|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-250 |
0e+00 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 512.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSISQQKGLI 80
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQPRT 240
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRT 240
|
250
....*....|
gi 2790487083 241 RQFLEKFLVQ 250
Cdd:PRK11264 241 RQFLEKFLLQ 250
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-247 |
1.04e-165 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 457.15 E-value: 1.04e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSIsqqkglIRSL 83
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKD------INKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQPRTRQF 243
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAF 235
|
....
gi 2790487083 244 LEKF 247
Cdd:COG1126 236 LSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-222 |
5.20e-136 |
|
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: 381.11 E-value: 5.20e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDtaksisQQKGLIRSL 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT------DDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03262 75 RQKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-244 |
9.67e-132 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 372.21 E-value: 9.67e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKS------ISQQ 76
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDrdgelvPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 77 KGLIRsLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
Cdd:COG4598 88 RQLQR-IRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQ 236
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPK 246
|
....*...
gi 2790487083 237 QPRTRQFL 244
Cdd:COG4598 247 SERLRQFL 254
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-245 |
7.41e-112 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 321.27 E-value: 7.41e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSIsqqkglIRSL 83
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVD------ERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQPRTRQF 243
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEF 235
|
..
gi 2790487083 244 LE 245
Cdd:PRK09493 236 LQ 237
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-244 |
3.09e-100 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 295.45 E-value: 3.09e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqKGL 79
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSE----REL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 80 iRSLRQHVGFVFQSFNLFPHRTVLENIiEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:COG1135 78 -RAARRKIGMIFQHFNLLSSRTVAENV-ALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQP 238
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSE 235
|
....*.
gi 2790487083 239 RTRQFL 244
Cdd:COG1135 236 LTRRFL 241
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-244 |
6.09e-98 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 286.14 E-value: 6.09e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSaIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSISQQKglI 80
Cdd:COG4161 1 MS-IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKA--I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAkSLFADPQQPRT 240
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQTEAF 236
|
....
gi 2790487083 241 RQFL 244
Cdd:COG4161 237 AHYL 240
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-248 |
3.01e-96 |
|
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: 282.10 E-value: 3.01e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRV-GDITID----TAKSISQQKG 78
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVeGEQLYHmpgrNGPLVPADEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 79 LIRSLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQ 237
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|.
gi 2790487083 238 PRTRQFLEKFL 248
Cdd:TIGR03005 241 ERTREFLSKVI 251
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-244 |
1.03e-95 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 280.36 E-value: 1.03e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNlVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSISQQKglIR 81
Cdd:PRK11124 2 SIQLNG-INCFYGAHqALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKA--IR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAkSLFADPQQPRTR 241
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQPQTEAFK 237
|
...
gi 2790487083 242 QFL 244
Cdd:PRK11124 238 NYL 240
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-225 |
1.92e-91 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 268.84 E-value: 1.92e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSA-IDVKNLVKKFH----GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisQ 75
Cdd:COG1136 1 MSPlLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSE--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 76 QKGLIRslRQHVGFVFQSFNLFPHRTVLENIiEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
Cdd:COG1136 79 ELARLR--RRHIGFVFQFFNLLPELTALENV-ALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487083 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARdVADRAIFMDQGRIVEQ 225
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgTTIVMVTHDPELAA-RADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-222 |
2.14e-89 |
|
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: 263.20 E-value: 2.14e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqKGL 79
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSE----KEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 80 IRSLRQHVGFVFQSFNLFPHRTVLENIiEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:cd03255 77 AAFRRRHIGFVFQSFNLLPDLTALENV-ELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487083 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDvADRAIFMDQGRI 222
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-244 |
1.55e-88 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 262.60 E-value: 1.55e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSISQQ-----KG 78
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvadKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 79 LIRSLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGLAGK-ETSYPRRLSGGQQQRVAIAR 157
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQ 237
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
....*..
gi 2790487083 238 PRTRQFL 244
Cdd:PRK10619 246 PRLQQFL 252
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-236 |
7.39e-88 |
|
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: 260.21 E-value: 7.39e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTaksisQQKGL 79
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTL-----LSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 80 IRSLRQHVGFVFQSFNLFPHRTVLENIiEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:cd03258 77 LRKARRRIGMIFQHFNLLSSRTVFENV-ALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487083 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQ 236
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELGlTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-241 |
5.61e-86 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 259.65 E-value: 5.61e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDtaksisqqkGLI 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT---------GLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRqHVGFVFQSFNLFPHRTVLENIIEGPViVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:COG3842 74 PEKR-NVGMVFQDYALFPHLTVAENVAFGLR-MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFadpQQPR 239
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIY---ERPA 228
|
..
gi 2790487083 240 TR 241
Cdd:COG3842 229 TR 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-245 |
9.36e-86 |
|
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: 264.07 E-value: 9.36e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKF-----HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSISqqkg 78
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRS---- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 79 lIRSLRQHVGFVFQ----SFNlfPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGL-AGKETSYPRRLSGGQQQRV 153
Cdd:COG1123 337 -LRELRRRVQMVFQdpysSLN--PRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLF 232
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
250
....*....|...
gi 2790487083 233 ADPQQPRTRQFLE 245
Cdd:COG1123 494 ANPQHPYTRALLA 506
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-236 |
1.00e-83 |
|
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: 249.56 E-value: 1.00e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqkglIRS 82
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN--------LRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 LRQHVGFVFQsfN----LFpHRTVLENIIEGPVIvKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
Cdd:COG1122 73 LRRKVGLVFQ--NpddqLF-APTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487083 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQ 236
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-244 |
2.86e-83 |
|
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: 248.74 E-value: 2.86e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqQKGLIRs 82
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLS----EKELYE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 LRQHVGFVFQSFNLFPHRTVLENI----IEGPVIvkgePKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
Cdd:COG1127 80 LRRRIGMLFQGGALFDSLTVFENVafplREHTDL----SEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPqQ 237
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-D 234
|
....*..
gi 2790487083 238 PRTRQFL 244
Cdd:COG1127 235 PWVRQFL 241
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-231 |
1.71e-80 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 241.88 E-value: 1.71e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 2 SAIDVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqKGLi 80
Cdd:COG3638 1 PMLELRNLSKRYPGGTpALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRG----RAL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRQHVGFVFQSFNLFPHRTVLENIIEG--------PVIVKGEPKDEaTARARELLAKVGLAGKETSYPRRLSGGQQQR 152
Cdd:COG3638 76 RRLRRRIGMIFQQFNLVPRLSVLTNVLAGrlgrtstwRSLLGLFPPED-RERALEALERVGLADKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNlHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
3-244 |
1.86e-80 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 241.82 E-value: 1.86e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDtAKSISQQKGLIRS 82
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFD-GQDIYDKKIDVVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 LRQHVGFVFQSFNLFPhRTVLENIIEGPVIVKGEPKDEATARARELLAKVGL----AGKETSYPRRLSGGQQQRVAIARA 158
Cdd:TIGR00972 80 LRRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQP 238
Cdd:TIGR00972 159 LAVEPEVLLLDEPTSALDPIATGKIEELIQELK-KKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEK 237
|
....*.
gi 2790487083 239 RTRQFL 244
Cdd:TIGR00972 238 RTEDYI 243
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-243 |
2.60e-79 |
|
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: 238.56 E-value: 2.60e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSISQQKglirsL 83
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYR-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENIiEGPVIVKGE-PKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENV-AFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADpQQPRTR 241
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKELGlTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS-DDPLVR 233
|
..
gi 2790487083 242 QF 243
Cdd:cd03261 234 QF 235
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-224 |
4.62e-79 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 238.45 E-value: 4.62e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFH----GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtaksisqq 76
Cdd:COG1116 5 APALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 77 kgliRSLRQHVGFVFQSFNLFPHRTVLENIIEGPVIvKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
Cdd:COG1116 76 ----TGPGPDRGVVFQEPALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 157 RALAMRPDVILFDEPTSALDP----ELVGEVLntiRQLAQEKRTMVIVTHemsfarDV------ADRAIFMDQ--GRIVE 224
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDAltreRLQDELL---RLWQETGKTVLFVTH------DVdeavflADRVVVLSArpGRIVE 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-244 |
2.42e-78 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 239.66 E-value: 2.42e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSaIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSISQqkgli 80
Cdd:COG1118 1 MS-IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRE----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 rslRqHVGFVFQSFNLFPHRTVLENIIEGPViVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:COG1118 75 ---R-RVGFVFQHYALFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 161 MRPDVILFDEPTSALD----PELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQ 236
Cdd:COG1118 150 VEPEVLLLDEPFGALDakvrKELRRWLRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPA 226
|
....*...
gi 2790487083 237 QPRTRQFL 244
Cdd:COG1118 227 TPFVARFL 234
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-245 |
1.46e-77 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 233.80 E-value: 1.46e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqkgliRSL 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP---------AEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENIIegpVI--VKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:COG1131 72 RRRIGYVPQEPALYPDLTVRENLR---FFarLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLfadpqqprTR 241
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL--------KA 220
|
....
gi 2790487083 242 QFLE 245
Cdd:COG1131 221 RLLE 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-228 |
4.88e-77 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 232.25 E-value: 4.88e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqKGLIRS 82
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLK-----RREIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 LRQHVGFVFQSFNLFPHRTVLENIiEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:COG2884 77 LRRRIGVVFQDFRLLPDRTVYENV-ALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487083 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-244 |
2.92e-76 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 234.31 E-value: 2.92e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTAKSisqQKGL 79
Cdd:PRK11153 2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDL-TALS---EKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 80 iRSLRQHVGFVFQSFNLFPHRTVLENIIEgPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:PRK11153 78 -RKARRQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQP 238
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHP 235
|
....*.
gi 2790487083 239 RTRQFL 244
Cdd:PRK11153 236 LTREFI 241
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-245 |
1.64e-75 |
|
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: 229.30 E-value: 1.64e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKF----HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtaksisqQKG 78
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV--------TRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 79 LIRSLRQHVGFVFQ----SFNlfPHRTVLENIIEgPVIVKGEPKDEAtaRARELLAKVGLAGKE-TSYPRRLSGGQQQRV 153
Cdd:COG1124 73 RRKAFRRRVQMVFQdpyaSLH--PRHTVDRILAE-PLRIHGLPDREE--RIAELLEQVGLPPSFlDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLF 232
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|...
gi 2790487083 233 ADPQQPRTRQFLE 245
Cdd:COG1124 228 AGPKHPYTRELLA 240
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-221 |
5.37e-74 |
|
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: 222.83 E-value: 5.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTaksisqQKGLIRSL 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTD------LEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENIIEGpvivkgepkdeatararellakvglagketsyprrLSGGQQQRVAIARALAMRP 163
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-231 |
8.44e-74 |
|
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: 224.75 E-value: 8.44e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtaksISQQKGLIRS 82
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDI-----NKLKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 LRQHVGFVFQSFNLFPHRTVLENIIEGPVIVK-------GEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
Cdd:cd03256 76 LRRQIGMIFQQFNLIERLSVLENVLSGRLGRRstwrslfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487083 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-226 |
1.98e-73 |
|
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: 222.78 E-value: 1.98e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTAKSISqqkglirsl 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPE--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENIIEGPViVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGLK-LRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-235 |
3.98e-72 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 224.18 E-value: 3.98e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTaksisqqkglI 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD----------L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRQHVGFVFQSFNLFPHRTVLENIiEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:COG3839 71 PPKDRNIAMVFQSYALYPHMTVYENI-AFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHE----MSFardvADRAIFMDQGRIVEQGPAKSLFADP 235
Cdd:COG3839 150 REPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-225 |
7.37e-72 |
|
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: 218.88 E-value: 7.37e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHG----QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDitidtaKSISQQkgl 79
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG------EPVTGP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 80 irslRQHVGFVFQSFNLFPHRTVLENIIEGPVIvKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:cd03293 72 ----GPDRGYVFQQDALLPWLTVLDNVALGLEL-QGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487083 160 AMRPDVILFDEPTSALDP---ELVGEVLntIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQ--GRIVEQ 225
Cdd:cd03293 147 AVDPDVLLLDEPFSALDAltrEQLQEEL--LDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-244 |
9.92e-72 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 221.50 E-value: 9.92e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDitidtaKSISQQKglIRS 82
Cdd:COG1125 2 IEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDG------EDIRDLD--PVE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 LRQHVGFVFQSFNLFPHRTVLENIiegpVIV---KGEPKDEATARARELLAKVGLAGKETS--YPRRLSGGQQQRVAIAR 157
Cdd:COG1125 74 LRRRIGYVIQQIGLFPHMTVAENI----ATVprlLGWDKERIRARVDELLELVGLDPEEYRdrYPHELSGGQQQRVGVAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 158 ALAMRPDVILFDEPTSALDP----ELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:COG1125 150 ALAADPPILLMDEPFGALDPitreQLQDELLRLQREL---GKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILA 226
|
250
....*....|.
gi 2790487083 234 DPQQPRTRQFL 244
Cdd:COG1125 227 NPANDFVADFV 237
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-231 |
3.34e-71 |
|
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: 217.43 E-value: 3.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDtAKSISQQKGLIRSL 83
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLD-GKDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPhRTVLENIIEGPVIVKGEPKDEATARARELLAKVGLAG--KETSYPRRLSGGQQQRVAIARALAM 161
Cdd:cd03260 80 RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-244 |
6.22e-71 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 217.98 E-value: 6.22e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 2 SAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTiRV-GDITIDtAKSISQQKGLI 80
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGA-RVeGEILLD-GEDIYDPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRQHVGFVFQSFNLFPHrTVLENIIEGPVIVKGEPKDEATARARELLAKVGL----AGKETSYPRRLSGGQQQRVAIA 156
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQ 236
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDPISTAKIEELILELK-KDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPK 245
|
....*...
gi 2790487083 237 QPRTRQFL 244
Cdd:COG1117 246 DKRTEDYI 253
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-226 |
1.96e-70 |
|
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: 215.45 E-value: 1.96e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqKGL 79
Cdd:cd03257 2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLS-----RRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 80 IRSLRQHVGFVFQ----SFNlfPHRTVLENIIEGPVIVKGEPKDEATARAR-ELLAKVGLAGK-ETSYPRRLSGGQQQRV 153
Cdd:cd03257 77 RKIRRKEIQMVFQdpmsSLN--PRMTIGEQIAEPLRIHGKLSKKEARKEAVlLLLVGVGLPEEvLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487083 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELgLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-241 |
2.25e-70 |
|
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: 218.38 E-value: 2.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI-NLLEQP--EGGTIRVGDITIDTAKsisqQ 76
Cdd:COG0444 2 LEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlGLLPPPgiTSGEILFDGEDLLKLS----E 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 77 KGLiRSLR-QHVGFVFQ----SFNlfPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGLAGKET---SYPRRLSGG 148
Cdd:COG0444 78 KEL-RKIRgREIQMIFQdpmtSLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERrldRYPHELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGlAILFITHDLGVVAEIADRVAVMYAGRIVEEGP 234
|
250
....*....|....
gi 2790487083 228 AKSLFADPQQPRTR 241
Cdd:COG0444 235 VEELFENPRHPYTR 248
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-221 |
2.40e-70 |
|
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: 214.64 E-value: 2.40e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 6 VKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqkglIRSL 83
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS--------LKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNL-FPHRTVLENIIEGPVIvKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:cd03225 74 RRKVGLVFQNPDDqFFGPTVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487083 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-247 |
1.46e-68 |
|
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: 212.31 E-value: 1.46e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 16 QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTaksisQQKGLIRSLRQHVGFVFQsfn 95
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITA-----KKKKKLKDLRKKVGLVFQ--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 96 lFPH-----RTVLENIIEGPVIVkGEPKDEATARARELLAKVGL--AGKETSyPRRLSGGQQQRVAIARALAMRPDVILF 168
Cdd:TIGR04521 90 -FPEhqlfeETVYKDIAFGPKNL-GLSEEEAEERVKEALELVGLdeEYLERS-PFELSGGQMRRVAIAGVLAMEPEVLIL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 169 DEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPqqprtrQFLEKF 247
Cdd:TIGR04521 167 DEPTAGLDPKGRKEILDLFKRLHKEKgLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV------DELEKI 240
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-237 |
3.79e-67 |
|
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: 215.92 E-value: 3.79e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLeQPEGGTIRvGDITIDtAKSISQQKGLI 80
Cdd:COG1123 4 LLEVRDLSVRYPGGDvpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL-LPHGGRIS-GEVLLD-GRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSlrQHVGFVFQSF--NLFPHrTVLENIIEGPVIvKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
Cdd:COG1123 81 RG--RRIGMVFQDPmtQLNPV-TVGDQIAEALEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQ 237
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-228 |
7.36e-67 |
|
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: 206.52 E-value: 7.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 2 SAIDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDitidtaKSISQ-- 75
Cdd:COG4181 7 PIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAG------QDLFAld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 76 QKGLIRSLRQHVGFVFQSFNLFPHRTVLENIIEgPVIVKGEPkdEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
Cdd:COG4181 81 EDARARLRARHVGFVFQSFQLLPTLTALENVML-PLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487083 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDvADRAIFMDQGRIVEQGPA 228
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGtTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAA 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-246 |
6.68e-66 |
|
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: 204.46 E-value: 6.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDitidtaKSISQQKGLirS 82
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDG------EDIREQDPV--E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 LRQHVGFVFQSFNLFPHRTVLENIIEGPVIvKGEPKDEATARARELLAKVGLAGKE--TSYPRRLSGGQQQRVAIARALA 160
Cdd:cd03295 73 LRRKIGYVIQQIGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQPR 239
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDF 231
|
....*..
gi 2790487083 240 TRQFLEK 246
Cdd:cd03295 232 VAEFVGA 238
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-234 |
7.95e-66 |
|
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: 204.45 E-value: 7.95e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgDITIDtAKSISQQKGL-IR 81
Cdd:TIGR02315 2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSG-----SILLE-GTDITKLRGKkLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVK-------GEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVA 154
Cdd:TIGR02315 76 KLRRRIGMIFQHYNLIERLTVLENVLHGRLGYKptwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINlHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
.
gi 2790487083 234 D 234
Cdd:TIGR02315 236 E 236
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-234 |
3.43e-65 |
|
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: 203.43 E-value: 3.43e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSISQqkglir 81
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWE------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 sLRQHVGFVFQS-FNLFPHRTV-------LENIiegpvivkGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRV 153
Cdd:TIGR04520 75 -IRKKVGMVFQNpDNQFVGATVeddvafgLENL--------GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLF 232
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIF 224
|
..
gi 2790487083 233 AD 234
Cdd:TIGR04520 225 SQ 226
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-235 |
8.32e-65 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 206.49 E-value: 8.32e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKF-----------------------HGQTV-LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPE 56
Cdd:COG4175 1 MPKIEVRNLYKIFgkrperalklldqgkskdeilekTGQTVgVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 57 GGTIRVGDITIDTAKsisqQKGLIRSLRQHVGFVFQSFNLFPHRTVLENIiEGPVIVKGEPKDEATARARELLAKVGLAG 136
Cdd:COG4175 81 AGEVLIDGEDITKLS----KKELRELRRKKMSMVFQHFALLPHRTVLENV-AFGLEIQGVPKAERRERAREALELVGLAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 137 KETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP----ELVGEVLntirQL-AQEKRTMVIVTHEMSFARDVA 211
Cdd:COG4175 156 WEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrEMQDELL----ELqAKLKKTIVFITHDLDEALRLG 231
|
250 260
....*....|....*....|....
gi 2790487083 212 DRAIFMDQGRIVEQGPAKSLFADP 235
Cdd:COG4175 232 DRIAIMKDGRIVQIGTPEEILTNP 255
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-244 |
1.86e-64 |
|
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: 200.64 E-value: 1.86e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDItiDTAKSISQQKGlirs 82
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE--DATDVPVQERN---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 lrqhVGFVFQSFNLFPHRTVLENIIEGPVIVKGE---PKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:cd03296 76 ----VGFVFQHYALFRHMTVFDNVAFGLRVKPRSerpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQP 238
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASP 231
|
....*.
gi 2790487083 239 RTRQFL 244
Cdd:cd03296 232 FVYSFL 237
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-245 |
1.93e-64 |
|
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: 201.72 E-value: 1.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 7 KNLVKKFHGQTV-LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVG--DITIDTAKSISQqkglIRsl 83
Cdd:cd03294 27 KEEILKKTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDgqDIAAMSRKELRE----LR-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENIIEGpVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03294 101 RKKISMVFQSFALLPHRTVLENVAFG-LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQPRTRQ 242
Cdd:cd03294 180 DILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVRE 259
|
...
gi 2790487083 243 FLE 245
Cdd:cd03294 260 FFR 262
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-244 |
1.94e-63 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 198.06 E-value: 1.94e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTvLHgIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTAKSISQQKglirsl 83
Cdd:COG3840 2 LRLDDLTYRYGDFP-LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-TALPPAERP------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 rqhVGFVFQSFNLFPHRTVLENIIEG--PvivKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:COG3840 73 ---VSMLFQENNLFPHLTVAQNIGLGlrP---GLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQPRT 240
Cdd:COG3840 147 KRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
....
gi 2790487083 241 RQFL 244
Cdd:COG3840 227 AAYL 230
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-247 |
3.10e-62 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 198.72 E-value: 3.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVG--DITidtakSISQQKg 78
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGgrDIT-----RLPPQK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 79 lirslrQHVGFVFQSFNLFPHRTVLENIIEGpVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
Cdd:TIGR03265 76 ------RDYGIVFQSYALFPNLTVADNIAYG-LKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFadpQQ 237
Cdd:TIGR03265 149 LATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIY---RH 225
|
250
....*....|
gi 2790487083 238 PRTRqFLEKF 247
Cdd:TIGR03265 226 PATP-FVADF 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-248 |
3.52e-62 |
|
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: 194.76 E-value: 3.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDitidtaKSISQqkglIRSL 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG------KDITN----LPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENIIEGpVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03300 71 KRPVNTVFQNYALFPHLTVFENIAFG-LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFadpQQPRTRq 242
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIY---EEPANR- 225
|
....*.
gi 2790487083 243 FLEKFL 248
Cdd:cd03300 226 FVADFI 231
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-222 |
2.05e-61 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 191.95 E-value: 2.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqkglIRSL 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP--------PPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHrTVLENIIEGPVIVKGEPKDEataRARELLAKVGLA----GKETSyprRLSGGQQQRVAIARAL 159
Cdd:COG4619 73 RRQVAYVPQEPALWGG-TVRDNLPFPFQLRERKFDRE---RALELLERLGLPpdilDKPVE---RLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487083 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEgRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-236 |
3.09e-61 |
|
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: 192.27 E-value: 3.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTAKSISQ--QKGLIR 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI-TGLPPHEiaRLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SlrqhvgfvFQSFNLFPHRTVLENIIEGPVIVKGEP---------KDEATARARELLAKVGLAGKETSYPRRLSGGQQQR 152
Cdd:cd03219 80 T--------FQIPRLFPELTVLENVMVAAQARTGSGlllararreEREARERAEELLERVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLF 232
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
....
gi 2790487083 233 ADPQ 236
Cdd:cd03219 232 NNPR 235
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-236 |
1.80e-60 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 191.02 E-value: 1.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTAKSISQ--QKG 78
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-TGLPPHRiaRLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 79 LIRSlrqhvgfvFQSFNLFPHRTVLENIIEGPVIVKGEP--------------KDEATARARELLAKVGLAGKETSYPRR 144
Cdd:COG0411 81 IART--------FQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreEREARERAEELLERVGLADRADEPAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 145 LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
250
....*....|...
gi 2790487083 224 EQGPAKSLFADPQ 236
Cdd:COG0411 233 AEGTPAEVRADPR 245
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-232 |
2.64e-60 |
|
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: 190.64 E-value: 2.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDitidtaKSISQQKGliRS 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG------RDLASLSR--RE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 LRQHVGFVFQS----FNL----------FPHRTVLeniiegpvivkGEPKDEATARARELLAKVGLAGKETSYPRRLSGG 148
Cdd:COG1120 73 LARRIAYVPQEppapFGLtvrelvalgrYPHLGLF-----------GRPSAEDREAVEEALERTGLEHLADRPVDELSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
Cdd:COG1120 142 ERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
....*
gi 2790487083 228 AKSLF 232
Cdd:COG1120 222 PEEVL 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-248 |
7.12e-60 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 192.63 E-value: 7.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgDITID----TAKSISQQKGL 79
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEG-----QIFIDgedvTHRSIQQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 80 IrslrqhvgfVFQSFNLFPHRTVLENIIEGpVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:PRK11432 82 M---------VFQSYALFPHMSLGENVGYG-LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFadpQQP 238
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY---RQP 228
|
250
....*....|
gi 2790487083 239 RTRqFLEKFL 248
Cdd:PRK11432 229 ASR-FMASFM 237
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-222 |
7.87e-60 |
|
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: 186.45 E-value: 7.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqkgliRSL 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP---------EEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENIiegpvivkgepkdeatararellakvglagketsyprRLSGGQQQRVAIARALAMRP 163
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-241 |
2.65e-59 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 190.33 E-value: 2.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKF---------HGQTV--LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVG--DITidta 70
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqDIT---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 71 kSISQQKglIRSLRQHVGFVFQ----SFNlfPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGL----AGKetsYP 142
Cdd:COG4608 84 -GLSGRE--LRPLRRRMQMVFQdpyaSLN--PRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrpehADR---YP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 143 RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQG 220
Cdd:COG4608 156 HEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDL-QDELglTYLFISHDLSVVRHISDRVAVMYLG 234
|
250 260
....*....|....*....|.
gi 2790487083 221 RIVEQGPAKSLFADPQQPRTR 241
Cdd:COG4608 235 KIVEIAPRDELYARPLHPYTQ 255
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-250 |
5.09e-59 |
|
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: 186.99 E-value: 5.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqkgliRSL 83
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP---------REA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENI-IEGPVivKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIrYFAEL--YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLfadpQQPRTRQ 242
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL----REEIGEE 226
|
....*...
gi 2790487083 243 FLEKFLVQ 250
Cdd:COG4555 227 NLEDAFVA 234
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-217 |
2.84e-58 |
|
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: 183.97 E-value: 2.84e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDItiDTAKSISQQKGLIRslRQ 85
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQ--ETPPLNSKKASKFR--RE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 86 HVGFVFQSFNLFPHRTVLENIIEGPVIVKGePKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKL-SKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2790487083 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFM 217
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-232 |
2.40e-57 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 182.60 E-value: 2.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAksisqqkgli 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 rslRQHVGFVFQSFNL---FPhRTVLEniiegpvIVK----------GEPKDEATARARELLAKVGLAGKETSYPRRLSG 147
Cdd:COG1121 74 ---RRRIGYVPQRAEVdwdFP-ITVRD-------VVLmgrygrrglfRRPSRADREAVDEALERVGLEDLADRPIGELSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEqGP 227
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GP 221
|
....*
gi 2790487083 228 AKSLF 232
Cdd:COG1121 222 PEEVL 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-233 |
2.83e-57 |
|
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: 193.51 E-value: 2.83e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtaKSISqqkglI 80
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL---RQID-----P 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRQHVGFVFQSFNLFpHRTVLENIIEGpvivkgepKDEAT-ARARELLAKVGLAGKETSYP-----------RRLSGG 148
Cdd:COG2274 545 ASLRRQIGVVLQDVFLF-SGTIRENITLG--------DPDATdEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPA 228
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTH 693
|
....*
gi 2790487083 229 KSLFA 233
Cdd:COG2274 694 EELLA 698
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-234 |
2.09e-56 |
|
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: 179.55 E-value: 2.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKkFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSIsqqkgliRS 82
Cdd:cd03224 1 LEVENLNA-GYGKSqILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH-------ER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 LRQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKDEATARARELLAKvgLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:cd03224 73 ARAGIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487083 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFAD 234
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-245 |
2.96e-56 |
|
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: 187.97 E-value: 2.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHG----QTVLHGIDLEVEQGEVVAIIGPSGSGKT-TLLRSINLLeqPEGGTIRVGDITID----TAK 71
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLL--PDPAAHPSGSILFDgqdlLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 72 SISQqkglIRSLR-QHVGFVFQ----SFNlfPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGLAGKET---SYPR 143
Cdd:COG4172 82 SERE----LRRIRgNRIAMIFQepmtSLN--PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERrldAYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 144 RLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMaLLLITHDLGVVRRFADRVAVMRQGEI 235
|
250 260
....*....|....*....|...
gi 2790487083 223 VEQGPAKSLFADPQQPRTRQFLE 245
Cdd:COG4172 236 VEQGPTAELFAAPQHPYTRKLLA 258
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-248 |
9.37e-56 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 182.21 E-value: 9.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSaIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDitidtaKSISQqkglI 80
Cdd:PRK10851 1 MS-IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG------TDVSR----L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRQHVGFVFQSFNLFPHRTVLENIIEG-PVIVKGEPKDEATARAR--ELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:PRK10851 70 HARDRKVGFVFQHYALFRHMTVFDNIAFGlTVLPRRERPNAAAIKAKvtQLLEMVQLAHLADRYPAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQ 236
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPA 229
|
250
....*....|..
gi 2790487083 237 qprTRQFLEkFL 248
Cdd:PRK10851 230 ---TRFVLE-FM 237
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-250 |
2.33e-55 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 179.51 E-value: 2.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQT-----VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTI----------------RV 62
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 63 GDITIDTAKSISQQKGLIRSLRQHVGFVFQ--SFNLFpHRTVLENIIEGPVIVkGEPKDEATARARELLAKVGLagkETS 140
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGL---DES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 141 Y----PRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIF 216
Cdd:PRK13651 158 YlqrsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIF 237
|
250 260 270
....*....|....*....|....*....|....
gi 2790487083 217 MDQGRIVEQGPAKSLFADpqqprtrqflEKFLVQ 250
Cdd:PRK13651 238 FKDGKIIKDGDTYDILSD----------NKFLIE 261
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-226 |
4.02e-55 |
|
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: 175.91 E-value: 4.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDItiDTAKSISQQKGlirsl 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR--DVTDLPPKDRD----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 rqhVGFVFQSFNLFPHRTVLENIiEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03301 74 ---IAMVFQNYALYPHMTVYDNI-AFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-245 |
6.81e-55 |
|
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: 184.12 E-value: 6.81e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQ-----------TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI-NLLEQpeGGTIRVGDITIDTAK 71
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALlRLIPS--EGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 72 sisqQKGLiRSLRQHVGFVFQ----SFNlfPHRTVLENIIEGPVIVK-GEPKDEATARARELLAKVGL-AGKETSYPRRL 145
Cdd:COG4172 354 ----RRAL-RPLRRRMQVVFQdpfgSLS--PRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLdPAARHRYPHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 146 SGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDL-QREHglAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
250 260
....*....|....*....|..
gi 2790487083 224 EQGPAKSLFADPQQPRTRQFLE 245
Cdd:COG4172 506 EQGPTEQVFDAPQHPYTRALLA 527
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-245 |
9.92e-55 |
|
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: 184.58 E-value: 9.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtaKSISQQkgli 80
Cdd:COG4987 333 SLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL---RDLDED---- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 rSLRQHVGFVFQSFNLFpHRTVLENIIegpvIVKGEPKDEAtarARELLAKVGLAGKETSYP-----------RRLSGGQ 149
Cdd:COG4987 406 -DLRRRIAVVPQRPHLF-DTTLRENLR----LARPDATDEE---LWAALERVGLGDWLAALPdgldtwlgeggRRLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAK 229
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG-RTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHE 554
|
250
....*....|....*.
gi 2790487083 230 SLFAdpQQPRTRQFLE 245
Cdd:COG4987 555 ELLA--QNGRYRQLYQ 568
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-236 |
1.85e-54 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 176.75 E-value: 1.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqQKGLiRSLRQHVGFVFQsfnlFP 98
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKK---NKKL-KPLRKKVGIVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 99 H-----RTVLENIIEGPvIVKGEPKDEATARARELLAKVGLAGK-ETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:PRK13634 95 EhqlfeETVEKDICFGP-MNFGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487083 173 SALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQ 236
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKEKGlTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-221 |
2.20e-54 |
|
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: 172.57 E-value: 2.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHG--QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqkglIR 81
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD--------LE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SLRQHVGFVFQSFNLFpHRTVLENIiegpvivkgepkdeatararellakvglagketsyprrLSGGQQQRVAIARALAM 161
Cdd:cd03228 73 SLRKNIAYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGR 221
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAKG-KTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
11-246 |
4.20e-54 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 178.12 E-value: 4.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 11 KKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgDITIDTAKSISQQKGLIRSL-RQHVGF 89
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAG-----QIFIDGENIMKQSPVELREVrRKKIGM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 90 VFQSFNLFPHRTVLENIIEGPVIVkGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFD 169
Cdd:TIGR01186 76 VFQQFALFPHMTILQNTSLGPELL-GWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487083 170 EPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQPRTRQFLEK 246
Cdd:TIGR01186 155 EAFSALDPLIRDSMQDELKKLqATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-236 |
5.14e-54 |
|
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: 174.01 E-value: 5.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVG--DITIDTAKSISqqkg 78
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgeDITGLPPHRIA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 79 lirslRQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKDEATA--------RARELLAKvgLAGketsyprRLSGGQQ 150
Cdd:COG0410 77 -----RLGIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLervyelfpRLKERRRQ--RAG-------TLSGGEQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKS 230
Cdd:COG0410 143 QMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAE 222
|
....*.
gi 2790487083 231 LFADPQ 236
Cdd:COG0410 223 LLADPE 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-227 |
9.32e-54 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 182.29 E-value: 9.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLE---QPEGGTIRVGDITIdtaKSISQQkglirSLRQHVGFVF 91
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTL---VNLLLrfyDPTSGRILIDGVDI---RDLTLE-----SLRRQIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 92 QSFNLFpHRTVLENIIEGpvivkgepKDEAT----------ARARELLAK--------VGLAGketsypRRLSGGQQQRV 153
Cdd:COG1132 421 QDTFLF-SGTIRENIRYG--------RPDATdeeveeaakaAQAHEFIEAlpdgydtvVGERG------VNLSGGQRQRI 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487083 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGP 227
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMKG-RTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-221 |
1.47e-53 |
|
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: 170.12 E-value: 1.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtaksisqQKGLIRSLRQ 85
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI--------AKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 86 HVGFVFQsfnlfphrtvleniiegpvivkgepkdeatararellakvglagketsyprrLSGGQQQRVAIARALAMRPDV 165
Cdd:cd00267 74 RIGYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487083 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-222 |
1.55e-53 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 172.21 E-value: 1.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqKGLIRS 82
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLR-----GRAIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 LRQHVGFVFQSFNLFPHRTVLENIIEgPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:cd03292 76 LRRKIGVVFQDFRLLPDRNVYENVAF-ALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-235 |
1.93e-53 |
|
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: 176.06 E-value: 1.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 22 IDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITI-DTAKSISqqkglIRSLRQHVGFVFQSFNLFPHR 100
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqDSARGIF-----LPPHRRRIGYVFQEARLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 101 TVLENIIEGpviVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELV 180
Cdd:COG4148 93 SVRGNLLYG---RKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487083 181 GEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADP 235
Cdd:COG4148 170 AEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-235 |
2.26e-53 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 176.68 E-value: 2.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDtakSISQQKglirsl 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT---HVPAEN------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 rQHVGFVFQSFNLFPHRTVLENIIEGpVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:PRK09452 86 -RHVNTVFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADP 235
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKAL-QRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-226 |
3.93e-53 |
|
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: 169.92 E-value: 3.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 5 DVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqkgliRSLR 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSP--------KELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 85 QHVGFVFQSfnlfphrtvleniiegpvivkgepkdeatararelLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPD 164
Cdd:cd03214 73 RKIAYVPQA-----------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 165 VILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERgKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-221 |
2.03e-52 |
|
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: 169.35 E-value: 2.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSiSQqkglIRS 82
Cdd:TIGR02673 2 IEFHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRG-RQ----LPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 LRQHVGFVFQSFNLFPHRTVLENIIEgPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:TIGR02673 77 LRRRIGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487083 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:TIGR02673 156 PPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-233 |
3.68e-52 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 170.58 E-value: 3.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqkglIR 81
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET--------VW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SLRQHVGFVFQS-FNLFPHRTV-------LENIiegpvivkGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRV 153
Cdd:PRK13635 78 DVRRQVGMVFQNpDNQFVGATVqddvafgLENI--------GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDvADRAIFMDQGRIVEQGPAKSLF 232
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLsITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
.
gi 2790487083 233 A 233
Cdd:PRK13635 229 K 229
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-173 |
2.05e-51 |
|
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: 164.36 E-value: 2.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtaksisqQKGLIRSLRQHVGFVFQSFNLFP 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL--------TDDERKSLRKEIGYVFQDPQLFP 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487083 99 HRTVLENIIEGpVIVKGEPKDEATARARELLAKVGLAGKE----TSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:pfam00005 73 RLTVRENLRLG-LLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-233 |
2.38e-51 |
|
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: 175.33 E-value: 2.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 2 SAIDVKNLVKKFH-GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqkgli 80
Cdd:COG4988 335 PSIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDP-------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRQHVGFVFQSFNLFpHRTVLENIIEGpvivKGEPKDEATARArelLAKVGLAGKETSYP-----------RRLSGGQ 149
Cdd:COG4988 407 ASWRRQIAWVPQNPYLF-AGTIRENLRLG----RPDASDEELEAA---LEAAGLDEFVAALPdgldtplgeggRGLSGGQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAK 229
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG-RTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHE 556
|
....
gi 2790487083 230 SLFA 233
Cdd:COG4988 557 ELLA 560
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-226 |
2.67e-51 |
|
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: 166.32 E-value: 2.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 22 IDLEVEqGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTaksiSQQKGLIRSLRQHVGFVFQSFNLFPHRT 101
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD----SRKKINLPPQQRKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 102 VLENIIEGpviVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVG 181
Cdd:cd03297 92 VRENLAFG---LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2790487083 182 EVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03297 169 QLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-244 |
4.83e-51 |
|
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: 166.36 E-value: 4.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFhGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVG--DITidtaksisqqkgLIR 81
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkDIT------------NLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SLRQHVGFVFQSFNLFPHRTVLENIIEGpVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:cd03299 68 PEKRDISYVPQNYALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQPRT 240
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFV 226
|
....
gi 2790487083 241 RQFL 244
Cdd:cd03299 227 AEFL 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-247 |
2.50e-50 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 174.14 E-value: 2.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqKGLIRSLRQHVGFVFQSFNLF 97
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDA----DALAQLRREHFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 98 PHRTVLENIiEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:PRK10535 99 SHLTAAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487083 178 ELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAK--------SLFADPQQPRTRQFLEKF 247
Cdd:PRK10535 178 HSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQekvnvaggTEPVVNTASGWRQFVSGF 254
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-239 |
6.84e-50 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 164.48 E-value: 6.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqKGLIRs 82
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDK-----KSLLE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 LRQHVGFVFQSFN--LFPhRTVLENIIEGPVIVkGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK13639 76 VRKTVGIVFQNPDdqLFA-PTVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487083 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQPR 239
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
18-222 |
1.08e-49 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 162.20 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTAKSISQQKGLIRSLrqhVGFVFQSFNLF 97
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEV-TNLSYSQKIILRREL---IGYIFQSFNLI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 98 PHRTVLENIiEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:NF038007 96 PHLSIFDNV-ALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2790487083 178 ELVGEVLNTIRQLAQEKRTMVIVTHEMSfARDVADRAIFMDQGRI 222
Cdd:NF038007 175 KNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-244 |
2.77e-49 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 164.75 E-value: 2.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNL--VKK--FHGQ-TV--LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDItiDTAKSi 73
Cdd:PRK11308 6 LQAIDLKKHypVKRglFKPErLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQ--DLLKA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 74 sqQKGLIRSLRQHVGFVFQ----SFNlfPHRTVlENIIEGPVIVKGE-PKDEATARARELLAKVGLAGKETS-YPRRLSG 147
Cdd:PRK11308 83 --DPEAQKLLRQKIQIVFQnpygSLN--PRKKV-GQILEEPLLINTSlSAAERREKALAMMAKVGLRPEHYDrYPHMFSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsYVFISHDLSVVEHIADEVMVMYLGRCVEKG 237
|
250
....*....|....*...
gi 2790487083 227 PAKSLFADPQQPRTRQFL 244
Cdd:PRK11308 238 TKEQIFNNPRHPYTQALL 255
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-226 |
1.49e-48 |
|
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: 159.24 E-value: 1.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidtaksisqqKGL-IRSLR 84
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV--------------FGKpLEKER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 85 QHVGFVFQSFNL---FPhRTVLENIIEGPVIVKG---EPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
Cdd:cd03235 68 KRIGYVPQRRSIdrdFP-ISVRDVVLMGLYGHKGlfrRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487083 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDqGRIVEQG 226
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-231 |
6.73e-48 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 164.81 E-value: 6.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVG--DITIDTAKSiSQQKGli 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgePVRFRSPRD-AQAAG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 rslrqhVGFVFQSFNLFPHRTVLENI-----IEGPVIVKgepKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
Cdd:COG1129 81 ------IAIIHQELNLVPNLSVAENIflgrePRRGGLID---WRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487083 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-235 |
8.92e-48 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 160.40 E-value: 8.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQT-----VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSISQQKG 78
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 79 LIRS--------LRQHVGFVFQ--SFNLFpHRTVLENIIEGPVIVkGEPKDEATARARELLAKVGLagkETSY----PRR 144
Cdd:PRK13631 102 NPYSkkiknfkeLRRRVSMVFQfpEYQLF-KDTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGL---DDSYlersPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 145 LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
250
....*....|.
gi 2790487083 225 QGPAKSLFADP 235
Cdd:PRK13631 257 TGTPYEIFTDQ 267
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-244 |
3.10e-47 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 157.95 E-value: 3.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDtAKSISQQKGLIRs 82
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLG-GRSIFNYRDVLE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 LRQHVGFVFQSFNLFPhRTVLENIIEGPVIVKGEPKDEATARARELLAKVGL----AGKETSYPRRLSGGQQQRVAIARA 158
Cdd:PRK14271 99 FRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQP 238
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
....*.
gi 2790487083 239 RTRQFL 244
Cdd:PRK14271 257 ETARYV 262
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-203 |
4.99e-47 |
|
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: 154.94 E-value: 4.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqkglirSL 83
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE---------DY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENIIegpVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:COG4133 74 RRRLAYLGHADGLKPELTVRENLR---FWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE 203
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-235 |
5.73e-47 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 158.43 E-value: 5.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 34 IIGPSGSGKTTLLRSINLLEQPEGGTIRVG--DITidtaksisqqkgLIRSLRQHVGFVFQSFNLFPHRTVLENIiEGPV 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDgeDVT------------NVPPHLRHINMVFQSYALFPHMTVEENV-AFGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 112 IVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLa 191
Cdd:TIGR01187 68 KMRKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI- 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2790487083 192 QEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADP 235
Cdd:TIGR01187 147 QEQLgiTFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-223 |
6.66e-47 |
|
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: 154.72 E-value: 6.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 5 DVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDitidtaKSISQqkgliRSL 83
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG------KPIKA-----KER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQS--FNLFpHRTVLENIIEGpvivkGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:cd03226 70 RKSIGYVMQDvdYQLF-TDSVREELLLG-----LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487083 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-207 |
6.75e-47 |
|
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: 154.12 E-value: 6.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqKGLIRsLRQHVGFVFQSF 94
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSR-----KGLLE-RRQRVGLVFQDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 95 N--LFpHRTVLENIIEGPVIVkGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:TIGR01166 78 DdqLF-AADVDQDVAFGPLNL-GLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|....*
gi 2790487083 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFA 207
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-244 |
1.37e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 155.39 E-value: 1.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSIN-LLEQPEGGTIRvGDITIdTAKSISQQKGL 79
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrLLELNEEARVE-GEVRL-FGRNIYSPDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 80 IRSLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVK-GEPKDEATARARELLAKVGL----AGKETSYPRRLSGGQQQRVA 154
Cdd:PRK14267 80 PIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGlVKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFAD 234
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
250
....*....|
gi 2790487083 235 PQQPRTRQFL 244
Cdd:PRK14267 239 PEHELTEKYV 248
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-221 |
1.63e-46 |
|
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: 154.51 E-value: 1.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSA-IDVKNLVKKF--HGQ-----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRV--GDITIDTA 70
Cdd:COG4778 1 MTTlLEVENLSKTFtlHLQggkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 71 KSISQQkglIRSLRQH-VGFVFQSFNLFPHRTVLENIIEgPVIVKGEPKDEATARARELLAKVGLagketsyPRRL---- 145
Cdd:COG4778 81 QASPRE---ILALRRRtIGYVSQFLRVIPRVSALDVVAE-PLLERGVDREEARARARELLARLNL-------PERLwdlp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 146 ----SGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:COG4778 150 patfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-237 |
2.77e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 155.71 E-value: 2.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTAKSISQQkglIRSLRQHVGFVFQsfnlFP 98
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITI-THKTKDKY---IRPVRKRIGMVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 99 HRTVLENIIEGPVIVK----GEPKDEATARARELLAKVGLAGKETSY-PRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:PRK13646 95 ESQLFEDTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487083 174 ALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQ 237
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDEnKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKK 239
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-244 |
3.28e-46 |
|
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: 153.83 E-value: 3.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSIsqqkgliRSLRQ 85
Cdd:TIGR03410 3 VSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPH-------ERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 86 HVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPK---DEATAR---ARELLAkvglagketsypRR---LSGGQQQRVAIA 156
Cdd:TIGR03410 76 GIAYVPQGREIFPRLTVEENLLTGLAALPRRSRkipDEIYELfpvLKEMLG------------RRggdLSGGQQQQLAIA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLfadp 235
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL---- 219
|
....*....
gi 2790487083 236 QQPRTRQFL 244
Cdd:TIGR03410 220 DEDKVRRYL 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-232 |
3.91e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 155.21 E-value: 3.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSaIDVKNLVKKFHGQT-----VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTAKSISq 75
Cdd:PRK13637 1 MS-IKIENLTHIYMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 76 qkglIRSLRQHVGFVFQ--SFNLFpHRTVLENIIEGPVIVkGEPKDEATARARELLAKVGLAG---KETSyPRRLSGGQQ 150
Cdd:PRK13637 78 ----LSDIRKKVGLVFQypEYQLF-EETIEKDIAFGPINL-GLSEEEIENRVKRAMNIVGLDYedyKDKS-PFELSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
Cdd:PRK13637 151 RRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPR 230
|
...
gi 2790487083 230 SLF 232
Cdd:PRK13637 231 EVF 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-244 |
6.52e-46 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 153.78 E-value: 6.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINlleqpeggtiRVGDI--TIDTAKSISQQKGLIR 81
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSIN----------RMNDLnpEVTITGSIVYNGHNIY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 S-------LRQHVGFVFQSFNLFPHrTVLENIIEGPVI--VKGEPK-DEATARA----------RELLAKVGLAgketsy 141
Cdd:PRK14239 76 SprtdtvdLRKEIGMVFQQPNPFPM-SIYENVVYGLRLkgIKDKQVlDEAVEKSlkgasiwdevKDRLHDSALG------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 142 prrLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:PRK14239 149 ---LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGD 224
|
250 260
....*....|....*....|...
gi 2790487083 222 IVEQGPAKSLFADPQQPRTRQFL 244
Cdd:PRK14239 225 LIEYNDTKQMFMNPKHKETEDYI 247
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-244 |
7.63e-46 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 153.86 E-value: 7.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHG----QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtaksisQQ 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-------TG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 77 KGLIRslrqhvGFVFQSFNLFPHRTVLENIIEGPVIvKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
Cdd:COG4525 74 PGADR------GVVFQKDALLPWLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 157 RALAMRPDVILFDEPTSALDP---ELVGEVLNTIRQLAQekRTMVIVTHEMSFARDVADRAIFMD--QGRIVEQ------ 225
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDAltrEQMQELLLDVWQRTG--KGVFLITHSVEEALFLATRLVVMSpgPGRIVERleldfs 224
|
250 260
....*....|....*....|....*
gi 2790487083 226 ------GPAKSLFADPQQPRTRQFL 244
Cdd:COG4525 225 rrflagEDARAIKSDPAFIALREEL 249
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
8-226 |
1.82e-45 |
|
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: 151.49 E-value: 1.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 8 NLVKKFHGQTVLHgIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSIsqqkglirslRQHV 87
Cdd:cd03298 4 DKIRFSYGEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA----------DRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 88 GFVFQSFNLFPHRTVLENIIEGPVivkgePKDEATARARE----LLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03298 73 SMLFQENNLFAHLTVEQNVGLGLS-----PGLKLTAEDRQaievALARVGLAGLEKRLPGELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-231 |
2.05e-45 |
|
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: 151.50 E-value: 2.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHG--QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAksisqqkglIR 81
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTD---------RK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SLRQHVGFVFQSFNLFPHRTVLENI-IEGpvIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:cd03263 72 AARQSLGYCPQFDALFDELTVREHLrFYA--RLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487083 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-234 |
2.38e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 152.93 E-value: 2.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHG------QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDItiDTAKsisqqK 77
Cdd:PRK13633 5 IKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGL--DTSD-----E 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 78 GLIRSLRQHVGFVFQSfnlfPHRTVLENIIEGPVIVKGE----PKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRV 153
Cdd:PRK13633 78 ENLWDIRNKAGMVFQN----PDNQIVATIVEEDVAFGPEnlgiPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLF 232
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGiTIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
..
gi 2790487083 233 AD 234
Cdd:PRK13633 233 KE 234
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-234 |
3.79e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 152.59 E-value: 3.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTAKSISQQkglIRSLRQHVGFVFQsfnlFP 98
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLI-TSTSKNKD---IKQIRKKVGLVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 99 H-----RTVLENIIEGPVIVkGEPKDEATARARELLAKVGLAGK--ETSyPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK13649 95 EsqlfeETVLKDVAFGPQNF-GVSQEEAEALAREKLALVGISESlfEKN-PFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 172 TSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFAD 234
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-234 |
4.76e-45 |
|
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: 151.39 E-value: 4.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQP-EGGTIRVGDitidtaksisQQKGL 79
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFG----------ERRGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 80 --IRSLRQHVGFVFQSFNLFPHR--TVLEniiegpVIVKG---------EPKDEATARARELLAKVGLAGKETSYPRRLS 146
Cdd:COG1119 71 edVWELRKRIGLVSPALQLRFPRdeTVLD------VVLSGffdsiglyrEPTDEQRERARELLELLGLAHLADRPFGTLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 147 GGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQ 225
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAA 224
|
....*....
gi 2790487083 226 GPAKSLFAD 234
Cdd:COG1119 225 GPKEEVLTS 233
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-222 |
6.59e-45 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 151.37 E-value: 6.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAksisqqkglirslRQ 85
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-------------RE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 86 HVGFVFQSFNLFPHRTVLENIIEGpviVKGEPKDeataRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:PRK11247 82 DTRLMFQDARLLPWKKVIDNVGLG---LKGQWRD----AALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487083 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHGfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-226 |
1.00e-44 |
|
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: 149.27 E-value: 1.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGeVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDItidtakSISQQKgliRSL 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ------DVLKQP---QKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLEnIIEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03264 71 RRRIGYLPQEFGVYPNFTVRE-FLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-228 |
2.18e-44 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 149.92 E-value: 2.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsiSQQKGLIRS 82
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWS--PAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 -LRQH--VGFVFqsfnlfphrTVLEnIIEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:PRK13548 80 vLPQHssLSFPF---------TVEE-VVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487083 160 A------MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPA 228
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIvVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-244 |
4.17e-44 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 149.42 E-value: 4.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGgTIRVGDITIDTAKSISQQKGLI 80
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELES-EVRVEGRVEFFNQNIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRQHVGFVFQSFNLFPhRTVLENIIEGPVIVKGEPK------DEATARARELLAKVglAGKETSYPRRLSGGQQQRVA 154
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKleiddiVESALKDADLWDEI--KHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLA-QEKRTMVIVTHEMSFARDVADRAIFMDQ-----GRIVEQGPA 228
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLT 240
|
250
....*....|....*.
gi 2790487083 229 KSLFADPQQPRTRQFL 244
Cdd:PRK14258 241 KKIFNSPHDSRTREYV 256
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-244 |
9.39e-44 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 148.14 E-value: 9.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQ--PEGgtiRV-GDITIDtAKSISQQK 77
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEA---RVsGEVYLD-GQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 78 glIRSLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVK-GEPKDEATARARELLAKVGL----AGKETSYPRRLSGGQQQR 152
Cdd:PRK14247 77 --VIELRRRVQMVFQIPNPIPNLSIFENVALGLKLNRlVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLF 232
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
250
....*....|..
gi 2790487083 233 ADPQQPRTRQFL 244
Cdd:PRK14247 234 TNPRHELTEKYV 245
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-231 |
1.02e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 149.49 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDtaksisqqkgliRS 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD------------PE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 LRQHVGFVFQSFNLFPHRTVLEniiegpVIV-----KGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:COG4152 69 DRRRIGYLPEERGLYPKMKVGE------QLVylarlKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487083 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-235 |
1.44e-43 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 147.95 E-value: 1.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisQQKGLIRS- 82
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSP--WELARRRAv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 LRQH--VGFVFqsfnlfphrTVLENIIEGpVIVKGEPKDEATARARELLAKVGLAG-KETSYPRrLSGGQQQRVAIARAL 159
Cdd:COG4559 80 LPQHssLAFPF---------TVEEVVALG-RAPHGSSAAQDRQIVREALALVGLAHlAGRSYQT-LSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 160 A-------MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLF 232
Cdd:COG4559 149 AqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVL 228
|
...
gi 2790487083 233 ADP 235
Cdd:COG4559 229 TDE 231
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-238 |
1.49e-43 |
|
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: 150.65 E-value: 1.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 22 IDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTaksiSQQKGLIRSLRQHVGFVFQSFNLFPHRT 101
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFD----SRKGIFLPPEKRRIGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 102 VLENIIEGPVIVKGEPKDEATARARELLAKVGLAGKetsYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVG 181
Cdd:TIGR02142 92 VRGNLRYGMKRARPSERRISFERVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487083 182 EVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQP 238
Cdd:TIGR02142 169 EILPYLERLHAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLP 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-229 |
2.61e-43 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 147.47 E-value: 2.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 2 SAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLL---EQPEGGTIRVGDITIDTAKSISQQkg 78
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARD-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 79 lIRSLRQHVGFVFQSFNLFPHRTVLENIIEGPVivKGEP---------KDEATARARELLAKVGLAGKETSYPRRLSGGQ 149
Cdd:PRK09984 81 -IRKSRANTGYIFQQFNLVNRLSVLENVLIGAL--GSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQGPA 228
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYALRYCERIVALRQGHVFYDGSS 237
|
.
gi 2790487083 229 K 229
Cdd:PRK09984 238 Q 238
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-226 |
3.82e-43 |
|
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: 145.05 E-value: 3.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRV-GDITIDTAKSisqqkglirs 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdGKSYQKNIEA---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 lRQHVGFVFQSFNLFPHRTVLENIIEGPVIvKGEPKdeatARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:cd03268 71 -LRRIGALIEAPGFYPNLTARENLRLLARL-LGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487083 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-231 |
1.17e-42 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 144.43 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVG--DITIDTaksisqqkgliR 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAghDVVREP-----------R 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SLRQHVGFVFQSFNLFPHRTVLENI-IEGPVivKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:cd03265 70 EVRRRIGIVFQDLSVDDELTGWENLyIHARL--YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487083 161 MRPDVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-229 |
1.97e-42 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 150.56 E-value: 1.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDtaksisqqkglIRS 82
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-----------IRS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 ----LRQHVGFVFQSFNLFPHRTVLENIIEG--PVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
Cdd:COG3845 74 prdaIALGIGMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-236 |
2.21e-42 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 144.02 E-value: 2.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTAKSISQ--QKG 78
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLPMHKraRLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 79 LirslrqhvGFVFQSFNLFPHRTVLENI---IEgpviVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
Cdd:COG1137 80 I--------GYLPQEASIFRKLTVEDNIlavLE----LRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQekRTM-VIVT-HEMSFARDVADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKE--RGIgVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILN 225
|
...
gi 2790487083 234 DPQ 236
Cdd:COG1137 226 NPL 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-226 |
2.94e-42 |
|
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: 142.80 E-value: 2.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqkglirsl 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENIIEGPVIvKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-246 |
2.95e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 144.75 E-value: 2.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 2 SAIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqkgl 79
Cdd:PRK13632 6 VMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 80 IRSLRQHVGFVFQS-FNLFPHRTV-------LENiiegpvivKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQ 151
Cdd:PRK13632 78 LKEIRKKIGIIFQNpDNQFIGATVeddiafgLEN--------KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 152 RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKS 230
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTrKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKE 228
|
250
....*....|....*.
gi 2790487083 231 LFADpqqprtRQFLEK 246
Cdd:PRK13632 229 ILNN------KEILEK 238
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-223 |
3.13e-42 |
|
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: 141.41 E-value: 3.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAksisqqkGLIRSL 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA-------SPRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQsfnlfphrtvleniiegpvivkgepkdeatararellakvglagketsyprrLSGGQQQRVAIARALAMRP 163
Cdd:cd03216 74 RAGIAMVYQ----------------------------------------------------LSVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-234 |
3.28e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 145.26 E-value: 3.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtaKSISQQKGlIRSLRQHVGFVFQsfnlFP 98
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVV---SSTSKQKE-IKPVRKKVGVVFQ----FP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 99 H-----RTVLENIIEGPVIVkGEPKDEATARARELLAKVGLAGK--ETSyPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK13643 94 EsqlfeETVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLADEfwEKS-PFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 172 TSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFAD 234
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-244 |
3.59e-42 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 147.29 E-value: 3.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgDITIDtaksiSQQKGLIRSL 83
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAG-----QIMLD-----GVDLSHVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENIIEGpviVKGE--PKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:PRK11607 90 QRPINMMFQSYALFPHMTVEQNIAFG---LKQDklPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 162 RPDVILFDEPTSALDPELVGEV-LNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQPRT 240
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
....
gi 2790487083 241 RQFL 244
Cdd:PRK11607 247 AEFI 250
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-225 |
7.77e-42 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 146.14 E-value: 7.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqkgl 79
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 80 irSLRQhVGFVFQSFNLFPHRTVLENIIEGPVIvKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:PRK11650 74 --ADRD-IAMVFQNYALYPHMSVRENMAYGLKI-RGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487083 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIvEQ 225
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGGVA-EQ 215
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-233 |
1.55e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 143.33 E-value: 1.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQT---VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRV-GD-ITIDTAKSIsq 75
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDlLTEENVWDI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 76 qkglirslRQHVGFVFQS-FNLFPHRTV-------LENiiegpvivKGEPKDEATARARELLAKVGLAGKETSYPRRLSG 147
Cdd:PRK13650 80 --------RHKIGMVFQNpDNQFVGATVeddvafgLEN--------KGIPHEEMKERVNEALELVGMQDFKEREPARLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSfarDVA--DRAIFMDQGRIVE 224
Cdd:PRK13650 144 GQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVIsITHDLD---EVAlsDRVLVMKNGQVES 220
|
....*....
gi 2790487083 225 QGPAKSLFA 233
Cdd:PRK13650 221 TSTPRELFS 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-234 |
1.58e-41 |
|
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: 148.41 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 21 GIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGT--IRVGDITIDTAKSISQQKGlirSLRQHVGFVFQSFNLFP 98
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPDGRG---RAKRYIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 99 HRTVLENIIEGpvIVKGEPKDEATARARELLAKVGLAGKET-----SYPRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:TIGR03269 379 HRTVLDNLTEA--IGLELPDELARMKAVITLKMVGFDEEKAeeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487083 174 ALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFAD 234
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-233 |
3.40e-41 |
|
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: 140.82 E-value: 3.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 14 HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtaKSISqqkglIRSLRQHVGFVFQS 93
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI---RDIS-----RKSLRSMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 94 FNLFPhRTVLENIIEGPVIVKGEPKDEA--TARARELLAK--------VGLAGKetsyprRLSGGQQQRVAIARALAMRP 163
Cdd:cd03254 86 TFLFS-GTIMENIRLGRPNATDEEVIEAakEAGAHDFIMKlpngydtvLGENGG------NLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-231 |
4.27e-41 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 142.53 E-value: 4.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 11 KKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVG--DITIDTAKsisqqkglirsLRQHVG 88
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAgyDVVREPRK-----------VRRSIG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 89 FVFQSFNLFPHRTVLENIiEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILF 168
Cdd:TIGR01188 70 IVPQYASVDEDLTGRENL-EMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 169 DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:TIGR01188 149 DEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-233 |
8.89e-41 |
|
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: 140.06 E-value: 8.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtaKSISQQkglirSLRQHVGFVFQSF 94
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI---REVTLD-----SLRRAIGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 95 NLFpHRTVLENIIEGPVIVKGEPKDEATARAR---ELLA-------KVGLAGketsypRRLSGGQQQRVAIARALAMRPD 164
Cdd:cd03253 85 VLF-NDTIGYNIRYGRPDATDEEVIEAAKAAQihdKIMRfpdgydtIVGERG------LKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487083 165 VILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-226 |
9.94e-41 |
|
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: 139.23 E-value: 9.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 23 DLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqkglirsLRQHVGFVFQSFNLFPHRTV 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP----------YQRPVSMLFQENNLFAHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 103 LENI---IEGPVIVKGEPKDEATARAREllakVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPEL 179
Cdd:TIGR01277 88 RQNIglgLHPGLKLNAEQQEKVVDAAQQ----VGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2790487083 180 VGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:TIGR01277 164 REEMLALVKQLCSERqRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-231 |
1.08e-40 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 139.72 E-value: 1.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 23 DLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITiDTAKSISQQKglirslrqhVGFVFQSFNLFPHRTV 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRP---------VSMLFQENNLFSHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 103 LENIIEGPvivkgEPKDEATARARELLA----KVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPE 178
Cdd:PRK10771 89 AQNIGLGL-----NPGLKLNAAQREKLHaiarQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790487083 179 LVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:PRK10771 164 LRQEMLTLVSQVCQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-245 |
2.02e-40 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 139.97 E-value: 2.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSA-IDVKNLVKKFHGQT---------VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTa 70
Cdd:COG4167 1 MSAlLEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 71 KSISQqkgliRSlrQHVGFVFQ----SFNlfPHRTVLEnIIEGPVIVKgepkDEATARAREL-----LAKVGLAGKETS- 140
Cdd:COG4167 80 GDYKY-----RC--KHIRMIFQdpntSLN--PRLNIGQ-ILEEPLRLN----TDLTAEEREErifatLRLVGLLPEHANf 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 141 YPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMD 218
Cdd:COG4167 146 YPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLEL-QEKLgiSYIYVSQHLGIVKHISDKVLVMH 224
|
250 260
....*....|....*....|....*..
gi 2790487083 219 QGRIVEQGPAKSLFADPQQPRTRQFLE 245
Cdd:COG4167 225 QGEVVEYGKTAEVFANPQHEVTKRLIE 251
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-236 |
2.04e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 140.26 E-value: 2.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFH-GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqkglIR 81
Cdd:PRK13647 4 IIEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEN--------EK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SLRQHVGFVFQSFN--LFPhRTVLENIIEGPVIVkGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:PRK13647 76 WVRSKVGLVFQDPDdqVFS-STVWDDVAFGPVNM-GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487083 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGpAKSLFADPQ 236
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDED 229
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-247 |
2.99e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 139.96 E-value: 2.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqQKGLiRSLRQHVGFVFQsfnlFP 98
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETG---NKNL-KKLRKKVSLVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 99 H-----RTVLENIIEGPVIVkGEPKDEATARARELLAKVGLAGKETSY-PRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:PRK13641 95 EaqlfeNTVLKDVEFGPKNF-GFSEDEAKEKALKWLKKVGLSEDLISKsPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQ--------QPRTRQFL 244
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwlkkhyldEPATSRFA 253
|
...
gi 2790487083 245 EKF 247
Cdd:PRK13641 254 SKL 256
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-226 |
4.80e-40 |
|
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: 137.72 E-value: 4.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtaKSISQQkgli 80
Cdd:cd03245 2 RIEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI---RQLDPA---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 rSLRQHVGFVFQSFNLFpHRTVLENIIEGPVIVKgepkDEATARARELLAKVGLAGKetsYP-----------RRLSGGQ 149
Cdd:cd03245 75 -DLRRNIGYVPQDVTLF-YGTLRDNITLGAPLAD----DERILRAAELAGVTDFVNK---HPngldlqigergRGLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487083 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFArDVADRAIFMDQGRIVEQG 226
Cdd:cd03245 146 RQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK-TLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
3-239 |
9.77e-40 |
|
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: 145.39 E-value: 9.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDI---TIDTAksisqqk 77
Cdd:TIGR03375 463 EIEFRNVSFAYPGQEtpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVdirQIDPA------- 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 78 glirSLRQHVGFVFQSFNLFpHRTVLENIIEGpvivKGEPKDEATARARELlakVGLAGKETSYP-----------RRLS 146
Cdd:TIGR03375 536 ----DLRRNIGYVPQDPRLF-YGTLRDNIALG----APYADDEEILRAAEL---AGVTEFVRRHPdgldmqigergRSLS 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 147 GGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFArDVADRAIFMDQGRIVEQG 226
Cdd:TIGR03375 604 GGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK-TLVLVTHRTSLL-DLVDRIIVMDNGRIVADG 681
|
250
....*....|...
gi 2790487083 227 PAKSLFADPQQPR 239
Cdd:TIGR03375 682 PKDQVLEALRKGR 694
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-234 |
9.83e-40 |
|
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: 137.36 E-value: 9.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKF--HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqkglIR 81
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT--------LA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SLRQHVGFVFQSFNLFpHRTVLENIIEGpvivkgepKDEATARARELLAKVGLA---------GKETSYPRR---LSGGQ 149
Cdd:cd03251 73 SLRRQIGLVSQDVFLF-NDTVAENIAYG--------RPGATREEVEEAARAANAhefimelpeGYDTVIGERgvkLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAK 229
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHE 221
|
....*
gi 2790487083 230 SLFAD 234
Cdd:cd03251 222 ELLAQ 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-226 |
1.00e-39 |
|
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: 143.79 E-value: 1.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTL---LRSINLLEQPEGGTI----------------RVGD 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLmhvLRGMDQYEPTSGRIIyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 65 --------ITIDTAKSISQQKGLIRSLRQHVGFVFQ-SFNLFPHRTVLENIIEG-PVIvkGEPKDEATARARELLAKVGL 134
Cdd:TIGR03269 81 pcpvcggtLEPEEVDFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEAlEEI--GYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 135 AGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADR 213
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGiSMVLTSHWPEVIEDLSDK 238
|
250
....*....|...
gi 2790487083 214 AIFMDQGRIVEQG 226
Cdd:TIGR03269 239 AIWLENGEIKEEG 251
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
15-243 |
1.22e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 138.44 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqKGLIRsLRQHVGFVFQS- 93
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSR-----KGLMK-LRESVGMVFQDp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 94 -FNLFPhRTVLENIIEGPVIVkGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:PRK13636 92 dNQLFS-ASVYQDVSFGAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487083 173 SALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQPRTRQF 243
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKVNL 241
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-235 |
2.08e-39 |
|
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: 136.13 E-value: 2.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTAKSISQqkgliRSl 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLPMHK-----RA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENII---EgpviVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:cd03218 74 RLGIGYLPQEASIFRKLTVEENILavlE----IRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487083 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADP 235
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
15-235 |
3.44e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 137.04 E-value: 3.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDI-TIDTAKsisqqkglIRSLRQHVGFVFQS 93
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdTGDFSK--------LQGIRKLVGIVFQN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 94 FNL-FPHRTVLENIIEGPVIVkGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:PRK13644 86 PETqFVGRTVEEDLAFGPENL-CLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLFADP 235
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-236 |
5.59e-39 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 138.62 E-value: 5.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEqpeggTIRVGDITIDtaksiSQQKGLI 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLE-----DITSGDLFIG-----EKRMNDV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRQHVGFVFQSFNLFPHRTVLENIIEGpVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK11000 71 PPAERGVGMVFQSYALYPHLSVAENMSFG-LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487083 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQ 236
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
8-225 |
6.25e-39 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 135.33 E-value: 6.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 8 NLVKKFH-GQT---VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgditIDTAKSISQQKGLIRS- 82
Cdd:PRK11629 10 NLCKRYQeGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV------IFNGQPMSKLSSAAKAe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 LRQH-VGFVFQSFNLFPHRTVLENIIEgPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:PRK11629 84 LRNQkLGFIYQFHHLLPDFTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487083 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVaDRAIFMDQGRIVEQ 225
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTaFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-227 |
6.29e-39 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 135.97 E-value: 6.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHG---------QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDitidtaK 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRG------E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 72 SISQQKGL-IRSLRQHVGFVFQ----SFNlfPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGLAGKETS-YPRRL 145
Cdd:PRK10419 75 PLAKLNRAqRKAFRRDIQMVFQdsisAVN--PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDkRPPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 146 SGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
...
gi 2790487083 225 QGP 227
Cdd:PRK10419 233 TQP 235
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-227 |
7.65e-39 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 135.21 E-value: 7.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqKGLIRS- 82
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPS----RELAKRl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 --LRQHVGFVFQ-------SFNLFPHRtvleniiegpvivKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRV 153
Cdd:COG4604 78 aiLRQENHINSRltvrelvAFGRFPYS-------------KGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487083 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELgKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-227 |
2.64e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 132.61 E-value: 2.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPE---GGTIRVGDITIDTaksisqqkglIRS 82
Cdd:COG4136 4 LENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTA----------LPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 LRQHVGFVFQSFNLFPHRTVLENIIEGpvIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:COG4136 74 EQRRIGILFQDDLLFPHLSVGENLAFA--LPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487083 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHemsfarDVADRAifmDQGRIVEQGP 227
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIpALLVTH------DEEDAP---AAGRVLDLGN 208
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-241 |
2.76e-38 |
|
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: 140.27 E-value: 2.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqkgliRSLRQHVGFVFQSF 94
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR--------EELGRHIGYLPQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 95 NLFPHrTVLENIiegpvivkGEPKDEA------TARARELLAK--------VGLAGketsypRRLSGGQQQRVAIARALA 160
Cdd:COG4618 416 ELFDG-TIAENIar-----fGDADPEKvvaaakLAGVHEMILRlpdgydtrIGEGG------ARLSGGQRQRIGLARALY 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 161 MRPDVILFDEPTSALDPElvGE--VLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKSLFADPQQP 238
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDE--GEaaLAAAIRALKARGATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVLARLARP 560
|
...
gi 2790487083 239 RTR 241
Cdd:COG4618 561 AAA 563
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-244 |
3.24e-38 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 134.06 E-value: 3.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAksisqqkGLIRs 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP-------GAER- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 lrqhvGFVFQSFNLFPHRTVLENIIEGpVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:PRK11248 73 -----GVVFQNEGLLPWRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAAN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMV-IVTHEMSFARDVADRAIFM--DQGRIVEQ------------GP 227
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVlLITHDIEEAVFMATELVLLspGPGRVVERlplnfarrfvagES 226
|
250
....*....|....*..
gi 2790487083 228 AKSLFADPQQPRTRQFL 244
Cdd:PRK11248 227 SRSIKSDPQFIAMREYV 243
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
19-245 |
4.75e-38 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 133.75 E-value: 4.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDtAKSISQQKGLIRSLRQHVGFVFQSFNLFP 98
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFH-GKNLYAPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 99 hRTVLENIIEGPVI--VKGEpKDEATARA----------RELLAKVGLAgketsyprrLSGGQQQRVAIARALAMRPDVI 166
Cdd:PRK14243 105 -KSIYDNIAYGARIngYKGD-MDELVERSlrqaalwdevKDKLKQSGLS---------LSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 167 LFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMD---------QGRIVEQGPAKSLFADPQQ 237
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSPQQ 252
|
....*...
gi 2790487083 238 PRTRQFLE 245
Cdd:PRK14243 253 QATRDYVS 260
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-244 |
5.29e-38 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 137.09 E-value: 5.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 24 LEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDItiDTAKSISQQKGLIRslRQHVGFVFQSFNLFPHRTVL 103
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGV--DIAKISDAELREVR--RKKIAMVFQSFALMPHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 104 ENIIEGpVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEV 183
Cdd:PRK10070 125 DNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487083 184 LNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQPRTRQFL 244
Cdd:PRK10070 204 QDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-233 |
6.76e-38 |
|
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: 132.61 E-value: 6.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqkgliRSLRQHVGFVFQSF 94
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP--------AWLRRQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 95 NLFpHRTVLENIIEGPVIVKGEPKDEAT--ARARELLAKVGLaGKETSYPRR---LSGGQQQRVAIARALAMRPDVILFD 169
Cdd:cd03252 86 VLF-NRSIRDNIALADPGMSMERVIEAAklAGAHDFISELPE-GYDTIVGEQgagLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487083 170 EPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
14-207 |
9.60e-38 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 131.82 E-value: 9.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 14 HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgdITIDTAKSISQQKGLIRSlrQHVGFVFQS 93
Cdd:PRK10584 21 HELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSL--VGQPLHQMDEEARAKLRA--KHVGFVFQS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 94 FNLFPHRTVLENIiEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:PRK10584 97 FMLIPTLNALENV-ELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190
....*....|....*....|....*....|....*
gi 2790487083 174 ALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFA 207
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLA 210
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
3-233 |
1.19e-37 |
|
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: 139.32 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFH--GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDtaksisqqkGL- 79
Cdd:TIGR03797 451 AIEVDRVTFRYRpdGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLA---------GLd 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 80 IRSLRQHVGFVFQSFNLFPHrTVLENIIEGPVIvkgePKDEATARAREllakVGLAGKETSYP-----------RRLSGG 148
Cdd:TIGR03797 522 VQAVRRQLGVVLQNGRLMSG-SIFENIAGGAPL----TLDEAWEAARM----AGLAEDIRAMPmgmhtviseggGTLSGG 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPA 228
Cdd:TIGR03797 593 QRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL---KVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTY 668
|
....*
gi 2790487083 229 KSLFA 233
Cdd:TIGR03797 669 DELMA 673
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-217 |
2.13e-37 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 137.42 E-value: 2.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 2 SAIDVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqkgli 80
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA-------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRQHVGFVFQSFNLFPhRTVLENIIEGpvivKGEPKDEATARArelLAKVGLAGKETSYP-----------RRLSGGQ 149
Cdd:TIGR02857 392 DSWRDQIAWVPQHPFLFA-GTIAENIRLA----RPDASDAEIREA---LERAGLDEFVAALPqgldtpigeggAGLSGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487083 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFM 217
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-233 |
2.71e-37 |
|
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: 131.12 E-value: 2.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLvkKFH-----GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLEQ---PEGGTIRVGDITIdtaKSISq 75
Cdd:cd03249 1 IEFKNV--SFRypsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTV---VSLLERfydPTSGEILLDGVDI---RDLN- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 76 qkglIRSLRQHVGFVFQSFNLFPhRTVLENIIEGpvivkgepKDEATARARELLAKVGLA---------GKET---SYPR 143
Cdd:cd03249 72 ----LRWLRSQIGLVSQEPVLFD-GTIAENIRYG--------KPDATDEEVEEAAKKANIhdfimslpdGYDTlvgERGS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 144 RLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDvADRAIFMDQGRIV 223
Cdd:cd03249 139 QLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVV 216
|
250
....*....|
gi 2790487083 224 EQGPAKSLFA 233
Cdd:cd03249 217 EQGTHDELMA 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-222 |
2.93e-37 |
|
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: 128.87 E-value: 2.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHG--QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqkgliR 81
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP--------N 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SLRQHVGFVFQSFNLFPHrTVLENIiegpvivkgepkdeatararellakvglagketsyprrLSGGQQQRVAIARALAM 161
Cdd:cd03246 73 ELGDHVGYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487083 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQGRI 222
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-235 |
3.43e-37 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 134.97 E-value: 3.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITID--TAKSISQQkg 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEalSARAASRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 79 lIRSLRQHVGFVFQsfnlFPHRTVLEnIIEGPVIVKGEPKDEATARA-RELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:PRK09536 79 -VASVPQDTSLSFE----FDVRQVVE-MGRTPHRSRFDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487083 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADP 235
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-220 |
3.71e-37 |
|
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: 130.28 E-value: 3.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDtaksisqQKGLIRSLrqhvgfVFQSFNLFP 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-------EPGPDRMV------VFQNYSLLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 99 HRTVLENI-IEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:TIGR01184 68 WLTVRENIaLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2790487083 178 ELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQG 220
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-241 |
1.92e-36 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 131.37 E-value: 1.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 21 GIDLEVEQGEVVAIIGPSGSGKTTLLRS-INLLEQPEGGTIRVG-DITidtaksiSQQKGLIRSLRQHVGFVFQ----SF 94
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAiIGLVKATDGEVAWLGkDLL-------GMKDDEWRAVRSDIQMIFQdplaSL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 95 NlfPHRTVLENIIEGPVIVKGE-PKDEATARARELLAKVGLAGKETS-YPRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:PRK15079 112 N--PRMTIGEIIAEPLRTYHPKlSRQEVKDRVKAMMLKVGLLPNLINrYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 173 SALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQPRTR 241
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQREMGlSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTK 259
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-247 |
3.52e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 134.57 E-value: 3.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtaKSISQQkgli 80
Cdd:PRK11160 338 SLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI---ADYSEA---- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 rSLRQHVGFVFQSFNLFPHrTVLENIIegpvIVKGEPKDEataRARELLAKVGLAGKETSYP----------RRLSGGQQ 150
Cdd:PRK11160 411 -ALRQAISVVSQRVHLFSA-TLRDNLL----LAAPNASDE---ALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAKS 230
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK-TVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQE 559
|
250
....*....|....*..
gi 2790487083 231 LFAdpQQPRTRQFLEKF 247
Cdd:PRK11160 560 LLA--QQGRYYQLKQRL 574
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-244 |
7.64e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 127.86 E-value: 7.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 2 SAIDVKNLVKKF---HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSISQQKG 78
Cdd:PRK14246 6 SAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 79 LirSLRQHVGFVFQSFNLFPHRTVLENIIEgPVIVKG-EPKDEATARARELLAKVGL----AGKETSYPRRLSGGQQQRV 153
Cdd:PRK14246 86 I--KLRKEVGMVFQQPNPFPHLSIYDNIAY-PLKSHGiKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:PRK14246 163 TIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI-AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
250
....*....|.
gi 2790487083 234 DPQQPRTRQFL 244
Cdd:PRK14246 242 SPKNELTEKYV 252
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-226 |
7.78e-36 |
|
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: 125.74 E-value: 7.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 14 HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSIN--LLEQPEGGTIRVGDITIDtaksisqqkglIRSLRQHVGFVF 91
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD-----------KRSFRKIIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 92 QSFNLFPHRTVLENIiegpvivkgepkdeatararELLAKVglagketsypRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:cd03213 89 QDDILHPTLTVRETL--------------------MFAAKL----------RGLSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487083 172 TSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS---FArdVADRAIFMDQGRIVEQG 226
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSseiFE--LFDKLLLLSQGRVIYFG 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-226 |
8.88e-36 |
|
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: 126.62 E-value: 8.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLeQPEGGTIRvGDITIDTAKSISQQkglirsLRQHVGFVFQSFNLF 97
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-VEGGGTTS-GQILFNGQPRKPDQ------FQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 98 PHRTVLENIIEGPVIVKGEPKDEATARAR---ELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:cd03234 94 PGLTVRETLTYTAILRLPRKSSDAIRKKRvedVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 175 LDPELVGEVLNTIRQLAQEKRTMVIVTHE-MSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-233 |
9.36e-36 |
|
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: 133.30 E-value: 9.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtaksisqQKGLIRSLRQHVGFVFQSF 94
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL--------ADYTLASLRRQVALVSQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 95 NLFpHRTVLENIIEGPVIVKGEPKDEATARARELLAKV-----GLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFD 169
Cdd:TIGR02203 416 VLF-NDTIANNIAYGRTEQADRAEIERALAAAYAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILD 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487083 170 EPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:TIGR02203 495 EATSALDNESERLVQAALERLMQG-RTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLA 556
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
15-223 |
1.65e-35 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 126.14 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSISqqkglIRSLRQHVGFVFQSF 94
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRE-----VPFLRRQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 95 NLFPHRTVLENIIEgPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:PRK10908 89 HLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2790487083 175 LDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:PRK10908 168 LDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-226 |
1.86e-35 |
|
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: 125.56 E-value: 1.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQT----VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDItiDTAKSIsqqkgl 79
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF--DVVKEP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 80 iRSLRQHVGFVFQSFNLFPHRTVLENIiEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:cd03266 74 -AEARRRLGFVSDSTGLYDRLTARENL-EYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487083 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-226 |
2.11e-35 |
|
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: 132.64 E-value: 2.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 17 TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRsinLLEQ---PEGGTIRVGDITIdtaKSISQQkglirSLRQHVGFVFQS 93
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLAR---LLFRfydVTSGRILIDGQDI---RDVTQA-----SLRAAIGIVPQD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 94 FNLFpHRTVLENIIEGpvivkgepKDEAT-------ARARELLAKV-GL-AGKETSYPRR---LSGGQQQRVAIARALAM 161
Cdd:COG5265 441 TVLF-NDTIAYNIAYG--------RPDASeeeveaaARAAQIHDFIeSLpDGYDTRVGERglkLSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487083 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQG 226
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREVARG-RTTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-213 |
2.64e-35 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 124.27 E-value: 2.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 13 FHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidTAKSIS---QQKGLIRSL----RQ 85
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA-----GGARVAyvpQRSEVPDSLpltvRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 86 HVgfvfqSFNLFPHRTVLeniiegpvivkGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:NF040873 77 LV-----AMGRWARRGLW-----------RRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2790487083 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADR 213
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADP 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-222 |
5.88e-35 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 130.57 E-value: 5.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidtaksisqQKGLirslrq 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-------------PKGL------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 86 HVGFVFQSFNLFPHRTVLENIIEG--PVIVKGEPKDEAT-----------------------------ARARELLAKVGL 134
Cdd:COG0488 62 RIGYLPQEPPLDDDLTVLDTVLDGdaELRALEAELEELEaklaepdedlerlaelqeefealggweaeARAEEILSGLGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 135 AGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDpelvgevLNTIR----QLAQEKRTMVIVTHEMSFARD 209
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIEwleeFLKNYPGTVLVVSHDRYFLDR 214
|
250
....*....|...
gi 2790487083 210 VADRAIFMDQGRI 222
Cdd:COG0488 215 VATRILELDRGKL 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-244 |
1.29e-34 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 130.75 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 29 GEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqkGLIRSLRQHVGFVFQS--FNLFPHRTVLENI 106
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP-----GKLQALRRDIQFIFQDpyASLDPRQTVGDSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 107 IEgPVIVKG-EPKDEATARARELLAKVGLAGKET-SYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVL 184
Cdd:PRK10261 425 ME-PLRVHGlLPGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQII 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487083 185 NTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQPRTRQFL 244
Cdd:PRK10261 504 NLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-226 |
1.34e-34 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 130.08 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLEQ---PEGGTIRVGDITIdtaKSISqqkglIRSLRQHVGFVFQSFN 95
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRvfdPQSGRILIDGTDI---RTVT-----RASLRRNIAVVFQDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 96 LFpHRTVLENIIEGpvivKGEPKDEATARARELLAKVG-LAGKETSYP-------RRLSGGQQQRVAIARALAMRPDVIL 167
Cdd:PRK13657 420 LF-NRSIEDNIRVG----RPDATDEEMRAAAERAQAHDfIERKPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487083 168 FDEPTSALDPEL---VGEVLNTIRQlaqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQG 226
Cdd:PRK13657 495 LDEATSALDVETeakVKAALDELMK----GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-236 |
2.07e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 124.48 E-value: 2.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDitidtaKSISQQKglIR 81
Cdd:PRK13648 8 IVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN------QAITDDN--FE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SLRQHVGFVFQS-FNLFPHRTV-------LENiiegpvivKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRV 153
Cdd:PRK13648 80 KLRKHIGIVFQNpDNQFVGSIVkydvafgLEN--------HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDvADRAIFMDQGRIVEQGPAKSLF 232
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIIsITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
....
gi 2790487083 233 ADPQ 236
Cdd:PRK13648 231 DHAE 234
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-245 |
6.64e-34 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 122.95 E-value: 6.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDitiDTAKSISQQKglIRSL 83
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG---ENIPAMSRSR--LYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENIiegpvivkGEPKDEATARAREL--------LAKVGLAGKETSYPRRLSGGQQQRVAI 155
Cdd:PRK11831 83 RKRMSMLFQSGALFTDMNVFDNV--------AYPLREHTQLPAPLlhstvmmkLEAVGLRGAAKLMPSELSGGMARRAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFAD 234
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAN 234
|
250
....*....|.
gi 2790487083 235 PqQPRTRQFLE 245
Cdd:PRK11831 235 P-DPRVRQFLD 244
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-233 |
7.57e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 123.76 E-value: 7.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 2 SAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqkgliR 81
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA---------R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SLRQHVGFVFQSFNLFPHRTVLENI-IEGPVIvkGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK13537 77 HARQRVGVVPQFDNLDPDFTVRENLlVFGRYF--GLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-249 |
8.13e-34 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 122.50 E-value: 8.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 2 SAIDVKNLVKKFHGQTVlHGIDLEVEQGEVVAIIGPSGSGKT-TLLRSINLLeqPEGGTIRVGDITID-TAKSISQQKGl 79
Cdd:PRK10418 3 QQIELRNIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGIL--PAGVRQTAGRVLLDgKPVAPCALRG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 80 irslrQHVGFVFQ----SFNlfPHRTVLENIIEgPVIVKGEPKDEATARAreLLAKVGLAGKET---SYPRRLSGGQQQR 152
Cdd:PRK10418 79 -----RKIATIMQnprsAFN--PLHTMHTHARE-TCLALGKPADDATLTA--ALEAVGLENAARvlkLYPFEMSGGMLQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
250
....*....|....*...
gi 2790487083 232 FADPQQPRTRQFLEKFLV 249
Cdd:PRK10418 229 FNAPKHAVTRSLVSAHLA 246
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-235 |
9.15e-34 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 128.69 E-value: 9.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 16 QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgdiTIDtAKSISQQKGliRSLRQHVGFVFQSFN 95
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV-----LLD-GVPLVQYDH--HYLHRQVALVGQEPV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 96 LFpHRTVLENIIEGpviVKGEPKDEATARARELLAKVGLAGKETSYPR-------RLSGGQQQRVAIARALAMRPDVILF 168
Cdd:TIGR00958 566 LF-SGSVRENIAYG---LTDTPDEEIMAAAKAANAHDFIMEFPNGYDTevgekgsQLSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487083 169 DEPTSALDPElvgevlntIRQLAQE-----KRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLFADP 235
Cdd:TIGR00958 642 DEATSALDAE--------CEQLLQEsrsraSRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-223 |
1.13e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 122.12 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTV-----LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINlleqpegGTIRV--GDITIDtAKSISQQ 76
Cdd:COG1101 2 LELKNLSKTFNPGTVnekraLDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIA-------GSLPPdsGSILID-GKDVTKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 77 KGLIRSlrQHVGFVFQ--SFNLFPHRTVLENII------EGPVIVKGEPKDEaTARARELLAKVGLaGKEtsypRR---- 144
Cdd:COG1101 74 PEYKRA--KYIGRVFQdpMMGTAPSMTIEENLAlayrrgKRRGLRRGLTKKR-RELFRELLATLGL-GLE----NRldtk 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 145 ---LSGGQQQrvaiARALAM----RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIF 216
Cdd:COG1101 146 vglLSGGQRQ----ALSLLMatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNRLIM 221
|
....*..
gi 2790487083 217 MDQGRIV 223
Cdd:COG1101 222 MHEGRII 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-229 |
1.43e-33 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 121.34 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MS-AIDVKNLVKKFHGQ----------------------TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEG 57
Cdd:COG1134 1 MSsMIEVENVSKSYRLYhepsrslkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 58 GTIRVgditidtaksisqqKGLIRSLRQhVGFVFQsfnlfPHRTVLENIIEGPVIVkGEPKDEATARARELLAKVGLaGK 137
Cdd:COG1134 81 GRVEV--------------NGRVSALLE-LGAGFH-----PELTGRENIYLNGRLL-GLSRKEIDEKFDEIVEFAEL-GD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 138 ETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIF 216
Cdd:COG1134 139 FIDQPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIW 218
|
250
....*....|...
gi 2790487083 217 MDQGRIVEQGPAK 229
Cdd:COG1134 219 LEKGRLVMDGDPE 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-244 |
1.61e-33 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 121.57 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTI----RVGDITIDTAKSISQQKGLir 81
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmRDGQLRDLYALSEAERRRL-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 sLRQHVGFVFQSF--NLFPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGLAGKETS-YPRRLSGGQQQRVAIARA 158
Cdd:PRK11701 87 -LRTEWGFVHQHPrdGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAARIDdLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQ 237
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGlAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQH 245
|
....*..
gi 2790487083 238 PRTrQFL 244
Cdd:PRK11701 246 PYT-QLL 251
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
10-242 |
2.52e-33 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 123.45 E-value: 2.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 10 VKKFHGQTVLHgIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDIT-IDTAKSISqqkglIRSLRQHVG 88
Cdd:PRK11144 6 FKQQLGDLCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFDAEKGIC-----LPPEKRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 89 FVFQSFNLFPHRTVLENIIEGpviVKgePKDEAtararELLAKVGLAGKE---TSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:PRK11144 80 YVFQDARLFPHYKVRGNLRYG---MA--KSMVA-----QFDKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQ----QPRT 240
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmrpwLPKE 229
|
..
gi 2790487083 241 RQ 242
Cdd:PRK11144 230 EQ 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-226 |
2.55e-33 |
|
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: 118.95 E-value: 2.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQ--TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqkglir 81
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SLRQHVGFVFQSFNLFpHRTVLENIiegpvivkgepkdeatararellakvglagketsyPRRLSGGQQQRVAIARALAM 161
Cdd:cd03247 72 ALSSLISVLNQRPYLF-DTTLRNNL-----------------------------------GRRFSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487083 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSfARDVADRAIFMDQGRIVEQG 226
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK-TLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-244 |
2.87e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 125.97 E-value: 2.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKT-TLLRSINLLEQPEGGTIRvGDITIDTAKSISQQKG 78
Cdd:PRK15134 6 LAIENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVVYPS-GDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 79 LIRSLR-QHVGFVFQS--FNLFPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGL---AGKETSYPRRLSGGQQQR 152
Cdd:PRK15134 85 TLRGVRgNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
250
....*....|...
gi 2790487083 232 FADPQQPRTRQFL 244
Cdd:PRK15134 245 FSAPTHPYTQKLL 257
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-234 |
3.09e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 122.04 E-value: 3.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTA-KSISQqkglIRSLRQHVGFVFQ--SFN 95
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlKKIKE----VKRLRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 96 LFpHRTVLENIIEGPVIVkGEPKDEATARARELLAKVGLAGKETSY-PRRLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:PRK13645 103 LF-QETIEKDIAFGPVNL-GENKQEAYKKVPELLKLVQLPEDYVKRsPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487083 175 LDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFAD 234
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-244 |
3.34e-33 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 126.51 E-value: 3.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 6 VKNLVKKFH--GQTV--LHGIDLEVEQGEVVAIIGPSGSGKT-TLLRSINLLEQpEGGTIRVGDITI-----DTAKSISQ 75
Cdd:PRK10261 15 VENLNIAFMqeQQKIaaVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMLLrrrsrQVIELSEQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 76 QKGLIRSLR-QHVGFVFQS--FNLFPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGLAGKET---SYPRRLSGGQ 149
Cdd:PRK10261 94 SAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTilsRYPHQLSGGM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPA 228
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIfITHDMGVVAEIADRVLVMYQGEAVETGSV 253
|
250
....*....|....*.
gi 2790487083 229 KSLFADPQQPRTRQFL 244
Cdd:PRK10261 254 EQIFHAPQHPYTRALL 269
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-241 |
8.24e-33 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 119.94 E-value: 8.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTI----RVGDITIDTAKSISQQKGL 79
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyimRSGAELELYQLSEAERRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 80 IRSlrqHVGFVFQSFNLFPHRTVLE--NIIEGPVIVKGEPKDEATARARELLAKVGL-AGKETSYPRRLSGGQQQRVAIA 156
Cdd:TIGR02323 84 MRT---EWGFVHQNPRDGLRMRVSAgaNIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADP 235
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGlAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
|
....*.
gi 2790487083 236 QQPRTR 241
Cdd:TIGR02323 241 QHPYTQ 246
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-236 |
1.12e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 120.29 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEG---GTIRVGDITIdTAKSISQqkglirsLRQHVGFVFQS- 93
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITL-TAKTVWD-------IREKVGIVFQNp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 94 FNLFPHRTV-------LENiiegpvivKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVI 166
Cdd:PRK13640 94 DNQFVGATVgddvafgLEN--------RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487083 167 LFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKSLFADPQ 236
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNlTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-226 |
1.21e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 119.32 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITID--TAKSISqQKGLIRSl 83
Cdd:PRK11300 8 VSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglPGHQIA-RMGVVRT- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 rqhvgfvFQSFNLFPHRTVLEN------------IIEG----PVIVKGEpkDEATARARELLAKVGLagkeTSYPRR--- 144
Cdd:PRK11300 86 -------FQHVRLFREMTVIENllvaqhqqlktgLFSGllktPAFRRAE--SEALDRAATWLERVGL----LEHANRqag 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 145 -LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMV-IVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PRK11300 153 nLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVlLIEHDMKLVMGISDRIYVVNQGTP 232
|
....
gi 2790487083 223 VEQG 226
Cdd:PRK11300 233 LANG 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
1.27e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 119.91 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGT--IRVGDITidtaksisqqK 77
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSvlIRGEPIT----------K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 78 GLIRSLRQHVGFVFQSFN--LFPhRTVLENIIEGPVIVKgepKDEATA--RARELLAKVGLAGKETSYPRRLSGGQQQRV 153
Cdd:PRK13652 71 ENIREVRKFVGLVFQNPDdqIFS-PTVEQDIAFGPINLG---LDEETVahRVSSALHMLGLEELRDRVPHHLSGGEKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLF 232
Cdd:PRK13652 147 AIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIF 226
|
...
gi 2790487083 233 ADP 235
Cdd:PRK13652 227 LQP 229
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-221 |
2.60e-32 |
|
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: 117.19 E-value: 2.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInLLE-QPEGGTIRVGDitidtaksisqqkglirslrqHVGFVFQS--- 93
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-LGElEKLSGSVSVPG---------------------SIAYVSQEpwi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 94 FNlfphRTVLENIIegpvivKGEPKDEAtaRARELLAKVGL--------AGKETSYPRR---LSGGQQQRVAIARALAMR 162
Cdd:cd03250 78 QN----GTIRENIL------FGKPFDEE--RYEKVIKACALepdleilpDGDLTEIGEKginLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487083 163 PDVILFDEPTSALDPElVGEVL--NTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGR 221
Cdd:cd03250 146 ADIYLLDDPLSAVDAH-VGRHIfeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-224 |
5.10e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 122.48 E-value: 5.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDiTIDTAksisqqkglirSL 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE-TVKIG-----------YF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGfvfqsfNLFPHRTVLENIIEGpvivkGEPKDEATARAreLLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMR 162
Cdd:COG0488 384 DQHQE------ELDPDKTVLDELRDG-----APGGTEQEVRG--YLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487083 163 PDVILFDEPTSALDPELVgEVLNTIrqLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:COG0488 451 PNVLLLDEPTNHLDIETL-EALEEA--LDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
19-226 |
5.50e-32 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 123.08 E-value: 5.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLEQ---PEGGTIRVGDITIDTAKSisqqkgliRSLRQHVGFVFQSFN 95
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKTTL---INLLQRvydPTVGQILIDGIDINTVTR--------ESLRKSIATVFQDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 96 LFpHRTVLENIIEGPVIVKGEPKDEATA----------RARELLAKVGLAGKetsyprRLSGGQQQRVAIARALAMRPDV 165
Cdd:TIGR01192 420 LF-NRSIRENIRLGREGATDEEVYEAAKaaaahdfilkRSNGYDTLVGERGN------RLSGGERQRLAIARAILKNAPI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487083 166 ILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQG 226
Cdd:TIGR01192 493 LVLDEATSALDVETEARVKNAIDALRKN-RTTFIIAHRLSTVRN-ADLVLFLDQGRLIEKG 551
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-245 |
5.79e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 122.51 E-value: 5.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 7 KNLVKKFHGQ-TVLHGIDLEVEQGEVVAIIGPSGSGKTT----LLRSINlleqpeggtiRVGDITIDTAKSISQQKGLIR 81
Cdd:PRK15134 289 KGILKRTVDHnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN----------SQGEIWFDGQPLHNLNRRQLL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SLRQHVGFVFQSFN--LFPHRTVLENIIEG-PVIVKGEPKDEATARARELLAKVGL-AGKETSYPRRLSGGQQQRVAIAR 157
Cdd:PRK15134 359 PVRHRIQVVFQDPNssLNPRLNVLQIIEEGlRVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQ 236
Cdd:PRK15134 439 ALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLfISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQ 518
|
....*....
gi 2790487083 237 QPRTRQFLE 245
Cdd:PRK15134 519 QEYTRQLLA 527
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-244 |
9.20e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 118.69 E-value: 9.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 22 IDLEVEQGEVVAIIGPSGSGKT-TLLRSINLLEQPegGTIRVGDITID----TAKSISQQKGLIRSlrqHVGFVFQS--F 94
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKLEFNgqdlQRISEKERRNLVGA---EVAMIFQDpmT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 95 NLFPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGL---AGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK11022 101 SLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487083 172 TSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQPRTRQFL 244
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALL 254
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-233 |
1.70e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 117.12 E-value: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQT---VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSIN-LLEQPEGgtirvgDITIDTAKSISQQkgl 79
Cdd:PRK13642 5 LEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDgLFEEFEG------KVKIDGELLTAEN--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 80 IRSLRQHVGFVFQS-FNLFPHRTVLENIIEGpVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
Cdd:PRK13642 76 VWNLRRKIGMVFQNpDNQFVGATVEDDVAFG-MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487083 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-222 |
2.44e-31 |
|
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: 113.68 E-value: 2.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 10 VKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVG--DITIDTAKSISQQK-GLIRSLRQH 86
Cdd:cd03215 7 VRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgkPVTRRSPRDAIRAGiAYVPEDRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 87 VGfvfqsfnLFPHRTVLENIIegpvivkgepkdeatararellakvglagketsYPRRLSGGQQQRVAIARALAMRPDVI 166
Cdd:cd03215 87 EG-------LVLDLSVAENIA---------------------------------LSSLLSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487083 167 LFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-239 |
4.05e-31 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 114.99 E-value: 4.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqkgLI 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP-------LH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK10895 74 ARARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487083 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFADPQQPR 239
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
3-233 |
1.98e-30 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 119.08 E-value: 1.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSISqqkgli 80
Cdd:TIGR01846 455 AITFENIRFRYAPDSpeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAW------ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 rsLRQHVGFVFQSFNLFpHRTVLENIIEGPvivKGEPKDEATARARellakvgLAGKE---TSYPR-----------RLS 146
Cdd:TIGR01846 529 --LRRQMGVVLQENVLF-SRSIRDNIALCN---PGAPFEHVIHAAK-------LAGAHdfiSELPQgyntevgekgaNLS 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 147 GGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQG 226
Cdd:TIGR01846 596 GGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR-GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESG 673
|
....*..
gi 2790487083 227 PAKSLFA 233
Cdd:TIGR01846 674 RHEELLA 680
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-202 |
3.15e-30 |
|
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: 117.46 E-value: 3.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqkgliRSLRQHVGFVFQSF 94
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ--------DEVRRRVSVCAQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 95 NLFpHRTVLENIIegpvIVKGEPKDEATARArelLAKVGLA--------GKET---SYPRRLSGGQQQRVAIARALAMRP 163
Cdd:TIGR02868 419 HLF-DTTVRENLR----LARPDATDEELWAA---LERVGLAdwlralpdGLDTvlgEGGARLSGGERQRLALARALLADA 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTH 202
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-236 |
2.41e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 110.59 E-value: 2.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTAKS---ISqqkglirs 82
Cdd:COG4674 13 VEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDL-TGLDeheIA-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 lRQHVGFVFQSFNLFPHRTVLENIIegpVIVKGE----------PKDEATARARELLAKVGLAGKETSYPRRLSGGQQQR 152
Cdd:COG4674 84 -RLGIGRKFQKPTVFEELTVFENLE---LALKGDrgvfaslfarLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 153 VAIARALAMRPDVILFDEPTSALDP---ELVGEVLNTIRQlaqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPVAGMTDaetERTAELLKSLAG----KHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLD 235
|
....*..
gi 2790487083 230 SLFADPQ 236
Cdd:COG4674 236 EVQADPR 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-223 |
7.15e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.57 E-value: 7.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 10 VKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTaKSISQqkglirSLRQHVGF 89
Cdd:COG1129 259 VEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRI-RSPRD------AIRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 90 V---FQSFNLFPHRTVLENII--------EGPVIvkgePKDEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIAR 157
Cdd:COG1129 332 VpedRKGEGLVLDLSIRENITlasldrlsRGGLL----DRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAK 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487083 158 ALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:COG1129 408 WLATDPKVLILDEPTRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-226 |
9.27e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 109.33 E-value: 9.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDitidtaKSISQQKGliRSL 83
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD------KPISMLSS--RQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQsfnlfpHRTVLENIIEGPVIVKGE-----------PKDEA-TARARELLAKVGLAGKETSyprRLSGGQQQ 151
Cdd:PRK11231 75 ARRLALLPQ------HHLTPEGITVRELVAYGRspwlslwgrlsAEDNArVNQAMEQTRINHLADRRLT---DLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487083 152 RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-228 |
1.30e-28 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 108.62 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI--NLLEQPEGGTIRVGDITIdTAKSISQ--QKGLir 81
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDI-LELSPDEraRAGI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 slrqhvGFVFQS---------FNLFphRTVLENIIEGPVIVKgepkdEATARARELLAKVGLAgkeTSYPRR-----LSG 147
Cdd:COG0396 80 ------FLAFQYpveipgvsvSNFL--RTALNARRGEELSAR-----EFLKLLKEKMKELGLD---EDFLDRyvnegFSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHemsFAR----DVADRAIFMDQGRIV 223
Cdd:COG0396 144 GEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH---YQRildyIKPDFVHVLVDGRIV 220
|
....*
gi 2790487083 224 EQGPA 228
Cdd:COG0396 221 KSGGK 225
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-234 |
2.60e-28 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 112.83 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 17 TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLrsiNLLEQ-PEGGTIRVGDITIDTAKSISQQkglirsLRQHVGFVFQSFN 95
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFrSPKGVKGSGSVLLNGMPIDAKE------MRAISAYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 96 LFPHRTVLENIIEGPVIVKGE--PKDEATARARELLAKVGL---AGKETSYPRR---LSGGQQQRVAIARALAMRPDVIL 167
Cdd:TIGR00955 110 FIPTLTVREHLMFQAHLRMPRrvTKKEKRERVDEVLQALGLrkcANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS---FarDVADRAIFMDQGRIVEQGP---AKSLFAD 234
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSselF--ELFDKIILMAEGRVAYLGSpdqAVPFFSD 260
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-234 |
3.17e-28 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 107.27 E-value: 3.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSinLLEQPEGGTirvGDITIDtAKSISQQKgLIRSLRQHVGFVFQSFNLF 97
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGT--LCGDPRATS---GRIVFD-GKDITDWQ-TAKIMREAVAIVPEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 98 PHRTVLENIIEGPVIVKGEPKDEATARARELLAKvgLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:PRK11614 93 SRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487083 178 ELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFAD 234
Cdd:PRK11614 171 IIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-226 |
5.63e-28 |
|
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: 106.46 E-value: 5.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 17 TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidtaksisqqKGLIRS-LRQHVGFVfqsfn 95
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV--------------RGRVSSlLGLGGGFN----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 96 lfPHRTVLENI-IEGpvIVKGEPKDEATARARELLAKVGLaGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:cd03220 97 --PELTGRENIyLNG--RLLGLSRKEIDEKIDEIIEFSEL-GDFIDLPvKTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03220 172 VGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-202 |
5.98e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 111.44 E-value: 5.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 2 SAIDVKNL-VKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLeQPEGGtirvGDITIDTAKSI---SQQK 77
Cdd:COG4178 361 GALALEDLtLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL-WPYGS----GRIARPAGARVlflPQRP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 78 GLIR-SLRQHVgfvfqsfnLFPHrtvleniiegpvivkgEPKDEATARARELLAKVGLA------GKETSYPRRLSGGQQ 150
Cdd:COG4178 436 YLPLgTLREAL--------LYPA----------------TAEAFSDAELREALEAVGLGhlaerlDEEADWDQVLSLGEQ 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2790487083 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTH 202
Cdd:COG4178 492 QRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-228 |
7.21e-28 |
|
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: 110.90 E-value: 7.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 16 QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRvgditIDTAkSISQQKGliRSLRQHVGFVFQSFN 95
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVR-----LDGA-DLKQWDR--ETFGKHIGYLPQDVE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 96 LFPHrTVLENIIEGPVIVKGEPKDEAT--ARARELLAK--------VGLAGKEtsyprrLSGGQQQRVAIARALAMRPDV 165
Cdd:TIGR01842 403 LFPG-TVAENIARFGENADPEKIIEAAklAGVHELILRlpdgydtvIGPGGAT------LSGGQRQRIALARALYGDPKL 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487083 166 ILFDEPTSALDPElvGE--VLNTIRQLAQEKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPA 228
Cdd:TIGR01842 476 VVLDEPNSNLDEE--GEqaLANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGER 537
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-233 |
2.32e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 105.86 E-value: 2.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 12 KFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqKGLIrSLRQHVGFVF 91
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSK-----RGLL-ALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 92 QSfnlfPHRTVLENIIEGPVIVK----GEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVIL 167
Cdd:PRK13638 84 QD----PEQQIFYTDIDSDIAFSlrnlGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487083 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-227 |
3.46e-27 |
|
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: 104.11 E-value: 3.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKF--HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtaKSISQQKglir 81
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI---SKIGLHD---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 sLRQHVGFVFQSFNLFPHrTVLENIiegpvivkgEPKDEAT-ARARELLAKVGLAGKETSYPRRL-----------SGGQ 149
Cdd:cd03244 76 -LRSRISIIPQDPVLFSG-TIRSNL---------DPFGEYSdEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487083 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGP 227
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-221 |
4.17e-27 |
|
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: 101.76 E-value: 4.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDitidtaksisqqkglirsl 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 rqhvgfvfqsfnlfphrtvleniiegpvivkgepkdeatararellakvglaGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03221 62 ----------------------------------------------------TVKIGYFEQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487083 164 DVILFDEPTSALDPELVgEVLntIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:cd03221 90 NLLLLDEPTNHLDLESI-EAL--EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
15-233 |
6.24e-27 |
|
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: 108.67 E-value: 6.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqkglIRSLRQHVGFVFQSF 94
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID--------RHTLRQFINYLPQEP 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 95 NLFPHrTVLENIIEGPVIVKGEPKDEATARARELLAKV-----GLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFD 169
Cdd:TIGR01193 558 YIFSG-SILENLLLGAKENVSQDEIWAACEIAEIKDDIenmplGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILD 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487083 170 EPTSALDPELVGEVLNTIRQLaQEKrTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKSLFA 233
Cdd:TIGR01193 637 ESTSNLDTITEKKIVNNLLNL-QDK-TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLD 697
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-231 |
8.66e-27 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 107.71 E-value: 8.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 7 KNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLeQPEGGTirVGDITID----TAKSI--SQQKGLI 80
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGTY--EGEIIFEgeelQASNIrdTERAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 rslrqhvgFVFQSFNLFPHRTVLENIIEGPVIVKGEPKD--EATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
Cdd:PRK13549 86 --------IIHQELALVKELSVLENIFLGNEITPGGIMDydAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-235 |
1.10e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 108.01 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHG-IDLEVEQGEVVAIIGPSGSGKTTLLrsiNLLEQ--PEGGTIRVGDITIdtaKSISQQkgli 80
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLL---NALLGflPYQGSLKINGIEL---RELDPE---- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 rSLRQHVGFVFQSFNLFpHRTVLENIIEGPVIVKGEPKDEATARAR--ELLAKV--GLAG--KETSypRRLSGGQQQRVA 154
Cdd:PRK11174 420 -SWRKHLSWVGQNPQLP-HGTLRDNVLLGNPDASDEQLQQALENAWvsEFLPLLpqGLDTpiGDQA--AGLSVGQAQRLA 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKSLFAD 234
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ-TTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQA 573
|
.
gi 2790487083 235 P 235
Cdd:PRK11174 574 G 574
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-229 |
2.21e-26 |
|
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: 101.45 E-value: 2.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPE--GGTIRVGDITIdTAKSISQqkgliRSl 83
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDI-TDLPPEE-----RA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSfnlfphrtvleniiegPVIVKGepkdeatARARELLAKVGLAgketsyprrLSGGQQQRVAIARALAMRP 163
Cdd:cd03217 76 RLGIFLAFQY----------------PPEIPG-------VKNADFLRYVNEG---------FSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH-EMSFARDVADRAIFMDQGRIVEQGPAK 229
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-226 |
2.37e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 106.79 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDT-AKSISQQKGlirs 82
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKlDHKLAAQLG---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 lrqhVGFVFQSFNLFPHRTVLENIIEGPVIVK---GEPK---DEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
Cdd:PRK09700 82 ----IGIIYQELSVIDELTVLENLYIGRHLTKkvcGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-224 |
3.74e-26 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 101.57 E-value: 3.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 16 QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI--NLLEQPEGGTIRVGDITIDtaksisqqkglirslrqhvgfvfqs 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFG------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 94 fnlfPHRTVLENIiegpvivkgePKDEATARARELLAKVGLAgkeTSY-----PRRLSGGQQQRVAIARALAMRPDVILF 168
Cdd:COG2401 98 ----REASLIDAI----------GRKGDFKDAVELLNAVGLS---DAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487083 169 DEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVA-DRAIFMDQGRIVE 224
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLARRAGiTLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-222 |
5.02e-26 |
|
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: 101.39 E-value: 5.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLE---QPEGGTIRVgditidTAKSISQQKGliRSLRQHVGFVFQSF 94
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTV---VALLEnfyQPQGGQVLL------DGKPISQYEH--KYLHSKVSLVGQEP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 95 NLFPhRTVLENIIEGpviVKGEPKDEATARARELLAKVGLAGKETSYPR-------RLSGGQQQRVAIARALAMRPDVIL 167
Cdd:cd03248 98 VLFA-RSLQDNIAYG---LQSCSFECVKEAAQKAHAHSFISELASGYDTevgekgsQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2790487083 168 FDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRI 222
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-226 |
8.52e-26 |
|
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: 105.87 E-value: 8.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 6 VKNLVKKFH--GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAksisqqkglIRSL 83
Cdd:TIGR01257 931 VKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN---------LDAV 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENIIEGPVIvKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:TIGR01257 1002 RQSLGMCPQHNILFHHLTVAEHILFYAQL-KGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDA 1080
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:TIGR01257 1081 KVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-238 |
1.16e-25 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 102.50 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGgtiRVGDITIDTAKSIS-- 74
Cdd:PRK09473 10 DALLDVKDLRVTFSTPdgdvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANG---RIGGSATFNGREILnl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 75 QQKGLIRSLRQHVGFVFQ----SFNlfPHRTVLENIIEGPVIVKGEPKDEATARARELLAKVGL--AGKE-TSYPRRLSG 147
Cdd:PRK09473 87 PEKELNKLRAEQISMIFQdpmtSLN--PYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMpeARKRmKMYPHEFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYG 244
|
250
....*....|..
gi 2790487083 227 PAKSLFADPQQP 238
Cdd:PRK09473 245 NARDVFYQPSHP 256
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-226 |
2.03e-25 |
|
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: 100.10 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 6 VKNLVK-KFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGD-ITIDTAKSISQQKGLIRSL 83
Cdd:cd03267 23 LKSLFKrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVPWKRRKKFLRRIGVVFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGF---VFQSFNLFPHrtvleniiegpviVKGEPKDEATARARELLAKVGLaGKETSYP-RRLSGGQQQRVAIARAL 159
Cdd:cd03267 103 KTQLWWdlpVIDSFYLLAA-------------IYDLPPARFKKRLDELSELLDL-EELLDTPvRQLSLGQRMRAEIAAAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487083 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03267 169 LHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTsHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-227 |
2.69e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.83 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDItidtaksisQQKGLI 80
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV---------PVPARA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRQHVGFVFQSFNLFPHRTVLENIIegpVIVK--GEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
Cdd:PRK13536 110 RLARARIGVVPQFDNLDLEFTVRENLL---VFGRyfGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR-IVEQGP 227
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRkIAEGRP 256
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-244 |
7.05e-25 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 99.09 E-value: 7.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKK-------FHGQTV--LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTaksis 74
Cdd:PRK15112 5 LEVRNLSKTfryrtgwFRRQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 75 qqkGLIRSLRQHVGFVFQ--SFNLFPhRTVLENIIEGPVIVKGEPKDEATARA-RELLAKVGLAGKETSY-PRRLSGGQQ 150
Cdd:PRK15112 80 ---GDYSYRSQRIRMIFQdpSTSLNP-RQRISQILDFPLRLNTDLEPEQREKQiIETLRQVGLLPDHASYyPHMLAPGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLEL-QEKQgiSYIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
250
....*....|....*.
gi 2790487083 229 KSLFADPQQPRTRQFL 244
Cdd:PRK15112 235 ADVLASPLHELTKRLI 250
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
11-205 |
9.90e-25 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 102.27 E-value: 9.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 11 KKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInlleqpeGGTIRVGDITidtAKSISQQKGLIRSLRQHVGFV 90
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQGNNFT---GTILANNRKPTKQILKRTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 91 FQSFNLFPHRTVLENIIEGPVI--VKGEPKDEATARARELLAKVGLAGKET-----SYPRRLSGGQQQRVAIARALAMRP 163
Cdd:PLN03211 146 TQDDILYPHLTVRETLVFCSLLrlPKSLTKQEKILVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINP 225
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPS 267
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-226 |
1.12e-24 |
|
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: 97.47 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgDITIDTAKsisqqkgLIRSL 83
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSG-----EIIFDGHP-------WTRKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENIiEGPVIVKGEPKdeatARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:TIGR03740 69 LHKIGSLIESPPLYENLTARENL-KVHTTLLGLPD----SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHP 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:TIGR03740 144 KLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQG 206
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-234 |
1.38e-24 |
|
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: 101.44 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLeQPEGGTirVGDITIDTAKSISQqkGLIRSL 83
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGTW--DGEIYWSGSPLKAS--NIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPK---DEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARAL 159
Cdd:TIGR02633 77 RAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRmayNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487083 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFAD 234
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSED 231
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-224 |
1.72e-24 |
|
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: 101.41 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 22 IDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqkglIRSLRQHVGFVFQSFNLFPHrt 101
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN--------REAYRQLFSAVFSDFHLFDR-- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 102 vleniiegpviVKGEPKDEATARARELLAKVGLAGKeTSY------PRRLSGGQQQRVAIARALAMRPDVILFDEPTSAL 175
Cdd:COG4615 421 -----------LLGLDGEADPARARELLERLELDHK-VSVedgrfsTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQ 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487083 176 DP--------ELVGEvlntirqLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVE 224
Cdd:COG4615 489 DPefrrvfytELLPE-------LKARGKTVIAISHDDRYF-DLADRVLKMDYGKLVE 537
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-202 |
2.07e-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: 96.27 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDitidtaKSISQQKGlirSLRQ 85
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG------TPLAEQRD---EPHE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 86 HVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKDeatarARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:TIGR01189 74 NILYLGHLPGLKPELSALENLHFWAAIHGGAQRT-----IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 2790487083 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH 202
Cdd:TIGR01189 149 WILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-231 |
1.22e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 98.97 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAK-SISQQKGLIrs 82
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIY-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 lrqhvgFVFQSFNLFPHRTVLENIIegpvivKGEPKDEAT-ARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALaM 161
Cdd:PRK15439 90 ------LVPQEPLLFPNLSVKENIL------FGLPKRQASmQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGL-M 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487083 162 RPDVIL-FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:PRK15439 157 RDSRILiLDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-224 |
1.46e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 98.44 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 8 NLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSISqqkglirSLRQHV 87
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTA-------ALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 88 GFVFQSFNLFPHRTVLENIIEGPVIVKGEPKDEAT--ARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLGQLPHKGGIVNRRLlnYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADR-AIFMDqGRIVE 224
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAiTVFKD-GRYVA 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-210 |
1.94e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.40 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqkgliRSLRQHVGFVFQSF 94
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP--------EIYRQQVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 95 NLFPHrTVLENIIEGPVIVKGEPKDEATARArelLAKVGLAgkETSYPRR---LSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK10247 91 TLFGD-TVYDNLIFPWQIRNQQPDPAIFLDD---LERFALP--DTILTKNiaeLSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2790487083 172 TSALDPELVGEVLNTIRQLAQEKRTMVI-VTH---EMSFARDV 210
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLwVTHdkdEINHADKV 207
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-202 |
5.91e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.63 E-value: 5.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSISQ------QKGLIRSLrqhvg 88
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchylghRNAMKPAL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 89 fvfqsfnlfphrTVLENIIEGPVIVKGEPKDEATArarelLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILF 168
Cdd:PRK13539 89 ------------TVAENLEFWAAFLGGEELDIAAA-----LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 2790487083 169 DEPTSALDPELVGEVLNTIR-QLAQEkrTMVIV-TH 202
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRaHLAQG--GIVIAaTH 185
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-227 |
9.49e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 94.38 E-value: 9.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFH--------GQTV-------------LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIR 61
Cdd:COG4586 1 IIEVENLSKTYRvyekepglKGALkglfrreyreveaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 62 VGDITidtaksISQQKgliRSLRQHVGFVF-------------QSFNLFPHrtvleniiegpviVKGEPKDEATARAREL 128
Cdd:COG4586 81 VLGYV------PFKRR---KEFARRIGVVFgqrsqlwwdlpaiDSFRLLKA-------------IYRIPDAEYKKRLDEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 129 LAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSfa 207
Cdd:COG4586 139 VELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTsHDMD-- 216
|
250 260
....*....|....*....|...
gi 2790487083 208 rDV---ADRAIFMDQGRIVEQGP 227
Cdd:COG4586 217 -DIealCDRVIVIDHGRIIYDGS 238
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-207 |
4.37e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 90.25 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 20 HGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDitidtaKSISQQKGlirSLRQhvgfvfqsfNLF-- 97
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG------EPIRRQRD---EYHQ---------DLLyl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 98 -------PHRTVLENI-----IEGPVivkgepKDEATARArelLAKVGLAGKETSYPRRLSGGQQQRVAIAR-ALAMRPD 164
Cdd:PRK13538 80 ghqpgikTELTALENLrfyqrLHGPG------DDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARlWLTRAPL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2790487083 165 VILfDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVT--HEMSFA 207
Cdd:PRK13538 151 WIL-DEPFTAIDKQGVARLEALLAQHA-EQGGMVILTthQDLPVA 193
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-226 |
5.24e-22 |
|
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: 90.16 E-value: 5.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKF--HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqkglIR 81
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP--------LE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SLRQHVGFVFQSFNLFPHrTVLENIiegpvivkgEPKDEATarARELLAkvglAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:cd03369 79 DLRSSLTIIPQDPTLFSG-TIRSNL---------DPFDEYS--DEEIYG----ALRVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487083 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQG 226
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-237 |
7.34e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.55 E-value: 7.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 6 VKNL-VKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTAKSISQ--QKGL--I 80
Cdd:COG3845 260 VENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI-TGLSPRErrRLGVayI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRQHVGfvfqsfnLFPHRTVLENII----EGPVIVKG--EPKDEATARARELLAKVGLAGKETSYP-RRLSGGQQQRV 153
Cdd:COG3845 339 PEDRLGRG-------LVPDMSVAENLIlgryRRPPFSRGgfLDRKAIRAFAEELIEEFDVRTPGPDTPaRSLSGGNQQKV 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 154 AIARALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKS 230
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLD---VGaieFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAE 488
|
....*..
gi 2790487083 231 lfADPQQ 237
Cdd:COG3845 489 --ATREE 493
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-233 |
9.82e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 93.54 E-value: 9.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLeqpeggT----IRVGDITIDtakSISQQKGLIRSLRQHVGFVFQSF 94
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTI---ANLL------TrfydIDEGEILLD---GHDLRDYTLASLRNQVALVSQNV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 95 NLFpHRTVLENIIEGPVIVKGEPKDEATAR---ARELLAK--------VGLAGKEtsyprrLSGGQQQRVAIARALAMRP 163
Cdd:PRK11176 427 HLF-NDTIANNIAYARTEQYSREQIEEAARmayAMDFINKmdngldtvIGENGVL------LSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLA 567
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-226 |
1.27e-21 |
|
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: 88.86 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 11 KKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLL----EQPEGgTIRVGDITIDTAKSISQQkglirslrqH 86
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegnVSVEG-DIHYNGIPYKEFAEKYPG---------E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 87 VGFVFQSFNLFPHRTVLENIiegpvivkgepkdEATARARellakvglaGKEtsYPRRLSGGQQQRVAIARALAMRPDVI 166
Cdd:cd03233 85 IIYVSEEDVHFPTLTVRETL-------------DFALRCK---------GNE--FVRGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487083 167 LFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTheMSFARDVA----DRAIFMDQGRIVEQG 226
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS--LYQASDEIydlfDKVLVLYEGRQIYYG 202
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3-235 |
1.33e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 93.24 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqkglIRS 82
Cdd:PRK10789 315 DVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ--------LDS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 LRQHVGFVFQSFNLFPHrTVLENIIEGpvivkgepKDEATARARELLAKvgLA-----------GKETSYPRR---LSGG 148
Cdd:PRK10789 387 WRSRLAVVSQTPFLFSD-TVANNIALG--------RPDATQQEIEHVAR--LAsvhddilrlpqGYDTEVGERgvmLSGG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPA 228
Cdd:PRK10789 456 QKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNH 533
|
....*..
gi 2790487083 229 KSLFADP 235
Cdd:PRK10789 534 DQLAQQS 540
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-231 |
2.60e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 89.66 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 7 KNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqkgliRSLRQH 86
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS--------KEVARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 87 VGFVFQSFNLFPHRTVLENIIEG-----PVIVKGEPKDE-ATARARELLAKVGLAGKETSyprRLSGGQQQRVAIARALA 160
Cdd:PRK10253 83 IGLLAQNATTPGDITVQELVARGryphqPLFTRWRKEDEeAVTKAMQATGITHLADQSVD---TLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487083 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNREKgYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-202 |
3.19e-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: 87.93 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDtaksisQQKGlirSL 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD------FQRD---SI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENIiegpvivKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03231 72 ARGLLYLGHAPGIKTTLSVLENL-------RFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGR 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH 202
Cdd:cd03231 145 PLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-234 |
3.20e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 92.49 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 16 QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLrSINLLEQPeggTIRVGDITIdtaksisqqkglirslRQHVGFVFQSFN 95
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLI-SAMLGELP---PRSDASVVI----------------RGTVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 96 LFpHRTVLENIIEGPVI--VKGEPKDEATARARELLAKVGlaGKETSYPRR---LSGGQQQRVAIARALAMRPDVILFDE 170
Cdd:PLN03130 690 IF-NATVRDNILFGSPFdpERYERAIDVTALQHDLDLLPG--GDLTEIGERgvnISGGQKQRVSMARAVYSNSDVYIFDD 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487083 171 PTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKSLFAD 234
Cdd:PLN03130 767 PLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-202 |
3.52e-21 |
|
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: 86.82 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgditidtaksisqqkglIRSLRQHVGFVfqsf 94
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-------------------GMPEGEDLLFL---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 95 nlfPHRTVLeniiegpvivkgepkdeATARARELLAkvglagketsYP--RRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:cd03223 70 ---PQRPYL-----------------PLGTLREQLI----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEAT 119
|
170 180 190
....*....|....*....|....*....|.
gi 2790487083 173 SALDPelvgEVLNTIRQLAQEKRTMVI-VTH 202
Cdd:cd03223 120 SALDE----ESEDRLYQLLKELGITVIsVGH 146
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
7-224 |
4.03e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 88.69 E-value: 4.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 7 KNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLrsiNLLeqpEG----GTIRvGDITIDTA----KSI--SQQ 76
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLM---KVL---SGvyphGSYE-GEILFDGEvcrfKDIrdSEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 77 KGLIrslrqhvgFVFQSFNLFPHRTVLENIIEGPVIVKGEPKD--EATARARELLAKVGLAGKETSYPRRLSGGQQQRVA 154
Cdd:NF040905 78 LGIV--------IIHQELALIPYLSIAENIFLGNERAKRGVIDwnETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-245 |
5.15e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 87.27 E-value: 5.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKF---HGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInLLEQPEGGTI-----RVGDITIdTAK 71
Cdd:COG4170 1 MPLLDIRNLTIEIdtpQGRVkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAI-CGITKDNWHVtadrfRWNGIDL-LKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 72 SISQQKGLIRslrQHVGFVFQ--SFNLFPHRTVLENIIEgpVI----VKG---EPKDEATARARELLAKVGLAGKE---T 139
Cdd:COG4170 79 SPRERRKIIG---REIAMIFQepSSCLDPSAKIGDQLIE--AIpswtFKGkwwQRFKWRKKRAIELLHRVGIKDHKdimN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 140 SYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMD 218
Cdd:COG4170 154 SYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLY 233
|
250 260
....*....|....*....|....*..
gi 2790487083 219 QGRIVEQGPAKSLFADPQQPRTRQFLE 245
Cdd:COG4170 234 CGQTVESGPTEQILKSPHHPYTKALLR 260
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-231 |
5.21e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.99 E-value: 5.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSisqqkgliRSLRQHVGFVFQSF 94
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS--------KAFARKVAYLPQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 95 NLFPHRTVLENIIEGPVI---VKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK10575 95 PAAEGMTVRELVAIGRYPwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487083 172 TSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSQERGLTVIaVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-233 |
6.78e-20 |
|
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: 88.46 E-value: 6.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI-NLLEQPEGgtirvgDITIDTAKSISQQKGLIR--SLRqhvgfvfqsfn 95
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALlAEMDKVEG------HVHMKGSVAYVPQQAWIQndSLR----------- 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 96 lfphrtvlENIIEGPVIvkGEPKDEATARARELLAKVGL--AGKETSYPRR---LSGGQQQRVAIARALAMRPDVILFDE 170
Cdd:TIGR00957 717 --------ENILFGKAL--NEKYYQQVLEACALLPDLEIlpSGDRTEIGEKgvnLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487083 171 PTSALDPELVGEVL-NTIRQLAQEK-RTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKSLFA 233
Cdd:TIGR00957 787 PLSAVDAHVGKHIFeHVIGPEGVLKnKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
14-232 |
7.10e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.09 E-value: 7.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 14 HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINlleqpegGTIRV--GDITIdtaksisQQKGLIRSLRQH-VGFV 90
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALM-------GFVRLasGKISI-------LGQPTRQALQKNlVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 91 FQSFNL---FPhrTVLENIIE----GPVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:PRK15056 84 PQSEEVdwsFP--VLVEDVVMmgryGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487083 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIfMDQGRIVEQGPAKSLF 232
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTF 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-225 |
7.94e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 87.75 E-value: 7.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAI-DVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRV--GDITIDTAKSiSQQK 77
Cdd:PRK10762 1 MQALlQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgKEVTFNGPKS-SQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 78 GlirslrqhVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPK---DEATARARELLAKVGLAGKETSYPRRLSGGQQQRVA 154
Cdd:PRK10762 80 G--------IGIIHQELNLIPQLTIAENIFLGREFVNRFGRidwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790487083 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADR-AIFMDQGRIVEQ 225
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDvTVFRDGQFIAER 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-190 |
9.91e-20 |
|
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: 87.68 E-value: 9.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDiTIdtaksisqqkglirsl 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE-TV---------------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 rqHVGFVFQSF-NLFPHRTVLENIIEG-PVIVKGepKDEATARAreLLAKVGLAGKETSYP-RRLSGGQQQRVAIARALA 160
Cdd:TIGR03719 386 --KLAYVDQSRdALDPNKTVWEEISGGlDIIKLG--KREIPSRA--YVGRFNFKGSDQQKKvGQLSGGERNRVHLAKTLK 459
|
170 180 190
....*....|....*....|....*....|
gi 2790487083 161 MRPDVILFDEPTSALDpelvgevLNTIRQL 190
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLD-------VETLRAL 482
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-231 |
1.92e-19 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 85.94 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 2 SAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLeQPEGGTIRVGDITIdtaksISQQKGLIR 81
Cdd:NF000106 12 NAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*-GPDAGRRPWRF*TW-----CANRRALRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SLRQHVGFVFQSFNLFPHRtvlENIIEGPVIVKGEPKDeATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:NF000106 86 TIG*HRPVR*GRRESFSGR---ENLYMIGR*LDLSRKD-ARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-232 |
7.00e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 85.80 E-value: 7.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQT---VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInLLEQPEGGTIRVgditidtaksisqqkgl 79
Cdd:PLN03232 614 AISIKNGYFSWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM-LGELSHAETSSV----------------- 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 80 irSLRQHVGFVFQSFNLFpHRTVLENIIEGPvivKGEPKD-----EATARAREL-------LAKVGLAGKEtsyprrLSG 147
Cdd:PLN03232 676 --VIRGSVAYVPQVSWIF-NATVRENILFGS---DFESERywraiDVTALQHDLdllpgrdLTEIGERGVN------ISG 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGP 227
Cdd:PLN03232 744 GQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGT 822
|
....*
gi 2790487083 228 AKSLF 232
Cdd:PLN03232 823 FAELS 827
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-220 |
8.15e-19 |
|
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: 81.14 E-value: 8.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSinLLEQPEGGTIRvGDITIDTaksisqqKGLIRSLRQHVGFVFQSFNLFP 98
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDV--LAGRKTAGVIT-GEILING-------RPLDKNFQRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 99 HRTVLENIiegpvivkgepkdeatararELLAKVglagketsypRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPE 178
Cdd:cd03232 93 NLTVREAL--------------------RFSALL----------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2790487083 179 LVGEVLNTIRQLAQEKRTMVIVTHEMS---FARdvADRAIFMDQG 220
Cdd:cd03232 143 AAYNIVRFLKKLADSGQAILCTIHQPSasiFEK--FDRLLLLKRG 185
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-178 |
1.37e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 84.40 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditiDTAKsisqqkglirsl 83
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG----ETVK------------ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 rqhVGFVFQSF-NLFPHRTVLENIIEGPVIVK-GepKDEATARAreLLAKVGLAGKETSYP-RRLSGGQQQRVAIARALA 160
Cdd:PRK11819 389 ---LAYVDQSRdALDPNKTVWEEISGGLDIIKvG--NREIPSRA--YVGRFNFKGGDQQKKvGVLSGGERNRLHLAKTLK 461
|
170
....*....|....*...
gi 2790487083 161 MRPDVILFDEPTSALDPE 178
Cdd:PRK11819 462 QGGNVLLLDEPTNDLDVE 479
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-224 |
1.47e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 5 DVKNLVKKFHGQtvLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVG--DITIDTA-KSISQQKGLIR 81
Cdd:PRK09700 267 EVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNgkDISPRSPlDAVKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SLRQHVGFvfqsfnlFPHRTVLENIIEGPVIVKG---------EPKDEA-TARARELLAKVGLAGKETSYpRRLSGGQQQ 151
Cdd:PRK09700 345 ESRRDNGF-------FPNFSIAQNMAISRSLKDGgykgamglfHEVDEQrTAENQRELLALKCHSVNQNI-TELSGGNQQ 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 152 RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-224 |
2.15e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 83.87 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 22 IDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKsisqqkglIRSLRQHVGFVFQSFNLFPHrt 101
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ--------PEDYRKLFSAVFTDFHLFDQ-- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 102 vleniIEGPvivKGEPKDEATARA----RELLAKVGLAGKETSYPrRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:PRK10522 412 -----LLGP---EGKPANPALVEKwlerLKMAHKLELEDGRISNL-KLSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2790487083 178 ----ELVGEVLNTIRQLAQekrTMVIVTHEMSFArDVADRAIFMDQGRIVE 224
Cdd:PRK10522 483 hfrrEFYQVLLPLLQEMGK---TIFAISHDDHYF-IHADRLLEMRNGQLSE 529
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-227 |
5.19e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 80.64 E-value: 5.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI--NLLE--QPEGGTIRvGDITID---TAKSISQQKGLIRS-LRQH 86
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGggAPRGARVT-GDVTLNgepLAAIDAPRLARLRAvLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 87 V--GFVFQ-----SFNLFPH-RTVLENIIEgpvivKGEPKDEATARArellAKVGLAGKETSyprRLSGGQQQRVAIARA 158
Cdd:PRK13547 92 AqpAFAFSareivLLGRYPHaRRAGALTHR-----DGEIAWQALALA----GATALVGRDVT---TLSGGELARVQFARV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487083 159 LAM---------RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGP 227
Cdd:PRK13547 160 LAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLaIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-223 |
6.43e-18 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 82.25 E-value: 6.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTI------RVGDITIDTAKSISQQ 76
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenaNIGYYAQDHAYDFEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 77 KGLIRSLRQHvgfvfqsfnlfphrtvleniiegpvivKGEPKDEATARAreLLAKVGLAGKETSYP-RRLSGGQQQRVAI 155
Cdd:PRK15064 399 LTLFDWMSQW---------------------------RQEGDDEQAVRG--TLGRLLFSQDDIKKSvKVLSGGEKGRMLF 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487083 156 ARALAMRPDVILFDEPTSALDPELVgEVLNTirQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMDMESI-ESLNM--ALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-229 |
8.27e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.88 E-value: 8.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI-NLLeqPEGGTIRVGDITID--TAKSISQQKGLirsLRQHV--GF---V 90
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMaGLL--PGQGEILLNGRPLSdwSAAELARHRAY---LSQQQspPFampV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 91 FQSFNLFPHRtvleniiegpvivkGEPKDEATARARELLAKVGLAGKetsYPR---RLSGGQQQRVAIARAL-----AMR 162
Cdd:COG4138 87 FQYLALHQPA--------------GASSEAVEQLLAQLAEALGLEDK---LSRpltQLSGGEWQRVRLAAVLlqvwpTIN 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487083 163 PD--VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
Cdd:COG4138 150 PEgqLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-223 |
2.50e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.73 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 5 DVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAK---SISQQKGLIR 81
Cdd:PRK11288 255 EVRLRLDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSprdAIRAGIMLCP 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SLRQHVGFVfqsfnlfPHRTVLENI--------IEGPVIVKGEPKDEATARARELLaKVGLAGKETSYpRRLSGGQQQRV 153
Cdd:PRK11288 335 EDRKAEGII-------PVHSVADNInisarrhhLRAGCLINNRWEAENADRFIRSL-NIKTPSREQLI-MNLSGGNQQKA 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 154 AIARALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:PRK11288 406 ILGRWLSEDMKVILLDEPTRGID---VGakhEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-228 |
1.34e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.63 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDtAKSISqqkglirs 82
Cdd:NF033858 266 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD-AGDIA-------- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 83 LRQHVGFVFQSFNLFPHRTVLENIiegpvivkgE--------PKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVA 154
Cdd:NF033858 337 TRRRVGYMSQAFSLYGELTVRQNL---------ElharlfhlPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLS 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 155 IARALAMRPDVILFDEPTSALDP-------ELVGEvlntirqLAQEKR-TMVIVTHEMSFA-RdvADRAIFMDQGRIVEQ 225
Cdd:NF033858 408 LAVAVIHKPELLILDEPTSGVDPvardmfwRLLIE-------LSREDGvTIFISTHFMNEAeR--CDRISLMHAGRVLAS 478
|
....
gi 2790487083 226 G-PA 228
Cdd:NF033858 479 DtPA 482
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-220 |
1.70e-16 |
|
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: 75.83 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDtakSISQQKGLIRSlRQHVGFVFQSF 94
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNES---EPSFEATRSRN-RYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 95 NLFpHRTVLENIIEGPVIVKGEPKdeATARARELLAKVGLA--GKETSYPRR---LSGGQQQRVAIARALAMRPDVILFD 169
Cdd:cd03290 89 WLL-NATVEENITFGSPFNKQRYK--AVTDACSLQPDIDLLpfGDQTEIGERginLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 170 EPTSALDPELVGEVLNT--IRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQG 220
Cdd:cd03290 166 DPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-190 |
2.21e-16 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 77.75 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLrSINLLEQPEGGTirvGDITIdtaksISQQKG---LI 80
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL-SLITGDHPQGYS---NDLTL-----FGRRRGsgeTI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRQHVGFVFQSFNLfPHR---TVLENIIEG---PVIVKGEPKDEATARARELLAKVGLAGKETSYP-RRLSGGQQQRV 153
Cdd:PRK10938 332 WDIKKHIGYVSSSLHL-DYRvstSVRNVILSGffdSIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLA 410
|
170 180 190
....*....|....*....|....*....|....*..
gi 2790487083 154 AIARALAMRPDVILFDEPTSALDPelvgevLNtiRQL 190
Cdd:PRK10938 411 LIVRALVKHPTLLILDEPLQGLDP------LN--RQL 439
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-221 |
2.39e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 77.67 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidtAKSISqqkglirslrqhVGFVFQSF 94
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-------QPGIK------------VGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 95 NLFPHRTVLENIIEGPVIVK-------------GEPKDEATARARE---------------LLAKVGLAGKETSYP---- 142
Cdd:TIGR03719 78 QLDPTKTVRENVEEGVAEIKdaldrfneisakyAEPDADFDKLAAEqaelqeiidaadawdLDSQLEIAMDALRCPpwda 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 143 --RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVG--EvlntiRQLAQEKRTMVIVTHEMSFARDVADRAIFMD 218
Cdd:TIGR03719 158 dvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAwlE-----RHLQEYPGTVVAVTHDRYFLDNVAGWILELD 232
|
...
gi 2790487083 219 QGR 221
Cdd:TIGR03719 233 RGR 235
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-234 |
3.10e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.86 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQ--TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtaksisQQKGLi 80
Cdd:PLN03130 1237 SIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI-------SKFGL- 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRQHVGFVFQS---------FNLFP---HRTV-LENIIEgpvivKGEPKDEATARARELLAKVGLAGKEtsyprrLSG 147
Cdd:PLN03130 1309 MDLRKVLGIIPQApvlfsgtvrFNLDPfneHNDAdLWESLE-----RAHLKDVIRRNSLGLDAEVSEAGEN------FSV 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRqlaQEKR--TMVIVTHEMSFARDvADRAIFMDQGRIVEQ 225
Cdd:PLN03130 1378 GQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIR---EEFKscTMLIIAHRLNTIID-CDRILVLDAGRVVEF 1453
|
....*....
gi 2790487083 226 GPAKSLFAD 234
Cdd:PLN03130 1454 DTPENLLSN 1462
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-233 |
3.23e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 77.45 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLE---QPEGGTIRVGDITIdtaKSISQQkg 78
Cdd:PRK10790 340 RIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTL---ASLLMgyyPLTEGEIRLDGRPL---SSLSHS-- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 79 lirSLRQHVGFVFQSFNLFPHrTVLENIIEGpvivkgepKDEATARARELLAKVGLAGKETSYP-----------RRLSG 147
Cdd:PRK10790 412 ---VLRQGVAMVQQDPVVLAD-TFLANVTLG--------RDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSV 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 148 GQQQRVAIARALAMRPDVILFDEPTSALDP---ELVGEVLNTIRqlaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
Cdd:PRK10790 480 GQKQLLALARVLVQTPQILILDEATANIDSgteQAIQQALAAVR----EHTTLVVIAHRLSTIVE-ADTILVLHRGQAVE 554
|
....*....
gi 2790487083 225 QGPAKSLFA 233
Cdd:PRK10790 555 QGTHQQLLA 563
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-248 |
1.04e-15 |
|
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: 73.98 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 24 LEVEQG-----EVVAIIGPSGSGKTTLLRSINLLEQPEGGTI--RVGDITIDTAKSISQQKGLIRSLRQHVGFVFQSFNL 96
Cdd:cd03237 15 LEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIeiELDTVSYKPQYIKADYEGTVRDLLSSITKDFYTHPY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 97 FPHRTV----LENIIEgpvivkgepkdeataraRELlakvglagketsypRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:cd03237 95 FKTEIAkplqIEQILD-----------------REV--------------PELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487083 173 SALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIfmdqgrIVEQGPAKSLFADPQQPRtRQFLEKFL 248
Cdd:cd03237 144 AYLDVEQRLMASKVIRRFAENnEKTAFVVEHDIIMIDYLADRLI------VFEGEPSVNGVANPPQSL-RSGMNRFL 213
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-220 |
4.36e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 74.37 E-value: 4.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSinLLEQPEGGTIRVGDItidtaksISQQKGLIRSLRQHVGFVFQSFNLF 97
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNV--LAERVTTGVITGGDR-------LVNGRPLDSSFQRSIGYVQQQDLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 98 PHRTVLENII-----EGPVIVKGEPKDEATARARELL-------AKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPDV 165
Cdd:TIGR00956 849 PTSTVRESLRfsaylRQPKSVSKSEKMEYVEEVIKLLemesyadAVVGVPGEG------LNVEQRKRLTIGVELVAKPKL 922
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487083 166 ILF-DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS---FARdvADRAIFMDQG 220
Cdd:TIGR00956 923 LLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSailFEE--FDRLLLLQKG 979
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-241 |
8.23e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 72.53 E-value: 8.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPE----GGTIRVGDItiDTAKS 72
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSdgwvKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDI--DLLRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 73 ISQQKgliRSLRQH-VGFVFQSFN--LFPHRTVLENIIEG-PV-IVKGEPKDEATARAR---ELLAKVGLAGKE---TSY 141
Cdd:PRK15093 79 SPRER---RKLVGHnVSMIFQEPQscLDPSERVGRQLMQNiPGwTYKGRWWQRFGWRKRraiELLHRVGIKDHKdamRSF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 142 PRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQG 220
Cdd:PRK15093 156 PYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNtTILLISHDLQMLSQWADKINVLYCG 235
|
250 260
....*....|....*....|.
gi 2790487083 221 RIVEQGPAKSLFADPQQPRTR 241
Cdd:PRK15093 236 QTVETAPSKELVTTPHHPYTQ 256
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-244 |
1.13e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 73.22 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 8 NLVKKFHGQT---VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINllEQPEGGTIRV-GDITIDtakSISQQKgLIRSL 83
Cdd:TIGR00956 63 RKLKKFRDTKtfdILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIA--SNTDGFHIGVeGVITYD---GITPEE-IKKHY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPHRTVLENI-----IEGPVI-VKGEPKDEATARAREL-LAKVGLA-GKET----SYPRRLSGGQQQ 151
Cdd:TIGR00956 137 RGDVVYNAETDVHFPHLTVGETLdfaarCKTPQNrPDGVSREEYAKHIADVyMATYGLShTRNTkvgnDFVRGVSGGERK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 152 RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMS-FARDVADRAIFMDQGRIVEQGP-- 227
Cdd:TIGR00956 217 RVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiYQCSqDAYELFDKVIVLYEGYQIYFGPad 296
|
250 260
....*....|....*....|...
gi 2790487083 228 -AKSLFAD-----PQQPRTRQFL 244
Cdd:TIGR00956 297 kAKQYFEKmgfkcPDRQTTADFL 319
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-236 |
1.43e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 72.89 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAksisqqkGLiRSLRQHvgfvfqsFNLF 97
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAY-------GL-RELRRQ-------FSMI 1389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 98 PHRTVLeniIEGPVIVKGEPKDEATA----RARELlakVGLAGKETSY-----PRRLSG------GQQQRVAIARALAMR 162
Cdd:PTZ00243 1390 PQDPVL---FDGTVRQNVDPFLEASSaevwAALEL---VGLRERVASEsegidSRVLEGgsnysvGQRQLMCMARALLKK 1463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487083 163 -PDVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMsfaRDVA--DRAIFMDQGRIVEQGPAKSLFADPQ 236
Cdd:PTZ00243 1464 gSGFILMDEATANIDPALDRQIQATVMS-AFSAYTVITIAHRL---HTVAqyDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-204 |
2.16e-14 |
|
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: 72.12 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 27 EQGEVVAIIGPSGSGKTTllrSINLLeqpeGGTIR--VGDITIDTAKSisqqkgliRSLRQHVGFVFQSFnlfphrtvLE 104
Cdd:COG1245 97 KKGKVTGILGPNGIGKST---ALKIL----SGELKpnLGDYDEEPSWD--------EVLKRFRGTELQDY--------FK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 105 NIIEG--------------PVIVKGEPK------DEaTARARELLAKVGLagkETSYPRR---LSGGQQQRVAIARALAM 161
Cdd:COG1245 154 KLANGeikvahkpqyvdliPKVFKGTVRellekvDE-RGKLDELAEKLGL---ENILDRDiseLSGGELQRVAIAAALLR 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2790487083 162 RPDVILFDEPTSALDpelVGEVLN---TIRQLAQEKRTMVIVTHEM 204
Cdd:COG1245 230 DADFYFFDEPSSYLD---IYQRLNvarLIRELAEEGKYVLVVEHDL 272
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-205 |
2.38e-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: 70.47 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 18 VLHGIDLeVEQGEVVAIIGPSGSGKTTLLRsinlleqpeggtIRVGDITIDTAKSISQQ--KGLIRSLRqhvGFVFQSFn 95
Cdd:cd03236 16 KLHRLPV-PREGQVLGLVGPNGIGKSTALK------------ILAGKLKPNLGKFDDPPdwDEILDEFR---GSELQNY- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 96 lfphrtvLENIIEGPV--IVKGEPKDE----ATARARELLAKVGLAGKETSYPRR-------------LSGGQQQRVAIA 156
Cdd:cd03236 79 -------FTKLLEGDVkvIVKPQYVDLipkaVKGKVGELLKKKDERGKLDELVDQlelrhvldrnidqLSGGELQRVAIA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2790487083 157 RALAMRPDVILFDEPTSALDpelVGEVLN---TIRQLAQEKRTMVIVTHEMS 205
Cdd:cd03236 152 AALARDADFYFFDEPSSYLD---IKQRLNaarLIRELAEDDNYVLVVEHDLA 200
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-224 |
2.76e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.91 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 3 AIDVKNLVKKFHGQtvlhgidleVEQGEVVAIIGPSGSGKTTLLRSinLLEQ--PEGGTIRVGditidtaksisqQKGLI 80
Cdd:PRK11147 328 QIDGKQLVKDFSAQ---------VQRGDKIALIGPNGCGKTTLLKL--MLGQlqADSGRIHCG------------TKLEV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRQHVGfvfqsfNLFPHRTVLENIIEGP--VIVKGepkdeataRARELLakvglagketSY-------PRR------- 144
Cdd:PRK11147 385 AYFDQHRA------ELDPEKTVMDNLAEGKqeVMVNG--------RPRHVL----------GYlqdflfhPKRamtpvka 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 145 LSGGQQQRVAIARaLAMRP-DVILFDEPTSALDPELVgEVLNTIrqLAQEKRTMVIVTHEMSFARD-VADRAIFMDQGRI 222
Cdd:PRK11147 441 LSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDVETL-ELLEEL--LDSYQGTVLLVSHDRQFVDNtVTECWIFEGNGKI 516
|
..
gi 2790487083 223 VE 224
Cdd:PRK11147 517 GR 518
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-233 |
3.54e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 71.69 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTV-LHGIDLEVEQGEVVAIIGPSGSGKTTLL------RSInlleqpEGGTIRV--GDITidtaksisqQKGLIRSLRQ 85
Cdd:NF033858 12 GKTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKI------QQGRVEVlgGDMA---------DARHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 86 HVGFVFQSF--NLFPHRTVLENIiegpvivkGEPKDEATARARELLAKVGL-------AGKetsyprrLSGGQQQRVAIA 156
Cdd:NF033858 77 RIAYMPQGLgkNLYPTLSVFENLdffg-rlfGQDAAERRRRIDELLRATGLapfadrpAGK-------LSGGMKQKLGLC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 157 RALAMRPDVILFDEPTSALDP-------ELVgevlNTIRqlaQEKRTM-VIV-THEMSFARDVaDRAIFMDQGRIVEQGP 227
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVDPlsrrqfwELI----DRIR---AERPGMsVLVaTAYMEEAERF-DWLVAMDAGRVLATGT 220
|
....*.
gi 2790487083 228 AKSLFA 233
Cdd:NF033858 221 PAELLA 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-215 |
5.77e-14 |
|
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: 70.97 E-value: 5.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 25 EVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgditiDTAKSIS--------QQKGLIRS-LRQHVGFVFQSfN 95
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------DEDLKISykpqyispDYDGTVEEfLRSANTDDFGS-S 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 96 LFPHRTV----LENIIEGPVivkgepkdeatararellakvglagketsypRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:COG1245 434 YYKTEIIkplgLEKLLDKNV-------------------------------KDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2790487083 172 TSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAI 215
Cdd:COG1245 483 SAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLM 527
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-215 |
6.53e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.61 E-value: 6.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 24 LEVE-----QGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrVGDITI---------DTAKSISQqkgLIRSLRQHVGf 89
Cdd:PRK13409 355 LEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-DPELKIsykpqyikpDYDGTVED---LLRSITDDLG- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 90 vfQSF--NLFPHRTVLENIIEGPVivkgepkdeatararellakvglagketsypRRLSGGQQQRVAIARALAMRPDVIL 167
Cdd:PRK13409 430 --SSYykSEIIKPLQLERLLDKNV-------------------------------KDLSGGELQRVAIAACLSRDADLYL 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2790487083 168 FDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAI 215
Cdd:PRK13409 477 LDEPSAHLDVEQRLAVAKAIRRIAEEREaTALVVDHDIYMIDYISDRLM 525
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-223 |
6.68e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.75 E-value: 6.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINlleqpeggtirvGDITIDTAKSISQQKGLI 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN------------GEVLLDDGRIIYEQDLIV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRQHvgfvfqsfnlfPHR----TVLENIIEG--------------PVIVKGEPKDEA-------------------TA 123
Cdd:PRK11147 69 ARLQQD-----------PPRnvegTVYDFVAEGieeqaeylkryhdiSHLVETDPSEKNlnelaklqeqldhhnlwqlEN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 124 RARELLAKVGL-AGKETSyprRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPElvgevlnTIRQLAQ----EKRTMV 198
Cdd:PRK11147 138 RINEVLAQLGLdPDAALS---SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE-------TIEWLEGflktFQGSII 207
|
250 260
....*....|....*....|....*
gi 2790487083 199 IVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:PRK11147 208 FISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-222 |
9.04e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.03 E-value: 9.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 10 VKKFHGQTVlHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTaksISQQKGL------IRSL 83
Cdd:PRK10762 260 VDNLSGPGV-NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT---RSPQDGLangivyISED 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVF-----QSFNLfphrTVLENIIEGPVIVKGEPKDEATARARELL--------AKVGLagketsyprrLSGGQQ 150
Cdd:PRK10762 336 RKRDGLVLgmsvkENMSL----TALRYFSRAGGSLKHADEQQAVSDFIRLFniktpsmeQAIGL----------LSGGNQ 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487083 151 QRVAIARALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-220 |
1.55e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.04 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 26 VEQGEVVAIIGPSGSGKTTLLRSINlleqpeggtirvGDITIDTAKSISQQKGLIRSLRQhvgfVFQSFNLFPHRTVLEN 105
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLT------------GDTTVTSGDATVAGKSILTNISD----VHQNMGYCPQFDAIDD 2025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 106 IIEGP------VIVKGEPKDEATARARELLAKVGLagkeTSYPRRL----SGGQQQRVAIARALAMRPDVILFDEPTSAL 175
Cdd:TIGR01257 2026 LLTGRehlylyARLRGVPAEEIEKVANWSIQSLGL----SLYADRLagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2790487083 176 DPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQG 220
Cdd:TIGR01257 2102 DPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-204 |
1.56e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.22 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRvgditidtaksisqqkgliRSL 83
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-------------------RNG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 RQHVGFVFQSFNLFPhrtVLENIIEGPVIVKGEPKDEATARArelLAKVGlAGKETSYP-RRLSGGQQQRVAIARALAMR 162
Cdd:PRK09544 66 KLRIGYVPQKLYLDT---TLPLTVNRFLRLRPGTKKEDILPA---LKRVQ-AGHLIDAPmQKLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2790487083 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEM 204
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLmVSHDL 181
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-230 |
1.86e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 25 EVEQGEVVAIIGPSGSGKTTLLRSI-NLLEQPegGTIRVGDITIDT--AKSISQQKGLIrSLRQHVGF---VFQSFNLFP 98
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMaGLLPGS--GSIQFAGQPLEAwsAAELARHRAYL-SQQQTPPFampVFQYLTLHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 99 HrtvleniiegpvivKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA-LAMRPDV------ILFDEP 171
Cdd:PRK03695 95 P--------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790487083 172 TSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKS 230
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
18-178 |
2.59e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.80 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRvgditIDTAKSISQQKGlirslrQHVGFVFQSFNLF 97
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQ-----IDGKTATRGDRS------RFMAYLGHLPGLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 98 PHRTVLENIiegpVIVKGEPKDEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:PRK13543 95 ADLSTLENL----HFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
.
gi 2790487083 178 E 178
Cdd:PRK13543 171 E 171
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-204 |
3.06e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.68 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 26 VEQGEVVAIIGPSGSGKTTllrSINLLeqpeGGTIR--VGDITIDTAKSisqqkgliRSLRQHVGFVFQSFnlfphrtvL 103
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTT---AVKIL----SGELIpnLGDYEEEPSWD--------EVLKRFRGTELQNY--------F 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 104 ENIIEG--------------PVIVKGepkdeataRARELLAKVGLAGKETSYPRR-------------LSGGQQQRVAIA 156
Cdd:PRK13409 153 KKLYNGeikvvhkpqyvdliPKVFKG--------KVRELLKKVDERGKLDEVVERlglenildrdiseLSGGELQRVAIA 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2790487083 157 RALAMRPDVILFDEPTSALDpelVGEVLN---TIRQLAqEKRTMVIVTHEM 204
Cdd:PRK13409 225 AALLRDADFYFFDEPTSYLD---IRQRLNvarLIRELA-EGKYVLVVEHDL 271
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-234 |
5.30e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 5.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 7 KNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI-NLLEQPEGGTIRVG-DITIDTAKsisqqkgliRSLR 84
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLfGIYQKDSGSILFQGkEIDFKSSK---------EALE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 85 QHVGFVFQSFNLFPHRTVLENI------IEGPVIVKGEPKDEATARARELLAKVGLAGKETSyprrLSGGQQQRVAIARA 158
Cdd:PRK10982 73 NGISMVHQELNLVLQRSVMDNMwlgrypTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVAT----LSVSQMQMIEIAKA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487083 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFAD 234
Cdd:PRK10982 149 FSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMD 224
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-226 |
6.07e-13 |
|
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: 65.04 E-value: 6.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInlleqpeggtirvgditIDTAKSISQQKGLIRSLRQHVGFVFQsfnlfp 98
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG-----------------LYASGKARLISFLPKFSRNKLIFIDQ------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 99 hrtvLENIIegpvivkgepkdeatararellaKVGLA----GKETSyprRLSGGQQQRVAIARALAMRPD--VILFDEPT 172
Cdd:cd03238 68 ----LQFLI-----------------------DVGLGyltlGQKLS---TLSGGELQRVKLASELFSEPPgtLFILDEPS 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFM------DQGRIVEQG 226
Cdd:cd03238 118 TGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVL-SSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-226 |
6.39e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.35 E-value: 6.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPE--GGTIRV-GDITIDTAKSISQQKGLI 80
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFkGKDLLELSPEDRAGEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 81 RSLRQHVGFVFQSFNLFPHRTV----------------LENIIEGPVIVKGEPKDEATARarellAKVGlagketsyprr 144
Cdd:PRK09580 82 MAFQYPVEIPGVSNQFFLQTALnavrsyrgqepldrfdFQDLMEEKIALLKMPEDLLTRS-----VNVG----------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 145 LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVA-DRAIFMDQGRIV 223
Cdd:PRK09580 146 FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIV 225
|
...
gi 2790487083 224 EQG 226
Cdd:PRK09580 226 KSG 228
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-228 |
7.95e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.20 E-value: 7.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInlLEQPeGGTIRVGDITIDtAKSISQQKGLIRSl 83
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--AGHP-AYKILEGDILFK-GESILDLEPEERA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 rqHVGfVFQSFNlFPhrtvleniIEGPVI---------------VKGEPKDEATARARELLAKVGLAGKETSYPRR---- 144
Cdd:CHL00131 83 --HLG-IFLAFQ-YP--------IEIPGVsnadflrlaynskrkFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRnvne 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 145 -LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHemsFAR--D--VADRAIFMDQ 219
Cdd:CHL00131 151 gFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH---YQRllDyiKPDYVHVMQN 227
|
....*....
gi 2790487083 220 GRIVEQGPA 228
Cdd:CHL00131 228 GKIIKTGDA 236
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-233 |
9.18e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.69 E-value: 9.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDItiDTAKsisqqkglirslrqhvgfvfqsFNLF 97
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDC--DVAK----------------------FGLT 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 98 PHRTVLENIIEGPVIVKG----------EPKD----EATARA--RELLAK--VGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:PLN03232 1307 DLRRVLSIIPQSPVLFSGtvrfnidpfsEHNDadlwEALERAhiKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARAL 1386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487083 160 AMRPDVILFDEPTSALDPELVGEVLNTIRqlaQEKR--TMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIR---EEFKscTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLS 1458
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-220 |
3.59e-12 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 64.49 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 14 HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIR-VGDItidtakSISQQKGLIR--SLRQHVGFV 90
Cdd:cd03291 48 VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKhSGRI------SFSSQFSWIMpgTIKENIIFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 91 FqSFNLFPHRTVLENIIEGPVIVKGEPKDEAtarareLLAKVGLAgketsyprrLSGGQQQRVAIARALAMRPDVILFDE 170
Cdd:cd03291 122 V-SYDEYRYKSVVKACQLEEDITKFPEKDNT------VLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790487083 171 PTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQG 220
Cdd:cd03291 186 PFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLK-KADKILILHEG 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-235 |
3.97e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.57 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSinLLEQPEGGTIRVGditidTAKSIS---QQKGLIRSlrqhvgfvfqsf 94
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQS--LLSQFEISEGRVW-----AERSIAyvpQQAWIMNA------------ 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 95 nlfphrTVLENIIegpvivKGEPKDEA----TARARELLAKVGL--AGKETSYPRR---LSGGQQQRVAIARALAMRPDV 165
Cdd:PTZ00243 736 ------TVRGNIL------FFDEEDAArladAVRVSQLEADLAQlgGGLETEIGEKgvnLSGGQKARVSLARAVYANRDV 803
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487083 166 ILFDEPTSALDPElVGE-VLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKSLFADP 235
Cdd:PTZ00243 804 YLLDDPLSALDAH-VGErVVEECFLGALAGKTRVLATHQVHVV-PRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-221 |
4.40e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.14 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 10 VKKFHGQ--TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidtaksisqQKGLirslrqHV 87
Cdd:PRK11819 12 VSKVVPPkkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP-------------APGI------KV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 88 GFVFQSFNLFPHRTVLENIIEGPVIVK-------------GEPKDE---------------ATARARELLAKVGLAGKET 139
Cdd:PRK11819 73 GYLPQEPQLDPEKTVRENVEEGVAEVKaaldrfneiyaayAEPDADfdalaaeqgelqeiiDAADAWDLDSQLEIAMDAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 140 SYP------RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVG--EvlntiRQLAQEKRTMVIVTHEMSFARDVA 211
Cdd:PRK11819 153 RCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAwlE-----QFLHDYPGTVVAVTHDRYFLDNVA 227
|
250
....*....|
gi 2790487083 212 DRAIFMDQGR 221
Cdd:PRK11819 228 GWILELDRGR 237
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-222 |
6.12e-12 |
|
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: 64.85 E-value: 6.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 22 IDLEVEQGEVVAIIGPSGSGKTTLLRSI-NLLEQPEGGTIRVGDITIDT---AKSISQQKGLIRSLRQHVGFVfqsfnlf 97
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIrnpAQAIRAGIAMVPEDRKRHGIV------- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 98 PHRTVLENIIEGPV-IVKGEPKDEATARARELLAKVGLAGKETSYP----RRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:TIGR02633 352 PILGVGKNITLSVLkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790487083 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-222 |
1.11e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.92 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 22 IDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTAKSISQqkglirslRQHVGFVF-----QSFNL 96
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEI-NALSTAQ--------RLARGLVYlpedrQSSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 97 FPHRTVLENIIEGPVIVKG---EPKDEAtARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:PRK15439 353 YLDAPLAWNVCALTHNRRGfwiKPAREN-AVLERYRRALNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790487083 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-216 |
1.65e-11 |
|
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: 60.46 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 28 QGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSISQQKGLIRSLRQHVGfvfqsfnlfphrtvlenii 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASG------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 108 egpvivkgepkdeatararellakvglagketsyprrlSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVL--- 184
Cdd:smart00382 62 --------------------------------------SGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlle 103
|
170 180 190
....*....|....*....|....*....|....*
gi 2790487083 185 ---NTIRQLAQEKRTMVIVTHEMSFARDVADRAIF 216
Cdd:smart00382 104 elrLLLLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-212 |
2.00e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.50 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTAKSISQQKglirsl 83
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQ------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 84 rqhVGFVFQSFNLFPHRTVLENIIEgpvivkgEPKDEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMR 162
Cdd:PRK13540 76 ---LCFVGHRSGINPYLTLRENCLY-------DIHFSPGAVGITELCRLFSLEHLIDYPcGLLSSGQKRQVALLRLWMSK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790487083 163 PDVILFDEPTSALDpELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVAD 212
Cdd:PRK13540 146 AKLWLLDEPLVALD-ELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-247 |
3.42e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.60 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgDITiDTAKSISQQKGLIRSLrqhvgfvfqsfnlfp 98
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV---DIK-GSAALIAISSGLNGQL--------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 99 hrTVLENiIEGPVIVKGEPKDEatarARELLAKV---GLAGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:PRK13545 101 --TGIEN-IELKGLMMGLTKEK----IKEIIPEIiefADIGKFIYQPvKTYSSGMKSRLGFAISVHINPDILVIDEALSV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 175 LDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFAdpqqpRTRQFLEKF 247
Cdd:PRK13545 174 GDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD-----HYDEFLKKY 241
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-227 |
5.33e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.17 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 29 GEVVAIIGPSGSGKTTLLRSinLLEQPEGGTIRvGDITI-------DTAKSISqqkglirslrqhvGFVFQSFNLFPHRT 101
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDV--LAGRKTGGYIE-GDIRIsgfpkkqETFARIS-------------GYCEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 102 VLENIIEG-----PVIVKGEPKDEATARARELL-------AKVGLAGKETsyprrLSGGQQQRVAIARALAMRPDVILFD 169
Cdd:PLN03140 970 VRESLIYSaflrlPKEVSKEEKMMFVDEVMELVeldnlkdAIVGLPGVTG-----LSTEQRKRLTIAVELVANPSIIFMD 1044
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 170 EPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSF-ARDVADRAIFMDQ-GRIVEQGP 227
Cdd:PLN03140 1045 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLMKRgGQVIYSGP 1104
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-238 |
6.73e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 6.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLvkKFHGQT-----VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGD------ITIDTAKS 72
Cdd:PTZ00265 383 IQFKNV--RFHYDTrkdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdINLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 73 ----ISQQKGLI-RSLRQHVGFVFQS-----------------------------------FNLFPHRTVLENIIEGPVI 112
Cdd:PTZ00265 461 kigvVSQDPLLFsNSIKNNIKYSLYSlkdlealsnyynedgndsqenknkrnscrakcagdLNDMSNTTDSNELIEMRKN 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 113 VKGEPKDEATARARELLAK---VGLAGK-ET---SYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPE---LVGE 182
Cdd:PTZ00265 541 YQTIKDSEVVDVSKKVLIHdfvSALPDKyETlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseyLVQK 620
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2790487083 183 VLNTIRqlAQEKRTMVIVTHEMSFARDVadRAIFMDQGRivEQGPAKSLFADPQQP 238
Cdd:PTZ00265 621 TINNLK--GNENRITIIIAHRLSTIRYA--NTIFVLSNR--ERGSTVDVDIIGEDP 670
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
144-222 |
7.53e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.48 E-value: 7.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 144 RLSGGQQQRVAIARALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQG 220
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
..
gi 2790487083 221 RI 222
Cdd:PRK13549 482 KL 483
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-248 |
8.94e-11 |
|
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: 59.12 E-value: 8.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 25 EVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtakSISQQKglirslrqhvgfvfqsfnlfphrtvle 104
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP----VYKPQY--------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 105 niiegpvivkgepkdeatararellakvglagketsypRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVL 184
Cdd:cd03222 70 --------------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAA 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487083 185 NTIRQLAQE-KRTMVIVTHEMSFARDVADRAIfmdqgrIVEQGPAKSLFADPQQPrTRQFLEKFL 248
Cdd:cd03222 112 RAIRRLSEEgKKTALVVEHDLAVLDYLSDRIH------VFEGEPGVYGIASQPKG-TREGINRFL 169
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-223 |
1.17e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.96 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI--NLLEQPEGGTIRVGDITIDTaKSISQ--------------QKGLIr 81
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYGRNISGTVFKDGKEVDV-STVSDaidaglayvtedrkGYGLN- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 sLRQHVGFVFQSFNL--FPHRTVLENIIEgpVIVKGEPKDEATARARELLAKVGlagketsyprRLSGGQQQRVAIARAL 159
Cdd:NF040905 353 -LIDDIKRNITLANLgkVSRRGVIDENEE--IKVAEEYRKKMNIKTPSVFQKVG----------NLSGGNQQKVVLSKWL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487083 160 AMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:NF040905 420 FTDPDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-220 |
1.58e-10 |
|
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: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 14 HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIR-VGDItidtakSISQQKGLIR--SLRQHVGFV 90
Cdd:TIGR01271 437 YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKhSGRI------SFSPQTSWIMpgTIKDNIIFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 91 FqSFNLFPHRTVLENIIEGPVIVKGEPKDEAtarareLLAKVGLAgketsyprrLSGGQQQRVAIARALAMRPDVILFDE 170
Cdd:TIGR01271 511 L-SYDEYRYTSVIKACQLEEDIALFPEKDKT------VLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790487083 171 PTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQG 220
Cdd:TIGR01271 575 PFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-189 |
1.66e-10 |
|
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: 60.69 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKF--HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEggtirvGDITID--TAKSISQQK-- 77
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE------GEIQIDgvSWNSVTLQTwr 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 78 ---GLIrslRQHVgFVFQ-SF--NLFPHRtvleniiegpvivkgEPKDEATARAREllaKVGLAGKETSYPRR------- 144
Cdd:TIGR01271 1292 kafGVI---PQKV-FIFSgTFrkNLDPYE---------------QWSDEEIWKVAE---EVGLKSVIEQFPDKldfvlvd 1349
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2790487083 145 ----LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQ 189
Cdd:TIGR01271 1350 ggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-233 |
1.78e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 60.73 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTL-LRSINLLEQPEGgtirvgDITIDtakSISQQKGLIRSLRQHVGFVFQSFNL 96
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFRINESAEG------EIIID---GLNIAKIGLHDLRFKITIIPQDPVL 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 97 FPHrTVLENIieGPVivkGEPKDEATARARELlakVGLAGKETSYPRRL-----------SGGQQQRVAIARALAMRPDV 165
Cdd:TIGR00957 1372 FSG-SLRMNL--DPF---SQYSDEEVWWALEL---AHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487083 166 ILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDVAdRAIFMDQGRIVEQGPAKSLFA 233
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
145-224 |
2.15e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 145 LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR--- 221
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLvag 471
|
...
gi 2790487083 222 IVE 224
Cdd:PRK10982 472 IVD 474
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-189 |
3.13e-10 |
|
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: 59.10 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKF--HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGgtirvgDITIDtakSISQQKGLIR 81
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG------DIQID---GVSWNSVPLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 82 SLRQHVGFVFQSFNLF--PHRTVLENiiegpvivKGEPKDEATARAREllaKVGLAGKETSYPRRL-----------SGG 148
Cdd:cd03289 74 KWRKAFGVIPQKVFIFsgTFRKNLDP--------YGKWSDEEIWKVAE---EVGLKSVIEQFPGQLdfvlvdggcvlSHG 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2790487083 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQ 189
Cdd:cd03289 143 HKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ 183
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
121-222 |
6.86e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 6.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 121 ATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDpelvgevLNTIRQLAQE----KR 195
Cdd:PRK15064 131 AEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------INTIRWLEDVlnerNS 203
|
90 100 110
....*....|....*....|....*....|.
gi 2790487083 196 TMVIVTHEMSFARDV----ADraifMDQGRI 222
Cdd:PRK15064 204 TMIIISHDRHFLNSVcthmAD----LDYGEL 230
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-234 |
8.49e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 8.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI-NLLEQPEGGtiRVGDITIDTAKSISQQKGL 79
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALaGELPLLSGE--RQSQFSHITRLSFEQLQKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 80 IRSlrqhvgfVFQSFN---LFPH-----RTVLEniiegpvIVKGEPKDeaTARARELLAKVGLagkETSYPRR---LSGG 148
Cdd:PRK10938 79 VSD-------EWQRNNtdmLSPGeddtgRTTAE-------IIQDEVKD--PARCEQLAQQFGI---TALLDRRfkyLSTG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
Cdd:PRK10938 140 ETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGER 219
|
....*.
gi 2790487083 229 KSLFAD 234
Cdd:PRK10938 220 EEILQQ 225
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-212 |
1.22e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 56.46 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 31 VVAIIGPSGSGKTTLLRSINLL---EQPEGGTIRVGDITIDTAKSISQQKGLIRSLRQHVGF-VFQSFNlfphrtVLENI 106
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKYAltgELPPNSKGGAHDPKLIREGEVRAQVKLAFENANGKKYtITRSLA------ILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 107 IegpvIVKGEPKDEATARAREllakvglagketsyprRLSGGQQQ------RVAIARALAMRPDVILFDEPTSALDPELV 180
Cdd:cd03240 98 I----FCHQGESNWPLLDMRG----------------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENI 157
|
170 180 190
....*....|....*....|....*....|....
gi 2790487083 181 GEVLNTI--RQLAQEKRTMVIVTHEMSFaRDVAD 212
Cdd:cd03240 158 EESLAEIieERKSQKNFQLIVITHDEEL-VDAAD 190
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
141-205 |
2.18e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 2.18e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487083 141 YPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP---ELVGEVLNTIRQLAQekRTMVIVTHEMS 205
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKAD--KTIITIAHRIA 1420
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-233 |
2.43e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 53.37 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLVKKFHG--QTVLHGIDLEVEQGEVVAIIGPSGSGKTTL----LRSINLLEqpeggtirvGDITIDtakSISQQK 77
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD---------GKIVID---GIDISK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 78 GLIRSLRQHVGFVFQS---------FNLFPHRTVLEN-------IIEGPVIVKGEPKdeatararellakvGLAGKETSY 141
Cdd:cd03288 88 LPLHTLRSRLSIILQDpilfsgsirFNLDPECKCTDDrlwealeIAQLKNMVKSLPG--------------GLDAVVTEG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 142 PRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPElVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGR 221
Cdd:cd03288 154 GENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGI 231
|
250
....*....|..
gi 2790487083 222 IVEQGPAKSLFA 233
Cdd:cd03288 232 LVECDTPENLLA 243
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
119-210 |
4.78e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 119 DEATARARELLAKVGLAGK-ETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDpelVGEVLNTIRQLAQEKRTM 197
Cdd:PLN03073 318 YTAEARAASILAGLSFTPEmQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTF 394
|
90
....*....|...
gi 2790487083 198 VIVTHEMSFARDV 210
Cdd:PLN03073 395 IVVSHAREFLNTV 407
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
15-205 |
1.34e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.06 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgdiTIDTAKSI---SQQKGL-IRSLRQHVGFV 90
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL-----TKPAKGKLfyvPQRPYMtLGTLRDQIIYP 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 91 FQSFNLFPH---RTVLENIIEG---PVIVKGEPKDEATARARELLakvglagketsyprrlSGGQQQRVAIARALAMRPD 164
Cdd:TIGR00954 539 DSSEDMKRRglsDKDLEQILDNvqlTHILEREGGWSAVQDWMDVL----------------SGGEKQRIAMARLFYHKPQ 602
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2790487083 165 VILFDEPTSALDPELVGEvlntIRQLAQEKR-TMVIVTHEMS 205
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGY----MYRLCREFGiTLFSVSHRKS 640
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
23-216 |
1.48e-07 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 51.54 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 23 DLEVE-QGEVVAIIGPSGSGKTTLLRSINLL-----------------EQPEGGTIRVgDITIDTAKSISQQKGLIRSLR 84
Cdd:COG3593 16 DLSIElSDDLTVLVGENNSGKSSILEALRLLlgpsssrkfdeedfylgDDPDLPEIEI-ELTFGSLLSRLLRLLLKEEDK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 85 QHVGFVFQSFN--LFPHRTVLENIIEGPVIVKGEPKD---EATARARELLAK---VGLAGKETSYPRRLSGGQQQRVAIA 156
Cdd:COG3593 95 EELEEALEELNeeLKEALKALNELLSEYLKELLDGLDlelELSLDELEDLLKslsLRIEDGKELPLDRLGSGFQRLILLA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487083 157 RALAM-------RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIF 216
Cdd:COG3593 175 LLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVPLENIR 241
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
29-202 |
1.82e-07 |
|
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: 49.67 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 29 GEVVAIIGPSGSGKTTLLRSINLLeqpeggtirVGDITIDTAKSISQQKGLIRSLrQHVGFVFqsfnlfphrtvleniie 108
Cdd:cd03227 21 GSLTIITGPNGSGKSTILDAIGLA---------LGGAQSATRRRSGVKAGCIVAA-VSAELIF----------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 109 gpvIVKGepkdeatararellakvglagketsyprrLSGGQQQRVAIARALA----MRPDVILFDEPTSALDPELVGEVL 184
Cdd:cd03227 74 ---TRLQ-----------------------------LSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALA 121
|
170
....*....|....*...
gi 2790487083 185 NTIRQLAQEKRTMVIVTH 202
Cdd:cd03227 122 EAILEHLVKGAQVIVITH 139
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
123-224 |
2.68e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 123 ARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDpelVGEVLNTIRQLAQEKRTMVIVT 201
Cdd:PRK10636 127 SRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILIS 203
|
90 100
....*....|....*....|...
gi 2790487083 202 HEMSFARDVADRAIFMDQGRIVE 224
Cdd:PRK10636 204 HDRDFLDPIVDKIIHIEQQSLFE 226
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-234 |
3.85e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 21 GIDLEVEqgevVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgditidtaksisqqkglIRSLRQHVGFVFQsfnlfpHR 100
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTV-------------------FRSAKVRMAVFSQ------HH 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 101 TVLENIIEGPVI-----VKGEPKDeataRARELLAKVGLAGKETSYPR-RLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:PLN03073 582 VDGLDLSSNPLLymmrcFPGVPEQ----KLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNH 657
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 175 LDPELVgEVLntIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVeqgPAKSLFAD 234
Cdd:PLN03073 658 LDLDAV-EAL--IQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVT---PFHGTFHD 711
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-226 |
9.24e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.41 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTL-------------LRSIN--------LLEQPEggtirVGDIT-IDTAKSIsQQ 76
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLSayarqflgQMDKPD-----VDSIEgLSPAIAI-DQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 77 KGLIRSLRQHVGFVFQSFNLFphRTVLENIiegpvivkgepkdeaTARAR-ELLAKVGLA----GKETSyprRLSGGQQQ 151
Cdd:cd03270 85 KTTSRNPRSTVGTVTEIYDYL--RLLFARV---------------GIRERlGFLVDVGLGyltlSRSAP---TLSGGEAQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 152 RVAIARALAMRPDVIL--FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFM------DQGRIV 223
Cdd:cd03270 145 RIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIR-AADHVIDIgpgagvHGGEIV 223
|
...
gi 2790487083 224 EQG 226
Cdd:cd03270 224 AQG 226
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
19-227 |
1.11e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 48.38 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI------NLL----EQPEGGTIRVGDITIDTAKSISQQkgLI-RSLRQ-- 85
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTlypalaRRLhlkkEQPGNHDRIEGLEHIDKVIVIDQS--PIgRTPRSnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 86 --HVGfVFQSF-NLFP--------HRTVLENIIEGPVI--VKGEPKDEA---------TARARELLAKVGLA----GKET 139
Cdd:cd03271 89 atYTG-VFDEIrELFCevckgkryNRETLEVRYKGKSIadVLDMTVEEAleffenipkIARKLQTLCDVGLGyiklGQPA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 140 SYprrLSGGQQQRVAIARALAMR---PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIF 216
Cdd:cd03271 168 TT---LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK-CADWIID 243
|
250
....*....|....*..
gi 2790487083 217 MDQ------GRIVEQGP 227
Cdd:cd03271 244 LGPeggdggGQVVASGT 260
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-222 |
1.36e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 16 QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgditidtaksisqqkGLIRSLRqhVGFVFQsfn 95
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-----------------GLAKGIK--LGYFAQ--- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 96 lfpHRTVLENIIEGPV--IVKGEPKdEATARARELLAKVGLAG-KETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:PRK10636 383 ---HQLEFLRADESPLqhLARLAPQ-ELEQKLRDYLGGFGFQGdKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2790487083 173 SALDPELvgevlntiRQLAQE-----KRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PRK10636 459 NHLDLDM--------RQALTEalidfEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-247 |
1.39e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.27 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTI-RVGDITIdtaksISQQKGLIRSLrqhvgfvfqsfnlf 97
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdRNGEVSV-----IAISAGLSGQL-------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 98 phrTVLENIiEGPVIVKGEPKDEATARARELLAKVGLaGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSALD 176
Cdd:PRK13546 101 ---TGIENI-EFKMLCMGFKRKEIKAMTPKIIEFSEL-GEFIYQPvKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790487083 177 PELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFadpqqPRTRQFLEKF 247
Cdd:PRK13546 176 QTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL-----PKYEAFLNDF 241
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-202 |
1.50e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 47.31 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 4 IDVKNLvKKFHGQTVlhgIDLEveqGEVVAIIGPSGSGKTTLLRSINLL---EQPEGGTIRVGDITIDTAKS-----ISQ 75
Cdd:COG0419 5 LRLENF-RSYRDTET---IDFD---DGLNLIVGPNGAGKSTILEAIRYAlygKARSRSKLRSDLINVGSEEAsveleFEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 76 QKGLIRSLRqhvgfvFQS-FNLFPH------RTVLENIIEGPVIVK-----GEPKDEATARARELLAKVGLAGK------ 137
Cdd:COG0419 78 GGKRYRIER------RQGeFAEFLEakpserKEALKRLLGLEIYEElkerlKELEEALESALEELAELQKLKQEilaqls 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790487083 138 ETSYPRRLSGGQQQRVAIARALAMrpdviLFDepTSALDPELVGEVLNTIRQLAqekrtmvIVTH 202
Cdd:COG0419 152 GLDPIETLSGGERLRLALADLLSL-----ILD--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
145-232 |
1.50e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 145 LSGGQQQRVAIARALAMRPDVILF--DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE---MSFArdvadraifmdq 219
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGITYilDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLA------------ 544
|
90
....*....|...
gi 2790487083 220 GRIVEQGPAKSLF 232
Cdd:PRK00635 545 DRIIDIGPGAGIF 557
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-204 |
2.35e-05 |
|
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: 45.00 E-value: 2.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 145 LSGGQQQRVAIARALAMR---PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEM 204
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
99-202 |
1.94e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.99 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 99 HRTVLENIIEGPVIVKGEPKDEATARARELLAKVGLAGKETSYprRLSGGQQQ---RVAIARALAMRPDVILFDEPTSAL 175
Cdd:pfam13304 193 KLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAF--ELSDGTKRllaLLAALLSALPKGGLLLIDEPESGL 270
|
90 100
....*....|....*....|....*..
gi 2790487083 176 DPELVGEVLNTIRQLAQEKRTMVIVTH 202
Cdd:pfam13304 271 HPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
13-52 |
2.93e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.96 E-value: 2.93e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2790487083 13 FHGQTVlhgidlEVEQGEVVAIIGPSGSGKTTLLRSINLL 52
Cdd:pfam13555 12 FDGHTI------PIDPRGNTLLTGPSGSGKSTLLDAIQTL 45
|
|
| ABC_ATPase |
pfam09818 |
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. ... |
146-224 |
3.57e-04 |
|
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. This entry also includes MRB1590 from Trypanosoma brucei brucei has a central ATPase domain homologous to this domain.
Pssm-ID: 462914 Cd Length: 282 Bit Score: 41.04 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 146 SGGQQQRVAIARALAMRPDVILFDEPTSA--------LDPELVG---EVLNTIRQLAQEKR-----TMVIVTHEMSFARD 209
Cdd:pfam09818 159 SGSTSQAANIMEALEAGASLLLIDEDTSAtnfmirdeRMQALVSkdkEPITPFVDRVRSLYddlgvSTILVVGGSGDYLD 238
|
90
....*....|....*
gi 2790487083 210 VADRAIFMDQGRIVE 224
Cdd:pfam09818 239 VADTVILMDEYRPSD 253
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
145-227 |
7.69e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 145 LSGGQQQRVAIARAL---AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADraifmdqgR 221
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VAD--------Y 880
|
....*.
gi 2790487083 222 IVEQGP 227
Cdd:PRK00635 881 VLELGP 886
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
10-202 |
1.63e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.40 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 10 VKKFHGQTVLHGIDLE-VEQGEVVAIIGPSGSGKTTLLRSINLleQPEGGTIRVGDiTIDTAKSISQQKGLIRslrqhVG 88
Cdd:cd03279 8 LKNFGPFREEQVIDFTgLDNNGLFLICGPTGAGKSTILDAITY--ALYGKTPRYGR-QENLRSVFAPGEDTAE-----VS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 89 FVFQSFNLFpHRtvleniiegpviVKGEPKDEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAM------ 161
Cdd:cd03279 80 FTFQLGGKK-YR------------VERSRGLDYDQFTRIVLLPQGEFDRFLARPvSTLSGGETFLASLSLALALsevlqn 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2790487083 162 ----RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH 202
Cdd:cd03279 147 rggaRLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISH 191
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
143-246 |
2.22e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.06 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 143 RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIvtheMSFAR------DVADRAIF 216
Cdd:PLN03140 335 RGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVL----MSLLQpapetfDLFDDIIL 410
|
90 100 110
....*....|....*....|....*....|....*...
gi 2790487083 217 MDQGRIVEQGPAKSL--------FADPQQPRTRQFLEK 246
Cdd:PLN03140 411 LSEGQIVYQGPRDHIleffescgFKCPERKGTADFLQE 448
|
|
| MobB |
COG1763 |
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ... |
31-46 |
2.30e-03 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 441369 [Multi-domain] Cd Length: 162 Bit Score: 37.47 E-value: 2.30e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-236 |
2.75e-03 |
|
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: 38.84 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 145 LSGGQQQRVAIARALAMRPDVILF--DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQ--- 219
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIR-AADYVIDIGPgag 567
|
90 100
....*....|....*....|
gi 2790487083 220 ---GRIVEQGPAKSLFADPQ 236
Cdd:TIGR00630 568 ehgGEVVASGTPEEILANPD 587
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
31-49 |
2.78e-03 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 37.90 E-value: 2.78e-03
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
8-62 |
3.68e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 38.63 E-value: 3.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790487083 8 NLVKKFHGQTVLHGIDLeveQGEVVAIIGPSGSGKTTLLRSI--NLLEQPEGGTIRV 62
Cdd:COG5635 162 NLLERIESLKRLELLEA---KKKRLLILGEPGSGKTTLLRYLalELAERYLDAEDPI 215
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
136-201 |
4.89e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 37.24 E-value: 4.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 136 GKETSYPRRLSGGQQQRVAIARALAM-RPD---VILFDEPTSALDPELVGEVLNTIRQLAqeKRTMVIVT 201
Cdd:cd03272 150 QDEQQEMQQLSGGQKSLVALALIFAIqKCDpapFYLFDEIDAALDAQYRTAVANMIKELS--DGAQFITT 217
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
23-52 |
5.81e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.60 E-value: 5.81e-03
10 20 30
....*....|....*....|....*....|
gi 2790487083 23 DLEVEQGEVVAIIGPSGSGKTTLLRSINLL 52
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDALRFL 44
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
145-212 |
5.88e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 5.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790487083 145 LSGGQQQRVAIARALAMRPD---VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMsfarDV---AD 212
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNL----DViktAD 896
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
32-69 |
5.91e-03 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 36.04 E-value: 5.91e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2790487083 32 VAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgdITIDT 69
Cdd:cd01127 2 TLVLGTTGSGKTTSIVIPLLDQAARGGSV----IITDP 35
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
31-65 |
6.16e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.37 E-value: 6.16e-03
10 20 30
....*....|....*....|....*....|....*
gi 2790487083 31 VVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDI 65
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDE 35
|
|
| PEPCK_HprK |
cd00820 |
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the ... |
15-64 |
6.20e-03 |
|
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the first committed step in the diversion of tricarboxylic acid cycle intermediates toward gluconeogenesis. It catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate to yield phosphoenolpyruvate and carbon dioxide, using a nucleotide molecule (ATP or GTP) for the phosphoryl transfer, and has a strict requirement for divalent metal ions for activity. PEPCK's separate into two phylogenetic groups based on their nucleotide substrate specificity (the ATP-, and GTP-dependent groups).HprK/P, the bifunctional histidine-containing protein kinase/phosphatase, controls the phosphorylation state of the phosphocarrier protein HPr and regulates the utilization of carbon sources by gram-positive bacteria. It catalyzes both the ATP-dependent phosphorylation of HPr and its dephosphorylation by phosphorolysis. PEPCK and the C-terminal catalytic domain of HprK/P are structurally similar with conserved active site residues suggesting that these two phosphotransferases have related functions.
Pssm-ID: 238418 [Multi-domain] Cd Length: 107 Bit Score: 35.35 E-value: 6.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2790487083 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLlrsinLLEQPEGGTIRVGD 64
Cdd:cd00820 1 GTTSLHGVLVDVYGKVGVLITGDSGIGKTEL-----ALELIKRKHRLVGD 45
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
26-54 |
6.55e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.07 E-value: 6.55e-03
10 20 30
....*....|....*....|....*....|
gi 2790487083 26 VEQGE-VVAIIGPSGSGKTTLLRSinLLEQ 54
Cdd:COG3267 39 LAQGGgFVVLTGEVGTGKTTLLRR--LLER 66
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
1-202 |
6.98e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 36.87 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 1 MSAIDVKNLvKKFhgqtvlhgIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEG---GTIRVG-------------- 63
Cdd:COG4938 1 IKSISIKNF-GPF--------KEAELELKPLTLLIGPNGSGKSTLIQALLLLLQSNFiylPAERSGparlypslvrelsd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790487083 64 -DITIDTAKSISQQKGLIRSLRQHVGFVFQSFNLFphrtvLENIIEGPVIVKGEPKDEatararELLAKVGLAGKETSyP 142
Cdd:COG4938 72 lGSRGEYTADFLAELENLEILDDKSKELLEQVEEW-----LEKIFPGKVEVDASSDLV------RLVFRPSGNGKRIP-L 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790487083 143 RRLSGGQQQRVAIARALAMRP---DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH 202
Cdd:COG4938 140 SNVGSGVSELLPILLALLSAAkpgSLLIIEEPEAHLHPKAQSALAELLAELANSGVQVIIETH 202
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
145-189 |
7.51e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 34.90 E-value: 7.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790487083 145 LSGGQQQR---VAIARALAM----------RPDVILFDEPTSALDPELVGEVLNTIRQ 189
Cdd:pfam13558 33 LSGGEKQLlayLPLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| YejR |
COG0523 |
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ... |
39-68 |
8.09e-03 |
|
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];
Pssm-ID: 440289 [Multi-domain] Cd Length: 318 Bit Score: 37.07 E-value: 8.09e-03
10 20 30
....*....|....*....|....*....|....*
gi 2790487083 39 GSGKTTLLRsiNLLEQPEGGTIRV-----GDITID 68
Cdd:COG0523 14 GAGKTTLLN--HLLANPEGRRIAVivnefGEVGID 46
|
|
| |
