALPD-------KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 658758220 178 kqnaIKIYDLInelNKSLNTSF-----VVVTHDLELADKLGKIAYLDDGKLA 224
Cdd:TIGR00957 1454 ----LETDNLI---QSTIRTQFedctvLTIAHRLNTIMDYTRVIVLDKGEVA 1498
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-227 |
1.76e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 17 DGQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLDTATSGSAKIKNQ--DVAKLSRTEQAAFRNkNLGFIY 93
Cdd:PLN03232 625 DSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSvaYVPQVSWIFNATVRE-NILFGS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 94 QFHHLLMeFSAVENVAMPL---LIKGLNAKEAKEQALQmldkvglahrsehkpsaLSGGERQRVAIARALVTKPALVLAD 170
Cdd:PLN03232 704 DFESERY-WRAIDVTALQHdldLLPGRDLTEIGERGVN-----------------ISGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 171 EPTGNLDKQNAIKIYD--LINELNkslNTSFVVVTHDLELADKLGKIAYLDDGklAIKE 227
Cdd:PLN03232 766 DPLSALDAHVAHQVFDscMKDELK---GKTRVLVTNQLHFLPLMDRIILVSEG--MIKE 819
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
2-204 |
1.76e-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: 51.29 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 2 NDLVISCQNLSKVYQDGQNQVEVLkgvDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKnqdvaklsrteq 81
Cdd:TIGR00954 448 QDNGIKFENIPLVTPNGDVLIESL---SFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP------------ 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 82 aafRNKNLGFIYQFHHLLMEfSAVENVAMPLLIKGLNAKEAKEQAL-QMLDKVGLAHRSEHKPS---------ALSGGER 151
Cdd:TIGR00954 513 ---AKGKLFYVPQRPYMTLG-TLRDQIIYPDSSEDMKRRGLSDKDLeQILDNVQLTHILEREGGwsavqdwmdVLSGGEK 588
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 658758220 152 QRVAIARALVTKPALVLADEPTGNLdkqnAIKIYDLINELNKSLNTSFVVVTH 204
Cdd:TIGR00954 589 QRIAMARLFYHKPQFAILDECTSAV----SVDVEGYMYRLCREFGITLFSVSH 637
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
25-208 |
1.76e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 50.31 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 25 LKGVDLSLNQGDMLAIVGSSGSGKSTLLHilGTLDTATSGSAKIKNQDVAKLSRTEQAAF----------------RNKN 88
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIN--DTLYPALARRLHLKKEQPGNHDRIEGLEHidkvividqspigrtpRSNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 89 LGFIYQFHHLLMEFSAVENVA------MPLLIKGLN--------AKEAKE---------QALQMLDKVGLAHRSEHKPSA 145
Cdd:cd03271 89 ATYTGVFDEIRELFCEVCKGKrynretLEVRYKGKSiadvldmtVEEALEffenipkiaRKLQTLCDVGLGYIKLGQPAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658758220 146 -LSGGERQRVAIARAL---VTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTsFVVVTHDLEL 208
Cdd:cd03271 169 tLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNT-VVVIEHNLDV 234
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
35-210 |
1.82e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 35 GDMLAIVGSSGSGKSTLLHI-LGTLdTATSGSAKIKNqdvaKLsrtEQAAFRnknlgfiyQFHHLL-MEFSAVENVA--- 109
Cdd:PRK11147 345 GDKIALIGPNGCGKTTLLKLmLGQL-QADSGRIHCGT----KL---EVAYFD--------QHRAELdPEKTVMDNLAegk 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 110 MPLLIKGlnakeAKEQALQMLDKVgLAH--RSEHKPSALSGGERQRVAIARaLVTKPA-LVLADEPTGNLDkqnaIKIYD 186
Cdd:PRK11147 409 QEVMVNG-----RPRHVLGYLQDF-LFHpkRAMTPVKALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLD----VETLE 477
|
170 180
....*....|....*....|....
gi 658758220 187 LINELNKSLNTSFVVVTHDLELAD 210
Cdd:PRK11147 478 LLEELLDSYQGTVLLVSHDRQFVD 501
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-177 |
2.09e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 3 DLVISCQNLSKVYQDgqnqvEVL-KGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKnqDVAKLSRTEQ 81
Cdd:PRK11819 322 DKVIEAENLSKSFGD-----RLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG--ETVKLAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 82 aaFR-----NKNlgfIYQfhhllmEFS------AVENVAMP--LLIKGLNAKEAKEQalqmlDKVGLahrsehkpsaLSG 148
Cdd:PRK11819 395 --SRdaldpNKT---VWE------EISggldiiKVGNREIPsrAYVGRFNFKGGDQQ-----KKVGV----------LSG 448
|
170 180
....*....|....*....|....*....
gi 658758220 149 GERQRVAIARALVTKPALVLADEPTGNLD 177
Cdd:PRK11819 449 GERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-222 |
3.06e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 19 QNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHilgTLDTATSGSAKIKNQDVAKLSRTEQAAFRNKNLGFIY----- 93
Cdd:TIGR00956 71 TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLK---TIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDVVYnaetd 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 94 -QFHHL----LMEFSA----VENvamplLIKGLNAKE-AKEQALQMLDKVGLAHRSEHKPS-----ALSGGERQRVAIAR 158
Cdd:TIGR00956 148 vHFPHLtvgeTLDFAArcktPQN-----RPDGVSREEyAKHIADVYMATYGLSHTRNTKVGndfvrGVSGGERKRVSIAE 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 159 ALVTKPALVLADEPTGNLDKQNAikiYDLINELNKSLN----TSFVVVTHDLELADKL-GKIAYLDDGK 222
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLDSATA---LEFIRALKTSANildtTPLVAIYQCSQDAYELfDKVIVLYEGY 288
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-177 |
3.21e-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: 49.85 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 6 ISCQNLSKVYQDGQNQVevLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLdTATSGSAKIKNQDVAKLSRTEQaafr 85
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKW---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 86 NKNLGFIYQfhhLLMEFSAVenvamplLIKGL--NAKEAKEQALQMLDKVGLAHRSEHKPS-----------ALSGGERQ 152
Cdd:cd03289 76 RKAFGVIPQ---KVFIFSGT-------FRKNLdpYGKWSDEEIWKVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQ 145
|
170 180
....*....|....*....|....*
gi 658758220 153 RVAIARALVTKPALVLADEPTGNLD 177
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLD 170
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
28-223 |
4.23e-07 |
|
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: 49.82 E-value: 4.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 28 VDLSLNQGDMLAIVGSSGSGKSTLLH-ILGTLDTATSGSAKIKNQDVAklSRTEQAAFRNKnLGFI---YQFHHLLMEFS 103
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVD--IRNPAQAIRAG-IAMVpedRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 104 AVENVAMPLL-----IKGLNAKEAKEQALQMLDKVGLAHRSEHKP-SALSGGERQRVAIARALVTKPALVLADEPTGNLD 177
Cdd:TIGR02633 356 VGKNITLSVLksfcfKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 658758220 178 KQNAIKIYDLINELNKSlNTSFVVVTHdlELADKLG---KIAYLDDGKL 223
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQE-GVAIIVVSS--ELAEVLGlsdRVLVIGEGKL 481
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-222 |
4.33e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 22 VEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEqaAFRNkNLGFIYQFHHLLME 101
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE--ALEN-GISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 102 FSAVENVAM---PLliKGLNAKEAK--EQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNL 176
Cdd:PRK10982 88 RSVMDNMWLgryPT--KGMFVDQDKmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 658758220 177 DKQNAIKIYDLINELnKSLNTSFVVVTHDLELADKL-GKIAYLDDGK 222
Cdd:PRK10982 166 TEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLcDEITILRDGQ 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-224 |
4.84e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKlsrteqaafrnknlgfiYQFHHLLMEFS 103
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGA-----------------YGLRELRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 104 AVENvaMPLLIKG---------LNAKEAKEQAlqMLDKVGLAHR--SEHK---------PSALSGGERQRVAIARALVTK 163
Cdd:PTZ00243 1388 MIPQ--DPVLFDGtvrqnvdpfLEASSAEVWA--ALELVGLRERvaSESEgidsrvlegGSNYSVGQRQLMCMARALLKK 1463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658758220 164 -PALVLADEPTGN----LDKQnaikiydlINELNKSLNTSFVVVT--HDLELADKLGKIAYLDDGKLA 224
Cdd:PTZ00243 1464 gSGFILMDEATANidpaLDRQ--------IQATVMSAFSAYTVITiaHRLHTVAQYDKIIVMDHGAVA 1523
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
25-210 |
6.24e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.41 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 25 LKGVDLSLNQGDMLAIVGSSGSGKSTL----LHILGTLDTATSGSA-------KIKNQDVAK---LSRT---EQAAFRNK 87
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtIYAEGQRRYVESLSAyarqflgQMDKPDVDSiegLSPAiaiDQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 88 ---NLGFIYQFHHLLmefsavenvamplliKGLNAKEAKEQALQMLDKVGLAHRS-EHKPSALSGGERQRVAIARALVTK 163
Cdd:cd03270 91 prsTVGTVTEIYDYL---------------RLLFARVGIRERLGFLVDVGLGYLTlSRSAPTLSGGEAQRIRLATQIGSG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 658758220 164 PALVL--ADEPTGNLDKQNAIKIYDLINELNKSLNTsFVVVTHDLE---LAD 210
Cdd:cd03270 156 LTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNT-VLVVEHDEDtirAAD 206
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
29-224 |
6.58e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 29 DLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLS------RTEQAAFRNKNlgfiyqfhHLLME- 101
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSfeqlqkLVSDEWQRNNT--------DMLSPg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 102 -----FSAVENVampllikgLNAKEAKEQALQMLDKVGLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNL 176
Cdd:PRK10938 95 eddtgRTTAEII--------QDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 658758220 177 DKQNAIKIYDLINELNKSLNTSFVVVTHDLELADKLGKIAYLDDGKLA 224
Cdd:PRK10938 167 DVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLA 214
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
40-188 |
9.82e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.56 E-value: 9.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 40 IVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTeQAAFRNKNLGfiyqfhhLLMEFSAVENVAMPLLIkgLNA 119
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP-YCTYIGHNLG-------LKLEMTVFENLKFWSEI--YNS 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658758220 120 KEAKEQALQMLDkvgLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLI 188
Cdd:PRK13541 101 AETLYAAIHYFK---LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-191 |
1.80e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGtlDTATSGSakIKNQDVAKLSRTEQAAFRnKNLGFIYQFH-HL---- 98
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGV--ITGGDRLVNGRPLDSSFQ-RSIGYVQQQDlHLptst 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 99 ---LMEFSA----------------VENVampllIKGLNAKEAKEqALqmldkVGLAHrsehkpSALSGGERQRVAIARA 159
Cdd:TIGR00956 853 vreSLRFSAylrqpksvsksekmeyVEEV-----IKLLEMESYAD-AV-----VGVPG------EGLNVEQRKRLTIGVE 915
|
170 180 190
....*....|....*....|....*....|...
gi 658758220 160 LVTKPALVL-ADEPTGNLDKQNAIKIYDLINEL 191
Cdd:TIGR00956 916 LVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-173 |
2.89e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.43 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 5 VISCQNLSKVYQDgqnqVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILgtldtatSGSAKIK-------NQDVAkls 77
Cdd:NF033858 1 VARLEGVSHRYGK----TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AGARKIQqgrvevlGGDMA--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 78 rteQAAFRN--------------KNLgfiYqfhhllMEFSAVENVAMPLLIKGLNAKEAKEQALQMLDKVGLA---HRSE 140
Cdd:NF033858 67 ---DARHRRavcpriaympqglgKNL---Y------PTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLApfaDRPA 134
|
170 180 190
....*....|....*....|....*....|...
gi 658758220 141 HKpsaLSGGERQRVAIARALVTKPALVLADEPT 173
Cdd:NF033858 135 GK---LSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
117-206 |
3.33e-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: 47.32 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 117 LNAKEAKE---------QALQMLDKVGLAHRSEHKPS-ALSGGERQRVAIARAL---VTKPALVLADEPTGNLDKQNAIK 183
Cdd:TIGR00630 791 MTVEEAYEffeavpsisRKLQTLCDVGLGYIRLGQPAtTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKK 870
|
90 100
....*....|....*....|...
gi 658758220 184 IYDLINELNKSLNTsFVVVTHDL 206
Cdd:TIGR00630 871 LLEVLQRLVDKGNT-VVVIEHNL 892
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-181 |
3.39e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.53 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 18 GQNQVEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTA--TSGSAKI----KNQDV-AKLS-RTEQAAFRNKNL 89
Cdd:PLN03140 889 TEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRIsgfpKKQETfARISgYCEQNDIHSPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 90 ----GFIYQ-FHHLLMEFSAVENV----AMPLLIKGLNAKEAKeqalqmldkVGLAhrsehKPSALSGGERQRVAIARAL 160
Cdd:PLN03140 969 tvreSLIYSaFLRLPKEVSKEEKMmfvdEVMELVELDNLKDAI---------VGLP-----GVTGLSTEQRKRLTIAVEL 1034
|
170 180
....*....|....*....|.
gi 658758220 161 VTKPALVLADEPTGNLDKQNA 181
Cdd:PLN03140 1035 VANPSIIFMDEPTSGLDARAA 1055
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-223 |
4.01e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.43 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIKNQDVAKLSRTEqaaFRnKNLGFIYQFHHLlmeFS 103
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMD---LR-KVLGIIPQAPVL---FS 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 104 AVENVAMPLLIKGLNAK--EAKEQAlQMLDKV-----GLAHRSEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNL 176
Cdd:PLN03130 1327 GTVRFNLDPFNEHNDADlwESLERA-HLKDVIrrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 658758220 177 DKQNAIKIYDLINELNKSlnTSFVVVTHDLELADKLGKIAYLDDGKL 223
Cdd:PLN03130 1406 DVRTDALIQKTIREEFKS--CTMLIIAHRLNTIIDCDRILVLDAGRV 1450
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-212 |
4.27e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 9 QNLSKVYQDGqnqvEVLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGSAKIknqdvaklsrTEQAafrnkN 88
Cdd:PRK15064 323 ENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW----------SENA-----N 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 89 LGFIYQFHHllMEFSAVENVaMPLLIKGLNAKEaKEQALQ-MLDKVgLAHRSEHKPSA--LSGGERQRVAIARALVTKPA 165
Cdd:PRK15064 384 IGYYAQDHA--YDFENDLTL-FDWMSQWRQEGD-DEQAVRgTLGRL-LFSQDDIKKSVkvLSGGEKGRMLFGKLMMQKPN 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 658758220 166 LVLADEPTGNLDKQNaikiydlINELNKSLNT---SFVVVTHDLELADKL 212
Cdd:PRK15064 459 VLVMDEPTNHMDMES-------IESLNMALEKyegTLIFVSHDREFVSSL 501
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
27-177 |
6.05e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 27 GVDLSlnqgDMLAIVGSSGSGKSTLLHILGTLDTATSGSakiknqdVAKLSRTEQAAFRNknlgfiyqfHHLlmefSAVE 106
Cdd:PLN03073 531 GIDLD----SRIAMVGPNGIGKSTILKLISGELQPSSGT-------VFRSAKVRMAVFSQ---------HHV----DGLD 586
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658758220 107 NVAMPLLIKGLNAKEAKEQALQM-LDKVGLAHRSEHKPS-ALSGGERQRVAIARALVTKPALVLADEPTGNLD 177
Cdd:PLN03073 587 LSSNPLLYMMRCFPGVPEQKLRAhLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-209 |
8.09e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLLHILG-----------TLDTATSGSAK----IKnqdvaklsrteqaafrnKN 88
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysndlTLFGRRRGSGEtiwdIK-----------------KH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 89 LGFIYQFHHLLMEFSA-VENVamplLIKGL-------NAKEAKEQAL--QMLDKVGLAHRSEHKP-SALSGGERQRVAIA 157
Cdd:PRK10938 338 IGYVSSSLHLDYRVSTsVRNV----ILSGFfdsigiyQAVSDRQQKLaqQWLDILGIDKRTADAPfHSLSWGQQRLALIV 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 658758220 158 RALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELA 209
Cdd:PRK10938 414 RALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-208 |
1.32e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 24 VLKGVDLSLNQGDMLAIVGSSGSGKSTLLHIL-GTLDTATS--GSAK-IKnqdvaklsrteqaafrnknLGFIYQfHHLl 99
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLaGELAPVSGeiGLAKgIK-------------------LGYFAQ-HQL- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 100 mEFSAVENVAMPLLIKgLNAKEAKEQALQMLDKVGLAHRSEHKPSA-LSGGERQRVAIARALVTKPALVLADEPTGNLDk 178
Cdd:PRK10636 386 -EFLRADESPLQHLAR-LAPQELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD- 462
|
170 180 190
....*....|....*....|....*....|...
gi 658758220 179 qnaikiYDLINELNKSL---NTSFVVVTHDLEL 208
Cdd:PRK10636 463 ------LDMRQALTEALidfEGALVVVSHDRHL 489
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
117-207 |
1.61e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 117 LNAKEAKEQALQMLDKVGLAHRSEHKPS-ALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKsl 195
Cdd:PLN03073 315 IDAYTAEARAASILAGLSFTPEMQVKATkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK-- 392
|
90
....*....|..
gi 658758220 196 ntSFVVVTHDLE 207
Cdd:PLN03073 393 --TFIVVSHARE 402
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
41-205 |
2.84e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 41 VGSSGSGKSTLLHILGTLDTATSGSAKI-KNQDVAKLsRTEQAAFRNKN-LGFIYQFHHLLMEFSAVEN--VAMPLLIK- 115
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLdPNERLGKL-RQDQFAFEEFTvLDTVIMGHTELWEVKQERDriYALPEMSEe 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 116 -GLNAKE------------AKEQALQMLDKVGLAHRSEHKP-SALSGGERQRVAIARALVTKPALVLADEPTGNLDKqNA 181
Cdd:PRK15064 112 dGMKVADlevkfaemdgytAEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI-NT 190
|
170 180
....*....|....*....|....
gi 658758220 182 IKIydLINELNKSlNTSFVVVTHD 205
Cdd:PRK15064 191 IRW--LEDVLNER-NSTMIIISHD 211
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-206 |
3.79e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.13 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 2 NDLVISC---QNLSKVY-------QDGQNQVEVLKG------VDLSLNQGDMLAIVGSSGSGKSTLLHILGTLDTATSGS 65
Cdd:PRK11288 230 RDQLVQAmvgREIGDIYgyrprplGEVRLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQ 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 66 AKIKNQDVAklSRTEQAAFR---------NKNLGfIYQFHhllmefSAVENV---AMPLLIKG---LNAKEAKEQALQML 130
Cdd:PRK11288 310 VYLDGKPID--IRSPRDAIRagimlcpedRKAEG-IIPVH------SVADNInisARRHHLRAgclINNRWEAENADRFI 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658758220 131 DKVGLAHRSEHKP-SALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSlNTSFVVVTHDL 206
Cdd:PRK11288 381 RSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDL 456
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-212 |
5.25e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.98 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 34 QGDMLAIVGSSGSGKSTLLHILGtldtatsgsakiknqdvaklsrteqAAFRNKNLGFIYqfhhllmefsavenvampll 113
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALA-------------------------RELGPPGGGVIY-------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 114 ikgLNAKEAKEQALQMLDKVGLahrsEHKPSALSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLIN---- 189
Cdd:smart00382 36 ---IDGEDILEEVLDQLLLIIV----GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180
....*....|....*....|....
gi 658758220 190 -ELNKSLNTSFVVVTHDLELADKL 212
Cdd:smart00382 109 lLLKSEKNLTVILTTNDEKDLGPA 132
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
153-219 |
5.34e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.88 E-value: 5.34e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658758220 153 RVAIARALVTKPALVLADEPTGNLDKQN----AIKIYDLINELNKSLNTSFVVVTHDLELADKLGKIAYLD 219
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRSEYVE 1283
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
113-212 |
6.00e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 113 LIKGLNAKeakeqaLQMLDKVGLAHRSEHKPSA-LSGGERQRVAIARALVTKPALV--LADEPTGNLDKQNAIKIYDLIN 189
Cdd:PRK00635 449 VLQGLKSR------LSILIDLGLPYLTPERALAtLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIK 522
|
90 100
....*....|....*....|....*.
gi 658758220 190 ELNKSLNTsFVVVTHD---LELADKL 212
Cdd:PRK00635 523 KLRDQGNT-VLLVEHDeqmISLADRI 547
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
35-212 |
6.05e-05 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 42.45 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 35 GDMLAIVGSSGSGKST----LLHILG-----TL------DTATSGSAKIKNQDVAKLSRTeqaaFRNKN--LGFIYQfhh 97
Cdd:cd03278 22 PGLTAIVGPNGSGKSNiidaIRWVLGeqsakSLrgekmsDVIFAGSETRKPANFAEVTLT----FDNSDgrYSIISQ--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 98 llmefSAVENVampllikgLNAKEAKEQALqmldkvglahrsehkpSALSGGERQRVAIarALV-----TKPA-LVLADE 171
Cdd:cd03278 95 -----GDVSEI--------IEAPGKKVQRL----------------SLLSGGEKALTAL--ALLfaifrVRPSpFCVLDE 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 658758220 172 PTGNLDKQNAIKIYDLINELNKslNTSFVVVTHD---LELADKL 212
Cdd:cd03278 144 VDAALDDANVERFARLLKEFSK--ETQFIVITHRkgtMEAADRL 185
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
120-210 |
3.44e-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: 41.15 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 120 KEAKEQaLQMLDKVGLAHRSEHKPSA-LSGGERQRVAIARALVTKPALVL--ADEPTGNLDKQNAIKiydLINELN--KS 194
Cdd:TIGR00630 463 KEIRER-LGFLIDVGLDYLSLSRAAGtLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRR---LINTLKrlRD 538
|
90
....*....|....*....
gi 658758220 195 LNTSFVVVTHD---LELAD 210
Cdd:TIGR00630 539 LGNTLIVVEHDedtIRAAD 557
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
143-210 |
6.36e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 143 PSALSGGERQ------RVAIARALV-------TKPALVLaDEPTGNLDKQNAIKIYDLINELNKSLNTSFVVVTHDLELA 209
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAegiegdaPLPPLIL-DEPTVFLDSGHVSQLVDLVESMRRLGVEQIVVVSHDDELV 857
|
.
gi 658758220 210 D 210
Cdd:PRK02224 858 G 858
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
144-221 |
1.23e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.57 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 144 SALSGGERQRVAIARALVT---KPA-LVLADEPTGNLDKQNAIKIYDLINELNKslNTSFVVVTHD---LELADKLGKIA 216
Cdd:pfam02463 1076 DLLSGGEKTLVALALIFAIqkyKPApFYLLDEIDAALDDQNVSRVANLLKELSK--NAQFIVISLReemLEKADKLVGVT 1153
|
....*
gi 658758220 217 YLDDG 221
Cdd:pfam02463 1154 MVENG 1158
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
39-206 |
1.79e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.07 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 39 AIVGSSGSGKSTLLH-ILGTLDTATSGSAKIKNQDVAKLSRTEQAAFRNKNLGFIY-------QFHHLLME-----FSAV 105
Cdd:COG0419 27 LIVGPNGAGKSTILEaIRYALYGKARSRSKLRSDLINVGSEEASVELEFEHGGKRYrierrqgEFAEFLEAkpserKEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 106 ENVAMPLLIKGL--NAKEAKEQALQMLDKVGLAHRSEHK----------PSALSGGERQRVAIARALvtkpALVLaDepT 173
Cdd:COG0419 107 KRLLGLEIYEELkeRLKELEEALESALEELAELQKLKQEilaqlsgldpIETLSGGERLRLALADLL----SLIL-D--F 179
|
170 180 190
....*....|....*....|....*....|...
gi 658758220 174 GNLDKQNAIKIYDLINELnkslntsfVVVTHDL 206
Cdd:COG0419 180 GSLDEERLERLLDALEEL--------AIITHVI 204
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-212 |
1.91e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 38.88 E-value: 1.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658758220 144 SALSGGERQRVAIarALV-----TKPA-LVLADEPTGNLDKQNAIKIYDLINELNKslNTSFVVVTHD---LELADKL 212
Cdd:TIGR02168 1088 SLLSGGEKALTAL--ALLfaifkVKPApFCILDEVDAPLDDANVERFANLLKEFSK--NTQFIVITHNkgtMEVADQL 1161
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
127-173 |
1.93e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 1.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 658758220 127 LQMLDKVGL--------AhrsehkpSALSGGERQRVAIARALV---TKPALVLADEPT 173
Cdd:COG0178 807 LQTLQDVGLgyiklgqpA-------TTLSGGEAQRVKLASELSkrsTGKTLYILDEPT 857
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
146-191 |
2.08e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.62 E-value: 2.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 658758220 146 LSGGERQRVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINEL 191
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINEL 450
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
25-55 |
2.48e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 2.48e-03
10 20 30
....*....|....*....|....*....|..
gi 658758220 25 LKGVDLSLNQGDMLAIVGSSGSGKSTLLH-IL 55
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVNdIL 652
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
146-210 |
3.70e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.12 E-value: 3.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658758220 146 LSGGERQ------RVAIARALVTKPALVLADEPTGNLDKQNAIKIYDLINELNKSLnTSFVVVTHDLELAD 210
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKI-PQVIIVSHDEELKD 858
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
125-206 |
4.86e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 125 QALQMLDKVGLAHRSEHKP-SALSGGERQRVAIARAL---VTKPALVLADEPTGNLDKQNaikIYDLINELnKSLNT--- 197
Cdd:PRK00635 788 EKIHALCSLGLDYLPLGRPlSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHD---IKALIYVL-QSLTHqgh 863
|
....*....
gi 658758220 198 SFVVVTHDL 206
Cdd:PRK00635 864 TVVIIEHNM 872
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
25-58 |
5.25e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.74 E-value: 5.25e-03
10 20 30
....*....|....*....|....*....|....
gi 658758220 25 LKGVDLSLNQGDMLAIVGSSGSGKSTLlhILGTL 58
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTL--INETL 656
|
|
| ABC_MutS-like |
cd03283 |
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ... |
164-212 |
5.38e-03 |
|
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213250 [Multi-domain] Cd Length: 199 Bit Score: 36.89 E-value: 5.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 658758220 164 PALVLADE---PTGNLDKQNAIKIydLINELNKSlNTSFVVVTHDLELADKL 212
Cdd:cd03283 106 PVLFLLDEifkGTNSRERQAASAA--VLKFLKNK-NTIGIISTHDLELADLL 154
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
39-214 |
5.50e-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: 36.86 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 39 AIVGSSGSGKSTLLH-ILGTLDTATSGSAKIKNQDVAkLSRTEQAAfrnkNLGFIYQFHHLLMEfsaVENVamplliKGL 117
Cdd:cd03279 32 LICGPTGAGKSTILDaITYALYGKTPRYGRQENLRSV-FAPGEDTA----EVSFTFQLGGKKYR---VERS------RGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758220 118 NAKEAKEQAlqMLDKVGLAHRSEHKPSALSGGERQRVAIARALvtkpAL--VLA------------DEPTGNLDKQNAIK 183
Cdd:cd03279 98 DYDQFTRIV--LLPQGEFDRFLARPVSTLSGGETFLASLSLAL----ALseVLQnrggarlealfiDEGFGTLDPEALEA 171
|
170 180 190
....*....|....*....|....*....|.
gi 658758220 184 IYDLINELnKSLNTSFVVVTHDLELADKLGK 214
Cdd:cd03279 172 VATALELI-RTENRMVGVISHVEELKERIPQ 201
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
22-64 |
7.82e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 36.84 E-value: 7.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 658758220 22 VEVLKGVdlsLNQGDMLAIVGSSGSGKSTLL-HILGTLDTATSG 64
Cdd:PRK01889 185 LDVLAAW---LSGGKTVALLGSSGVGKSTLVnALLGEEVQKTGA 225
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
39-69 |
8.19e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.22 E-value: 8.19e-03
10 20 30
....*....|....*....|....*....|...
gi 658758220 39 AIVGSSGSGKSTLL-HILGTLDTATSG-SAKIK 69
Cdd:cd01854 89 VLVGQSGVGKSTLLnALLPELVLATGEiSEKLG 121
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
146-211 |
8.30e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 36.47 E-value: 8.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658758220 146 LSGGERQRVAIARALV---TKPA-LVLADEPTGNLDKQNAIKIYDLINELnkSLNTSFVVVTHD---LELADK 211
Cdd:cd03272 159 LSGGQKSLVALALIFAiqkCDPApFYLFDEIDAALDAQYRTAVANMIKEL--SDGAQFITTTFRpelLEVADK 229
|
|
| |
