|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-217 |
4.60e-87 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 257.23 E-value: 4.60e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQetsqgvqysDKTSQ 82
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD---------SKKDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMM 162
Cdd:COG1126 73 NKLRRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 163 LSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:COG1126 153 MEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVV 207
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-217 |
6.57e-80 |
|
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: 238.20 E-value: 6.57e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvqYSDKTSQRR 84
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL---------TDDKKNINE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 YQNAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLS 164
Cdd:cd03262 74 LRQKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1032718621 165 PEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVI 206
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-217 |
1.42e-67 |
|
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: 206.96 E-value: 1.42e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNM----VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSqgvqySD 78
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSE-----KE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 79 KTSQRRYQnaIGMVFQNYQLFPNFTVLDNVLEAPIAQKLaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIA 158
Cdd:cd03255 76 LAAFRRRH--IGFVFQSFNLLPDLTALENVELPLLLAGV-PKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 159 RAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHDTQFgEDFGTRIV 217
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPEL-AEYADRII 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-217 |
5.67e-66 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 203.79 E-value: 5.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 7 NLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGdrvlcqetsqGVQYSD-KTSQRRY 85
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVD----------GLKVNDpKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 86 QNAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSP 165
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 166 EIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLI 207
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-217 |
1.12e-65 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 203.49 E-value: 1.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAI-GDRVLCQETSQGVQYSDKT 80
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVgGEEIRLKPDRDGELVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQ-RRYQNAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIAR 159
Cdd:COG4598 88 RQlQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1032718621 160 AMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVV 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
9.25e-65 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 199.88 E-value: 9.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVS--NLKKAY-NGNM---VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDrvlcQETSQgv 74
Cdd:COG1136 1 MSPLLElrNLTKSYgTGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDG----QDISS-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 75 qYSDK--TSQRRyqNAIGMVFQNYQLFPNFTVLDNVLeapIAQKLA--PKSELLDQAMFLLDSVGLKDKADAYPSTLSGG 150
Cdd:COG1136 75 -LSERelARLRR--RHIGFVFQFFNLLPELTALENVA---LPLLLAgvSRKERRERARELLERVGLGDRLDHRPSQLSGG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032718621 151 QKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHDTQFGEdFGTRIV 217
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAA-RADRVI 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
2-217 |
1.82e-63 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 197.67 E-value: 1.82e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQGVQysdKTS 81
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQ---KGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 QRRYQNAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAM 161
Cdd:PRK11264 80 IRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1032718621 162 MLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAI 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-205 |
1.06e-62 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 195.69 E-value: 1.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAY----NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvqy 76
Cdd:COG1116 6 PALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 77 sDKTSQRRyqnaiGMVFQNYQLFPNFTVLDNVLEAPIAQKLaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVA 156
Cdd:COG1116 76 -TGPGPDR-----GVVFQEPALLPWLTVLDNVALGLELRGV-PKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 157 IARAMMLSPEIICFDEPTSALD---RESANQVgkLVQAIAKQGKGILVVTHD 205
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDaltRERLQDE--LLRLWQETGKTVLFVTHD 198
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-220 |
1.54e-62 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 194.85 E-value: 1.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqETSQGVQYSDKT 80
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF--DFSQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRyqnAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARA 160
Cdd:COG4161 79 LLRQ---KVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 161 MMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIVSSE 220
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYME 215
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-217 |
3.85e-62 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 194.12 E-value: 3.85e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAY-NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDrvlcqetsQGVQYSDK 79
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDG--------QDVTALRG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 80 TSQRRYQNAIGMVFQNYQLFPNFTVLDNVL-----EAPIAQKLAPK--SELLDQAMFLLDSVGLKDKADAYPSTLSGGQK 152
Cdd:COG3638 73 RALRRLRRRIGMIFQQFNLVPRLSVLTNVLagrlgRTSTWRSLLGLfpPEDRERALEALERVGLADKAYQRADQLSGGQQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032718621 153 QRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAK-QGKGILVVTHDTQFGEDFGTRIV 217
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDLARRYADRII 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-217 |
9.70e-62 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 192.19 E-value: 9.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 7 NLKKAY-NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQGVQYSdktsqRRY 85
Cdd:COG2884 6 NVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL-----RRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 86 qnaIGMVFQNYQLFPNFTVLDNVLEAPIAQKlAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSP 165
Cdd:COG2884 81 ---IGVVFQDFRLLPDRTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 166 EIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVL 208
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
5-216 |
2.87e-61 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 191.97 E-value: 2.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAI-GDRVLCQETSQG-VQYSDKTSQ 82
Cdd:TIGR03005 3 FSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVeGEQLYHMPGRNGpLVPADEKHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMM 162
Cdd:TIGR03005 83 RQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 163 LSPEIICFDEPTSALDRESANQVGKLVQAIAKQGK-GILVVTHDTQFGEDFGTRI 216
Cdd:TIGR03005 163 MRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDlTMLLVTHEMGFAREFADRV 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-205 |
3.78e-61 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 194.93 E-value: 3.78e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvqySDKTS 81
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV----------TGLPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 QRRYqnaIGMVFQNYQLFPNFTVLDNVlEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAM 161
Cdd:COG3842 75 EKRN---VGMVFQDYALFPHLTVAENV-AFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1032718621 162 MLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHD 195
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-205 |
1.49e-60 |
|
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: 188.88 E-value: 1.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvqySDKTSQ 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV----------TGVPPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRyqnAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMM 162
Cdd:cd03259 71 RR---NIGMVFQDYALFPHLTVAENIAFGLKLRGV-PKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1032718621 163 LSPEIICFDEPTSALDRESANQV-GKLVQAIAKQGKGILVVTHD 205
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELrEELKELQRELGITTIYVTHD 190
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-205 |
2.21e-60 |
|
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: 188.45 E-value: 2.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGN----MVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQEtsqgvqysd 78
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 79 ktsqrryQNAIGMVFQNYQLFPNFTVLDNVLeAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIA 158
Cdd:cd03293 72 -------GPDRGYVFQQDALLPWLTVLDNVA-LGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1032718621 159 RAMMLSPEIICFDEPTSALD---RESANQVgkLVQAIAKQGKGILVVTHD 205
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDaltREQLQEE--LLDIWRETGKTVLLVTHD 191
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-220 |
1.17e-59 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 187.53 E-value: 1.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRV--LCQETSqgvqysD 78
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPS------D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 79 KTSQRRYQNaIGMVFQNYQLFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIA 158
Cdd:PRK11124 75 KAIRELRRN-VGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 159 RAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIVSSE 220
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYME 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
5-205 |
6.84e-57 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 180.56 E-value: 6.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSqgvqySDKTSQRR 84
Cdd:COG1127 8 VRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSE-----KELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 YqnaIGMVFQNYQLFPNFTVLDNVlEAPIAQKLA-PKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMML 163
Cdd:COG1127 83 R---IGMLFQGGALFDSLTVFENV-AFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALAL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1032718621 164 SPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHD 201
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-217 |
2.84e-56 |
|
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: 176.61 E-value: 2.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQgvqysDKTSQ 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE-----LPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRyqnaIGMVFQNYQLFPNFTVLDNVleapiaqklapkselldqamflldsvglkdkadAYPstLSGGQKQRVAIARAMM 162
Cdd:cd03229 76 RR----IGMVFQDFALFPHLTVLENI---------------------------------ALG--LSGGQQQRVALARALA 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1032718621 163 LSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHDTQFGEDFGTRIV 217
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVV 172
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-217 |
8.38e-56 |
|
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: 177.14 E-value: 8.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAY-NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQGVqysdkts 81
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 qRRYqnaIGMVFQN--YQLFpNFTVLDNVLEAPIAQKLaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIAR 159
Cdd:COG1122 74 -RRK---VGLVFQNpdDQLF-APTVEEDVAFGPENLGL-PREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1032718621 160 AMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVI 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-205 |
1.99e-55 |
|
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: 184.34 E-value: 1.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGN-----MVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQGVqys 77
Cdd:COG1123 261 LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSL--- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 78 dktsqRRYQNAIGMVFQN--YQLFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGL-KDKADAYPSTLSGGQKQR 154
Cdd:COG1123 338 -----RELRRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQR 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 155 VAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHD 464
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-205 |
2.83e-55 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 179.57 E-value: 2.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvqYSDKT 80
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL---------FTNLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYqnaIGMVFQNYQLFPNFTVLDNVLEAPIAQKLaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARA 160
Cdd:COG1118 72 PRERR---VGFVFQHYALFPHMTVAENIAFGLRVRPP-SKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1032718621 161 MMLSPEIICFDEPTSALDRESANQVGK-LVQAIAKQGKGILVVTHD 205
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAKVRKELRRwLRRLHDELGGTTVFVTHD 193
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-217 |
6.74e-55 |
|
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: 175.45 E-value: 6.74e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAY-NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQetsqgVQYSDKTSQR 83
Cdd:cd03256 3 VENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINK-----LKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 84 RYqnaIGMVFQNYQLFPNFTVLDNVLEAPIAQK--------LAPKSELLdQAMFLLDSVGLKDKADAYPSTLSGGQKQRV 155
Cdd:cd03256 78 RQ---IGMIFQQFNLIERLSVLENVLSGRLGRRstwrslfgLFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032718621 156 AIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHDTQFGEDFGTRIV 217
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIV 216
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-217 |
9.42e-54 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 173.23 E-value: 9.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRV--LCQETSQGVQYSDKT 80
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinLVRDKDGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGLKDKA-DAYPSTLSGGQKQRVAIAR 159
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1032718621 160 AMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVI 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-217 |
1.76e-53 |
|
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: 170.73 E-value: 1.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNM--VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvqysDKTSQ 82
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL-----------TKLSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQN--YQLFpNFTVLDNVLEAPIAQKLaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARA 160
Cdd:cd03225 71 KELRRKVGLVFQNpdDQFF-GPTVEEEVAFGLENLGL-PEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1032718621 161 MMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVI 205
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
5-221 |
7.92e-53 |
|
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: 169.43 E-value: 7.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAY-NGNM---VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIaigdRVLCQETSqGVQYSDKT 80
Cdd:TIGR02982 4 IRNLNHYYgHGSLrkqVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSL----KVLGQELH-GASKKQLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRyqnAIGMVFQNYQLFPNFTVLDNV-LEAPIAQKLAPKsELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIAR 159
Cdd:TIGR02982 79 QLRR---RIGYIFQAHNLLGFLTARQNVqMALELQPNLSYQ-EARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032718621 160 AMMLSPEIICFDEPTSALDRESANQVGKLVQAIAK-QGKGILVVTHDTQFgEDFGTRIVSSEE 221
Cdd:TIGR02982 155 ALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKeQGCTILMVTHDNRI-LDVADRILQMED 216
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-217 |
1.29e-52 |
|
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: 169.79 E-value: 1.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAY-NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQEtsqgvQYSDKTS 81
Cdd:TIGR02315 2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKL-----RGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 QRRYqnaIGMVFQNYQLFPNFTVLDNVLEAPIAQK--------LAPKSELlDQAMFLLDSVGLKDKADAYPSTLSGGQKQ 153
Cdd:TIGR02315 77 LRRR---IGMIFQHYNLIERLTVLENVLHGRLGYKptwrsllgRFSEEDK-ERALSALERVGLADKAYQRADQLSGGQQQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 154 RVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHDTQFGEDFGTRIV 217
Cdd:TIGR02315 153 RVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIV 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-204 |
3.38e-52 |
|
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: 168.14 E-value: 3.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNM----VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQetsqgvqySDKT 80
Cdd:cd03258 4 LKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTL--------LSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNAIGMVFQNYQLFPNFTVLDNV---LEapIAQKlaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAI 157
Cdd:cd03258 76 ELRKARRRIGMIFQHFNLLSSRTVFENValpLE--IAGV--PKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1032718621 158 ARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTH 204
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITH 199
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-205 |
3.45e-52 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 171.41 E-value: 3.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGN----MVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgVQYSDKt 80
Cdd:COG1135 4 LENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL-------TALSER- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNAIGMVFQNYQLFPNFTVLDNVlEAPIaqKLA--PKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIA 158
Cdd:COG1135 76 ELRAARRKIGMIFQHFNLLSSRTVAENV-ALPL--EIAgvPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1032718621 159 RAMMLSPEIICFDEPTSALDRESANQVGKLVQAI-AKQGKGILVVTHD 205
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILDLLKDInRELGLTIVLITHE 200
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-217 |
7.28e-52 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 171.02 E-value: 7.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MA-LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvqySDK 79
Cdd:COG3839 1 MAsLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV----------TDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 80 TSQRRyqnAIGMVFQNYQLFPNFTVLDNV---LEapiAQKLaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVA 156
Cdd:COG3839 71 PPKDR---NIAMVFQSYALYPHMTVYENIafpLK---LRKV-PKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032718621 157 IARAMMLSPEIICFDEPTSALDRESANQV-GKLVQAIAKQGKGILVVTHD-----TqfgedFGTRIV 217
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKLRVEMrAEIKRLHRRLGTTTIYVTHDqveamT-----LADRIA 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-205 |
1.63e-51 |
|
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: 166.52 E-value: 1.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIaigdRVLCQETSQGVQYSDKTSQRR 84
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEV----LIDGEDISGLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 yqnaIGMVFQNYQLFPNFTVLDNVlEAPIAQKLA-PKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMML 163
Cdd:cd03261 79 ----MGMLFQSGALFDSLTVFENV-AFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1032718621 164 SPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHD 196
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-217 |
2.12e-51 |
|
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: 166.07 E-value: 2.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvqySDKTSQ 82
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI----------TGLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPNFTVLDNVLEAPIAQK---------LAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQ 153
Cdd:cd03219 71 EIARLGIGRTFQIPRLFPELTVLENVMVAAQARTgsglllaraRREEREARERAEELLERVGLADLADRPAGELSYGQQR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032718621 154 RVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVT 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-217 |
4.72e-50 |
|
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: 162.89 E-value: 4.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlcqetsqgvQYSDKT 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE----------DATDVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRyqnAIGMVFQNYQLFPNFTVLDNV---LEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAI 157
Cdd:cd03296 71 VQER---NVGFVFQHYALFRHMTVFDNVafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 158 ARAMMLSPEIICFDEPTSALDresaNQVGKLVQAIAKQ-----GKGILVVTHDTQFGEDFGTRIV 217
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALD----AKVRKELRRWLRRlhdelHVTTVFVTHDQEEALEVADRVV 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-217 |
4.90e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 162.54 E-value: 4.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDrvlcqetsqgvqYSDKTSQ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLG------------EDVARDP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPNFTVLDNVLeapIAQKL--APKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARA 160
Cdd:COG1131 69 AEVRRRIGYVPQEPALYPDLTVRENLR---FFARLygLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALA 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1032718621 161 MMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVA 202
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-217 |
6.28e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 159.21 E-value: 6.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlCQETSQGVQYsdktsqRR 84
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGK--PLSAMPPPEW------RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 yqnAIGMVFQNYQLFPNfTVLDNVLEAPIAQKLAPKSELLDQamfLLDSVGLKDKA-DAYPSTLSGGQKQRVAIARAMML 163
Cdd:COG4619 75 ---QVAYVPQEPALWGG-TVRDNLPFPFQLRERKFDRERALE---LLERLGLPPDIlDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 164 SPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHDTQFGEDFGTRIV 217
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVL 202
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-207 |
1.76e-48 |
|
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: 158.50 E-value: 1.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKC-----DQGNIAIGDRVLCQETSqgvqysDK 79
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDV------DV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 80 TSQRRYqnaIGMVFQNYQLFPnFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGL----KDKADAYpsTLSGGQKQRV 155
Cdd:cd03260 77 LELRRR---VGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALwdevKDRLHAL--GLSGGQQQRL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 156 AIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQgKGILVVTHDTQ 207
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQ 201
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-205 |
8.12e-48 |
|
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: 156.90 E-value: 8.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAY-NGNM---VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvQYSDKT 80
Cdd:cd03257 4 VKNLSVSFpTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDL--------LKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNAIGMVFQNYQ--LFPNFTVLDNVLEAP-IAQKLAPKSELLDQAMFLLDSVGL-KDKADAYPSTLSGGQKQRVA 156
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMssLNPRMTIGEQIAEPLrIHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1032718621 157 IARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHD 205
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-205 |
5.54e-47 |
|
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: 154.38 E-value: 5.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 21 FNCRID---PGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcQETSQGVqysDKTSQRRyqnAIGMVFQNYQ 97
Cdd:cd03297 13 FTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL-FDSRKKI---NLPPQQR---KIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 98 LFPNFTVLDNVLeapIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSAL 177
Cdd:cd03297 86 LFPHLNVRENLA---FGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180
....*....|....*....|....*....
gi 1032718621 178 DRESANQVGKLVQAIAKQGKG-ILVVTHD 205
Cdd:cd03297 163 DRALRLQLLPELKQIKKNLNIpVIFVTHD 191
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-217 |
2.87e-46 |
|
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: 152.41 E-value: 2.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlcqetsqgvqysDKTSQ 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR-------------DVTDL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPNFTVLDNvLEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMM 162
Cdd:cd03301 68 PPKDRDIAMVFQNYALYPHMTVYDN-IAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1032718621 163 LSPEIICFDEPTSALD----RESANQVGKLVQaiaKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:cd03301 147 REPKVFLMDEPLSNLDaklrVQMRAELKRLQQ---RLGTTTIYVTHDQVEAMTMADRIA 202
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-220 |
3.60e-46 |
|
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: 152.18 E-value: 3.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 7 NLKKAYNGNMV-IDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQGVQYsdktsqrrY 85
Cdd:cd03292 5 NVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPY--------L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 86 QNAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLAPKsELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSP 165
Cdd:cd03292 77 RRKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPR-EIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 166 EIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIVSSE 220
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALE 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-205 |
4.19e-46 |
|
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: 153.03 E-value: 4.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAY----NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVlcqetsqgVQYS 77
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRP--------VTRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 78 DKTSQRRyqnAIGMVFQNYQ--LFPNFTVLDNVLEAPIAQKLAPKSELLDQamfLLDSVGL-KDKADAYPSTLSGGQKQR 154
Cdd:COG1124 73 RRKAFRR---RVQMVFQDPYasLHPRHTVDRILAEPLRIHGLPDREERIAE---LLEQVGLpPSFLDRYPHQLSGGQRQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 155 VAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAI-AKQGKGILVVTHD 205
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHD 198
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-217 |
4.38e-46 |
|
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: 152.02 E-value: 4.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 6 SNLKKAYNGNMVI-DQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIaigdRVLCQETSQgVQYSDKTSQRR 84
Cdd:TIGR02673 5 HNVSKAYPGGVAAlHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQV----RIAGEDVNR-LRGRQLPLLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 YqnaIGMVFQNYQLFPNFTVLDNVLEAPIAQKlAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLS 164
Cdd:TIGR02673 80 R---IGVVFQDFRLLPDRTVYENVALPLEVRG-KKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1032718621 165 PEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:TIGR02673 156 PPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVI 208
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-205 |
1.40e-45 |
|
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: 151.24 E-value: 1.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlcqetsqgvqysDKTSQRR 84
Cdd:cd03300 3 LENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK-------------DITNLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 YQNAIGMVFQNYQLFPNFTVLDNVlEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLS 164
Cdd:cd03300 70 HKRPVNTVFQNYALFPHLTVFENI-AFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1032718621 165 PEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHD 190
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-205 |
1.59e-44 |
|
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: 149.42 E-value: 1.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvqySDKT 80
Cdd:COG0411 3 PLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI----------TGLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNAIGMVFQNYQLFPNFTVLDNVL--------EAPIAQKLAPKS------ELLDQAMFLLDSVGLKDKADAYPST 146
Cdd:COG0411 73 PHRIARLGIARTFQNPRLFPELTVLENVLvaaharlgRGLLAALLRLPRarreerEARERAEELLERVGLADRADEPAGN 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 147 LSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAI-AKQGKGILVVTHD 205
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHD 212
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-206 |
2.13e-44 |
|
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: 147.38 E-value: 2.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDrvlcQETSQgvqYSDKTSQRR 84
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNG----QETPP---LNSKKASKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 YQNAIGMVFQNYQLFPNFTVLDNvLEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLS 164
Cdd:TIGR03608 74 RREKLGYLFQNFALIENETVEEN-LDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1032718621 165 PEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDT 206
Cdd:TIGR03608 153 PPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP 194
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-217 |
2.46e-44 |
|
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: 148.47 E-value: 2.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlcqetsqgvqysDKTSQ 82
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE-------------DVRKE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 -RRYQNAIGMVFQNYQLFPNFTVLDNV-LEAPIAQKlaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARA 160
Cdd:COG4555 69 pREARRQIGVLPDERGLYDRLTVRENIrYFAELYGL--FDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1032718621 161 MMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVV 203
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-205 |
2.21e-43 |
|
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: 146.34 E-value: 2.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQetsqgvqYSDKTS 81
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAS-------LSRREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 QRRyqnaIGMVFQNYQLFPNFTVLDNVL------EAPIAQklaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRV 155
Cdd:COG1120 74 ARR----IAYVPQEPPAPFGLTVRELVAlgryphLGLFGR---PSAEDREAVEEALERTGLEHLADRPVDELSGGERQRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1032718621 156 AIARAMMLSPEIICFDEPTSALDreSANQ--VGKLVQAIAK-QGKGILVVTHD 205
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLD--LAHQleVLELLRRLAReRGRTVVMVLHD 197
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-217 |
3.16e-43 |
|
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: 144.32 E-value: 3.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 14 GNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlcqetsqgvqysdKTSQRRYQNAIGMVF 93
Cdd:cd03226 12 GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK--------------PIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 94 QN--YQLFPNfTVLDNVLeapIAQKLAPKSEllDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFD 171
Cdd:cd03226 78 QDvdYQLFTD-SVREELL---LGLKELDAGN--EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1032718621 172 EPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVL 197
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-217 |
3.27e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 145.62 E-value: 3.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlcqetsqgvqysdkt 80
Cdd:COG1121 5 PAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNAIGMVFQNYQLFPNF--TVLDnVLEAPIAQKLA----PKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQR 154
Cdd:COG1121 69 PPRRARRRIGYVPQRAEVDWDFpiTVRD-VVLMGRYGRRGlfrrPSRADREAVDEALERVGLEDLADRPIGELSGGQQQR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032718621 155 VAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVL 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-217 |
5.65e-43 |
|
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: 151.21 E-value: 5.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAYNGNM--VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCD---QGNIAIGDRVLCQetsqgvqy 76
Cdd:COG1123 4 LLEVRDLSVRYPGGDvpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLE-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 77 sdkTSQRRYQNAIGMVFQN--YQLFPnFTVLDNVLEAPIAQKLaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQR 154
Cdd:COG1123 76 ---LSEALRGRRIGMVFQDpmTQLNP-VTVGDQIAEALENLGL-SRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032718621 155 VAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHDTQFGEDFGTRIV 217
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVV 214
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
17-217 |
7.45e-43 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 143.71 E-value: 7.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 17 VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCqetsqGVQYSDKTSQRRyqNAIGMVFQNY 96
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVT-----NLSYSQKIILRR--ELIGYIFQSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 97 QLFPNFTVLDNVlEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSA 176
Cdd:NF038007 93 NLIPHLSIFDNV-ALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGN 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1032718621 177 LDRESANQVGKLVQAIAKQGKGILVVTHDTQfGEDFGTRIV 217
Cdd:NF038007 172 LDSKNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRII 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-217 |
8.68e-43 |
|
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: 142.15 E-value: 8.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKtsQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV----------LGKDIKKE--P 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPNFTVLDNVleapiaqklapkselldqamflldsvglkdkadaypsTLSGGQKQRVAIARAMM 162
Cdd:cd03230 69 EEVKRRIGYLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 163 LSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVA 166
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-207 |
9.74e-43 |
|
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: 144.11 E-value: 9.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAYNGN----MVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQ--Etsqgvq 75
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldE------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 76 ysDKTSQRRYQNaIGMVFQNYQLFPNFTVLDNV---LEapiaqkLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQK 152
Cdd:COG4181 82 --DARARLRARH-VGFVFQSFQLLPTLTALENVmlpLE------LAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1032718621 153 QRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAI-AKQGKGILVVTHDTQ 207
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPA 208
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-217 |
1.81e-42 |
|
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: 143.60 E-value: 1.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 6 SNLKKAYNGNM-VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDrvlcQETSQgvqySDKTSQRR 84
Cdd:cd03295 4 ENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDG----EDIRE----QDPVELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 yqnAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLaPKSELLDQAMFLLDSVGLKDK--ADAYPSTLSGGQKQRVAIARAMM 162
Cdd:cd03295 76 ---KIGYVIQQIGLFPHMTVEENIALVPKLLKW-PKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1032718621 163 LSPEIICFDEPTSALD---RES-ANQVGKLVQAIakqGKGILVVTHDTQFGEDFGTRIV 217
Cdd:cd03295 152 ADPPLLLMDEPFGALDpitRDQlQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIA 207
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-205 |
2.45e-42 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 146.63 E-value: 2.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 6 SNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGdrvlcqetsqGVQYSDKTSQRRY 85
Cdd:PRK09452 18 RGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD----------GQDITHVPAENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 86 QNAigmVFQNYQLFPNFTVLDNVLEAPIAQKLaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSP 165
Cdd:PRK09452 88 VNT---VFQSYALFPHMTVFENVAFGLRMQKT-PAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1032718621 166 EIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHD 204
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-205 |
4.65e-42 |
|
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: 143.17 E-value: 4.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 25 IDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgVQYSDKTSQRRYQNAIGMVFQNYQLFPNFTV 104
Cdd:cd03294 47 VREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDI-------AAMSRKELRELRRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 105 LDNVlEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALD----RE 180
Cdd:cd03294 120 LENV-AFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirRE 198
|
170 180
....*....|....*....|....*
gi 1032718621 181 SANQVGKLVqaiAKQGKGILVVTHD 205
Cdd:cd03294 199 MQDELLRLQ---AELQKTIVFITHD 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-217 |
9.42e-42 |
|
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: 138.92 E-value: 9.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvqysDKTSQRR 84
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI-----------AKLPLEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 YQNAIGMVFQnyqlfpnftvldnvleapiaqklapkselldqamflldsvglkdkadaypstLSGGQKQRVAIARAMMLS 164
Cdd:cd00267 71 LRRRIGYVPQ----------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1032718621 165 PEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVI 151
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-205 |
1.02e-41 |
|
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: 144.86 E-value: 1.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 22 NCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcQETSQGVqySDKTSQRRyqnaIGMVFQNYQLFPN 101
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL-QDSARGI--FLPPHRRR----IGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 102 FTVLDNVLeapIAQKLAPKSE---LLDQAMFLLdsvGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALD 178
Cdd:COG4148 92 LSVRGNLL---YGRKRAPRAErriSFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180
....*....|....*....|....*...
gi 1032718621 179 RESANQVGKLVQAIAKQGKG-ILVVTHD 205
Cdd:COG4148 166 LARKAEILPYLERLRDELDIpILYVSHS 193
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-205 |
1.42e-41 |
|
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: 139.92 E-value: 1.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQgvqysdkt 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 sqrrYQNAIGMVFQNYQLFPNFTVLDNVLeapIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARA 160
Cdd:COG4133 73 ----YRRRLAYLGHADGLKPELTVRENLR---FWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1032718621 161 MMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-217 |
1.67e-41 |
|
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: 139.98 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsqgvqysDKTSQRR 84
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV----------------FGKPLEK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 YQNAIGMVFQNYQLFPNF--TVLDNVLEAPIAQKLAPKS------ELLDQAmflLDSVGLKDKADAYPSTLSGGQKQRVA 156
Cdd:cd03235 66 ERKRIGYVPQRRSIDRDFpiSVRDVVLMGLYGHKGLFRRlskadkAKVDEA---LERVGLSELADRQIGELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032718621 157 IARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVL 203
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-175 |
1.45e-40 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 135.85 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 25 IDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvQYSDKTSQRRyqnAIGMVFQNYQLFPNFTV 104
Cdd:pfam00005 8 LNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL--------TDDERKSLRK---EIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 105 LDNVLEAPIAQKLApKSELLDQAMFLLDSVGLKDKAD----AYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTS 175
Cdd:pfam00005 77 RENLRLGLLLKGLS-KREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-217 |
1.68e-39 |
|
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: 135.33 E-value: 1.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNM--VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDrvlcqetsqgvqYSDKT 80
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING------------YSIRT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNAIGMVFQNYQLFPNFTVLDNV-LEAPIaqKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIAR 159
Cdd:cd03263 69 DRKAARQSLGYCPQFDALFDELTVREHLrFYARL--KGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1032718621 160 AMMLSPEIICFDEPTSALDRESANQVGKLVQAIaKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIA 203
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-204 |
2.20e-39 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 138.40 E-value: 2.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 6 SNLKKAYNGNM----VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgVQYSDK-- 79
Cdd:PRK11153 5 KNISKVFPQGGrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDL-------TALSEKel 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 80 TSQRRyqnAIGMVFQNYQLFPNFTVLDNV---LE------APIAQKLAPkselldqamfLLDSVGLKDKADAYPSTLSGG 150
Cdd:PRK11153 78 RKARR---QIGMIFQHFNLLSSRTVFDNValpLElagtpkAEIKARVTE----------LLELVGLSDKADRYPAQLSGG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 151 QKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTH 204
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITH 199
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-217 |
3.45e-39 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 135.76 E-value: 3.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNM----VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqeTSQGVqy 76
Cdd:COG4525 2 SMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV---TGPGA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 77 sdktsqRRyqnaiGMVFQNYQLFPNFTVLDNVleaPIAQKLA--PKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQR 154
Cdd:COG4525 77 ------DR-----GVVFQKDALLPWLNVLDNV---AFGLRLRgvPKAERRARAEELLALVGLADFARRRIWQLSGGMRQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032718621 155 VAIARAMMLSPEIICFDEPTSALD---RESANQVgkLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDaltREQMQEL--LLDVWQRTGKGVFLITHSVEEALFLATRLV 206
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-217 |
7.43e-39 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 137.14 E-value: 7.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDrvlcQETSQgVQYSDkt 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG----TDVSR-LHARD-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 sqRRyqnaIGMVFQNYQLFPNFTVLDNvleapIAQKLA-------PKSELLDQ-AMFLLDSVGLKDKADAYPSTLSGGQK 152
Cdd:PRK10851 74 --RK----VGFVFQHYALFRHMTVFDN-----IAFGLTvlprrerPNAAAIKAkVTQLLEMVQLAHLADRYPAQLSGGQK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032718621 153 QRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILV-VTHDTQFGEDFGTRIV 217
Cdd:PRK10851 143 QRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVfVTHDQEEAMEVADRVV 208
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-204 |
1.30e-38 |
|
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: 131.35 E-value: 1.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNM--VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQEtsqgvqysdkt 80
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNAIGMVFQNYQLFpNFTVLDNVLeapiaqklapkselldqamflldsvglkdkadaypstlSGGQKQRVAIARA 160
Cdd:cd03228 70 DLESLRKNIAYVPQDPFLF-SGTIRENIL--------------------------------------SGGQRQRIAIARA 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1032718621 161 MMLSPEIICFDEPTSALDRESANQVGKLVQAIAKqGKGILVVTH 204
Cdd:cd03228 111 LLRDPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAH 153
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-205 |
1.43e-38 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 136.39 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAI-GDRVlcqeTSQGVQYSDkts 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdGEDV----THRSIQQRD--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 qrryqnaIGMVFQNYQLFPNFTVLDNVLEAPIAQKLaPKSEL---LDQAMFLLDSVGLKDKadaYPSTLSGGQKQRVAIA 158
Cdd:PRK11432 80 -------ICMVFQSYALFPHMSLGENVGYGLKMLGV-PKEERkqrVKEALELVDLAGFEDR---YVDQISGGQQQRVALA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 159 RAMMLSPEIICFDEPTSALD---RESANQVGKLVQaiakQGKGI--LVVTHD 205
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDanlRRSMREKIRELQ----QQFNItsLYVTHD 196
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-217 |
2.57e-38 |
|
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: 135.31 E-value: 2.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 33 LLGPSGTGKTTFMRLINNLEKCDQGNIAIGdrvlcqetsqGVQYSDKTSQRRYqnaIGMVFQNYQLFPNFTVLDNVlEAP 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLD----------GEDVTNVPPHLRH---INMVFQSYALFPHMTVEENV-AFG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 113 IAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAI 192
Cdd:TIGR01187 67 LKMRKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI 146
|
170 180
....*....|....*....|....*.
gi 1032718621 193 AKQ-GKGILVVTHDTQFGEDFGTRIV 217
Cdd:TIGR01187 147 QEQlGITFVFVTHDQEEAMTMSDRIA 172
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-205 |
1.19e-37 |
|
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: 133.25 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGN----MVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEK---CDQGNIAIGDRVLcqetsqgVQ 75
Cdd:COG0444 2 LEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDL-------LK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 76 YSDKTSQRRYQNAIGMVFQNYQ--LFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGLKDK---ADAYPSTLSGG 150
Cdd:COG0444 75 LSEKELRKIRGREIQMIFQDPMtsLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPerrLDRYPHELSGG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1032718621 151 QKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHD 210
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-205 |
5.72e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 128.37 E-value: 5.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMR-LINNLEK--CDQGNIAIGDRVLCQEtsqgvqysdK 79
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPafSASGEVLLNGRRLTAL---------P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 80 TSQRRyqnaIGMVFQNYQLFPNFTVLDNVLEApIAQKLaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIAR 159
Cdd:COG4136 73 AEQRR----IGILFQDDLLFPHLSVGENLAFA-LPPTI-GRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1032718621 160 AMMLSPEIICFDEPTSALDRESANQVGKLV-QAIAKQGKGILVVTHD 205
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAALRAQFREFVfEQIRQRGIPALLVTHD 193
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-205 |
4.55e-36 |
|
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: 125.24 E-value: 4.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgVQYSDKTsqrr 84
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL-------ASLSPKE---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 yqnaigmvfqnyqlfpnftvldnvleapIAQKLApkseLLDQAMfllDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLS 164
Cdd:cd03214 71 ----------------------------LARKIA----YVPQAL---ELLGLAHLADRPFNELSGGERQRVLLARALAQE 115
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1032718621 165 PEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHD 157
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-205 |
5.61e-36 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 127.57 E-value: 5.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNM-----VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETsqgvqys 77
Cdd:TIGR04521 1 IKLKNVSYIYQPGTpfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKK------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 78 dKTSQRRYQNAIGMVFQN--YQLFPNfTVLDNVLEAPIAQKLaPKSELLDQAMFLLDSVGLKDK-ADAYPSTLSGGQKQR 154
Cdd:TIGR04521 74 -KKKLKDLRKKVGLVFQFpeHQLFEE-TVYKDIAFGPKNLGL-SEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 155 VAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:TIGR04521 151 VAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHS 202
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-205 |
6.77e-36 |
|
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: 126.30 E-value: 6.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYnGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKTSQ 82
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL----------NGKDITNLPPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRyqnAIGMVFQNYQLFPNFTVLDNvLEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMM 162
Cdd:cd03299 70 KR---DISYVPQNYALFPHMTVYKN-IAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1032718621 163 LSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHD 189
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-205 |
6.88e-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: 133.42 E-value: 6.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAYNGN--MVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQetsqgvqysdk 79
Cdd:COG2274 473 DIELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQ----------- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 80 TSQRRYQNAIGMVFQNYQLFpNFTVLDNVLeapIAQKLAPKSELLdQAmflLDSVGLKDKADAYP-----------STLS 148
Cdd:COG2274 542 IDPASLRRQIGVVLQDVFLF-SGTIRENIT---LGDPDATDEEII-EA---ARLAGLHDFIEALPmgydtvvgeggSNLS 613
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1032718621 149 GGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAkQGKGILVVTHD 205
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHR 669
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-207 |
1.91e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.92 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLekCD-------QGNIAIGDRVLcqetsqgv 74
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRM--NDlipgarvEGEILLDGEDI-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 75 qYSDKTSQ---RRYqnaIGMVFQNYQLFPnFTVLDNVLEAPIAQKLAPKSEL-------LDQAMfLLDSVglKDKADAYP 144
Cdd:COG1117 81 -YDPDVDVvelRRR---VGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELdeiveesLRKAA-LWDEV--KDRLKKSA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032718621 145 STLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQgKGILVVTHDTQ 207
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQ 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-217 |
2.17e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 124.87 E-value: 2.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNG-NMvidQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlcqetsqgvqysDKTS 81
Cdd:COG3840 2 LRLDDLTYRYGDfPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ-------------DLTA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 QRRYQNAIGMVFQNYQLFPNFTVLDNvleapIAQKLAPKSEL-------LDQAmflLDSVGLKDKADAYPSTLSGGQKQR 154
Cdd:COG3840 66 LPPAERPVSMLFQENNLFPHLTVAQN-----IGLGLRPGLKLtaeqraqVEQA---LERVGLAGLLDRLPGQLSGGQRQR 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032718621 155 VAIARAMMLSPEIICFDEPTSALD----RESANqvgkLVQAIAK-QGKGILVVTHDTQFGEDFGTRIV 217
Cdd:COG3840 138 VALARCLVRKRPILLLDEPFSALDpalrQEMLD----LVDELCReRGLTVLMVTHDPEDAARIADRVL 201
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-217 |
3.21e-35 |
|
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: 123.84 E-value: 3.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGeIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlcqetsqgvqySDKTSQ 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ------------DVLKQP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMM 162
Cdd:cd03264 68 QKLRRRIGYLPQEFGVYPNFTVREFLDYIAWLKGI-PSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 163 LSPEIICFDEPTSALDRESANQVGKLVQAIAKqGKGILVVTHDTQFGEDFGTRIV 217
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGE-DRIVILSTHIVEDVESLCNQVA 200
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-178 |
3.38e-35 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 126.77 E-value: 3.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAY---------NGNMV--IDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQets 71
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITG--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 72 qgvqySDKTSQRRYQNAIGMVFQNYQ--LFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGLK-DKADAYPSTLS 148
Cdd:COG4608 85 -----LSGRELRPLRRRMQMVFQDPYasLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRpEHADRYPHEFS 159
|
170 180 190
....*....|....*....|....*....|
gi 1032718621 149 GGQKQRVAIARAMMLSPEIICFDEPTSALD 178
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-216 |
7.12e-35 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 127.26 E-value: 7.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKTSq 82
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML----------DGVDLSHVPP- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 rrYQNAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMM 162
Cdd:PRK11607 89 --YQRPINMMFQSYALFPHMTVEQNIAFGLKQDKL-PKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 163 LSPEIICFDEPTSALDRESANQVG-KLVQAIAKQGKGILVVTHDTQFGEDFGTRI 216
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLRDRMQlEVVDILERVGVTCVMVTHDQEEAMTMAGRI 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-205 |
2.27e-34 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 123.25 E-value: 2.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQEtsqgvqysdktsq 82
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 rryQNAIGMVFQNYQLFPNFTVLDNVleapiaqKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMM 162
Cdd:PRK11247 80 ---REDTRLMFQDARLLPWKKVIDNV-------GLGLKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1032718621 163 LSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHD 193
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
5-204 |
2.76e-34 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 125.19 E-value: 2.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGnMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlcqetsqgvqysDKTSQRR 84
Cdd:NF040840 4 IENLSKDWKE-FKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGK-------------DITNLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 YQNAIGMVFQNYQLFPNFTVLDNvleapIAQKL----APKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARA 160
Cdd:NF040840 70 EKRGIAYVYQNYMLFPHKTVFEN-----IAFGLklrkVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1032718621 161 MMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTH 204
Cdd:NF040840 145 LIIEPKLLLLDEPLSALDVQTRDELIREMKRWHREfGFTAIHVTH 189
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-205 |
4.27e-34 |
|
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: 122.54 E-value: 4.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGN--MVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAI-GDRVLCQETSQGVqysdkts 81
Cdd:TIGR04520 3 VENVSFSYPESekPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVdGLDTLDEENLWEI------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 qRRyqnAIGMVFQN--YQlFPNFTVLDNVLEAPIAQKLaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIAR 159
Cdd:TIGR04520 76 -RK---KVGMVFQNpdNQ-FVGATVEDDVAFGLENLGV-PREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1032718621 160 AMMLSPEIICFDEPTSALDRESANQVGKLVQAIAK-QGKGILVVTHD 205
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHD 196
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-215 |
4.44e-34 |
|
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: 121.39 E-value: 4.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKTSQ 82
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF----------DGRDITGLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLAPKSELLDQ--AMFLLdsvgLKDKADAYPSTLSGGQKQRVAIARA 160
Cdd:cd03224 71 ERARAGIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERvyELFPR----LKERRKQLAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 161 MMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTR 215
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADR 201
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-205 |
4.70e-34 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 127.57 E-value: 4.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAY-NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQEtsqgvqysdkt 80
Cdd:COG4988 336 SIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL----------- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNAIGMVFQNYQLFPNfTVLDNVLeapIAQKLAPKSELLdQAmflLDSVGLKDKADAYP-----------STLSG 149
Cdd:COG4988 405 DPASWRRQIAWVPQNPYLFAG-TIRENLR---LGRPDASDEELE-AA---LEAAGLDEFVAALPdgldtplgeggRGLSG 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1032718621 150 GQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKqGKGILVVTHD 205
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHR 531
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-207 |
9.03e-34 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 127.15 E-value: 9.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 17 VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIaigdRVLCQETSQgvQYSDKTSQRRYQNaIGMVFQNY 96
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTY----RVAGQDVAT--LDADALAQLRREH-FGFIFQRY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 97 QLFPNFTVLDNVlEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSA 176
Cdd:PRK10535 96 HLLSHLTAAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190
....*....|....*....|....*....|.
gi 1032718621 177 LDRESANQVGKLVQAIAKQGKGILVVTHDTQ 207
Cdd:PRK10535 175 LDSHSGEEVMAILHQLRDRGHTVIIVTHDPQ 205
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-204 |
1.78e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 122.27 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNM-----VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQGVQYS 77
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 78 DKTSQR-----RYQNAIGMVFQ--NYQLFPNfTVLDNVLEAPIAQKLaPKSELLDQAMFLLDSVGLKDK-ADAYPSTLSG 149
Cdd:PRK13631 102 NPYSKKiknfkELRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGV-KKSEAKKLAKFYLNKMGLDDSyLERSPFGLSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 150 GQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITH 234
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
2-205 |
3.16e-33 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 120.19 E-value: 3.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIaigdrvlcqeTSQGVQYSDKTS 81
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI----------TLDGKPVEGPGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 QRryqnaiGMVFQNYQLFPNFTVLDNVleaPIAQKLA--PKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIAR 159
Cdd:PRK11248 71 ER------GVVFQNEGLLPWRNVQDNV---AFGLQLAgvEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIAR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1032718621 160 AMMLSPEIICFDEPTSALD---RESANQVgkLVQAIAKQGKGILVVTHD 205
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALDaftREQMQTL--LLKLWQETGKQVLLITHD 188
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-207 |
4.83e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 119.15 E-value: 4.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYN-GNM---VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSqgvqySD 78
Cdd:PRK11629 6 LQCDNLCKRYQeGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSS-----AA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 79 KTSQRRYQnaIGMVFQNYQLFPNFTVLDNVLEAPIAQKLAPKsELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIA 158
Cdd:PRK11629 81 KAELRNQK--LGFIYQFHHLLPDFTALENVAMPLLIGKKKPA-EINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1032718621 159 RAMMLSPEIICFDEPTSALDRESANQVGKLVQAI-AKQGKGILVVTHDTQ 207
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQ 207
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-216 |
8.03e-33 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 117.86 E-value: 8.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAI-GDRVLCqetsqgvqysDKTS 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaGHDVVR----------EPRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 QRRyqnAIGMVFQNYQLFPNFTVLDNVLeapIAQKLA--PKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIAR 159
Cdd:cd03265 71 VRR---RIGIVFQDLSVDDELTGWENLY---IHARLYgvPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1032718621 160 AMMLSPEIICFDEPTSALDRESANQVGKLVQAI-AKQGKGILVVTHDTQFGEDFGTRI 216
Cdd:cd03265 145 SLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRV 202
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-205 |
1.15e-32 |
|
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: 123.55 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAYNGNM-VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQGvqysdkt 80
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 sqrrYQNAIGMVFQNYQLFPNfTVLDNVLeapIAQKLAPKSELlDQAmflLDSVGLKDKADAYP-----------STLSG 149
Cdd:TIGR02857 394 ----WRDQIAWVPQHPFLFAG-TIAENIR---LARPDASDAEI-REA---LERAGLDEFVAALPqgldtpigeggAGLSG 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1032718621 150 GQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAkQGKGILVVTHD 205
Cdd:TIGR02857 462 GQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHR 516
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-204 |
1.73e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 122.43 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKT 80
Cdd:COG1129 3 PLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL----------DGEPVRFRS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNAIGMVFQNYQLFPNFTVLDNVL--EAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIA 158
Cdd:COG1129 73 PRDAQAAGIAIIHQELNLVPNLSVAENIFlgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1032718621 159 RAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:COG1129 153 RALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISH 198
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-178 |
2.15e-32 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 120.33 E-value: 2.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIV-SNLKKAY-NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQEtsqgvqysd 78
Cdd:PRK11650 1 MAGLKlQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 79 KTSQRryqnAIGMVFQNYQLFPNFTVLDN---------VLEAPIAQKLAPKSELLDQAMFLldsvglkdkaDAYPSTLSG 149
Cdd:PRK11650 72 EPADR----DIAMVFQNYALYPHMSVRENmayglkirgMPKAEIEERVAEAARILELEPLL----------DRKPRELSG 137
|
170 180
....*....|....*....|....*....
gi 1032718621 150 GQKQRVAIARAMMLSPEIICFDEPTSALD 178
Cdd:PRK11650 138 GQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-207 |
2.57e-32 |
|
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: 119.83 E-value: 2.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 27 PG-EIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcQETSQGVQYSdkTSQRRyqnaIGMVFQNYQLFPNFTVL 105
Cdd:TIGR02142 21 PGqGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL-FDSRKGIFLP--PEKRR----IGYVFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 106 DNvLEAPIAQKLAPKSELLDQAmfLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQV 185
Cdd:TIGR02142 94 GN-LRYGMKRARPSERRISFER--VIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180
....*....|....*....|...
gi 1032718621 186 GKLVQAIAKQ-GKGILVVTHDTQ 207
Cdd:TIGR02142 171 LPYLERLHAEfGIPILYVSHSLQ 193
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-204 |
3.85e-32 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 116.49 E-value: 3.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvqySDKTSQ 82
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI----------TKLPMH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMM 162
Cdd:cd03218 71 KRARLGIGYLPQEASIFRKLTVEENILAVLEIRGL-SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1032718621 163 LSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDH 191
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-217 |
1.58e-31 |
|
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: 120.64 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAYNGNM--VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQetsqgvqYSDK 79
Cdd:COG4987 333 SLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD-------LDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 80 TSQRRyqnaIGMVFQNYQLFpNFTVLDNVLeapIAQKLAPKSELLDqamfLLDSVGLKDKADAYP-----------STLS 148
Cdd:COG4987 406 DLRRR----IAVVPQRPHLF-DTTLRENLR---LARPDATDEELWA----ALERVGLGDWLAALPdgldtwlgeggRRLS 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032718621 149 GGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAkQGKGILVVTHDTQfGEDFGTRIV 217
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLA-GLERMDRIL 540
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-205 |
1.63e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 116.72 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNM-----VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIA--IGDRVLCQETSQG 73
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwiFKDEKNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 74 VQYSD-----KTSQRRYQNA------IGMVFQ--NYQLFPNfTVLDNVLEAPIAQKLaPKSELLDQAMFLLDSVGL-KDK 139
Cdd:PRK13651 81 EKVLEklviqKTRFKKIKKIkeirrrVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGV-SKEEAKKRAAKYIELVGLdESY 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032718621 140 ADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHD 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-206 |
2.18e-31 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 114.59 E-value: 2.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 8 LKKAY-NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQGVQYsdktsQRRyq 86
Cdd:PRK10908 7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPF-----LRR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 87 nAIGMVFQNYQLFPNFTVLDNVlEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPE 166
Cdd:PRK10908 80 -QIGMIFQDHHLLMDRTVYDNV-AIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1032718621 167 IICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDT 206
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-205 |
2.29e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 115.96 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSqgVQYSDKTS 81
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSI--FNYRDVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 QRRyqnAIGMVFQNYQLFPnFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGL----KDKADAYPSTLSGGQKQRVAI 157
Cdd:PRK14271 99 FRR---RVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1032718621 158 ARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQgKGILVVTHD 205
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHN 221
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-205 |
2.77e-31 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 117.44 E-value: 2.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MA-LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvqySDK 79
Cdd:PRK11000 1 MAsVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM----------NDV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 80 TSQRRyqnAIGMVFQNYQLFPNFTVLDN---------VLEAPIAQKLAPKSELLDQAMFLldsvglkdkaDAYPSTLSGG 150
Cdd:PRK11000 71 PPAER---GVGMVFQSYALYPHLSVAENmsfglklagAKKEEINQRVNQVAEVLQLAHLL----------DRKPKALSGG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1032718621 151 QKQRVAIARAMMLSPEIICFDEPTSALDreSANQVGKLVQaIAKQ----GKGILVVTHD 205
Cdd:PRK11000 138 QRQRVAIGRTLVAEPSVFLLDEPLSNLD--AALRVQMRIE-ISRLhkrlGRTMIYVTHD 193
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-204 |
3.83e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 113.97 E-value: 3.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlcqetsqgvqysDKT 80
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE-------------DIT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNA---IGMVFQNYQLFPNFTVLDN---VLEapiAQKLaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQR 154
Cdd:COG1137 69 HLPMHKRArlgIGYLPQEASIFRKLTVEDNilaVLE---LRKL-SKKEREERLEELLEEFGITHLRKSKAYSLSGGERRR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1032718621 155 VAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDH 194
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-204 |
8.77e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 118.34 E-value: 8.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 11 AYNGN-MVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGdrvlcqetsqGVQYSDkTSQRRYQNAI 89
Cdd:COG1132 348 SYPGDrPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID----------GVDIRD-LTLESLRRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 90 GMVFQNYQLFpNFTVLDNVLeapIAQKLAPKSELLdQAmflLDSVGLKDKADAYP-----------STLSGGQKQRVAIA 158
Cdd:COG1132 417 GVVPQDTFLF-SGTIRENIR---YGRPDATDEEVE-EA---AKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1032718621 159 RAMMLSPEIICFDEPTSALDRESAnqvgKLVQ-AIAK--QGKGILVVTH 204
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETE----ALIQeALERlmKGRTTIVIAH 533
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-205 |
9.51e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.02 E-value: 9.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYN-GNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqeTSQGVQYsDKTS 81
Cdd:PRK13639 2 LETRDLKYSYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI--------KGEPIKY-DKKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 QRRYQNAIGMVFQNY--QLFPNfTVLDNVLEAPIAQKLaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIAR 159
Cdd:PRK13639 73 LLEVRKTVGIVFQNPddQLFAP-TVEEDVAFGPLNLGL-SKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1032718621 160 AMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD 196
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-204 |
1.35e-30 |
|
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: 111.93 E-value: 1.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIaigdrvlcqeTSQGVQYSDKTSQRR 84
Cdd:cd03268 3 TNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI----------TFDGKSYQKNIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 YqnaIGMVFQNYQLFPNFTVLDNvLEAPIAQKLAPKSElldqAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLS 164
Cdd:cd03268 73 R---IGALIEAPGFYPNLTAREN-LRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1032718621 165 PEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSH 184
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
13-205 |
1.60e-30 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 111.36 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 13 NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvQYsDKTSQRRYQNAIGMV 92
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL--------DY-SRKGLLERRQRVGLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 93 FQN--YQLFPNfTVLDNVLEAPIAQKLAPK--SELLDQAMFLLDSVGLKDKAdayPSTLSGGQKQRVAIARAMMLSPEII 168
Cdd:TIGR01166 74 FQDpdDQLFAA-DVDQDVAFGPLNLGLSEAevERRVREALTAVGASGLRERP---THCLSGGEKKRVAIAGAVAMRPDVL 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 1032718621 169 CFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:TIGR01166 150 LLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTHD 186
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-217 |
1.81e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 113.29 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALI--VSNLKKAY-NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQGVQys 77
Cdd:PRK13647 1 MDNIieVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 78 dktsqrryqNAIGMVFQNY--QLFPNfTVLDNVLEAPIAQKLAPKsELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRV 155
Cdd:PRK13647 79 ---------SKVGLVFQDPddQVFSS-TVWDDVAFGPVNMGLDKD-EVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 156 AIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVI 209
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-205 |
2.48e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 112.78 E-value: 2.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNG--NMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKTsQ 82
Cdd:PRK13632 10 VENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI----------DGITISKEN-L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNyqlfPNFTVLDNVLEAPIA----QKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIA 158
Cdd:PRK13632 79 KEIRKKIGIIFQN----PDNQFIGATVEDDIAfgleNKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1032718621 159 RAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQG-KGILVVTHD 205
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHD 202
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
30-204 |
4.83e-30 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 113.82 E-value: 4.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 30 IVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCqETSQGVQYSdkTSQRRyqnaIGMVFQNYQLFPNFTVLDNvL 109
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF-DAEKGICLP--PEKRR----IGYVFQDARLFPHYKVRGN-L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 110 EAPIAQKLApksELLDQAMFLLdsvGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALD----RESANQV 185
Cdd:PRK11144 98 RYGMAKSMV---AQFDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlprkRELLPYL 171
|
170
....*....|....*....
gi 1032718621 186 GKLVQAIAKQgkgILVVTH 204
Cdd:PRK11144 172 ERLAREINIP---ILYVSH 187
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-204 |
6.73e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 111.47 E-value: 6.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSqgvqYSDKTS 81
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNI----YSPDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 QRRYQNAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLA-PKSELLDQAMFLLDSVGL----KDKADAYPSTLSGGQKQRVA 156
Cdd:PRK14267 80 PIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1032718621 157 IARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIaKQGKGILVVTH 204
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTH 206
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
12-204 |
7.19e-30 |
|
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: 110.94 E-value: 7.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 12 YNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLIN-NLEKCDQGNIAIGDRVLCQETSQGVqysdktsqRRYqnaIG 90
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgDLPPTYGNDVRLFGERRGGEDVWEL--------RKR---IG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 91 MV----FQNYQlfPNFTVLDNVLEAPIA-----QKlaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAM 161
Cdd:COG1119 82 LVspalQLRFP--RDETVLDVVLSGFFDsiglyRE--PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1032718621 162 MLSPEIICFDEPTSALDRESANQVGKLVQAIAKQG-KGILVVTH 204
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTH 201
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-207 |
1.45e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 110.25 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLIN-----NLEKCDQGNIAIGDRVLcqetsqgvqYS 77
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmndlNPEVTITGSIVYNGHNI---------YS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 78 DKTSQRRYQNAIGMVFQNYQLFPnFTVLDNVLEAPIAQKLAPKsELLDQAM-------FLLDSVglKDKADAYPSTLSGG 150
Cdd:PRK14239 77 PRTDTVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDK-QVLDEAVekslkgaSIWDEV--KDRLHDSALGLSGG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1032718621 151 QKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIaKQGKGILVVTHDTQ 207
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQ 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-205 |
1.49e-29 |
|
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: 109.86 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 18 IDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKTSQRRyqnaigMVFQNYQ 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL----------EGKQITEPGPDRM------VVFQNYS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 98 LFPNFTVLDNV-LEAPIAQKLAPKSE---LLDQAmflLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEP 173
Cdd:TIGR01184 65 LLPWLTVRENIaLAVDRVLPDLSKSErraIVEEH---IALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190
....*....|....*....|....*....|....*
gi 1032718621 174 TSALD---RESANQvgKLVQAIAKQGKGILVVTHD 205
Cdd:TIGR01184 142 FGALDaltRGNLQE--ELMQIWEEHRVTVLMVTHD 174
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-217 |
1.67e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 110.55 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALI-VSNLKKAYNG---------NMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQet 70
Cdd:PRK10419 1 MTLLnVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 71 sqgvqySDKTSQRRYQNAIGMVFQNY--QLFPNFTVLDNVLEaPIAQKLA-PKSELLDQAMFLLDSVGLKDK-ADAYPST 146
Cdd:PRK10419 79 ------LNRAQRKAFRRDIQMVFQDSisAVNPRKTVREIIRE-PLRHLLSlDKAERLARASEMLRAVDLDDSvLDKRPPQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 147 LSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHDTQFGEDFGTRIV 217
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVM 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-204 |
1.92e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 114.35 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKT 80
Cdd:COG3845 4 PALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI----------DGKPVRIRS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNAIGMVFQNYQLFPNFTVLDNV---LEaPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAI 157
Cdd:COG3845 74 PRDAIALGIGMVHQHFMLVPNLTVAENIvlgLE-PTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1032718621 158 ARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITH 199
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-218 |
3.34e-29 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 109.72 E-value: 3.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQgniAIGDRVlcQETSQGVQYSDKTSQ-- 82
Cdd:PRK09984 7 VEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDK---SAGSHI--ELLGRTVQREGRLARdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPNFTVLDNVLEAPIAQK---------LAPKSEllDQAMFLLDSVGLKDKADAYPSTLSGGQKQ 153
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENVLIGALGSTpfwrtcfswFTREQK--QRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032718621 154 RVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIaKQGKGILVVT--HDTQFGEDFGTRIVS 218
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDI-NQNDGITVVVtlHQVDYALRYCERIVA 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-217 |
3.74e-29 |
|
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: 108.35 E-value: 3.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 21 FNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGdrvlcqetsqGVQYSDKTSQRRyqnAIGMVFQNYQLFP 100
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN----------GVDVTAAPPADR---PVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 101 NFTVLDNV-LEAPIAQKLAPKSElldQAM-FLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALD 178
Cdd:cd03298 84 HLTVEQNVgLGLSPGLKLTAEDR---QAIeVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1032718621 179 RESANQVGKLVQAI-AKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:cd03298 161 PALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVV 200
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
25-204 |
4.27e-29 |
|
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: 107.64 E-value: 4.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 25 IDPGEIVILLGPSGTGKTTFMRLINNLEKC--DQGNIAIGDRvlcqetsqgvqysdKTSQRRYQNAIGMVFQNYQLFPNF 102
Cdd:cd03213 32 AKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGR--------------PLDKRSFRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 103 TVLDNVleapiaqklapkselldqaMFlldSVGLKdkadaypsTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESA 182
Cdd:cd03213 98 TVRETL-------------------MF---AAKLR--------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180
....*....|....*....|..
gi 1032718621 183 NQVGKLVQAIAKQGKGILVVTH 204
Cdd:cd03213 148 LQVMSLLRRLADTGRTIICSIH 169
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-205 |
5.52e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 109.72 E-value: 5.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 25 IDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQGVqysdktsqRRyqnAIGMVFQN--YQlFPNF 102
Cdd:PRK13635 30 VYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV--------RR---QVGMVFQNpdNQ-FVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 103 TVLDNV---LEapiaQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDR 179
Cdd:PRK13635 98 TVQDDVafgLE----NIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDP 173
|
170 180
....*....|....*....|....*...
gi 1032718621 180 ESANQVGKLVQAIAKQGkGILV--VTHD 205
Cdd:PRK13635 174 RGRREVLETVRQLKEQK-GITVlsITHD 200
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
3-207 |
8.52e-29 |
|
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: 108.13 E-value: 8.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvqySDKTSQ 82
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI----------THLPMH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMM 162
Cdd:TIGR04406 72 ERARLGIGYLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1032718621 163 LSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQ 207
Cdd:TIGR04406 152 TNPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVR 196
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-222 |
8.89e-29 |
|
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: 107.52 E-value: 8.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 17 VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLI--NNLekCDQGNIAI---GDRV-LCQETSQGVqysdkTSQRRyqNAIG 90
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYL--PDSGSILVrhdGGWVdLAQASPREI-----LALRR--RTIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 91 MVFQNYQLFPNFTVLDNVLEAPIAQKlAPKSELLDQAMFLLDSVGLKDK-ADAYPSTLSGGQKQRVAIARAMMLSPEIIC 169
Cdd:COG4778 97 YVSQFLRVIPRVSALDVVAEPLLERG-VDREEARARARELLARLNLPERlWDLPPATFSGGEQQRVNIARGFIADPPLLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1032718621 170 FDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIVSSEEF 222
Cdd:COG4778 176 LDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-204 |
1.26e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 109.92 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIaigdrvlcqeTSQGVQYSDKT 80
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI----------TVLGVPVPARA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 sqRRYQNAIGMVFQNYQLFPNFTVLDNVLeaPIAQKLAPKSELLDQAM-FLLDSVGLKDKADAYPSTLSGGQKQRVAIAR 159
Cdd:PRK13536 110 --RLARARIGVVPQFDNLDLEFTVRENLL--VFGRYFGMSTREIEAVIpSLLEFARLESKADARVSDLSGGMKRRLTLAR 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1032718621 160 AMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:PRK13536 186 ALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 |
1.31e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 107.90 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlcqetsqgvqysDKT 80
Cdd:COG4674 9 PILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGT-------------DLT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNA---IGMVFQNYQLFPNFTVLDNvLEapIAQKLA----------PKSELLDQAMFLLDSVGLKDKADAYPSTL 147
Cdd:COG4674 76 GLDEHEIArlgIGRKFQKPTVFEELTVFEN-LE--LALKGDrgvfaslfarLTAEERDRIEEVLETIGLTDKADRLAGLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032718621 148 SGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQgKGILVVTHDTQFGEDFGTRI 216
Cdd:COG4674 153 SHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGK-HSVVVVEHDMEFVRQIARKV 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-205 |
1.42e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.94 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQgvqysdKT 80
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPA------EL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRyqnaiGMVFQNYQL-FPnFTVLDnVLE---APIAQKLAPKSELLDQAMFLLDSVGLKDKadAYPsTLSGGQKQRVA 156
Cdd:PRK13548 75 ARRR-----AVLPQHSSLsFP-FTVEE-VVAmgrAPHGLSRAEDDALVAAALAQVDLAHLAGR--DYP-QLSGGEQQRVQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1032718621 157 IARAMM-LS-----PEIICFDEPTSALDreSANQ--VGKLVQAIA-KQGKGILVVTHD 205
Cdd:PRK13548 145 LARVLAqLWepdgpPRWLLLDEPTSALD--LAHQhhVLRLARQLAhERGLAVIVVLHD 200
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-204 |
1.50e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 109.12 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAigdrvLCQETSQGvqysdktS 81
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIS-----LCGEPVPS-------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 QRRYQNAIGMVFQNYQLFPNFTVLDNV--------LEAPIAQKLAPKselldqamfLLDSVGLKDKADAYPSTLSGGQKQ 153
Cdd:PRK13537 75 ARHARQRVGVVPQFDNLDPDFTVRENLlvfgryfgLSAAAARALVPP---------LLEFAKLENKADAKVGELSGGMKR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1032718621 154 RVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-217 |
2.26e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.31 E-value: 2.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVlcqetsqgvqysdktsq 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV----------------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 rryqnAIGMVFQNY-QLFPNFTVLDNVLE-APIAQKLAPKSELldqAMFLLDSvglkDKADAYPSTLSGGQKQRVAIARA 160
Cdd:COG0488 379 -----KIGYFDQHQeELDPDKTVLDELRDgAPGGTEQEVRGYL---GRFLFSG----DDAFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1032718621 161 MMLSPEIICFDEPTSALDRESANQvgkLVQAIAK-QGkGILVVTHDTQFGEDFGTRIV 217
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEA---LEEALDDfPG-TVLLVSHDRYFLDRVATRIL 500
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-204 |
2.36e-28 |
|
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: 104.82 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGdrvlcqetsqGVQYSDKTSQRR 84
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD----------GKEVSFASPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 YQNAIGMVFQnyqlfpnftvldnvleapiaqklapkselldqamflldsvglkdkadaypstLSGGQKQRVAIARAMMLS 164
Cdd:cd03216 73 RRAGIAMVYQ----------------------------------------------------LSVGERQMVEIARALARN 100
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1032718621 165 PEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:cd03216 101 ARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISH 140
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-203 |
4.50e-28 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 111.20 E-value: 4.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAY--NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsQGVqysDK 79
Cdd:TIGR03797 451 AIEVDRVTFRYrpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDL-----AGL---DV 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 80 TSQRRyqnAIGMVFQNYQLFPNfTVLDNVLEApiaqklAPKSelLDQAMFLLDSVGLKDKADAYP-----------STLS 148
Cdd:TIGR03797 523 QAVRR---QLGVVLQNGRLMSG-SIFENIAGG------APLT--LDEAWEAARMAGLAEDIRAMPmgmhtviseggGTLS 590
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 149 GGQKQRVAIARAMMLSPEIICFDEPTSALDRESanqvgklvQAIAKQGKGILVVT 203
Cdd:TIGR03797 591 GGQRQRLLIARALVRKPRILLFDEATSALDNRT--------QAIVSESLERLKVT 637
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-204 |
1.14e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.38 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNL-EKCDQGNIAiGDRVLcqeTSQGVQYSDKTS 81
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLiELYPEARVS-GEVYL---DGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 QRRyqnAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLA-PKSELLDQAMFLLDSVGL----KDKADAYPSTLSGGQKQRVA 156
Cdd:PRK14247 80 LRR---RVQMVFQIPNPIPNLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLC 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1032718621 157 IARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQgKGILVVTH 204
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTH 203
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-217 |
1.25e-27 |
|
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: 104.28 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlcqetsqGVQYSDKtsq 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK--------PLDIAAR--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 rryqNAIGMVFQNYQLFPNFTVLDNVLEapIAQ-KLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAM 161
Cdd:cd03269 70 ----NRIGYLPEERGLYPKMKVIDQLVY--LAQlKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1032718621 162 MLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVL 199
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-204 |
1.40e-27 |
|
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: 104.62 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYN-GNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDrvlcqetsQGVQYSDKTS 81
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG--------QDIREVTLDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 QRRyqnAIGMVFQNYQLFpNFTVLDN------------VLEAPIAQKLAPKSELLDQAMfllDSV----GLKdkadayps 145
Cdd:cd03253 73 LRR---AIGVVPQDTVLF-NDTIGYNirygrpdatdeeVIEAAKAAQIHDKIMRFPDGY---DTIvgerGLK-------- 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1032718621 146 tLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKqGKGILVVTH 204
Cdd:cd03253 138 -LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAH 194
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-205 |
1.51e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.07 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 18 IDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQgvqysdkTSQRRYQNAIGMVFQ--N 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGN-------KNLKKLRKKVSLVFQfpE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 96 YQLFPNfTVLDNVLEAPIAQKLAPKsELLDQAMFLLDSVGLKDK-ADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPT 174
Cdd:PRK13641 96 AQLFEN-TVLKDVEFGPKNFGFSED-EAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190
....*....|....*....|....*....|.
gi 1032718621 175 SALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHN 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-217 |
1.60e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.00 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetSQGVQysdktsqrr 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLR--------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 yqnaIGMVFQNYQLFPNFTVLDNVLEA--PIAQKLAPKSELLD---------------QAMF--------------LLDS 133
Cdd:COG0488 63 ----IGYLPQEPPLDDDLTVLDTVLDGdaELRALEAELEELEAklaepdedlerlaelQEEFealggweaearaeeILSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 134 VGLK-DKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESanqVGKLVQAIAKQGKGILVVTHDTQFGEDF 212
Cdd:COG0488 139 LGFPeEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEWLEEFLKNYPGTVLVVSHDRYFLDRV 215
|
....*
gi 1032718621 213 GTRIV 217
Cdd:COG0488 216 ATRIL 220
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-207 |
1.72e-27 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 104.48 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 25 IDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIaigdRVLCQETSQgvQYSDKTSQRRYQNaIGMVFQNYQLFPNFTV 104
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEV----SLVGQPLHQ--MDEEARAKLRAKH-VGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 105 LDNVlEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQ 184
Cdd:PRK10584 106 LENV-ELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180
....*....|....*....|....
gi 1032718621 185 VGKLVQAIAK-QGKGILVVTHDTQ 207
Cdd:PRK10584 185 IADLLFSLNReHGTTLILVTHDLQ 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
24-205 |
1.86e-27 |
|
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: 109.00 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 24 RIDPGEIVILLGPSGTGKTTFMRLINNLEKCdQGNIAIGDrvlcqetsQGVQYSDKTSQRRYQNAIGMVFQN-YQ-LFPN 101
Cdd:COG4172 308 TLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDG--------QDLDGLSRRALRPLRRRMQVVFQDpFGsLSPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 102 FTVLDNVLEAPIAQKLAP-KSELLDQAMFLLDSVGLK-DKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDR 179
Cdd:COG4172 379 MTVGQIIAEGLRVHGPGLsAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDV 458
|
170 180
....*....|....*....|....*..
gi 1032718621 180 ESANQVGKLVQAI-AKQGKGILVVTHD 205
Cdd:COG4172 459 SVQAQILDLLRDLqREHGLAYLFISHD 485
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-217 |
3.61e-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: 103.22 E-value: 3.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGN----MVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAI-GDRVLcqetsqgvqys 77
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdGFDVV----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 78 dkTSQRRYQNAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLAPKsELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAI 157
Cdd:cd03266 71 --KEPAEARRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGD-ELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 158 ARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVV 207
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-205 |
5.20e-27 |
|
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: 103.01 E-value: 5.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 24 RIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlcqetsqgvqysdktSQRRYQNAIGMVFQNYQL---FP 100
Cdd:TIGR03771 2 SADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA----------------SPGKGWRHIGYVPQRHEFawdFP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 101 nFTVLDNVLEAPiAQKLAP--KSELLDQAMF--LLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSA 176
Cdd:TIGR03771 66 -ISVAHTVMSGR-TGHIGWlrRPCVADFAAVrdALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTG 143
|
170 180
....*....|....*....|....*....
gi 1032718621 177 LDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:TIGR03771 144 LDMPTQELLTELFIELAGAGTAILMTTHD 172
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
14-204 |
5.22e-27 |
|
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: 103.39 E-value: 5.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 14 GNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSqgvqysdktsqRRYQNAIGMVF 93
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNL-----------RWLRSQIGLVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 94 QNYQLFPNfTVLDNVL------EAPIAQKLAPKSELLDqamFLldsVGLKDKAD----AYPSTLSGGQKQRVAIARAMML 163
Cdd:cd03249 84 QEPVLFDG-TIAENIRygkpdaTDEEVEEAAKKANIHD---FI---MSLPDGYDtlvgERGSQLSGGQKQRIAIARALLR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1032718621 164 SPEIICFDEPTSALDRESAnqvgKLVQ-AI--AKQGKGILVVTH 204
Cdd:cd03249 157 NPKILLLDEATSALDAESE----KLVQeALdrAMKGRTTIVIAH 196
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-207 |
6.30e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 103.43 E-value: 6.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MA-LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvqySDK 79
Cdd:PRK10895 1 MAtLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI----------SLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 80 TSQRRYQNAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIAR 159
Cdd:PRK10895 71 PLHARARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1032718621 160 AMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQ 207
Cdd:PRK10895 151 ALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVR 198
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-202 |
7.11e-27 |
|
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: 102.75 E-value: 7.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvqySDKT 80
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI----------TGLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNAIGMVFQNYQLFPNFTVLDNvLE--APIAQKLAPKSELLDQ--AMFLLdsvgLKDKADAYPSTLSGGQKQRVA 156
Cdd:COG0410 72 PHRIARLGIGYVPEGRRIFPSLTVEEN-LLlgAYARRDRAEVRADLERvyELFPR----LKERRRQRAGTLSGGEQQMLA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1032718621 157 IARAMMLSPEIICFDEPTSALdresA----NQVGKLVQAIAKQGKGILVV 202
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGL----AplivEEIFEIIRRLNREGVTILLV 192
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-216 |
7.80e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 105.89 E-value: 7.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 25 IDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqETSQGVQYSDKTSQRRYQNAIGMVFQNYQLFPNFTV 104
Cdd:PRK10070 51 IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI-------DGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 105 LDNVleaPIAQKLA--PKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESA 182
Cdd:PRK10070 124 LDNT---AFGMELAgiNAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190
....*....|....*....|....*....|....*
gi 1032718621 183 NQV-GKLVQAIAKQGKGILVVTHDTQFGEDFGTRI 216
Cdd:PRK10070 201 TEMqDELVKLQAKHQRTIVFISHDLDEAMRIGDRI 235
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-205 |
1.56e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 102.50 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQgvqysdKTSQ 82
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPW------ELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRyqnaiGMVFQNYQL-FPnFTVLDNVL--EAPIAQKLAPKSELLDQAMFLLDSVGLKDKAdaYPsTLSGGQKQRVAIAR 159
Cdd:COG4559 76 RR-----AVLPQHSSLaFP-FTVEEVVAlgRAPHGSSAAQDRQIVREALALVGLAHLAGRS--YQ-TLSGGEQQRVQLAR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1032718621 160 AM-------MLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:COG4559 147 VLaqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHD 199
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
24-178 |
2.46e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 103.51 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 24 RIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDrvlcqetsQGVQYSDKTSQRRYQNAIGMVFQN-Y-QLFPN 101
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQG--------QDLLKADPEAQKLLRQKIQIVFQNpYgSLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 102 FTVLDnVLEAP--IAQKLApKSELLDQAMFLLDSVGLK-DKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALD 178
Cdd:PRK11308 109 KKVGQ-ILEEPllINTSLS-AAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
20-204 |
2.98e-26 |
|
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: 100.71 E-value: 2.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 20 QFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlcqetsqgvqysDKTSQRRYQNAIGMVFQNYQLF 99
Cdd:TIGR01277 16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ-------------SHTGLAPYQRPVSMLFQENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 100 PNFTVLDNvleapIAQKLAPKSEL----LDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTS 175
Cdd:TIGR01277 83 AHLTVRQN-----IGLGLHPGLKLnaeqQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFS 157
|
170 180 190
....*....|....*....|....*....|
gi 1032718621 176 ALDRESANQVGKLVQAIAKQGK-GILVVTH 204
Cdd:TIGR01277 158 ALDPLLREEMLALVKQLCSERQrTLLMVTH 187
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
5-205 |
3.11e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 102.12 E-value: 3.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNM---VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETsqgvqysdkTS 81
Cdd:PRK13650 7 VKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEN---------VW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 QRRYQnaIGMVFQNY-QLFPNFTVLDNV---LEapiaQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAI 157
Cdd:PRK13650 78 DIRHK--IGMVFQNPdNQFVGATVEDDVafgLE----NKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1032718621 158 ARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHD 200
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-217 |
3.80e-26 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 105.27 E-value: 3.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFM--------------RLINNLEKCDQ-GNIAIGDRV---- 65
Cdd:TIGR03269 3 VKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMhvlrgmdqyeptsgRIIYHVALCEKcGYVERPSKVgepc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 66 -LCQET--SQGVQY--SDKTSQRRYQNAIGMVFQ-NYQLFPNFTVLDNVLEApIAQKLAPKSELLDQAMFLLDSVGLKDK 139
Cdd:TIGR03269 83 pVCGGTlePEEVDFwnLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEA-LEEIGYEGKEAVGRAVDLIEMVQLSHR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032718621 140 ADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVT-HDTQFGEDFGTRIV 217
Cdd:TIGR03269 162 ITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTsHWPEVIEDLSDKAI 240
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-205 |
4.87e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 102.11 E-value: 4.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKTS 81
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW----------DGEPLDPEDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 QRryqnaIGmvfqnYQ-----LFPNFTVLDNVLEapIAQ-KLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRV 155
Cdd:COG4152 71 RR-----IG-----YLpeergLYPKMKVGEQLVY--LARlKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1032718621 156 AIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQ 188
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-204 |
5.62e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 101.66 E-value: 5.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNM-----VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqeTSQGVQ 75
Cdd:PRK13637 1 MSIKIENLTHIYMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI---TDKKVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 76 YSDKTSQrryqnaIGMVFQ--NYQLFPNfTVLDNVLEAPIAQKLApKSELLDQAMFLLDSVGLK--DKADAYPSTLSGGQ 151
Cdd:PRK13637 78 LSDIRKK------VGLVFQypEYQLFEE-TIEKDIAFGPINLGLS-EEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1032718621 152 KQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGK-GILVVTH 204
Cdd:PRK13637 150 KRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSH 203
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-204 |
6.36e-26 |
|
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: 100.38 E-value: 6.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 14 GNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDrvlcqetsQGVQYSDKTSQRRYqnaIGMVF 93
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG--------HDVRDYTLASLRRQ---IGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 94 QNYQLFpNFTVLDNVL---------EAPIAQKLAPKSELLDQAMFLLDSV----GLKdkadaypstLSGGQKQRVAIARA 160
Cdd:cd03251 83 QDVFLF-NDTVAENIAygrpgatreEVEEAARAANAHEFIMELPEGYDTVigerGVK---------LSGGQRQRIAIARA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1032718621 161 MMLSPEIICFDEPTSALDRESAnqvgKLVQ-AIAK--QGKGILVVTH 204
Cdd:cd03251 153 LLKDPPILILDEATSALDTESE----RLVQaALERlmKNRTTFVIAH 195
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-205 |
2.16e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 99.68 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQGVQysdktsq 82
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRyqnaiGMV--FQNYQLFPNFTVLDNVLeapIAQKLAPKS-----------------ELLDQAMFLLDSVGLKDKADAY 143
Cdd:PRK11300 79 RM-----GVVrtFQHVRLFREMTVIENLL---VAQHQQLKTglfsgllktpafrraesEALDRAATWLERVGLLEHANRQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032718621 144 PSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:PRK11300 151 AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHD 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-204 |
2.35e-25 |
|
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: 97.29 E-value: 2.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNM--VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGdrvlCQETSQgvqysdkT 80
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD----GADISQ-------W 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNAIGMVFQNYQLFPNfTVLDNVLeapiaqklapkselldqamflldsvglkdkadaypstlSGGQKQRVAIARA 160
Cdd:cd03246 70 DPNELGDHVGYLPQDDELFSG-SIAENIL--------------------------------------SGGQRQRLGLARA 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1032718621 161 MMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:cd03246 111 LYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAH 154
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-204 |
3.13e-25 |
|
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: 98.71 E-value: 3.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 13 NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGniaigdRVLCQETSQGVqySDKTSQRRyqnAIGMV 92
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENG------RVLVDGHDLAL--ADPAWLRR---QVGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 93 FQNYQLFpNFTVLDNVL---EAPIAQKLAPKSELLDQAMFLLD-SVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEII 168
Cdd:cd03252 82 LQENVLF-NRSIRDNIAladPGMSMERVIEAAKLAGAHDFISElPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1032718621 169 CFDEPTSALDRESANQVGKLVQAIAKqGKGILVVTH 204
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAH 195
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-205 |
3.44e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 99.45 E-value: 3.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 14 GNMVI-DQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAI-GDRVLCQETSQGVQYSDKTSqrryqnaigM 91
Cdd:PRK11831 18 GNRCIfDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENIPAMSRSRLYTVRKRMS---------M 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 92 VFQNYQLFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFD 171
Cdd:PRK11831 89 LFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFD 168
|
170 180 190
....*....|....*....|....*....|....*
gi 1032718621 172 EPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:PRK11831 169 EPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHD 203
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-178 |
4.17e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 98.76 E-value: 4.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALI-VSNLKKAYNGNM---------VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqet 70
Cdd:COG4167 2 SALLeVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 71 sqgvQYSDktSQRRYQNaIGMVFQ--NYQLFPNFTVlDNVLEAPIaqKLAPK---SELLDQAMFLLDSVGL-KDKADAYP 144
Cdd:COG4167 78 ----EYGD--YKYRCKH-IRMIFQdpNTSLNPRLNI-GQILEEPL--RLNTDltaEEREERIFATLRLVGLlPEHANFYP 147
|
170 180 190
....*....|....*....|....*....|....
gi 1032718621 145 STLSGGQKQRVAIARAMMLSPEIICFDEPTSALD 178
Cdd:COG4167 148 HMLSSGQKQRVALARALILQPKIIIADEALAALD 181
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-205 |
6.30e-25 |
|
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: 101.68 E-value: 6.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNM----VIDQFNCRIDPGEIVILLGPSGTGKT----TFMRLINNLEKCDQGNIAIGDRVLcqetsqgV 74
Cdd:COG4172 7 LSVEDLSVAFGQGGgtveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDL-------L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 75 QYSDKTSQRRYQNAIGMVFQ------NyqlfPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGLKD---KADAYPS 145
Cdd:COG4172 80 GLSERELRRIRGNRIAMIFQepmtslN----PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDperRLDAYPH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032718621 146 TLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAI-AKQGKGILVVTHD 205
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHD 216
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
11-208 |
7.57e-25 |
|
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: 97.28 E-value: 7.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 11 AYNG--NMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGdrvlcqetsqGVQYSDKTSQRRYQNa 88
Cdd:cd03245 11 SYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLD----------GTDIRQLDPADLRRN- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 89 IGMVFQNYQLFpNFTVLDNV-LEAPIAQKlapkSELLDQAMFLldsvGLKDKADAYP-----------STLSGGQKQRVA 156
Cdd:cd03245 80 IGYVPQDVTLF-YGTLRDNItLGAPLADD----ERILRAAELA----GVTDFVNKHPngldlqigergRGLSGGQRQAVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 157 IARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKqGKGILVVTHDTQF 208
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSL 201
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-205 |
8.59e-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: 101.28 E-value: 8.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNG-NMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQetsqgvqySDKTS 81
Cdd:TIGR02868 335 LELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSS--------LDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 QRRyqnAIGMVFQNYQLFPNfTVLDNVLeapIAQKLAPKSELLDqamfLLDSVGLKDKADAYP-----------STLSGG 150
Cdd:TIGR02868 407 VRR---RVSVCAQDAHLFDT-TVRENLR---LARPDATDEELWA----ALERVGLADWLRALPdgldtvlgeggARLSGG 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 151 QKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAiAKQGKGILVVTHD 205
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHH 529
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-204 |
1.11e-24 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 101.33 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 17 VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKTsQRRYQNAIGMVFQNY 96
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL----------DGHDLADYT-LASLRRQVALVSQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 97 QLFpNFTVLDNVLEAPIAQklAPKSELLD--QAMFLLDSV-----GLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIIC 169
Cdd:TIGR02203 416 VLF-NDTIANNIAYGRTEQ--ADRAEIERalAAAYAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILI 492
|
170 180 190
....*....|....*....|....*....|....*
gi 1032718621 170 FDEPTSALDRESANQVGKLVQAIaKQGKGILVVTH 204
Cdd:TIGR02203 493 LDEATSALDNESERLVQAALERL-MQGRTTLVIAH 526
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-208 |
1.47e-24 |
|
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: 100.65 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAY----NGNM-VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQG--NIAIGDrvlcqetsqgvQYS 77
Cdd:TIGR03269 282 VRNVSKRYisvdRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVGD-----------EWV 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 78 DKTSQR-----RYQNAIGMVFQNYQLFPNFTVLDNVLEApIAQKLaPKSELLDQAMFLLDSVGLKDKA-----DAYPSTL 147
Cdd:TIGR03269 351 DMTKPGpdgrgRAKRYIGILHQEYDLYPHRTVLDNLTEA-IGLEL-PDELARMKAVITLKMVGFDEEKaeeilDKYPDEL 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 148 SGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGK-LVQAIAKQGKGILVVTHDTQF 208
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDF 490
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-204 |
1.66e-24 |
|
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: 95.89 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQgvqysdktsq 82
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 rrYQNAIGMVFQNYQLFPNFTVLDNV-LEAPIaqkLAPKSELLDQAmflLDSVGLKDKADAYPSTLSGGQKQRVAIARAM 161
Cdd:TIGR01189 71 --PHENILYLGHLPGLKPELSALENLhFWAAI---HGGAQRTIEDA---LAAVGLTGFEDLPAAQLSAGQQRRLALARLW 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1032718621 162 MLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
20-204 |
1.67e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.57 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 20 QFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKTSQRRyqnAIGMVFQNYQLF 99
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTL----------NGQDHTTTPPSRR---PVSMLFQENNLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 100 PNFTVLDNvleapIAQKLAPKSELLDQAMFLLDS----VGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTS 175
Cdd:PRK10771 84 SHLTVAQN-----IGLGLNPGLKLNAAQREKLHAiarqMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190
....*....|....*....|....*....|
gi 1032718621 176 ALDRESANQVGKLVQAI-AKQGKGILVVTH 204
Cdd:PRK10771 159 ALDPALRQEMLTLVSQVcQERQLTLLMVSH 188
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-211 |
4.79e-24 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 95.03 E-value: 4.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 17 VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsqgvqysdktsqrryqnaigmVFQNY 96
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV------------------------------DVPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 97 QLFPNFTVLDNVleapiaqklaPKSELLDQAMFLLDSVGLkdkADAY-----PSTLSGGQKQRVAIARAMMLSPEIICFD 171
Cdd:COG2401 95 QFGREASLIDAI----------GRKGDFKDAVELLNAVGL---SDAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1032718621 172 EPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHDTQFGED 211
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKLARRaGITLVVATHHYDVIDD 202
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-217 |
5.41e-24 |
|
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: 95.28 E-value: 5.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKTSQ 82
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRL----------DGEDITKLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPNFTVLDNVLEApiAQKLAPKSELLDQAMFLLDSVgLKDKADAYPSTLSGGQKQRVAIARAMM 162
Cdd:TIGR03410 71 ERARAGIAYVPQGREIFPRLTVEENLLTG--LAALPRRSRKIPDEIYELFPV-LKEMLGRRGGDLSGGQQQQLAIARALV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1032718621 163 LSPEIICFDEPTSALDRESANQVGKLVQAIAKQGK-GILVVTHDTQFGEDFGTRIV 217
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYY 203
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-205 |
1.07e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.45 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 11 AYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAI--GDRV--LCQETSqgvqySDKTSQRRYQ 86
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRagGARVayVPQRSE-----VPDSLPLTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 87 NAIGM-VFQNYQLFPNFTVLDNVLeapiaqklapkselLDQAmflLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSP 165
Cdd:NF040873 76 DLVAMgRWARRGLWRRLTRDDRAA--------------VDDA---LERVGLADLAGRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1032718621 166 EIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHD 178
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-223 |
1.14e-23 |
|
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: 92.13 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVlcqetsqGVQYsdktsq 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-------KIGY------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 rryqnaigmvfqnyqlfpnftvldnvleapiaqklapkselLDQamflldsvglkdkadaypstLSGGQKQRVAIARAMM 162
Cdd:cd03221 68 -----------------------------------------FEQ--------------------LSGGEKMRLALAKLLL 86
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032718621 163 LSPEIICFDEPTSALDRESANQvgkLVQAIAKQGKGILVVTHDTQFGEDFGTRIVSSEEFK 223
Cdd:cd03221 87 ENPNLLLLDEPTNHLDLESIEA---LEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-207 |
1.23e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 95.23 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 7 NLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGdRVLCQETSQGVQYSDKTSQRRyq 86
Cdd:PRK14243 15 NLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEG-KVTFHGKNLYAPDVDPVEVRR-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 87 nAIGMVFQNYQLFPNfTVLDNVLEAP-IAQKLAPKSELLDQAM---FLLDSVglKDKADAYPSTLSGGQKQRVAIARAMM 162
Cdd:PRK14243 92 -RIGMVFQKPNPFPK-SIYDNIAYGArINGYKGDMDELVERSLrqaALWDEV--KDKLKQSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1032718621 163 LSPEIICFDEPTSALDRESANQVGKLVQAIAKQgKGILVVTHDTQ 207
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQ 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
17-205 |
1.84e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 94.87 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 17 VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNL---EKCDQGNIAIGDRVLCQETSQGVQysDKtsqrryqnaIGMVF 93
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWDIR--EK---------VGIVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 94 QNY-QLFPNFTVLDNV---LEapiaQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIIC 169
Cdd:PRK13640 91 QNPdNQFVGATVGDDVafgLE----NRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 1032718621 170 FDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHD 203
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-207 |
1.99e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 94.34 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAY---NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqETSQGVQYSDKTS 81
Cdd:PRK14246 10 VFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVL--YFGKDIFQIDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 QRRyqnAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGL----KDKADAYPSTLSGGQKQRVAI 157
Cdd:PRK14246 88 LRK---EVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1032718621 158 ARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQgKGILVVTHDTQ 207
Cdd:PRK14246 165 ARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQ 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
9-204 |
2.66e-23 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 93.49 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 9 KKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLekcDQGNIAIGDRVLCQetsqGVQYSDKTSQRRyqna 88
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR---VEGGGTTSGQILFN----GQPRKPDQFQKC---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 89 IGMVFQNYQLFPNFTVLDNVLEAPIAQKLAPKSELLDQAM---FLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSP 165
Cdd:cd03234 83 VAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRvedVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDP 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 1032718621 166 EIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
11-208 |
3.68e-23 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 96.86 E-value: 3.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 11 AYNGNM--VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQetsqgvqySDKTSQRRyqnA 88
Cdd:TIGR03375 472 AYPGQEtpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQ--------IDPADLRR---N 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 89 IGMVFQNYQLFpNFTVLDN-VLEAPiaqkLAPKSELLDQAMFlldsVGLKDKADAYPS-----------TLSGGQKQRVA 156
Cdd:TIGR03375 541 IGYVPQDPRLF-YGTLRDNiALGAP----YADDEEILRAAEL----AGVTEFVRRHPDgldmqigergrSLSGGQRQAVA 611
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 157 IARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAkQGKGILVVTHDTQF 208
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSL 662
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-205 |
4.34e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.56 E-value: 4.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCdQGNIAIGDRVlcQETSQGVqYSDKTS 81
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGRV--EFFNQNI-YERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 82 QRRYQNAIGMVFQNYQLFPnFTVLDNVLEAPIAQKLAPKSELLD------QAMFLLDSVglKDKADAYPSTLSGGQKQRV 155
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDivesalKDADLWDEI--KHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1032718621 156 AIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGK-GILVVTHD 205
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHN 210
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-204 |
6.37e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.01 E-value: 6.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 7 NLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKTSQRRYQ 86
Cdd:PRK09700 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI----------NNINYNKLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 87 NAIGMVFQNYQLFPNFTVLDNVLeapIAQKLAPK---------SELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAI 157
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENLY---IGRHLTKKvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1032718621 158 ARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-217 |
6.95e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.84 E-value: 6.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYN-G----NMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlcqetsqgvqys 77
Cdd:COG1101 2 LELKNLSKTFNpGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 78 DKTSQRRYQNA--IGMVFQNYQL--FPNFTVLDNVLeapIAQK--------LAPKSELLDQAMFLLDSV--GLKDKADAY 143
Cdd:COG1101 69 DVTKLPEYKRAkyIGRVFQDPMMgtAPSMTIEENLA---LAYRrgkrrglrRGLTKKRRELFRELLATLglGLENRLDTK 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 144 PSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKL-VQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:COG1101 146 VGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLI 220
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-205 |
1.73e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 93.23 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 18 IDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIA-IGDRVLCQETSQgvqysdktsQRRYQNAIGMVFQN- 95
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLGMKDDE---------WRAVRSDIQMIFQDp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 96 -YQLFPNFTVLDnvleaPIAQKLA------PKSELLDQAMFLLDSVGL-KDKADAYPSTLSGGQKQRVAIARAMMLSPEI 167
Cdd:PRK15079 108 lASLNPRMTIGE-----IIAEPLRtyhpklSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKL 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 1032718621 168 ICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:PRK15079 183 IICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHD 221
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-204 |
3.84e-22 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 90.36 E-value: 3.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 13 NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGdrvlcqetsqGVQYSDkTSQRRYQNAIGMV 92
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILID----------GIDIRD-ISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 93 FQNYQLFPNfTVLDNV-LEAPIAQ-----KLAPKSELLDQAMFLLDsvGLKDKADAYPSTLSGGQKQRVAIARAMMLSPE 166
Cdd:cd03254 83 LQDTFLFSG-TIMENIrLGRPNATdeeviEAAKEAGAHDFIMKLPN--GYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1032718621 167 IICFDEPTSALDRESAnqvgKLVQ-AIAK--QGKGILVVTH 204
Cdd:cd03254 160 ILILDEATSNIDTETE----KLIQeALEKlmKGRTSIIIAH 196
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-204 |
4.00e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 91.72 E-value: 4.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 25 IDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqeTSQGVQYSDKTSQRRyqnaIGMVFQ--NYQLFPNf 102
Cdd:PRK13643 29 VKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVV---SSTSKQKEIKPVRKK----VGVVFQfpESQLFEE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 103 TVLDNVLEAPIAQKLApKSELLDQAMFLLDSVGL-KDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRES 181
Cdd:PRK13643 101 TVLKDVAFGPQNFGIP-KEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180
....*....|....*....|...
gi 1032718621 182 ANQVGKLVQAIAKQGKGILVVTH 204
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTH 202
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-204 |
4.55e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.55 E-value: 4.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDrvlcqetsQGVQYSDKT 80
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG--------GDIDDPDVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRY---QNAigmvfqnyqLFPNFTVLDNVleAPIAQKLAPKSELLDQAmflLDSVGLKDKADAYPSTLSGGQKQRVAI 157
Cdd:PRK13539 73 EACHYlghRNA---------MKPALTVAENL--EFWAAFLGGEELDIAAA---LEAVGLAPLAHLPFGYLSAGQKRRVAL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1032718621 158 ARaMMLSPEII-CFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:PRK13539 139 AR-LLVSNRPIwILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
17-204 |
8.77e-22 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 92.84 E-value: 8.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 17 VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQetsqgvqysdkTSQRRYQNAIGMVFQNY 96
Cdd:TIGR02204 355 ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQ-----------LDPAELRARMALVPQDP 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 97 QLFPNfTVLDNVL---------EAPIAQKLAPKSELLDQamflldsvgLKDKADAYPS----TLSGGQKQRVAIARAMML 163
Cdd:TIGR02204 424 VLFAA-SVMENIRygrpdatdeEVEAAARAAHAHEFISA---------LPEGYDTYLGergvTLSGGQRQRIAIARAILK 493
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1032718621 164 SPEIICFDEPTSALDRESANQVGKLVQAIAKqGKGILVVTH 204
Cdd:TIGR02204 494 DAPILLLDEATSALDAESEQLVQQALETLMK-GRTTLIIAH 533
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-205 |
1.28e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 91.83 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvqysDKT 80
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV-----------EAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNAIGMVFQNYQLFPNFTVlDNVLE---APIAQKLAPKSE----LLDQAMfllDSVGLKDKADAYPSTLSGGQKQ 153
Cdd:PRK09536 71 SARAASRRVASVPQDTSLSFEFDV-RQVVEmgrTPHRSRFDTWTEtdraAVERAM---ERTGVAQFADRPVTSLSGGERQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 154 RVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHD 198
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
27-207 |
1.90e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.69 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 27 PGEIVILLGPSGTGKTT----FMRLINNlekcdQGNIAIGDRVLCQETsqgvqysdktsqRR----YQNAIGMVFQ--NY 96
Cdd:PRK15134 311 PGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLN------------RRqllpVRHRIQVVFQdpNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 97 QLFPNFTVLDNVLEA-PIAQKLAPKSELLDQAMFLLDSVGLK-DKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPT 174
Cdd:PRK15134 374 SLNPRLNVLQIIEEGlRVHQPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190
....*....|....*....|....*....|....
gi 1032718621 175 SALDRESANQVGKLVQAI-AKQGKGILVVTHDTQ 207
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLqQKHQLAYLFISHDLH 487
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3-204 |
2.55e-21 |
|
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: 87.55 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGniaigdRVLCQETSQGVQYSDKTSQ 82
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAG------RVLLNGGPLDFQRDSIARG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRY---QNAIG---MVFQNYQLFPNFTVLDNVLEApiaqklapkselldqamflLDSVGLKDKADAYPSTLSGGQKQRVA 156
Cdd:cd03231 75 LLYlghAPGIKttlSVLENLRFWHADHSDEQVEEA-------------------LARVGLNGFEDRPVAQLSAGQQRRVA 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1032718621 157 IARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:cd03231 136 LARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-204 |
2.59e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 89.31 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 22 NCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQgvqysdkTSQRRYQNAIGMVFQ--NYQLF 99
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKN-------KKLKPLRKKVGIVFQfpEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 100 PNfTVLDNVLEAPIAQKlAPKSELLDQAMFLLDSVGL-KDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALD 178
Cdd:PRK13634 100 EE-TVEKDICFGPMNFG-VSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180
....*....|....*....|....*..
gi 1032718621 179 RESANQVGKLVQAIAK-QGKGILVVTH 204
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKeKGLTTVLVTH 204
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-204 |
4.27e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.61 E-value: 4.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 17 VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKTSQRRYQNAIGMVFQNy 96
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV----------DGLDTSDEENLWDIRNKAGMVFQN- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 97 qlfPNFTVLDNVLEAPIA---QKLA-PKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDE 172
Cdd:PRK13633 94 ---PDNQIVATIVEEDVAfgpENLGiPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190
....*....|....*....|....*....|...
gi 1032718621 173 PTSALDRESANQVGKLVQAIAKQ-GKGILVVTH 204
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKyGITIILITH 203
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
17-204 |
4.52e-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: 90.87 E-value: 4.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 17 VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQetsqgvqysdkTSQRRYQNAIGMVFQNY 96
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQ-----------WDRETFGKHIGYLPQDV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 97 QLFPNfTVLDNVL--------EAPI-AQKLAPKSELLdqamflldsVGLKDKADAY----PSTLSGGQKQRVAIARAMML 163
Cdd:TIGR01842 402 ELFPG-TVAENIArfgenadpEKIIeAAKLAGVHELI---------LRLPDGYDTVigpgGATLSGGQRQRIALARALYG 471
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1032718621 164 SPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITH 512
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
13-207 |
4.58e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.51 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 13 NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKTSQRRYQNAIGMV 92
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV----------SGIDTGDFSKLQGIRKLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 93 FQNYQL-FPNFTVLDNVLEAPIAQKLAPKS--ELLDQAmflLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIIC 169
Cdd:PRK13644 83 FQNPETqFVGRTVEEDLAFGPENLCLPPIEirKRVDRA---LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1032718621 170 FDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQ 207
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE 197
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
13-205 |
4.86e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.37 E-value: 4.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 13 NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGdrvlcqetSQGVQYSDKTSQRRYQNaIGMV 92
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFD--------GKPIDYSRKGLMKLRES-VGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 93 FQ--NYQLFpNFTVLDNVLEAPIAQKLaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICF 170
Cdd:PRK13636 88 FQdpDNQLF-SASVYQDVSFGAVNLKL-PEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVL 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 1032718621 171 DEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:PRK13636 166 DEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHD 201
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-204 |
7.71e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 90.27 E-value: 7.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAY--NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgVQYSDk 79
Cdd:PRK11160 338 SLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI-------ADYSE- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 80 tSQRRyqNAIGMVFQNYQLFpNFTVLDNVLeapIAQKLAPKSELLDqamfLLDSVGLKDKADAYPS----------TLSG 149
Cdd:PRK11160 410 -AALR--QAISVVSQRVHLF-SATLRDNLL---LAAPNASDEALIE----VLQQVGLEKLLEDDKGlnawlgeggrQLSG 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 150 GQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAkQGKGILVVTH 204
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITH 532
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
3-204 |
9.41e-21 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 86.68 E-value: 9.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSdktsq 82
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIF----------DGHPWT----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLaPKSELLDqamfLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMM 162
Cdd:TIGR03740 66 RKDLHKIGSLIESPPLYENLTARENLKVHTTLLGL-PDSRIDE----VLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1032718621 163 LSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:TIGR03740 141 NHPKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSH 182
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-205 |
2.13e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 86.76 E-value: 2.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 18 IDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSqgvqysDKTSqRRYQNAIGMVFQnyq 97
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTK------DKYI-RPVRKRIGMVFQ--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 98 lFPNFTVLDNVLEAPIaqKLAPKS------ELLDQAMFLLDSVGL-KDKADAYPSTLSGGQKQRVAIARAMMLSPEIICF 170
Cdd:PRK13646 93 -FPESQLFEDTVEREI--IFGPKNfkmnldEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 1032718621 171 DEPTSALDRESANQVGKLVQAIA-KQGKGILVVTHD 205
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHD 205
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-204 |
2.19e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.81 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 21 FNCRidPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlcqetsqgvqysdktsQRRYQNA-------IGMVF 93
Cdd:PRK11288 25 FDCR--AGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-----------------EMRFASTtaalaagVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 94 QNYQLFPNFTVLDNVLEAPIAQKLA--PKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFD 171
Cdd:PRK11288 86 QELHLVPEMTVAENLYLGQLPHKGGivNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190
....*....|....*....|....*....|...
gi 1032718621 172 EPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-204 |
3.74e-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: 84.50 E-value: 3.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLE--KCDQGNIAIGDRVLcqetsqgvqySDKT 80
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDI----------TDLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNAIGMVFQNYQLFPNFTVLDnvleapiaqklapkselldqamfLLDSVGLKdkadaypstLSGGQKQRVAIARA 160
Cdd:cd03217 71 PEERARLGIFLAFQYPPEIPGVKNAD-----------------------FLRYVNEG---------FSGGEKKRNEILQL 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1032718621 161 MMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:cd03217 119 LLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITH 162
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
17-204 |
4.42e-20 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 87.88 E-value: 4.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 17 VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGniaigdRVLCQEtsQGVQYSDKTSQRRyqnAIGMVFQNY 96
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHG------QVLVDG--VDLAIADPAWLRR---QMGVVLQEN 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 97 QLFpNFTVLDNVleaPIAQKLAPKSELLDQAM------FLLD-SVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIIC 169
Cdd:TIGR01846 541 VLF-SRSIRDNI---ALCNPGAPFEHVIHAAKlagahdFISElPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILI 616
|
170 180 190
....*....|....*....|....*....|....*
gi 1032718621 170 FDEPTSALDRESANQVGKLVQAIAkQGKGILVVTH 204
Cdd:TIGR01846 617 FDEATSALDYESEALIMRNMREIC-RGRTVIIIAH 650
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-207 |
5.01e-20 |
|
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: 87.88 E-value: 5.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNG--NMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQetsqgvqySDKT 80
Cdd:COG4618 331 LSVENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ--------WDRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYqnaIGMVFQNYQLFPNfTVLDN-----------VLEApiAQKlapkselldqamflldsVGLKD----KADAY-- 143
Cdd:COG4618 403 ELGRH---IGYLPQDVELFDG-TIAENiarfgdadpekVVAA--AKL-----------------AGVHEmilrLPDGYdt 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032718621 144 -----PSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQ 207
Cdd:COG4618 460 rigegGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS 528
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-205 |
6.99e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 85.14 E-value: 6.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFN---CRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQGVqysdk 79
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNL----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 80 tsqRRyqnAIGMVFQNY-QLFPNFTVLDNVLEAPIAQKLaPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIA 158
Cdd:PRK13642 80 ---RR---KIGMVFQNPdNQFVGATVEDDVAFGMENQGI-PREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1032718621 159 RAMMLSPEIICFDEPTSALDRESANQVGKLVQAIA-KQGKGILVVTHD 205
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHD 200
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
25-205 |
1.23e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 84.42 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 25 IDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDrvlcqetsQGVQYSDKTSQRRYqnaIGMVFQNyqlfPNFTV 104
Cdd:PRK13648 32 IPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN--------QAITDDNFEKLRKH---IGIVFQN----PDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 105 LDNVLEAPIA----QKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRE 180
Cdd:PRK13648 97 VGSIVKYDVAfgleNHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180
....*....|....*....|....*..
gi 1032718621 181 SANQVGKLVQAIaKQGKG--ILVVTHD 205
Cdd:PRK13648 177 ARQNLLDLVRKV-KSEHNitIISITHD 202
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-204 |
1.35e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.64 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGdrvlcqetsqGVQYSDKTSQRR 84
Cdd:PRK15439 14 ARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG----------GNPCARLTPAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 YQNAIGMVFQNYQLFPNFTVLDNvleapIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLS 164
Cdd:PRK15439 84 HQLGIYLVPQEPLLFPNLSVKEN-----ILFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1032718621 165 PEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISH 198
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-204 |
1.71e-19 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 81.98 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNM--VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGdrvlcqetsqGVQYSDKT 80
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLD----------GVPVSDLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRyqNAIGMVFQNYQLFpNFTVLDNVleapiaqklapkselldqamflldsvGLKdkadaypstLSGGQKQRVAIARA 160
Cdd:cd03247 71 KALS--SLISVLNQRPYLF-DTTLRNNL--------------------------GRR---------FSGGERQRLALARI 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1032718621 161 MMLSPEIICFDEPTSALDRESANQVGKLVQAIAKqGKGILVVTH 204
Cdd:cd03247 113 LLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITH 155
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-204 |
2.00e-19 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 82.90 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 17 VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgVQYSDKTsqrrYQNAIGMVFQNY 96
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI-------SQYEHKY----LHSKVSLVGQEP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 97 QLFPNfTVLDNvleapIAQKLAPKS-----ELLDQA-----MFLLDSvGLKDKADAYPSTLSGGQKQRVAIARAMMLSPE 166
Cdd:cd03248 98 VLFAR-SLQDN-----IAYGLQSCSfecvkEAAQKAhahsfISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 1032718621 167 IICFDEPTSALDRESANQVGKLVQAiAKQGKGILVVTH 204
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAH 207
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-204 |
2.03e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 86.05 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 22 NCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCdQGNIAIGDRVLCQetsqgvqySDKTSQRRYqnaIGMVFQNYQLFPN 101
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRE--------LDPESWRKH---LSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 102 fTVLDNVL-------EAPIAQKL--APKSELLDQAMFLLDSVgLKDKAdaypSTLSGGQKQRVAIARAMMLSPEIICFDE 172
Cdd:PRK11174 438 -TLRDNVLlgnpdasDEQLQQALenAWVSEFLPLLPQGLDTP-IGDQA----AGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190
....*....|....*....|....*....|....
gi 1032718621 173 PTSALDRESANQVgklVQAI--AKQGKGILVVTH 204
Cdd:PRK11174 512 PTASLDAHSEQLV---MQALnaASRRQTTLMVTH 542
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-205 |
9.71e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 82.36 E-value: 9.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 18 IDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetSQGVQYSDKTsqRRYQNAIGMVFQ--N 95
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI----PANLKKIKEV--KRLRKEIGLVFQfpE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 96 YQLFPNfTVLDNVLEAPIAQKlAPKSELLDQAMFLLDSVGL-KDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPT 174
Cdd:PRK13645 101 YQLFQE-TIEKDIAFGPVNLG-ENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190
....*....|....*....|....*....|..
gi 1032718621 175 SALDRESANQVGKLVQAIAK-QGKGILVVTHD 205
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKeYKKRIIMVTHN 210
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-204 |
1.24e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.70 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLK-KAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAI--GDRVLCqetsqgvqysd 78
Cdd:COG4178 362 ALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLF----------- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 79 kTSQRRYqnaigmvfqnyqlFPNFTvLDNVLEAPIAQKLAPKSELLDqamfLLDSVGLK------DKADAYPSTLSGGQK 152
Cdd:COG4178 431 -LPQRPY-------------LPLGT-LREALLYPATAEAFSDAELRE----ALEAVGLGhlaerlDEEADWDQVLSLGEQ 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 153 QRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAiAKQGKGILVVTH 204
Cdd:COG4178 492 QRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-217 |
1.74e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.37 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNM----VIDQFNCRIDPGEIVILLGPSGTGKT----TFMRLINNlekcdQGNIAIGDRVLCQETSQGV 74
Cdd:PRK10261 13 LAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQ-----AGGLVQCDKMLLRRRSRQV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 75 ----QYSDKTSQRRYQNAIGMVFQN--YQLFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADA---YPS 145
Cdd:PRK10261 88 ielsEQSAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTIlsrYPH 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032718621 146 TLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHDTQFGEDFGTRIV 217
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVL 240
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-205 |
1.85e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.83 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQetsqgvqYSDkt 80
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM-------LSS-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 sqRRYQNAIGMVFQNYQLFPNFTVLDNVLEA-----PIAQKLAPKSE-LLDQAMfllDSVGLKDKADAYPSTLSGGQKQR 154
Cdd:PRK11231 72 --RQLARRLALLPQHHLTPEGITVRELVAYGrspwlSLWGRLSAEDNaRVNQAM---EQTRINHLADRRLTDLSGGQRQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1032718621 155 VAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHD 197
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-206 |
2.44e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.14 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 13 NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSdKTSQRRYQNAIGMV 92
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLF----------EGEDIS-TLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 93 FQNYQLFPNfTVLDNVL-------EAPIAQKLAPksellDQAMFLLDSVGLKDKADAypstLSGGQKQRVAIARAMMLSP 165
Cdd:PRK10247 87 AQTPTLFGD-TVYDNLIfpwqirnQQPDPAIFLD-----DLERFALPDTILTKNIAE----LSGGEKQRISLIRNLQFMP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1032718621 166 EIICFDEPTSALDRESANQVGKLVQAIAK-QGKGILVVTHDT 206
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVReQNIAVLWVTHDK 198
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-208 |
2.48e-18 |
|
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: 82.91 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 6 SNLKKAYNGnmvidqFNCRIDPGEI----VI-LLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVlcqetSQGVQY---- 76
Cdd:COG1245 345 PDLTKSYGG------FSLEVEGGEIregeVLgIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKI-----SYKPQYispd 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 77 SDKTSQRRYQNAIGMVFQnyqlfpnftvlDNVLEAPIAQKLAPKsELLDQAMflldsvglkdkadaypSTLSGGQKQRVA 156
Cdd:COG1245 414 YDGTVEEFLRSANTDDFG-----------SSYYKTEIIKPLGLE-KLLDKNV----------------KDLSGGELQRVA 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1032718621 157 IARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIA-KQGKGILVVTHDTQF 208
Cdd:COG1245 466 IAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAeNRGKTAMVVDHDIYL 518
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-204 |
3.51e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 80.56 E-value: 3.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 22 NCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqeTSQGVQYSDKTSQRRyqnaIGMVFQ--NYQLF 99
Cdd:PRK13649 27 NLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLI---TSTSKNKDIKQIRKK----VGLVFQfpESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 100 PNfTVLDNVLEAP----IAQKLAPKSELLDQAMflldsVGLKDKA-DAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPT 174
Cdd:PRK13649 100 EE-TVLKDVAFGPqnfgVSQEEAEALAREKLAL-----VGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190
....*....|....*....|....*....|
gi 1032718621 175 SALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-203 |
4.93e-18 |
|
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: 78.84 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 4 IVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKcdqGNIAI-GDrvlcqetsqgVQYSDKTSQ 82
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE---GNVSVeGD----------IHYNGIPYK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 ---RRYQNAIGMVFQNYQLFPNFTVldnvleapiaqklapkSELLDQAmflldsvgLKDKADAYPSTLSGGQKQRVAIAR 159
Cdd:cd03233 76 efaEKYPGEIIYVSEEDVHFPTLTV----------------RETLDFA--------LRCKGNEFVRGISGGERKRVSIAE 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1032718621 160 AMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVT 203
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS 175
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-204 |
5.40e-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: 5.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 27 PGEIVILLGPSGTGKTTFM-----RLINNLEKcdQGNIAIGDRVLcqetsqgvqysDKTSQRRYQnaiGMVFQNYQLFPN 101
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMnalafRSPKGVKG--SGSVLLNGMPI-----------DAKEMRAIS---AYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 102 FTVLDNVL---------EAPIAQKLAPKSELLDQamflldsVGLKDKAD------AYPSTLSGGQKQRVAIARAMMLSPE 166
Cdd:TIGR00955 114 LTVREHLMfqahlrmprRVTKKEKRERVDEVLQA-------LGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPP 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 1032718621 167 IICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-216 |
6.61e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.83 E-value: 6.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 27 PGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQGVQysdktSQRRyqnAIGMVFQN--YQLFPNFTV 104
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQ-----ALRR---DIQFIFQDpyASLDPRQTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 105 LDNVLEAPIAQKLAPKSELLDQAMFLLDSVGLK-DKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESAN 183
Cdd:PRK10261 421 GDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRG 500
|
170 180 190
....*....|....*....|....*....|....
gi 1032718621 184 QVGKLVQAIAKQ-GKGILVVTHDTQFGEDFGTRI 216
Cdd:PRK10261 501 QIINLLLDLQRDfGIAYLFISHDMAVVERISHRV 534
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
27-205 |
6.67e-18 |
|
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: 77.86 E-value: 6.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 27 PGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGdrvlcqetsqGVQYSDKTSQRRYQNAIGMV---FQNYQLFPNFT 103
Cdd:cd03215 25 AGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD----------GKPVTRRSPRDAIRAGIAYVpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 104 VLDNVleapiaqklapkselldqamflldsvglkdkadAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESAN 183
Cdd:cd03215 95 VAENI---------------------------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180
....*....|....*....|..
gi 1032718621 184 QVGKLVQAIAKQGKGILVVTHD 205
Cdd:cd03215 142 EIYRLIRELADAGKAVLLISSE 163
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-204 |
7.68e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 81.69 E-value: 7.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 25 IDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgVQYSDKTSQRRyqnaIGMVFQNYQLFpNFTV 104
Cdd:TIGR00958 504 LHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL-------VQYDHHYLHRQ----VALVGQEPVLF-SGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 105 LDNVL----EAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRE 180
Cdd:TIGR00958 572 RENIAygltDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
170 180
....*....|....*....|....
gi 1032718621 181 SANQVGklvQAIAKQGKGILVVTH 204
Cdd:TIGR00958 652 CEQLLQ---ESRSRASRTVLLIAH 672
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-204 |
1.11e-17 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 77.97 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqeTSQGVQYSDKTSQ 82
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI--------DGKTATRGDRSRF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPNFTVLdNVLEAPIAQKLaPKSELLdqamflldSVGLKDKADAYPSTLSGGQKQRVAIARaMM 162
Cdd:PRK13543 84 MAYLGHLPGLKADLSTLENLHFL-CGLHGRRAKQM-PGSALA--------IVGLAGYEDTLVRQLSAGQKKRLALAR-LW 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1032718621 163 LSPE-IICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:PRK13543 153 LSPApLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
18-205 |
1.78e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 79.40 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 18 IDQFNCRIDPGEIVILLGPSGTGKT----TFMRLINNLEKCDQGNIAIGDRVLcqetsqgVQYSDKTSQRRYQNAIGMVF 93
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDL-------QRISEKERRNLVGAEVAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 94 QN--YQLFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGLKDKA---DAYPSTLSGGQKQRVAIARAMMLSPEII 168
Cdd:PRK11022 96 QDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 1032718621 169 CFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHD 213
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
27-204 |
1.98e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.39 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 27 PGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKT--SQRRyqnAIGMVFQNYQLFpNFTV 104
Cdd:PRK13657 360 PGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILI----------DGTDIRTVTraSLRR---NIAVVFQDAGLF-NRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 105 LDNVLeapIAQKLAPKSELLD-----QAM-FLLDSV-GLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSAL 177
Cdd:PRK13657 426 EDNIR---VGRPDATDEEMRAaaeraQAHdFIERKPdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180
....*....|....*....|....*..
gi 1032718621 178 DRESANQVGKLVQAIAKqGKGILVVTH 204
Cdd:PRK13657 503 DVETEAKVKAALDELMK-GRTTFIIAH 528
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-204 |
1.98e-17 |
|
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: 80.25 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 24 RIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcQETSQgvqysdkTSQRRyqnAIGMVFQNYQLFpNFT 103
Cdd:COG5265 380 EVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI-RDVTQ-------ASLRA---AIGIVPQDTVLF-NDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 104 VLDNVL-------EAPI--AQKLApksELLDqamFL------LDSV----GLKdkadaypstLSGGQKQRVAIARAMMLS 164
Cdd:COG5265 448 IAYNIAygrpdasEEEVeaAARAA---QIHD---FIeslpdgYDTRvgerGLK---------LSGGEKQRVAIARTLLKN 512
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1032718621 165 PEIICFDEPTSALDreSANQvgklvQAI------AKQGKGILVVTH 204
Cdd:COG5265 513 PPILIFDEATSALD--SRTE-----RAIqaalreVARGRTTLVIAH 551
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
13-204 |
2.28e-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: 76.04 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 13 NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIaigdrvlcqetsqgvqysdktsqrryqnaiGMV 92
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI------------------------------GMP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 93 FQNYQLFpnftvldnvleapIAQK-LAPKSELLDQAmflldsvglkdkadAYP--STLSGGQKQRVAIARAMMLSPEIIC 169
Cdd:cd03223 62 EGEDLLF-------------LPQRpYLPLGTLREQL--------------IYPwdDVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*
gi 1032718621 170 FDEPTSALDRESANQvgkLVQAIAKQGKGILVVTH 204
Cdd:cd03223 115 LDEATSALDEESEDR---LYQLLKELGITVISVGH 146
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-220 |
7.80e-17 |
|
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: 78.44 E-value: 7.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVlcqetsqGVQYSDktsQRR 84
Cdd:TIGR03719 325 AENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV-------KLAYVD---QSR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 yqnaigmvfqnYQLFPNFTVLDNVleapiaqklapkSELLDQAMflldsVGLKD-KADAYPS--------------TLSG 149
Cdd:TIGR03719 395 -----------DALDPNKTVWEEI------------SGGLDIIK-----LGKREiPSRAYVGrfnfkgsdqqkkvgQLSG 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032718621 150 GQKQRVAIARAMMLSPEIICFDEPTSALDRESanqVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIVSSE 220
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLDVET---LRALEEALLNFAGCAVVISHDRWFLDRIATHILAFE 514
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-204 |
8.78e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.38 E-value: 8.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 25 IDPGEIVILLGPSGTGKTTFM-----RLINNlekCDQGNIAIGDRVLCQETsqgvqysdktsQRRyqnaIGMVFQNYQLF 99
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLnalagRIQGN---NFTGTILANNRKPTKQI-----------LKR----TGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 100 PNFTVLDNVLEAPIAQklAPKSELLDQAMFLLDSV----GLKD-----KADAYPSTLSGGQKQRVAIARAMMLSPEIICF 170
Cdd:PLN03211 153 PHLTVRETLVFCSLLR--LPKSLTKQEKILVAESViselGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190
....*....|....*....|....*....|....
gi 1032718621 171 DEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-205 |
1.15e-16 |
|
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: 77.90 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 27 PGEIVILLGPSGTGKTTFMR-----LINNLekCDQGNIAIGDRVLcqetsqgvqysdktsqRRYQnaiGMVFQNYqlfpn 101
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKilsgeLKPNL--GDYDEEPSWDEVL----------------KRFR---GTELQDY----- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 102 FT-VLDNVLEApiAQK-----LAPK------SELLDQA------MFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMML 163
Cdd:COG1245 152 FKkLANGEIKV--AHKpqyvdLIPKvfkgtvRELLEKVdergklDELAEKLGLENILDRDISELSGGELQRVAIAAALLR 229
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1032718621 164 SPEIICFDEPTSALD-RESANqVGKLVQAIAKQGKGILVVTHD 205
Cdd:COG1245 230 DADFYFFDEPSSYLDiYQRLN-VARLIRELAEEGKYVLVVEHD 271
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-204 |
1.15e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 78.14 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNG--NMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKT 80
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL----------DGHDLRDYT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 -SQRRYQnaIGMVFQNYQLFpNFTVLDNVLEA--------PI--AQKLAPKSELLDQAMFLLDSVGLKDKAdaypsTLSG 149
Cdd:PRK11176 412 lASLRNQ--VALVSQNVHLF-NDTIANNIAYArteqysreQIeeAARMAYAMDFINKMDNGLDTVIGENGV-----LLSG 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 150 GQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQgKGILVVTH 204
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAH 537
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-205 |
1.90e-16 |
|
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: 75.06 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 17 VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlcqetsqgVQYSDKtsqRRYQNAIGMVF-QN 95
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL---------VPWKRR---KKFLRRIGVVFgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 96 YQLFPNFTVLD---------NVLEAPIAQKLAPKSELLDQAMFLLDSVglkdkadaypSTLSGGQKQRVAIARAMMLSPE 166
Cdd:cd03267 104 TQLWWDLPVIDsfyllaaiyDLPPARFKKRLDELSELLDLEELLDTPV----------RQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1032718621 167 IICFDEPTSALDRESANQVGK-LVQAIAKQGKGILVVTHD 205
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNfLKEYNRERGTTVLLTSHY 213
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-204 |
2.55e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.10 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKC--DQGNIAIgdrvlcqetsQGVQYSDKT 80
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYevTSGSILL----------DGEDILELS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLAPKS--ELLDQAMFLLDSVGLKDK-ADAY-PSTLSGGQKQRVA 156
Cdd:COG0396 71 PDERARAGIFLAFQYPVEIPGVSVSNFLRTALNARRGEELSarEFLKLLKEKMKELGLDEDfLDRYvNEGFSGGEKKRNE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1032718621 157 IARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH 198
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
9-208 |
4.33e-16 |
|
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: 73.66 E-value: 4.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 9 KKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTF-MRLINNLEKCDqGNIAIGDRVLCqeTSQ--------------- 72
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLlSALLGELEKLS-GSVSVPGSIAY--VSQepwiqngtirenilf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 73 GVQYSdktsQRRYQNAIgmvfQNYQLFPNFTVLDNVLEAPIAQKlapkselldqamflldsvGLkdkadaypsTLSGGQK 152
Cdd:cd03250 89 GKPFD----EERYEKVI----KACALEPDLEILPDGDLTEIGEK------------------GI---------NLSGGQK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1032718621 153 QRVAIARAMMLSPEIICFDEPTSALDRESANQV-GKLVQAIAKQGKGILVVTHDTQF 208
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGLLLNNKTRILVTHQLQL 190
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-216 |
4.72e-16 |
|
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: 76.59 E-value: 4.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNM--VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQgvqysdkt 80
Cdd:TIGR01257 1938 LRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD-------- 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 sqrryqnaigmVFQNYQLFPNFTVLDNVLEAPIAQKL------APKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQR 154
Cdd:TIGR01257 2010 -----------VHQNMGYCPQFDAIDDLLTGREHLYLyarlrgVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRK 2078
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 155 VAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRI 216
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRL 2140
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-204 |
5.63e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 75.92 E-value: 5.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 6 SNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKTSQRRY 85
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF----------QGKEIDFKSSKEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 86 QNAIGMVFQNYQLFPNFTVLDNVLEApiaqKLAPKSELLDQAMFLLDSVGLKDKAD------AYPSTLSGGQKQRVAIAR 159
Cdd:PRK10982 72 ENGISMVHQELNLVLQRSVMDNMWLG----RYPTKGMFVDQDKMYRDTKAIFDELDididprAKVATLSVSQMQMIEIAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1032718621 160 AMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:PRK10982 148 AFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISH 192
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-205 |
6.37e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.00 E-value: 6.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 27 PGEIVILLGPSGTGKTTFMR-----LINNLekCDQGNIAIGDRVLcqetsqgvqysdktsqRRYQnaiGMVFQNYqlfpn 101
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKilsgeLIPNL--GDYEEEPSWDEVL----------------KRFR---GTELQNY----- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 102 FTVLDNVlEAPIAQK-----LAPK------SELLDQA----MF--LLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLS 164
Cdd:PRK13409 152 FKKLYNG-EIKVVHKpqyvdLIPKvfkgkvRELLKKVdergKLdeVVERLGLENILDRDISELSGGELQRVAIAAALLRD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1032718621 165 PEIICFDEPTSALD-RESANqVGKLVQAIAKqGKGILVVTHD 205
Cdd:PRK13409 231 ADFYFFDEPTSYLDiRQRLN-VARLIRELAE-GKYVLVVEHD 270
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-205 |
9.74e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.89 E-value: 9.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGniaigdRVLCQetSQGVQYSdKTSQ 82
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKG------AVLWQ--GKPLDYS-KRGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQN--YQLFpnFTVLDNVLEAPIAQKLAPKSEL---LDQAMFLLDSVGLKDKAdayPSTLSGGQKQRVAI 157
Cdd:PRK13638 73 LALRQQVATVFQDpeQQIF--YTDIDSDIAFSLRNLGVPEAEItrrVDEALTLVDAQHFRHQP---IQCLSHGQKKRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1032718621 158 ARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHD 195
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-190 |
1.35e-15 |
|
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: 72.53 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 7 NLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTT----FMRLInnleKCDQGNIAIGDRVLCqetsqgvqysdKTSQ 82
Cdd:cd03244 9 SLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDIS-----------KIGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPNfTVLDNvleapiaqkLAPKSELLDQAMFL-LDSVGLKDKADAYP-----------STLSGG 150
Cdd:cd03244 74 HDLRSRISIIPQDPVLFSG-TIRSN---------LDPFGEYSDEELWQaLERVGLKEFVESLPggldtvveeggENLSVG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1032718621 151 QKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQ 190
Cdd:cd03244 144 QRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIR 183
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-205 |
1.75e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.04 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlcqETSQGVQYSDKTSQ 82
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR----DGQLRDLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRY--QNAIGMVFQNYQ--LFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGL-KDKADAYPSTLSGGQKQRVAI 157
Cdd:PRK11701 83 RRRllRTEWGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1032718621 158 ARAMMLSPEIICFDEPTSALDresanqVGklVQA---------IAKQGKGILVVTHD 205
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLD------VS--VQArlldllrglVRELGLAVVIVTHD 211
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-217 |
1.77e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 74.54 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMR-LINNLEKcDQGNiaigdrvlcqetsqgVQYSDK 79
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRtLVGELEP-DSGT---------------VKWSEN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 80 TSqrryqnaIGMVFQ-NYQLFPN-FTVLDnvleaPIAQKLAPKSEllDQAM--------FLLDSVGLKDKadaypsTLSG 149
Cdd:PRK15064 382 AN-------IGYYAQdHAYDFENdLTLFD-----WMSQWRQEGDD--EQAVrgtlgrllFSQDDIKKSVK------VLSG 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032718621 150 GQKQRVAIARAMMLSPEIICFDEPTSALDRESanqVGKLVQAIaKQGKGILV-VTHDTQFGEDFGTRIV 217
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES---IESLNMAL-EKYEGTLIfVSHDREFVSSLATRII 506
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-216 |
1.86e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 74.66 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYN--GNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvqysdKTSQ 82
Cdd:TIGR01257 931 VKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI------------ETNL 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPNFTVLDNVL-EAPIAQKLAPKSELLDQAMflLDSVGLKDKADAYPSTLSGGQKQRVAIARAM 161
Cdd:TIGR01257 999 DAVRQSLGMCPQHNILFHHLTVAEHILfYAQLKGRSWEEAQLEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAF 1076
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 162 MLSPEIICFDEPTSALDRESANQVGKLVQAIaKQGKGILVVTHDTQFGEDFGTRI 216
Cdd:TIGR01257 1077 VGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRI 1130
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-205 |
1.97e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.36 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 17 VIDQFNCRIDPGEIVILLGPSGTGKT----TFMRLINNLEKC-DQGNIAIgdrvlcqeTSQGVQYSDKTSQRRYQ-NAIG 90
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRF--------HGESLLHASEQTLRGVRgNKIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 91 MVFQN--YQLFPNFTvldnvLEAPIAQKL---------APKSELLDqamfLLDSVGLKDKA---DAYPSTLSGGQKQRVA 156
Cdd:PRK15134 96 MIFQEpmVSLNPLHT-----LEKQLYEVLslhrgmrreAARGEILN----CLDRVGIRQAAkrlTDYPHQLSGGERQRVM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1032718621 157 IARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:PRK15134 167 IAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHN 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
27-203 |
4.60e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.13 E-value: 4.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 27 PGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRvlcqetsqgvqysdKTSQRRYQNAI--GMVF-----QNYQLF 99
Cdd:COG1129 277 AGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK--------------PVRIRSPRDAIraGIAYvpedrKGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 100 PNFTVLDNVLeAPIAQKLAPkselldqaMFLLDSVGLKDKADAY--------PS------TLSGGQKQRVAIARAMMLSP 165
Cdd:COG1129 343 LDLSIRENIT-LASLDRLSR--------GGLLDRRRERALAEEYikrlriktPSpeqpvgNLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1032718621 166 EIICFDEPTSALDresanqVG------KLVQAIAKQGKGILVVT 203
Cdd:COG1129 414 KVLILDEPTRGID------VGakaeiyRLIRELAAEGKAVIVIS 451
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
27-203 |
5.72e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 71.74 E-value: 5.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 27 PGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCqetsqgvqYSDKT--SQRryqnaIGMVFQN--YQLFPNF 102
Cdd:PRK15112 38 EGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH--------FGDYSyrSQR-----IRMIFQDpsTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 103 TVlDNVLEAPIAQKLAPKSELLDQAMFL-LDSVGLK-DKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRE 180
Cdd:PRK15112 105 RI-SQILDFPLRLNTDLEPEQREKQIIEtLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180
....*....|....*....|....
gi 1032718621 181 SANQVGKLVQAI-AKQGKGILVVT 203
Cdd:PRK15112 184 MRSQLINLMLELqEKQGISYIYVT 207
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-205 |
6.78e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 72.25 E-value: 6.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 17 VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKcDQGNIAiGDRVlcqeTSQGVQYSDKTSQRRYQ---NAIGMVF 93
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVT-ADRF----RWNGIDLLKLSPRERRKiigREIAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 94 QNYQ--LFPNFTVLDNVLEA--------PIAQKLAPKSElldQAMFLLDSVGLKDKAD---AYPSTLSGGQKQRVAIARA 160
Cdd:COG4170 96 QEPSscLDPSAKIGDQLIEAipswtfkgKWWQRFKWRKK---RAIELLHRVGIKDHKDimnSYPHELTEGECQKVMIAMA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1032718621 161 MMLSPEIICFDEPTSALDRESANQVGKLVQAIAK-QGKGILVVTHD 205
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHD 218
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-203 |
8.27e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.22 E-value: 8.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 14 GNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqeTSQGVQYSDKTSQRRYQNAIGmvf 93
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI---RRQRDEYHQDLLYLGHQPGIK--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 94 qnyqlfPNFTVLDNVLeapIAQKLA-PKSEllDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDE 172
Cdd:PRK13538 87 ------TELTALENLR---FYQRLHgPGDD--EALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190
....*....|....*....|....*....|.
gi 1032718621 173 PTSALDRESANQVGKLVQAIAKQGkGILVVT 203
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQHAEQG-GMVILT 185
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-205 |
1.24e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 70.99 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALI-VSNLKKAYNGNM-VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQGVqysd 78
Cdd:PRK13652 1 MHLIeTRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 79 ktsqRRYqnaIGMVFQNyqlfPNFTVLDNVLEAPIAqkLAPKSELLDQAMF------LLDSVGLKDKADAYPSTLSGGQK 152
Cdd:PRK13652 77 ----RKF---VGLVFQN----PDDQIFSPTVEQDIA--FGPINLGLDEETVahrvssALHMLGLEELRDRVPHHLSGGEK 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1032718621 153 QRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:PRK13652 144 KRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQ 197
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
14-178 |
1.61e-14 |
|
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: 71.69 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 14 GNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQetsqgvqySDKTSQRRYqnaIGMVF 93
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKD--------IDRHTLRQF---INYLP 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 94 QNYQLFPNfTVLDNVLeapIAQKLAPKSELLDQAmflLDSVGLKDKADAYP-----------STLSGGQKQRVAIARAMM 162
Cdd:TIGR01193 555 QEPYIFSG-SILENLL---LGAKENVSQDEIWAA---CEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALL 627
|
170
....*....|....*.
gi 1032718621 163 LSPEIICFDEPTSALD 178
Cdd:TIGR01193 628 TDSKVLILDESTSNLD 643
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-204 |
1.70e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.06 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 27 PGEIVILLGPSGTGKTTfmrLINNL-EKCDQGNIAIGDRVLcqetsqGVQYSDKTSQRRyqnaIGMVFQNYQLFPNFTVL 105
Cdd:TIGR00956 788 PGTLTALMGASGAGKTT---LLNVLaERVTTGVITGGDRLV------NGRPLDSSFQRS----IGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 106 DNV-----LEAPIAQKLAPKSELLDQAMFLLdsvGLKDKADAYPST----LSGGQKQRVAIARAMMLSPEIICF-DEPTS 175
Cdd:TIGR00956 855 ESLrfsayLRQPKSVSKSEKMEYVEEVIKLL---EMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLFlDEPTS 931
|
170 180
....*....|....*....|....*....
gi 1032718621 176 ALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:TIGR00956 932 GLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-208 |
1.99e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.38 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 6 SNLKKAYNGnmvidqFNCRIDPGEI----VI-LLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVlcqetSQGVQYSDKT 80
Cdd:PRK13409 344 PDLTKKLGD------FSLEVEGGEIyegeVIgIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKI-----SYKPQYIKPD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNAIGMVFQNYQlfpnftvlDNVLEAPIAQKLAPKsELLDQAMflldsvglkdkadaypSTLSGGQKQRVAIARA 160
Cdd:PRK13409 413 YDGTVEDLLRSITDDLG--------SSYYKSEIIKPLQLE-RLLDKNV----------------KDLSGGELQRVAIAAC 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1032718621 161 MMLSPEIICFDEPTSALDRESANQVGKLVQAIA-KQGKGILVVTHDTQF 208
Cdd:PRK13409 468 LSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAeEREATALVVDHDIYM 516
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-208 |
3.48e-14 |
|
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: 70.73 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 7 NLKKAYNGN-MVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQG------NIAIGdrVLCQE---------- 69
Cdd:TIGR03719 9 RVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGearpqpGIKVG--YLPQEpqldptktvr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 70 --TSQGVQySDKTSQRRYqNAIGMVF-----QNYQLFPNFTVLDNVLEAPIAQKLAPKselLDQAMfllDSVGLKDKaDA 142
Cdd:TIGR03719 87 enVEEGVA-EIKDALDRF-NEISAKYaepdaDFDKLAAEQAELQEIIDAADAWDLDSQ---LEIAM---DALRCPPW-DA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032718621 143 YPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESanqVGKLVQAIAKQGKGILVVTHDTQF 208
Cdd:TIGR03719 158 DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES---VAWLERHLQEYPGTVVAVTHDRYF 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-204 |
3.90e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.42 E-value: 3.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIaigdRVLCQETSQgvqYSDKTSQ 82
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSI----LYLGKEVTF---NGPKSSQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 rryQNAIGMVFQNYQLFPNFTVLDNVL---EAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIAR 159
Cdd:PRK10762 78 ---EAGIGIIHQELNLIPQLTIAENIFlgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1032718621 160 AMMLSPEIICFDEPTSAL-DRESAnQVGKLVQAIAKQGKGILVVTH 204
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALtDTETE-SLFRVIRELKSQGRGIVYISH 199
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-223 |
4.91e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.24 E-value: 4.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 7 NLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqETSQGVQYSDKTSQRRyq 86
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL-------DGEHIQHYASKEVARR-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 87 naIGMVFQNYQLFPNFTVldnvleapiaQKLAPKSELLDQAMFL-------------LDSVGLKDKADAYPSTLSGGQKQ 153
Cdd:PRK10253 83 --IGLLAQNATTPGDITV----------QELVARGRYPHQPLFTrwrkedeeavtkaMQATGITHLADQSVDTLSGGQRQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032718621 154 RVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAK-QGKGILVVTHDTQFGEDFGTRIVSSEEFK 223
Cdd:PRK10253 151 RAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNReKGYTLAAVLHDLNQACRYASHLIALREGK 221
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-205 |
5.42e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 69.75 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 18 IDQFNCRIDPGEIVILLGPSGTGK--TTF--MRLInnlekCDQGNIAIGDRVLCQETsqgVQYSDKTSQRRYQNAIGMVF 93
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKsqTAFalMGLL-----AANGRIGGSATFNGREI---LNLPEKELNKLRAEQISMIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 94 QN--YQLFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGL---KDKADAYPSTLSGGQKQRVAIARAMMLSPEII 168
Cdd:PRK09473 104 QDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMpeaRKRMKMYPHEFSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 1032718621 169 CFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:PRK09473 184 IADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHD 221
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-205 |
9.43e-14 |
|
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: 68.16 E-value: 9.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 27 PGEIVILLGPSGTGKTTFMR-----LINNLEK-CDQGNiaigdrvlcqetsqgvqYSDKTSQRRyqnaiGMVFQNYqlfp 100
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKilagkLKPNLGKfDDPPD-----------------WDEILDEFR-----GSELQNY---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 101 nFTVLDN----VLEAPIAQKLAPKS------ELLDQA----MF--LLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLS 164
Cdd:cd03236 79 -FTKLLEgdvkVIVKPQYVDLIPKAvkgkvgELLKKKdergKLdeLVDQLELRHVLDRNIDQLSGGELQRVAIAAALARD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1032718621 165 PEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:cd03236 158 ADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHD 198
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-205 |
1.06e-13 |
|
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: 67.82 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 25 IDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqeTSQGVQYSDKTSQRRYQNAIgmvfqnYQLFpnFTV 104
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI--------ELDTVSYKPQYIKADYEGTV------RDLL--SSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 105 LDNVLEAPIAqklapKSELLDqamflldSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQ 184
Cdd:cd03237 86 TKDFYTHPYF-----KTEIAK-------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180
....*....|....*....|..
gi 1032718621 185 VGKLVQAIA-KQGKGILVVTHD 205
Cdd:cd03237 154 ASKVIRRFAeNNEKTAFVVEHD 175
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-204 |
5.00e-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: 67.16 E-value: 5.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCD--QGNIAIGDRVLcqeTSQGVQYSDKT 80
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPL---KASNIRDTERA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 sqrryqnAIGMVFQNYQLFPNFTVLDNVL---EAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYP-STLSGGQKQRVA 156
Cdd:TIGR02633 79 -------GIVIIHQELTLVPELSVAENIFlgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1032718621 157 IARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISH 199
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-208 |
5.78e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.07 E-value: 5.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVlcqetsqgvqysdktsqrr 84
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV------------------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 yqnAIGMVFQNYQ-LFPNFTVLDNVleapiaqklapkSELLDQAMflldsVGLKD-KADAYPS--------------TLS 148
Cdd:PRK11819 388 ---KLAYVDQSRDaLDPNKTVWEEI------------SGGLDIIK-----VGNREiPSRAYVGrfnfkggdqqkkvgVLS 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 149 GGQKQRVAIARAMMLSPEIICFDEPTSALDRESanqVGKLVQAIAKQGKGILVVTHDTQF 208
Cdd:PRK11819 448 GGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET---LRALEEALLEFPGCAVVISHDRWF 504
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-205 |
5.93e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.06 E-value: 5.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLKKAY-NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvLCQETSQGVQysdkt 80
Cdd:PRK15056 6 GIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI----LGQPTRQALQ----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 sqrryQNAIGMVFQNYQLFPNFTVL--DNVLEAPIAQK---LAPKS---ELLDQAmflLDSVGLKDKADAYPSTLSGGQK 152
Cdd:PRK15056 77 -----KNLVAYVPQSEEVDWSFPVLveDVVMMGRYGHMgwlRRAKKrdrQIVTAA---LARVDMVEFRHRQIGELSGGQK 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1032718621 153 QRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
25-204 |
7.44e-13 |
|
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: 64.57 E-value: 7.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 25 IDPGEIVILLGPSGTGKTTFMRLINNLEkcDQGNIAiGDRVLCQetsqgvQYSDKTSQRRyqnaIGMVFQNYQLFPNFTv 104
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGRK--TAGVIT-GEILING------RPLDKNFQRS----TGYVEQQDVHSPNLT- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 105 ldnVLEApiaqklapkselldqamfLLDSVGLKDkadaypstLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQ 184
Cdd:cd03232 96 ---VREA------------------LRFSALLRG--------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180
....*....|....*....|
gi 1032718621 185 VGKLVQAIAKQGKGILVVTH 204
Cdd:cd03232 147 IVRFLKKLADSGQAILCTIH 166
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
28-203 |
8.46e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.73 E-value: 8.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 28 GEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKTSQRRYQNAIGMVFQNYQ---LFPNFTV 104
Cdd:PRK09700 289 GEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRL----------NGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 105 LDNVleaPIAQKLapKSELLDQAMFLLDSVGLKDKADAYP--------------STLSGGQKQRVAIARAMMLSPEIICF 170
Cdd:PRK09700 359 AQNM---AISRSL--KDGGYKGAMGLFHEVDEQRTAENQRellalkchsvnqniTELSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190
....*....|....*....|....*....|...
gi 1032718621 171 DEPTSALDRESANQVGKLVQAIAKQGKGILVVT 203
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVMRQLADDGKVILMVS 466
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-202 |
4.20e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.36 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIaigdrvlcqeTSQGVQYSDKTSQ 82
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRI----------VFDGKDITDWQTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPNFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSvgLKDKADAYPSTLSGGQKQRVAIARAMM 162
Cdd:PRK11614 76 KIMREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1032718621 163 LSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVV 202
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLV 193
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-178 |
4.39e-12 |
|
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: 63.72 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAY--NGNMVIDQFNCRIDPGEIVILLGPSGTGKTT----FMRLINNlekcdQGNIAIgdrvlcqetsQGVQY 76
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLNT-----EGDIQI----------DGVSW 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 77 sDKTSQRRYQNAIGMVFQNYQLFpnftvldnvlEAPIAQKLAPKSELLDQAMF-LLDSVGLKDKADAYPS---------- 145
Cdd:cd03289 68 -NSVPLQKWRKAFGVIPQKVFIF----------SGTFRKNLDPYGKWSDEEIWkVAEEVGLKSVIEQFPGqldfvlvdgg 136
|
170 180 190
....*....|....*....|....*....|....
gi 1032718621 146 -TLSGGQKQRVAIARAMMLSPEIICFDEPTSALD 178
Cdd:cd03289 137 cVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-217 |
4.58e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.59 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALI-VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAI-GDRV---LCQETSQGVQ 75
Cdd:PRK11147 1 MSLIsIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDLIvarLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 76 YS--DKTSQ---------RRYQNAIGMVFQNYQlfpnftvlDNVLEapiaqKLAPKSELLD-QAMFLLDS------VGLK 137
Cdd:PRK11147 81 GTvyDFVAEgieeqaeylKRYHDISHLVETDPS--------EKNLN-----ELAKLQEQLDhHNLWQLENrinevlAQLG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 138 DKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDresanqvgklVQAIA------KQGKG-ILVVTHDTQFGE 210
Cdd:PRK11147 148 LDPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----------IETIEwlegflKTFQGsIIFISHDRSFIR 217
|
....*..
gi 1032718621 211 DFGTRIV 217
Cdd:PRK11147 218 NMATRIV 224
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-204 |
6.88e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.74 E-value: 6.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLInnlekcdQG----NIAIGDRVLcqetsQGVQYSD 78
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI-------AGhpayKILEGDILF-----KGESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 79 KTSQRRYQNAIGMVFQNYQLFPNFTVLDNVLEAPIA-QKLAPKSELlDQAMFL------LDSVGLKdkadayPSTL---- 147
Cdd:CHL00131 76 LEPEERAHLGIFLAFQYPIEIPGVSNADFLRLAYNSkRKFQGLPEL-DPLEFLeiinekLKLVGMD------PSFLsrnv 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032718621 148 ----SGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:CHL00131 149 negfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
125-205 |
8.37e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.79 E-value: 8.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 125 DQAMFLLDSVGLKDKA---DAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAI-AKQGKGIL 200
Cdd:PRK10418 116 ATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGML 195
|
....*
gi 1032718621 201 VVTHD 205
Cdd:PRK10418 196 LVTHD 200
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
28-217 |
1.20e-11 |
|
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: 61.78 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 28 GEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVlcqetsqgvqysdktsqrRYQNAIGMVFQnyqlfPNFTVLDN 107
Cdd:cd03220 48 GERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV------------------SSLLGLGGGFN-----PELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 108 VL---------EAPIAQKLApkselldqamFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALD 178
Cdd:cd03220 105 IYlngrllglsRKEIDEKID----------EIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 1032718621 179 RESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:cd03220 175 AAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRAL 213
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-205 |
1.59e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.41 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 24 RIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQEtsqgvqysdktsQRRYQNAIGMVF-QNYQLFPNF 102
Cdd:COG4586 44 TIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKR------------RKEFARRIGVVFgQRSQLWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 103 TVLD---------NVLEAPIAQKLAPKSELLDQAMFLLDSVglkdkadaypSTLSGGQKQRVAIARAMMLSPEIICFDEP 173
Cdd:COG4586 112 PAIDsfrllkaiyRIPDAEYKKRLDELVELLDLGELLDTPV----------RQLSLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190
....*....|....*....|....*....|...
gi 1032718621 174 TSALDRESANQVGKLVQAI-AKQGKGILVVTHD 205
Cdd:COG4586 182 TIGLDVVSKEAIREFLKEYnRERGTTILLTSHD 214
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-217 |
1.97e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.77 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNlEKCdQGNIAIGDRVLCQETSQGVQYSDKTSQ 82
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLT-GGGAPRGARVTGDVTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPnFTVLDNVL--EAPIAQKLAPKS----ELLDQAMFLLDSVGLkDKADAypSTLSGGQKQRVA 156
Cdd:PRK13547 80 RLARLRAVLPQAAQPAFA-FSAREIVLlgRYPHARRAGALThrdgEIAWQALALAGATAL-VGRDV--TTLSGGELARVQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032718621 157 IARAM---------MLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGK-GILVVTHDTQFGEDFGTRIV 217
Cdd:PRK13547 156 FARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlGVLAIVHDPNLAARHADRIA 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-204 |
2.35e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.74 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 21 FNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDR----------------VLCQE-------TSQGVQYS 77
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrskigVVSQDpllfsnsIKNNIKYS 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 78 -----DKTSQRRYQNAIGMVFQ---------------NYQLFPNFTVLDNVLEAPIAQKLAPKSELLD--QAMFLLDSV- 134
Cdd:PTZ00265 484 lyslkDLEALSNYYNEDGNDSQenknkrnscrakcagDLNDMSNTTDSNELIEMRKNYQTIKDSEVVDvsKKVLIHDFVs 563
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 135 GLKDKAD----AYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAI-AKQGKGILVVTH 204
Cdd:PTZ00265 564 ALPDKYEtlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAH 638
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
33-208 |
2.48e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.44 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 33 LLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetSQGVQysdktsqrryqnaIGMVFQNYQLFPNFTVLDNVLE-- 110
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARP---------APGIK-------------VGYLPQEPQLDPEKTVRENVEEgv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 111 APIAQKLAPKSEL------------------------------------LDQAMfllDSVGLKDkADAYPSTLSGGQKQR 154
Cdd:PRK11819 96 AEVKAALDRFNEIyaayaepdadfdalaaeqgelqeiidaadawdldsqLEIAM---DALRCPP-WDAKVTKLSGGERRR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1032718621 155 VAIARAMMLSPEIICFDEPTSALDRESanqVGKLVQAIAKQGKGILVVTHDTQF 208
Cdd:PRK11819 172 VALCRLLLEKPDMLLLDEPTNHLDAES---VAWLEQFLHDYPGTVVAVTHDRYF 222
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-205 |
2.60e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.28 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 1 MALIVS--NLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIaigdrvlcqetsqgvqysd 78
Cdd:PRK09544 1 MTSLVSleNVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 79 ktsQRRYQNAIGMVFQNYQLFPN-------FTVLD-NVLEAPI--AQKLAPKSELLDQAMflldsvglkdkadaypSTLS 148
Cdd:PRK09544 62 ---KRNGKLRIGYVPQKLYLDTTlpltvnrFLRLRpGTKKEDIlpALKRVQAGHLIDAPM----------------QKLS 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1032718621 149 GGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:PRK09544 123 GGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHD 180
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-205 |
3.50e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 61.01 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 21 FNCRIDPGEIVILLGPSGTGKTT-FMRLINNLEKcdQGNIAIGDRVLcqetsqgVQYSdKTSQRRY-------QNAIGM- 91
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTlLARMAGLLPG--QGEILLNGRPL-------SDWS-AAELARHraylsqqQSPPFAm 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 92 -VFQNYQLFpnftvldnvleapiAQKLAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMM-LSPEI-- 167
Cdd:COG4138 85 pVFQYLALH--------------QPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqVWPTInp 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1032718621 168 ----ICFDEPTSALDreSANQVG--KLVQAIAKQGKGILVVTHD 205
Cdd:COG4138 151 egqlLLLDEPMNSLD--VAQQAAldRLLRELCQQGITVVMSSHD 192
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-204 |
4.70e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 21 FNCriDPGEIVILLGPSGTGKTTFMRLI---------------------NNLEKCDQG----NIAIGDRVLCQETSQGVQ 75
Cdd:PTZ00265 1189 FSC--DSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndMTNEQDYQGdeeqNVGMKNVNEFSLTKEGGS 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 76 YSDKT------------------SQRRYQNAIGMVFQNYQLFpNFTVLDNVL---------EAPIAQKLAPKSELLDQam 128
Cdd:PTZ00265 1267 GEDSTvfknsgkilldgvdicdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKfgkedatreDVKRACKFAAIDEFIES-- 1343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 129 flldsvgLKDKADA----YPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIA-KQGKGILVVT 203
Cdd:PTZ00265 1344 -------LPNKYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIA 1416
|
.
gi 1032718621 204 H 204
Cdd:PTZ00265 1417 H 1417
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-205 |
5.70e-11 |
|
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: 61.35 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 21 FNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvqysDKTSQRRYQNAIGMVFQNYQLFP 100
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV-----------TADNREAYRQLFSAVFSDFHLFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 101 NFTVLDNVLEAPIAQklapksELLDQaMFLLDSVGLKDkaDAYPST-LSGGQKQRVAIARAMMLSPEIICFDEPTSALD- 178
Cdd:COG4615 420 RLLGLDGEADPARAR------ELLER-LELDHKVSVED--GRFSTTdLSQGQRKRLALLVALLEDRPILVFDEWAADQDp 490
|
170 180 190
....*....|....*....|....*....|....
gi 1032718621 179 -------REsanqvgkLVQAIAKQGKGILVVTHD 205
Cdd:COG4615 491 efrrvfyTE-------LLPELKARGKTVIAISHD 517
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-185 |
6.46e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 61.27 E-value: 6.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 13 NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQetsqgVQYSDKTSQrryqnaIGMV 92
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTK-----LQLDSWRSR------LAVV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 93 FQNYQLFPNfTVLDNV-LEAPIAQKlapksELLDQAMfLLDSV---------GLKDKADAYPSTLSGGQKQRVAIARAMM 162
Cdd:PRK10789 395 SQTPFLFSD-TVANNIaLGRPDATQ-----QEIEHVA-RLASVhddilrlpqGYDTEVGERGVMLSGGQKQRISIARALL 467
|
170 180
....*....|....*....|...
gi 1032718621 163 LSPEIICFDEPTSALDRESANQV 185
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEHQI 490
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-204 |
7.72e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.89 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAY-NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQetsqgvqysdkTSQR 83
Cdd:PRK10790 343 IDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSS-----------LSHS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 84 RYQNAIGMVFQN-----YQLFPNFTVLDNVLEAPIAQKLApKSELLDQAMFLLDsvGLKDKADAYPSTLSGGQKQRVAIA 158
Cdd:PRK10790 412 VLRQGVAMVQQDpvvlaDTFLANVTLGRDISEEQVWQALE-TVQLAELARSLPD--GLYTPLGEQGNNLSVGQKQLLALA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1032718621 159 RAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKgILVVTH 204
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTT-LVVIAH 533
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-178 |
9.49e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.08 E-value: 9.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYN--GNMVIDQFNCRIDPGEIVILLGPSGTGKTT----FMRLINNlekcdQGNIAIgdrvlcqetsQGVQY 76
Cdd:TIGR01271 1218 MDVQGLTAKYTeaGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTllsaLLRLLST-----EGEIQI----------DGVSW 1282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 77 SDKTSQRrYQNAIGMVFQnyQLFpnftvldnVLEAPIAQKLAPKSELLDQAMF-LLDSVGLKDKADAYPS---------- 145
Cdd:TIGR01271 1283 NSVTLQT-WRKAFGVIPQ--KVF--------IFSGTFRKNLDPYEQWSDEEIWkVAEEVGLKSVIEQFPDkldfvlvdgg 1351
|
170 180 190
....*....|....*....|....*....|....
gi 1032718621 146 -TLSGGQKQRVAIARAMMLSPEIICFDEPTSALD 178
Cdd:TIGR01271 1352 yVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
17-216 |
1.93e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.43 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 17 VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKcDQGNIAiGDRVLCQETSQgVQYSDKTSQRRYQNAIGMVFQNY 96
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVT-ADRMRFDDIDL-LRLSPRERRKLVGHNVSMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 97 Q--LFPNFTVLDNVLEA--------PIAQKLAPKSElldQAMFLLDSVGLKDKADA---YPSTLSGGQKQRVAIARAMML 163
Cdd:PRK15093 99 QscLDPSERVGRQLMQNipgwtykgRWWQRFGWRKR---RAIELLHRVGIKDHKDAmrsFPYELTEGECQKVMIAIALAN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1032718621 164 SPEIICFDEPTSALDRESANQVGKLVQAIAK-QGKGILVVTHDTQFGEDFGTRI 216
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKI 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-177 |
1.97e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.56 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 7 NLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCD--QGNIAIGDRVLcqeTSQGVQYSDktsqrr 84
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEEL---QASNIRDTE------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 yQNAIGMVFQNYQLFPNFTVLDNVLeapIAQKLAPKSELLDQAMF-----LLDSVGLKDKADAYPSTLSGGQKQRVAIAR 159
Cdd:PRK13549 81 -RAGIAIIHQELALVKELSVLENIF---LGNEITPGGIMDYDAMYlraqkLLAQLKLDINPATPVGNLGLGQQQLVEIAK 156
|
170
....*....|....*...
gi 1032718621 160 AMMLSPEIICFDEPTSAL 177
Cdd:PRK13549 157 ALNKQARLLILDEPTASL 174
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
27-204 |
2.10e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.86 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 27 PGEIVILLGPSGTGKTTFMRLINNLEKCD--QGNIAIGDRVLCQETsqgvqysdktsqrrYQNAIGMVFQNYQLFPNFTV 104
Cdd:PLN03140 905 PGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQET--------------FARISGYCEQNDIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 105 LDNV-----LEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADAYP--STLSGGQKQRVAIARAMMLSPEIICFDEPTSAL 177
Cdd:PLN03140 971 RESLiysafLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
170 180
....*....|....*....|....*..
gi 1032718621 178 DRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:PLN03140 1051 DARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-205 |
2.69e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.27 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 2 ALIVSNLK-KAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGdrvlcqetsqGVQYSDKT 80
Cdd:COG3845 257 VLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLD----------GEDITGLS 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNaiGMVF-----QNYQLFPNFTVLDN-VLEAPIAQKLAPKselldqamFLLDSVGLKDKA-------------- 140
Cdd:COG3845 327 PRERRRL--GVAYipedrLGRGLVPDMSVAENlILGRYRRPPFSRG--------GFLDRKAIRAFAeelieefdvrtpgp 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 141 DAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:COG3845 397 DTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISED 461
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-204 |
2.99e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.65 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIaigdrvlcqetsQGVQYSDKTSQ 82
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEI------------LFERQSIKKDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPNFTVLDNVLeapIAQKLAPKSELLDQAMFLLDSVGLKDkadaYP-STLSGGQKQRVAIARAM 161
Cdd:PRK13540 70 CTYQKQLCFVGHRSGINPYLTLRENCL---YDIHFSPGAVGITELCRLFSLEHLID----YPcGLLSSGQKRQVALLRLW 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1032718621 162 MLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:PRK13540 143 MSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-205 |
2.99e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 25 IDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDrvlcQETSQgvqysDKTSQRRYQnaiGMVF-----QNYQLF 99
Cdd:PRK15439 286 VRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNG----KEINA-----LSTAQRLAR---GLVYlpedrQSSGLY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 100 pnftvldnvLEAPIAQKLApkSELLDQAMFLLD-------------SVGLK-DKADAYPSTLSGGQKQRVAIARAMMLSP 165
Cdd:PRK15439 354 ---------LDAPLAWNVC--ALTHNRRGFWIKparenavleryrrALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASP 422
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1032718621 166 EIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:PRK15439 423 QLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSD 462
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-204 |
3.65e-10 |
|
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: 57.42 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNM--VIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDrvlcQETSqgvqysdKTSQ 82
Cdd:cd03369 9 VENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG----IDIS-------TIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRYQNAIGMVFQNYQLFPNfTVLDNvleapiaqkLAPKSELLDQAMFlldsVGLKDKADAypSTLSGGQKQRVAIARAMM 162
Cdd:cd03369 78 EDLRSSLTIIPQDPTLFSG-TIRSN---------LDPFDEYSDEEIY----GALRVSEGG--LNLSQGQRQLLCLARALL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1032718621 163 LSPEIICFDEPTSALDRESANQVGKLVQAiAKQGKGILVVTH 204
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIRE-EFTNSTILTIAH 182
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
24-217 |
5.94e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 57.40 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 24 RIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRV---LcqetsqgvqysdktsqrryqnAIGMVFQnyqlfP 100
Cdd:COG1134 48 EVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVsalL---------------------ELGAGFH-----P 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 101 NFTVLDNVL---------EAPIAQKLApkselldqamFLLDSVGLKDKADAyP-STLSGGQKQRVAIARAMMLSPEIICF 170
Cdd:COG1134 102 ELTGRENIYlngrllglsRKEIDEKFD----------EIVEFAELGDFIDQ-PvKTYSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1032718621 171 DEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGTRIV 217
Cdd:COG1134 171 DEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAI 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-205 |
1.38e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.48 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 25 IDPGEIVILLGPSGTGKTTFM-RLINNLEKcdQGNIAIGDRVLCQETSqgvqySDKTSQRRY--QN---AIGM-VFQNYQ 97
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLaRMAGLLPG--SGSIQFAGQPLEAWSA-----AELARHRAYlsQQqtpPFAMpVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 98 LFpnftvldnvlEAPIAQKLAPKSELLDqamfLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMM-LSPEI------ICF 170
Cdd:PRK03695 92 LH----------QPDKTRTEAVASALNE----VAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqVWPDInpagqlLLL 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1032718621 171 DEPTSALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHD 192
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-222 |
1.46e-09 |
|
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: 54.69 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 27 PGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDrvlcqetsqgvqysdktsqrryqnaigmvfqnyqlfpnftvld 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 107 nvleapiaqklapkselLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQV- 185
Cdd:smart00382 38 -----------------GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLl 100
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1032718621 186 -----GKLVQAIAKQGKGILVVTHDTQFGEDFGTRIVSSEEF 222
Cdd:smart00382 101 lleelRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRI 142
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-178 |
2.22e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.67 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 19 DQFNCRIDPGEIVILLGPSGTGKTTFMRLINNL------------EKCDQGNIAIGDRVlcQETSQGVQ-YSDKTsqrry 85
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLlpasegeawlfgQPVDAGDIATRRRV--GYMSQAFSlYGELT----- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 86 qnaigmVFQNY----QLFpnftvldNVLEAPIAQKLApksELLDQamFlldsvGLKDKADAYPSTLSGGQKQRVAIARAM 161
Cdd:NF033858 356 ------VRQNLelhaRLF-------HLPAAEIAARVA---EMLER--F-----DLADVADALPDSLPLGIRQRLSLAVAV 412
|
170
....*....|....*..
gi 1032718621 162 MLSPEIICFDEPTSALD 178
Cdd:NF033858 413 IHKPELLILDEPTSGVD 429
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
27-205 |
2.70e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.56 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 27 PGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETSQGVQYSDKTSQRRYQNAIGMvfqnyqlfpnfTVLD 106
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGM-----------TVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 107 NVL------EAPIAQKLAPKSELLDQAMFLldsVGLKDKADAYPSTLSGGQKQRVAIAraMMLSPEIICF--DEPTSALD 178
Cdd:PRK10575 105 LVAigrypwHGALGRFGAADREKVEEAISL---VGLKPLAHRLVDSLSGGERQRAWIA--MLVAQDSRCLllDEPTSALD 179
|
170 180
....*....|....*....|....*...
gi 1032718621 179 RESANQVGKLVQAIAKQ-GKGILVVTHD 205
Cdd:PRK10575 180 IAHQVDVLALVHRLSQErGLTVIAVLHD 207
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-193 |
6.30e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 6.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 25 IDPGEIVILLGPSGTGKTTFMRLINNleKCDQGNIAIGDRVlcqeTSQGVQYSDKTSQRRyqnaiGMVFQNYQL---FPN 101
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIAS--NTDGFHIGVEGVI----TYDGITPEEIKKHYR-----GDVVYNAETdvhFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 102 FTVLDNVLEAPIAQKLAPKSELLDQAMFLldsvglKDKADAYPSTL------------------SGGQKQRVAIARAMML 163
Cdd:TIGR00956 153 LTVGETLDFAARCKTPQNRPDGVSREEYA------KHIADVYMATYglshtrntkvgndfvrgvSGGERKRVSIAEASLG 226
|
170 180 190
....*....|....*....|....*....|
gi 1032718621 164 SPEIICFDEPTSALDRESANQVGKLVQAIA 193
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSATALEFIRALKTSA 256
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-205 |
6.57e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.36 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 22 NCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLcqetsqgvqysDKTSQRRYQNAIGMVFQNYQLFpn 101
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV-----------TAEQPEDYRKLFSAVFTDFHLF-- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 102 ftvlDNVLEapiAQKLAPKSELLDQamfLLDSVGLKDK---ADAYPST--LSGGQKQRVAIARAMMLSPEIICFDEPTSA 176
Cdd:PRK10522 410 ----DQLLG---PEGKPANPALVEK---WLERLKMAHKlelEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAAD 479
|
170 180 190
....*....|....*....|....*....|...
gi 1032718621 177 LD----RESANQVGKLVQAiakQGKGILVVTHD 205
Cdd:PRK10522 480 QDphfrREFYQVLLPLLQE---MGKTIFAISHD 509
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
146-205 |
7.68e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.25 E-value: 7.68e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 146 TLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESanqVGKLVQAIAKQGKGILVVTHD 205
Cdd:PLN03073 627 TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVLFQGGVLMVSHD 683
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-208 |
9.49e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.98 E-value: 9.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 15 NMVIDQFNCRIDPGEIVILLGPSGTGKTTFMR-LINNLEKCDQGNIAIGDRVlcqetsqgvqysdktsqrRYQNAIGMVF 93
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSV------------------AYVPQVSWIF 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 94 qnyqlfpNFTVLDNVLeapIAQKLapKSELLDQAmflLDSVGLKDKADAYPS-----------TLSGGQKQRVAIARAMM 162
Cdd:PLN03232 692 -------NATVRENIL---FGSDF--ESERYWRA---IDVTALQHDLDLLPGrdlteigergvNISGGQKQRVSMARAVY 756
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1032718621 163 LSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQF 208
Cdd:PLN03232 757 SNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHF 802
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
95-202 |
1.69e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.78 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 95 NYQLFPNFTVLDNVLEAPIA----QKLAPKSELLDQAMflldsvglkdkadaypSTLSGGQKQRVAIARAMMLSPEIICF 170
Cdd:PRK13549 366 ALDRFTGGSRIDDAAELKTIlesiQRLKVKTASPELAI----------------ARLSGGNQQKAVLAKCLLLNPKILIL 429
|
90 100 110
....*....|....*....|....*....|..
gi 1032718621 171 DEPTSALDRESANQVGKLVQAIAKQGKGILVV 202
Cdd:PRK13549 430 DEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI 461
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
30-208 |
1.92e-08 |
|
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: 52.61 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 30 IVILLGPSGTGKTTfmrLINNL------EKCDQGNIAIGDRVLCQETSQGVQYSdktsqRRYQNAIGmvfQNYQLFPNFT 103
Cdd:cd03240 24 LTLIVGQNGAGKTT---IIEALkyaltgELPPNSKGGAHDPKLIREGEVRAQVK-----LAFENANG---KKYTITRSLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 104 VLDNVLEAPIAQKLAPkselldqamfLLDSVGlkdkadaypsTLSGGQKQ------RVAIARAMMLSPEIICFDEPTSAL 177
Cdd:cd03240 93 ILENVIFCHQGESNWP----------LLDMRG----------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNL 152
|
170 180 190
....*....|....*....|....*....|....*
gi 1032718621 178 DRESANQvgKLVQAIAKQGKG----ILVVTHDTQF 208
Cdd:cd03240 153 DEENIEE--SLAEIIEERKSQknfqLIVITHDEEL 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-208 |
3.24e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGdrvlcqeTSQGVQYSDktsQRR 84
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG-------TKLEVAYFD---QHR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 YQnaigmvfqnyqLFPNFTVLDNVLEApiaqklapKSELLDQAM------FLLDSVGLKDKADAYPSTLSGGQKQRVAIA 158
Cdd:PRK11147 392 AE-----------LDPEKTVMDNLAEG--------KQEVMVNGRprhvlgYLQDFLFHPKRAMTPVKALSGGERNRLLLA 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1032718621 159 RAMMLSPEIICFDEPTSALDRESANQVGKLVQAIakQGKgILVVTHDTQF 208
Cdd:PRK11147 453 RLFLKPSNLLILDEPTNDLDVETLELLEELLDSY--QGT-VLLVSHDRQF 499
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
145-203 |
4.62e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 4.62e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1032718621 145 STLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVT 203
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIIS 448
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-205 |
4.74e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.61 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 28 GEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAI-GDRV--------------LCQE--TSQG------VQYSDKTSQRR 84
Cdd:PRK11288 279 GEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdGKPIdirsprdairagimLCPEdrKAEGiipvhsVADNINISARR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 YQNAIGMvfqnyqlfpnftVLDNVLEAPIA----QKLAPKSELLDQAMflldsvglkdkadaypSTLSGGQKQRVAIARa 160
Cdd:PRK11288 359 HHLRAGC------------LINNRWEAENAdrfiRSLNIKTPSREQLI----------------MNLSGGNQQKAILGR- 409
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1032718621 161 mMLSPEI--ICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:PRK11288 410 -WLSEDMkvILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSD 455
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
28-203 |
6.25e-08 |
|
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: 52.13 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 28 GEIVILLGPSGTGKTTFMR-LINNLEKCDQGNIAIgdrvlcqetsQGVQYSDKTSQRRYQNAIGMVFQNYQ---LFPNFT 103
Cdd:TIGR02633 286 GEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFI----------NGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 104 VLDNVLEAPIaQKLAPKSELLDQAMflLDSVG-----LKDKAdAYP----STLSGGQKQRVAIARAMMLSPEIICFDEPT 174
Cdd:TIGR02633 356 VGKNITLSVL-KSFCFKMRIDAAAE--LQIIGsaiqrLKVKT-ASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180
....*....|....*....|....*....
gi 1032718621 175 SALDRESANQVGKLVQAIAKQGKGILVVT 203
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQEGVAIIVVS 460
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-185 |
1.01e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.05 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 22 NCRIDPGEIVILLGPSGTGKTTFMR-LINNLEKCDQGNIAIGDRVlcqetsqgvqysdktsqrRYQNAIGMVFqnyqlfp 100
Cdd:PLN03130 637 NLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTV------------------AYVPQVSWIF------- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 101 NFTVLDNVL-EAPIaqklapKSELLDQAmflLDSVGLKDKADAYPS-----------TLSGGQKQRVAIARAMMLSPEII 168
Cdd:PLN03130 692 NATVRDNILfGSPF------DPERYERA---IDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVY 762
|
170
....*....|....*..
gi 1032718621 169 CFDEPTSALDRESANQV 185
Cdd:PLN03130 763 IFDDPLSALDAHVGRQV 779
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-208 |
1.04e-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: 50.79 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 18 IDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDRVLCQETsqgvqYSDKTSQRRYqnAIGMVFQNYQ 97
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPS-----FEATRSRNRY--SVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 98 LFpNFTVLDNV-LEAPIAQKlapkselldQAMFLLDSVGLKDKADAYPS-----------TLSGGQKQRVAIARAMMLSP 165
Cdd:cd03290 90 LL-NATVEENItFGSPFNKQ---------RYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1032718621 166 EIICFDEPTSALDRESANQVGK--LVQAIAKQGKGILVVTHDTQF 208
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY 204
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-204 |
1.10e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.95 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKKAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLE--KCDQGNIaigdrvlcqeTSQGVQYSDKT 80
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTV----------EFKGKDLLELS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 81 SQRRYQNAIGMVFQNYQLFP---NFTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVG-LKDKADAYPSTL----SGGQK 152
Cdd:PRK09580 72 PEDRAGEGIFMAFQYPVEIPgvsNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIAlLKMPEDLLTRSVnvgfSGGEK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 153 QRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-205 |
1.34e-07 |
|
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: 49.88 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 25 IDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAigdrvlcqetsqgvqysdktsqrryqnaigmvfqnyqlfpnftv 104
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE-------------------------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 105 LDNVLEAPIAQKLapkselldqamflldsvglkdkadaypsTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQ 184
Cdd:cd03222 58 WDGITPVYKPQYI----------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLN 109
|
170 180
....*....|....*....|..
gi 1032718621 185 VGKLVQAIAKQG-KGILVVTHD 205
Cdd:cd03222 110 AARAIRRLSEEGkKTALVVEHD 131
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
130-213 |
3.46e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.73 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 130 LLDSVGLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFG 209
Cdd:NF000106 128 LLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEA 207
|
....
gi 1032718621 210 EDFG 213
Cdd:NF000106 208 EQLA 211
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-208 |
3.90e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 33 LLGPSGTGKTTFMR-----LINNLEKCDQgNIAIGDRVLCQETS--QGVQYSDKTSQRRYQNAIGMVFQNYQL-FPNFTV 104
Cdd:PLN03073 208 LVGRNGTGKTTFLRymamhAIDGIPKNCQ-ILHVEQEVVGDDTTalQCVLNTDIERTQLLEEEAQLVAQQRELeFETETG 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 105 ------LDNVLEAPIAQKLA---PKSELLD------QAMFLLdsVGLKDKADAY---PSTLSGGQKQRVAIARAMMLSPE 166
Cdd:PLN03073 287 kgkganKDGVDKDAVSQRLEeiyKRLELIDaytaeaRAASIL--AGLSFTPEMQvkaTKTFSGGWRMRIALARALFIEPD 364
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1032718621 167 IICFDEPTSALDRESanqVGKLVQAIAKQGKGILVVTHDTQF 208
Cdd:PLN03073 365 LLLLDEPTNHLDLHA---VLWLETYLLKWPKTFIVVSHAREF 403
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
145-205 |
3.99e-07 |
|
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: 48.47 E-value: 3.99e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032718621 145 STLSGGQKQRVAIARAMMLSPE--IICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:cd03238 86 STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-208 |
3.99e-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: 50.33 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 25 IDPGEIVILLGPSGTGKTTFMR-LINNLEKCD-----QGNIA-IGDRVLCQETS--QGVQYSDKTSQRRYQNaigmVFQN 95
Cdd:TIGR00957 661 IPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEghvhmKGSVAyVPQQAWIQNDSlrENILFGKALNEKYYQQ----VLEA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 96 YQLFPNFTVLDNVLEAPIAQKlapkselldqamflldsvGLkdkadaypsTLSGGQKQRVAIARAMMLSPEIICFDEPTS 175
Cdd:TIGR00957 737 CALLPDLEILPSGDRTEIGEK------------------GV---------NLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190
....*....|....*....|....*....|....*....
gi 1032718621 176 ALDresaNQVGKLV--QAIAKQG----KGILVVTHDTQF 208
Cdd:TIGR00957 790 AVD----AHVGKHIfeHVIGPEGvlknKTRILVTHGISY 824
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
147-205 |
7.61e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 7.61e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1032718621 147 LSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSE 454
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-178 |
1.35e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 12 YNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINnlekcdqgniaiGDRvlcqetSQGvqYSDKTS---QRR---- 84
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLIT------------GDH------PQG--YSNDLTlfgRRRgsge 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 85 ----YQNAIGMV----FQNYQLfpNFTVLDNVLEA-----PIAQKLAPKSELLdqAMFLLDSVGL-KDKADAYPSTLSGG 150
Cdd:PRK10938 330 tiwdIKKHIGYVssslHLDYRV--STSVRNVILSGffdsiGIYQAVSDRQQKL--AQQWLDILGIdKRTADAPFHSLSWG 405
|
170 180
....*....|....*....|....*...
gi 1032718621 151 QKQRVAIARAMMLSPEIICFDEPTSALD 178
Cdd:PRK10938 406 QQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
27-204 |
5.70e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 27 PGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDrvlCQETSqgvqysdktSQRRYQNAIGmvfQNYQLFPNFTVLD 106
Cdd:PRK13541 25 PSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKN---CNINN---------IAKPYCTYIG---HNLGLKLEMTVFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 107 NVLeapIAQKLAPKSELLDQAMFLLDsvgLKDKADAYPSTLSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVG 186
Cdd:PRK13541 90 NLK---FWSEIYNSAETLYAAIHYFK---LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLN 163
|
170
....*....|....*...
gi 1032718621 187 KLVQAIAKQGKGILVVTH 204
Cdd:PRK13541 164 NLIVMKANSGGIVLLSSH 181
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
145-217 |
6.76e-06 |
|
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: 45.34 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 145 STLSGGQKQRVAIARAMMLSPEI----------ICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGT 214
Cdd:cd03279 122 STLSGGETFLASLSLALALSEVLqnrggarleaLFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQ 201
|
...
gi 1032718621 215 RIV 217
Cdd:cd03279 202 RLE 204
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
13-204 |
1.04e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 45.90 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 13 NGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGniaigdrVLCQETSQGVQYsdkTSQRRYQnAIGmV 92
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG-------RLTKPAKGKLFY---VPQRPYM-TLG-T 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 93 FQNYQLFPNfTVLDNVLEAPIAQKLAPKSELLDQAMFLLDSVGLKDKADaYPSTLSGGQKQRVAIARAMMLSPEIICFDE 172
Cdd:TIGR00954 531 LRDQIIYPD-SSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQD-WMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|..
gi 1032718621 173 PTSALdreSANQVGKLVQAIAKQGKGILVVTH 204
Cdd:TIGR00954 609 CTSAV---SVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-205 |
1.15e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 12 YNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetSQGVQYSdktsqrryqnaigm 91
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGIKLG-------------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 92 VFQNYQLfpNFTVLDnvlEAPIAQ--KLAPKsELLDQAMFLLDSVGLK-DKADAYPSTLSGGQKQRVAIARAMMLSPEII 168
Cdd:PRK10636 379 YFAQHQL--EFLRAD---ESPLQHlaRLAPQ-ELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLL 452
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1032718621 169 CFDEPTSALD---RESanqvgkLVQAIAKQGKGILVVTHD 205
Cdd:PRK10636 453 LLDEPTNHLDldmRQA------LTEALIDFEGALVVVSHD 486
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
148-220 |
1.44e-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: 45.42 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 148 SGGQKQ------RVAIARAMMLSPEIICFDEPTSALDRESANQVG-KLVQAIAKQGKG----ILVVTHDtqfgEDFGTRI 216
Cdd:TIGR00606 1201 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAhALVEIIKSRSQQrnfqLLVITHD----EDFVELL 1276
|
....
gi 1032718621 217 VSSE 220
Cdd:TIGR00606 1277 GRSE 1280
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-191 |
1.73e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 45.32 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 15 NMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIgdrvlcqetsQGVQYSDktsqrryqnaIGMVFQ 94
Cdd:TIGR00957 1299 DLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII----------DGLNIAK----------IGLHDL 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 95 NYQL--FPNFTVLdnvLEAPIAQKLAPKSELLDQAMFL-LDSVGLKDKADAYPS-----------TLSGGQKQRVAIARA 160
Cdd:TIGR00957 1359 RFKItiIPQDPVL---FSGSLRMNLDPFSQYSDEEVWWaLELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARA 1435
|
170 180 190
....*....|....*....|....*....|.
gi 1032718621 161 MMLSPEIICFDEPTSALDRESANqvgkLVQA 191
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLETDN----LIQS 1462
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
147-202 |
2.70e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 2.70e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 147 LSGGQKQRVAIARAMMLSPEIICFDEPTSALDresanqVG------KLVQAIAKQGKGILVV 202
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGID------VGakyeiyTIINELAAEGKGVIVI 460
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-178 |
8.59e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.04 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 25 IDPGEIVILLGPSGTGKTTFMRLINNLEKCDQGNIAIGDrvlCQETSQGVqysdkTSQRRyqnAIGMVFQNYQLFPNfTV 104
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD---CDVAKFGL-----TDLRR---VLSIIPQSPVLFSG-TV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 105 LDNvleapiaqkLAPKSELLDQAMF-LLDSVGLKDKADAYP-----------STLSGGQKQRVAIARAMMLSPEIICFDE 172
Cdd:PLN03232 1327 RFN---------IDPFSEHNDADLWeALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
....*.
gi 1032718621 173 PTSALD 178
Cdd:PLN03232 1398 ATASVD 1403
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
145-207 |
1.22e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 1.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 145 STLSGGQKQRVAIARAM--MLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQ 207
Cdd:PRK00635 475 ATLSGGEQERTALAKHLgaELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQ 539
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
146-204 |
1.37e-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: 42.31 E-value: 1.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032718621 146 TLSGGQKQRVAIARAmmLS-----PEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:TIGR00630 829 TLSGGEAQRIKLAKE--LSkrstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-205 |
1.50e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.15 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 3 LIVSNLKkAYNGNMVIDqfncrIDPGeIVILLGPSGTGKTTFM---------------RLINNL--EKCDQGNI----AI 61
Cdd:COG0419 5 LRLENFR-SYRDTETID-----FDDG-LNLIVGPNGAGKSTILeairyalygkarsrsKLRSDLinVGSEEASVelefEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 62 GDRVLCQETSQG---VQYSDKTSQRRyqNAIGMVFQNYQLFPNFTVLDNvLEAPIAQKLAPKSELLD-QAMFLLDSVGLK 137
Cdd:COG0419 78 GGKRYRIERRQGefaEFLEAKPSERK--EALKRLLGLEIYEELKERLKE-LEEALESALEELAELQKlKQEILAQLSGLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032718621 138 DkadayPSTLSGGQKQRVAIARAMMLspeIICFdeptSALDRESANQVGKLVQAIAkqgkgilVVTHD 205
Cdd:COG0419 155 P-----IETLSGGERLRLALADLLSL---ILDF----GSLDEERLERLLDALEELA-------IITHV 203
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
147-204 |
2.16e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.69 E-value: 2.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1032718621 147 LSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTH 204
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATH 840
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
145-207 |
2.77e-04 |
|
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: 40.70 E-value: 2.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032718621 145 STLSGGQKQRVAIAR--AMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQ 207
Cdd:cd03270 136 PTLSGGEAQRIRLATqiGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDED 200
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
147-208 |
3.73e-04 |
|
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: 39.65 E-value: 3.73e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032718621 147 LSGGQKQRVAIARAMML-----SPeIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQF 208
Cdd:cd03227 78 LSGGEKELSALALILALaslkpRP-LYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPEL 143
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
5-189 |
4.19e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 40.28 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 5 VSNLKKAYNGNM--VIDQFNCRIDPGEIVILLGPSGTGKTT----FMRLINNLEkcdqGNIAIgdrvlcqetsQGVQYSd 78
Cdd:cd03288 22 IHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSlslaFFRMVDIFD----GKIVI----------DGIDIS- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 79 KTSQRRYQNAIGMVFQNYQLFpnftvldnvlEAPIAQKLAPKSELLDQAMF-LLDSVGLKDKADAYPSTL---------- 147
Cdd:cd03288 87 KLPLHTLRSRLSIILQDPILF----------SGSIRFNLDPECKCTDDRLWeALEIAQLKNMVKSLPGGLdavvteggen 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1032718621 148 -SGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLV 189
Cdd:cd03288 157 fSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVV 199
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
145-217 |
5.31e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 145 STLSGGQKQRVAIARAMMLSP----------EIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQFGEDFGT 214
Cdd:TIGR00618 949 ATLSGGETFLASLSLALALADllstsggtvlDSLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPEFRERIPH 1028
|
...
gi 1032718621 215 RIV 217
Cdd:TIGR00618 1029 RIL 1031
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
147-216 |
5.69e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.38 E-value: 5.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032718621 147 LSGGQKQRVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVThdTQFGE--DFGTRI 216
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVL--NRFDEipDFVQFA 205
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-185 |
8.13e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.15 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 24 RIDPGEIVILLGPSGTGKT----TFMRLInnlEKCDqGNIAIGDRVLcqeTSQGVqysdktsqRRYQNAIGMVFQNYQLF 99
Cdd:PTZ00243 1332 RIAPREKVGIVGRTGSGKStlllTFMRMV---EVCG-GEIRVNGREI---GAYGL--------RELRRQFSMIPQDPVLF 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 100 pNFTVLDNV---LEAPIAQKLAPkselldqamflLDSVGLKDKADAYP-----------STLSGGQKQRVAIARAMMLSP 165
Cdd:PTZ00243 1397 -DGTVRQNVdpfLEASSAEVWAA-----------LELVGLRERVASESegidsrvleggSNYSVGQRQLMCMARALLKKG 1464
|
170 180
....*....|....*....|....*
gi 1032718621 166 E-IICFDEPTS----ALDRESANQV 185
Cdd:PTZ00243 1465 SgFILMDEATAnidpALDRQIQATV 1489
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
145-208 |
9.51e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 9.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032718621 145 STLSGGQKQRVAIARAMMLSPE---IICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQF 208
Cdd:PRK00635 1698 SSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPAL 1764
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
145-205 |
1.03e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 1.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032718621 145 STLSGGQKQRVAIARAMMLS---PEIICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHD 205
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHN 871
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
137-205 |
1.32e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 137 KDKADAYPSTLSGGQKQ------RVAIAR--------AMMLSPEIIcfDEPTSALDRESANQVGKLVQAIAKQGKG-ILV 201
Cdd:PRK02224 772 KDGEPLEPEQLSGGERAlfnlslRCAIYRllaegiegDAPLPPLIL--DEPTVFLDSGHVSQLVDLVESMRRLGVEqIVV 849
|
....
gi 1032718621 202 VTHD 205
Cdd:PRK02224 850 VSHD 853
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-183 |
1.46e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.00 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 10 KAYNGNMVIDQFNCRIDPGEIVILLGPSGTGKTTFMRLINNL------EkcdqgniaiGDRVLCQETsqgVQYSD-KTSQ 82
Cdd:NF040905 9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyE---------GEILFDGEV---CRFKDiRDSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718621 83 RRyqnAIGMVFQNYQLFPNFTVLDNV-LEAPIAQK-LAPKSELLDQAMFLLDSVGLKDKADAYPSTLSGGQKQRVAIARA 160
Cdd:NF040905 77 AL---GIVIIHQELALIPYLSIAENIfLGNERAKRgVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKA 153
|
170 180
....*....|....*....|....
gi 1032718621 161 MMLSPEIICFDEPTSAL-DRESAN 183
Cdd:NF040905 154 LSKDVKLLILDEPTAALnEEDSAA 177
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
167-208 |
3.56e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 38.18 E-value: 3.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1032718621 167 IICFDEPTSALDRESANQVGKLVQAIAKQGKGILVVTHDTQF 208
Cdd:COG4694 520 IVVIDDPVSSLDSNHRFAVASLLKELSKKAKQVIVLTHNLYF 561
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
24-48 |
5.33e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 36.36 E-value: 5.33e-03
10 20
....*....|....*....|....*
gi 1032718621 24 RIDPGEIVILLGPSGTGKTTFMRLI 48
Cdd:cd00009 15 ELPPPKNLLLYGPPGTGKTTLARAI 39
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
146-204 |
6.56e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 37.19 E-value: 6.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032718621 146 TLSGGQKQ------RVAIARAMMLSPEIICFDEPTSALDRESANQVGKLVQAIAKQGKGI---LVVTH 204
Cdd:PRK01156 801 SLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSDIpqvIMISH 868
|
|
| |
