|
Name |
Accession |
Description |
Interval |
E-value |
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6-260 |
0e+00 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 522.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 6 NPPAPAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTGSGK 85
Cdd:COG4598 2 TDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 86 SRIADRRQVERIRSELGMVFQSFNLWSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQ 165
Cdd:COG4598 82 LVPADRRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 166 RAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDM 245
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
250
....*....|....*
gi 752717930 246 FTNAKSERFRKFISG 260
Cdd:COG4598 242 FGNPKSERLRQFLSS 256
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
13-259 |
5.81e-162 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 448.29 E-value: 5.81e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgksrIADRR 92
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-----------TDSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIRSELGMVFQSFNLWSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARA 172
Cdd:COG1126 71 DINKLRRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 173 LAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAKSE 252
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
....*..
gi 752717930 253 RFRKFIS 259
Cdd:COG1126 231 RTRAFLS 237
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
13-236 |
1.97e-131 |
|
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: 369.94 E-value: 1.97e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksriADRR 92
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-----------DDKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIRSELGMVFQSFNLWSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARA 172
Cdd:cd03262 70 NINELRQKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752717930 173 LAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAI 236
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-260 |
2.74e-116 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 333.47 E-value: 2.74e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTGSGKSRIADRR 92
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIRSELGMVFQSFNLWSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIADK-RNHYPAHLSGGQQQRAAIAR 171
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 172 ALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAKS 251
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
....*....
gi 752717930 252 ERFRKFISG 260
Cdd:PRK10619 246 PRLQQFLKG 254
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-258 |
9.82e-116 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 331.29 E-value: 9.82e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksriADRR 92
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN-----------DPKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIRSELGMVFQSFNLWSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARA 172
Cdd:PRK09493 71 DERLIRQEAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 173 LAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAKSE 252
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
....*.
gi 752717930 253 RFRKFI 258
Cdd:PRK09493 231 RLQEFL 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
11-259 |
8.82e-110 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 316.69 E-value: 8.82e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 11 AAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptGSGKSRIAD 90
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITI-----DTARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 91 RRQVERIRSELGMVFQSFNLWSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIA 170
Cdd:PRK11264 77 KGLIRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 171 RALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAK 250
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
....*....
gi 752717930 251 SERFRKFIS 259
Cdd:PRK11264 237 QPRTRQFLE 245
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
13-259 |
4.14e-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: 4.14e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTGSGKSRIADRR 92
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNGPLVPADEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIRSELGMVFQSFNLWSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARA 172
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 173 LAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGR-TMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAKS 251
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDlTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
....*...
gi 752717930 252 ERFRKFIS 259
Cdd:TIGR03005 241 ERTREFLS 248
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
12-259 |
1.19e-92 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 273.04 E-value: 1.19e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 12 AITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMkptgsgkSRIADR 91
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDF-------SQKPSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 RQVERIRSELGMVFQSFNLWSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIAR 171
Cdd:COG4161 75 KAIRLLRQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 172 ALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRpQDMFTNAKS 251
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQT 233
|
....*...
gi 752717930 252 ERFRKFIS 259
Cdd:COG4161 234 EAFAHYLS 241
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
13-259 |
8.25e-90 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 269.25 E-value: 8.25e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSF----GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkpTG-SGKSR 87
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL----TAlSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 88 IADRRQVerirselGMVFQSFNLWSHKTVLENVmEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRA 167
Cdd:COG1135 78 RAARRKI-------GMIFQHFNLLSSRTVAENV-ALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 168 AIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMF 246
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVF 229
|
250
....*....|...
gi 752717930 247 TNAKSERFRKFIS 259
Cdd:COG1135 230 ANPQSELTRRFLP 242
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
12-259 |
7.72e-89 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 263.41 E-value: 7.72e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 12 AITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMkptgsgkSRIADR 91
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDF-------SKTPSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 RQVERIRSELGMVFQSFNLWSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIAR 171
Cdd:PRK11124 75 KAIRELRRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 172 ALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGrPQDMFTNAKS 251
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG-DASCFTQPQT 233
|
....*...
gi 752717930 252 ERFRKFIS 259
Cdd:PRK11124 234 EAFKNYLS 241
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-241 |
5.39e-87 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 258.05 E-value: 5.39e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 10 PAAITVRGLRKSFG----PVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkpTGSGK 85
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI----SSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 86 SRIADRRqveriRSELGMVFQSFNLWSHKTVLENVMeAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQ 165
Cdd:COG1136 78 RELARLR-----RRHIGFVFQFFNLLPELTALENVA-LPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 166 RAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARdVSSRVIFLHQGAIEEEGR 241
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAA-RADRVIRLRDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
13-236 |
5.26e-85 |
|
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: 252.80 E-value: 5.26e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFG----PVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgkSRI 88
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDI---------SKL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 89 ADRRQVERIRSELGMVFQSFNLWSHKTVLENVMeAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAA 168
Cdd:cd03255 72 SEKELAAFRRRHIGFVFQSFNLLPDLTALENVE-LPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 169 IARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDvSSRVIFLHQGAI 236
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
8-258 |
3.50e-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: 3.50e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 8 PAPAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkpTGsgksr 87
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDI----TG----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 88 iADRRQVERIRSELGMVFQSFNLWSHKTVLENVMeAPLHVQKR-SRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQR 166
Cdd:COG1127 72 -LSEKELYELRRRIGMLFQGGALFDSLTVFENVA-FPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 167 AAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDM 245
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
250
....*....|...
gi 752717930 246 FtNAKSERFRKFI 258
Cdd:COG1127 230 L-ASDDPWVRQFL 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
13-250 |
5.98e-82 |
|
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: 245.57 E-value: 5.98e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGP----VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKptgsgksri 88
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLL--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 89 aDRRQVERIRSELGMVFQSFNLWSHKTVLENVMeAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAA 168
Cdd:cd03258 73 -SGKELRKARRRIGMIFQHFNLLSSRTVFENVA-LPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 169 IARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFT 247
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
...
gi 752717930 248 NAK 250
Cdd:cd03258 231 NPQ 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-248 |
6.16e-78 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 239.23 E-value: 6.16e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 9 APAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPtgsgksri 88
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 89 ADRRQVerirselGMVFQSFNLWSHKTVLENVmEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAA 168
Cdd:COG3842 74 PEKRNV-------GMVFQDYALFPHLTVAENV-AFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 169 IARALAMRPKVMLFDEPTSALDPELVGEVLRVMRAL-AEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFT 247
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYE 225
|
.
gi 752717930 248 N 248
Cdd:COG3842 226 R 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
13-259 |
9.45e-74 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 228.15 E-value: 9.45e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSF----GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkpTG-SGKSR 87
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDL----TAlSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 88 IADRRQVerirselGMVFQSFNLWSHKTVLENVmeA-PLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQR 166
Cdd:PRK11153 78 RKARRQI-------GMIFQHFNLLSSRTVFDNV--AlPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 167 AAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDM 245
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
250
....*....|....
gi 752717930 246 FTNAKSERFRKFIS 259
Cdd:PRK11153 229 FSHPKHPLTREFIQ 242
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-252 |
5.17e-73 |
|
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: 231.33 E-value: 5.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 3 PSTNPPAPAAITVRGLRKSF-----GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIR 77
Cdd:COG1123 251 APAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 78 mkptgsgksrIADRRQVERIRSELGMVFQ----SFNlwSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGI-ADKR 152
Cdd:COG1123 331 ----------KLSRRSLRELRRRVQMVFQdpysSLN--PRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLA 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 153 NHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFL 231
Cdd:COG1123 399 DRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVM 478
|
250 260
....*....|....*....|.
gi 752717930 232 HQGAIEEEGRPQDMFTNAKSE 252
Cdd:COG1123 479 YDGRIVEDGPTEEVFANPQHP 499
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
7-256 |
1.63e-72 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 222.27 E-value: 1.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 7 PPAPAAITVRGLRKSF----GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGetirmkptg 82
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 83 sgksriadrRQVERIRSELGMVFQSFNL--WshKTVLENVMeAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLS 160
Cdd:COG1116 73 ---------KPVTGPGPDRGVVFQEPALlpW--LTVLDNVA-LGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 161 GGQQQRAAIARALAMRPKVMLFDEPTSALDP----ELVGEVLRVmraLAEEGRTMLVVTHemgfarDV------SSRVIF 230
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTH------DVdeavflADRVVV 211
|
250 260 270
....*....|....*....|....*....|...
gi 752717930 231 L--HQGAIEEE-----GRPQDMFTNAkSERFRK 256
Cdd:COG1116 212 LsaRPGRIVEEidvdlPRPRDRELRT-SPEFAA 243
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-241 |
3.23e-72 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 220.31 E-value: 3.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGP-VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETI-RMKptgsgksriad 90
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsRLK----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 91 RRQVERIRSELGMVFQSFNLWSHKTVLENVMeAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIA 170
Cdd:COG2884 71 RREIPYLRRRIGVVFQDFRLLPDRTVYENVA-LPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 752717930 171 RALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGR 241
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-250 |
4.55e-72 |
|
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: 220.28 E-value: 4.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSF-GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksriadR 91
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT-------------K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 RQVERIRSELGMVFQS-----FNlwshKTVLENVMEAPLHvQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQR 166
Cdd:COG1122 68 KNLRELRRKVGLVFQNpddqlFA----PTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 167 AAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMF 246
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
....
gi 752717930 247 TNAK 250
Cdd:COG1122 223 SDYE 226
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
11-245 |
1.53e-71 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 219.54 E-value: 1.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 11 AAITVRGLRKSF-GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMkptgsgksriA 89
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTA----------L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 90 DRRQVERIRSELGMVFQSFNLWSHKTVLENVM-----EAPLHvqkRS-----RAECLEEAEALLAKVGIADKRNHYPAHL 159
Cdd:COG3638 71 RGRALRRLRRRIGMIFQQFNLVPRLSVLTNVLagrlgRTSTW---RSllglfPPEDRERALEALERVGLADKAYQRADQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 160 SGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEE 238
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVF 227
|
....*..
gi 752717930 239 EGRPQDM 245
Cdd:COG3638 228 DGPPAEL 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
13-247 |
2.11e-71 |
|
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: 218.53 E-value: 2.11e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkpTGSGKSRIADRR 92
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIS---GLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVerirselGMVFQSFNLWSHKTVLENVMeAPLHVQ-KRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIAR 171
Cdd:cd03261 78 RM-------GMLFQSGALFDSLTVFENVA-FPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 172 ALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFT 247
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
12-260 |
1.49e-70 |
|
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: 217.16 E-value: 1.49e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 12 AITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCIN-MLETPD----AGEITVAGETIrmkptgsgks 86
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNrMNDLVPgvriEGKVLFDGQDI---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 87 rIADRRQVERIRSELGMVFQSFNLWShKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGI----ADKRNHYPAHLSGG 162
Cdd:TIGR00972 71 -YDKKIDVVELRRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 163 QQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEgRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRP 242
Cdd:TIGR00972 149 QQQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPT 227
|
250
....*....|....*...
gi 752717930 243 QDMFTNAKSERFRKFISG 260
Cdd:TIGR00972 228 EQIFTNPKEKRTEDYISG 245
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
13-245 |
3.11e-70 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 215.70 E-value: 3.11e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksriadrR 92
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA--------------R 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIRSELGMVFQSFNLWSHKTVLENV-MEAPLHvqKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIAR 171
Cdd:COG1131 67 DPAEVRRRIGYVPQEPALYPDLTVRENLrFFARLY--GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752717930 172 ALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDM 245
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-240 |
2.63e-69 |
|
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: 212.38 E-value: 2.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPtgsgksriADRR 92
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP--------PERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVerirselGMVFQSFNLWSHKTVLENVmeA-PLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIAR 171
Cdd:cd03259 73 NI-------GMVFQDYALFPHLTVAENI--AfGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 172 ALAMRPKVMLFDEPTSALDPELVGEVLRVMRAL-AEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEG 240
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
13-234 |
7.76e-69 |
|
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: 210.12 E-value: 7.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksriADRR 92
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT-----------DLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIRSELGMVFQSFNLWSHKTVLENVMEAplhvqkrsraecleeaeallakvgiadkrnhypahLSGGQQQRAAIARA 172
Cdd:cd03229 70 ELPPLRRRIGMVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARA 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752717930 173 LAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQG 234
Cdd:cd03229 115 LAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-258 |
5.68e-68 |
|
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: 210.43 E-value: 5.68e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 12 AITVRGLRKSFGP----VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTGsgksr 87
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 88 iADRRQVerirselGMVFQ----SFNlwSHKTVLENVMEaPLHVQKRSRAEclEEAEALLAKVGI-ADKRNHYPAHLSGG 162
Cdd:COG1124 76 -AFRRRV-------QMVFQdpyaSLH--PRHTVDRILAE-PLRIHGLPDRE--ERIAELLEQVGLpPSFLDRYPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 163 QQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRAL-AEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGR 241
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELT 222
|
250
....*....|....*..
gi 752717930 242 PQDMFTNAKSERFRKFI 258
Cdd:COG1124 223 VADLLAGPKHPYTRELL 239
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
11-246 |
4.11e-67 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 211.47 E-value: 4.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 11 AAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETI-RMKPtgsgksriA 89
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtDLPP--------K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 90 DRRqverirseLGMVFQSFNLWSHKTVLENvMEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAI 169
Cdd:COG3839 74 DRN--------IAMVFQSYALYPHMTVYEN-IAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 170 ARALAMRPKVMLFDEPTSALDPElvgevLRV-MRA-----LAEEGRTMLVVTHE----MGFArdvsSRVIFLHQGAIEEE 239
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDAK-----LRVeMRAeikrlHRRLGTTTIYVTHDqveaMTLA----DRIAVMNDGRIQQV 215
|
....*..
gi 752717930 240 GRPQDMF 246
Cdd:COG3839 216 GTPEELY 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
13-239 |
2.35e-66 |
|
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: 205.40 E-value: 2.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFG----PVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGEtirmkptgsgksri 88
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 89 adrrQVERIRSELGMVFQSFNLWSHKTVLENVMeAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAA 168
Cdd:cd03293 67 ----PVTGPGPDRGYVFQQDALLPWLTVLDNVA-LGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752717930 169 IARALAMRPKVMLFDEPTSALDP---ELVGEVLrvMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQ--GAIEEE 239
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDAltrEQLQEEL--LDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
13-251 |
7.41e-66 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 208.08 E-value: 7.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGET--IRMKPTgsgksriad 90
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlfTNLPPR--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 91 RRQVerirselGMVFQSFNLWSHKTVLENVMEApLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIA 170
Cdd:COG1118 74 ERRV-------GFVFQHYALFPHMTVAENIAFG-LRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 171 RALAMRPKVMLFDEPTSALDPELVGEVLRVMRAL-AEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNA 249
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRP 225
|
..
gi 752717930 250 KS 251
Cdd:COG1118 226 AT 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
13-240 |
2.44e-65 |
|
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: 203.12 E-value: 2.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSF----GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksrI 88
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLL----------K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 89 ADRRQVERIRSELGMVFQ----SFNlwSHKTVLENVMEAPLHVQKRSRAECLEEAEALLA-KVGIADKR-NHYPAHLSGG 162
Cdd:cd03257 72 LSRRLRKIRRKEIQMVFQdpmsSLN--PRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLvGVGLPEEVlNRYPHELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 163 QQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEG 240
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-243 |
3.35e-65 |
|
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: 202.80 E-value: 3.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINML-----ETPDAGEITVAGETIRmkptGSGKSR 87
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIY----DLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 88 IADRRQVerirselGMVFQSFNLWsHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIAD--KRNHYPAHLSGGQQQ 165
Cdd:cd03260 77 LELRRRV-------GMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 752717930 166 RAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEgRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQ 243
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-253 |
6.44e-65 |
|
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: 202.41 E-value: 6.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFG-PVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgKSRIADR 91
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDIN-------KLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 RQVeriRSELGMVFQSFNLWSHKTVLENVMEAPLH--------VQKRSRAEcLEEAEALLAKVGIADKRNHYPAHLSGGQ 163
Cdd:cd03256 74 RQL---RRQIGMIFQQFNLIERLSVLENVLSGRLGrrstwrslFGLFPKEE-KQRALAALERVGLLDKAYQRADQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 164 QQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALA-EEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRP 242
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPP 229
|
250
....*....|.
gi 752717930 243 QDmFTNAKSER 253
Cdd:cd03256 230 AE-LTDEVLDE 239
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-243 |
6.92e-64 |
|
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: 199.58 E-value: 6.92e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 1 MTPSTNPpapaAITVRGLRKSF----GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETI 76
Cdd:COG4181 1 MSSSSAP----IIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 77 -RMkptgsgksriaDRRQVERIRSE-LGMVFQSFNLWSHKTVLENVMeAPLHVqkRSRAECLEEAEALLAKVGIADKRNH 154
Cdd:COG4181 77 fAL-----------DEDARARLRARhVGFVFQSFQLLPTLTALENVM-LPLEL--AGRRDARARARALLERVGLGHRLDH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 155 YPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDvSSRVIFLHQ 233
Cdd:COG4181 143 YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRA 221
|
250
....*....|
gi 752717930 234 GAIEEEGRPQ 243
Cdd:COG4181 222 GRLVEDTAAT 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-234 |
2.13e-63 |
|
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: 197.30 E-value: 2.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 15 VRGLRKSF--GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgKSRIADRR 92
Cdd:cd03225 2 LKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT-------KLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QverirsELGMVFQS-----FNLwshkTVLENVMEAPLHvQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRA 167
Cdd:cd03225 75 R------KVGLVFQNpddqfFGP----TVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 168 AIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQG 234
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-260 |
4.80e-63 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 197.95 E-value: 4.80e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 1 MTPSTnPPAPAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCIN-MLE-TPDA---GEITVAGET 75
Cdd:COG1117 1 MTAPA-STLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNrMNDlIPGArveGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 76 IRmkptgsgksriADRRQVERIRSELGMVFQSFNLWShKTVLENVMEAP-LHvQKRSRAEcLEEA-EALLAKVGI----A 149
Cdd:COG1117 80 IY-----------DPDVDVVELRRRVGMVFQKPNPFP-KSIYDNVAYGLrLH-GIKSKSE-LDEIvEESLRKAALwdevK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 150 DKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDP-------ELvgevlrvMRALAEEgRTMLVVTHEMGFAR 222
Cdd:COG1117 146 DRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPistakieEL-------ILELKKD-YTIVIVTHNMQQAA 217
|
250 260 270
....*....|....*....|....*....|....*...
gi 752717930 223 DVSSRVIFLHQGAIEEEGRPQDMFTNAKSERFRKFISG 260
Cdd:COG1117 218 RVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYITG 255
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
13-253 |
1.75e-62 |
|
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: 196.37 E-value: 1.75e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGP-VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsGKSRIADR 91
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDI-------TKLRGKKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 RQVeriRSELGMVFQSFNLWSHKTVLENVMEAPLHVQKR--------SRAEcLEEAEALLAKVGIADKRNHYPAHLSGGQ 163
Cdd:TIGR02315 75 RKL---RRRIGMIFQHYNLIERLTVLENVLHGRLGYKPTwrsllgrfSEED-KERALSALERVGLADKAYQRADQLSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 164 QQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRP 242
Cdd:TIGR02315 151 QQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAP 230
|
250
....*....|.
gi 752717930 243 QdMFTNAKSER 253
Cdd:TIGR02315 231 S-ELDDEVLRH 240
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
13-244 |
1.07e-61 |
|
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: 194.31 E-value: 1.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksriadrR 92
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR--------------K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIRSELGMVFQSFNLWSHKTVLENV-MEAPLHvqKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIAR 171
Cdd:COG4555 68 EPREARRQIGVLPDERGLYDRLTVRENIrYFAELY--GLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752717930 172 ALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQD 244
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDE 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
15-248 |
3.07e-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: 192.65 E-value: 3.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 15 VRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETI-RMKPTgsgksriadrrq 93
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItGLPPH------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 94 vERIRSELGMVFQSFNLWSHKTVLENVMEAPLHVQK---------RSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQ 164
Cdd:cd03219 71 -EIARLGIGRTFQIPRLFPELTVLENVMVAAQARTGsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 165 QRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQD 244
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
....
gi 752717930 245 MFTN 248
Cdd:cd03219 230 VRNN 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-250 |
3.56e-61 |
|
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: 193.33 E-value: 3.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 9 APAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETI-RMKPtgsgkSR 87
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItGLPP-----HR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 88 IAdrrqverirsELGMV--FQSFNLWSHKTVLENVMEAPLHVQK--------------RSRAECLEEAEALLAKVGIADK 151
Cdd:COG0411 76 IA----------RLGIArtFQNPRLFPELTVLENVLVAAHARLGrgllaallrlprarREEREARERAEELLERVGLADR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 152 RNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRAL-AEEGRTMLVVTHEMGFARDVSSRVIF 230
Cdd:COG0411 146 ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVV 225
|
250 260
....*....|....*....|
gi 752717930 231 LHQGAIEEEGRPQDMFTNAK 250
Cdd:COG0411 226 LDFGRVIAEGTPAEVRADPR 245
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-258 |
1.28e-60 |
|
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: 190.91 E-value: 1.28e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPtgsgksriADRR 92
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP--------PHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVerirselGMVFQSFNLWSHKTVLENVmEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARA 172
Cdd:cd03300 73 PV-------NTVFQNYALFPHLTVFENI-AFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 173 LAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAKS 251
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPAN 224
|
....*..
gi 752717930 252 ERFRKFI 258
Cdd:cd03300 225 RFVADFI 231
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-260 |
2.45e-59 |
|
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: 189.01 E-value: 2.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 18 LRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgkSRIADRRQVERI 97
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDI---------AAMSRKELRELR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 98 RSELGMVFQSFNLWSHKTVLENVmEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRP 177
Cdd:cd03294 101 RKKISMVFQSFALLPHRTVLENV-AFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 178 KVMLFDEPTSALDP----ELVGEVLRVMralAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAKSER 253
Cdd:cd03294 180 DILLMDEAFSALDPlirrEMQDELLRLQ---AELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
....*..
gi 752717930 254 FRKFISG 260
Cdd:cd03294 257 VREFFRG 263
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
12-258 |
3.21e-58 |
|
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: 185.24 E-value: 3.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 12 AITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPtgsgksriADR 91
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP--------VQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 RQVerirselGMVFQSFNLWSHKTVLENVMEApLHVQKRSR----AECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRA 167
Cdd:cd03296 74 RNV-------GFVFQHYALFRHMTVFDNVAFG-LRVKPRSErppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 168 AIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMF 246
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVY 225
|
250
....*....|..
gi 752717930 247 TNAKSERFRKFI 258
Cdd:cd03296 226 DHPASPFVYSFL 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-251 |
2.30e-57 |
|
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: 190.88 E-value: 2.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 11 AAITVRGLRKSF--GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDA---GEITVAGETIRMKPtgsgk 85
Cdd:COG1123 3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELS----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 86 sriadrrqvERIRS-ELGMVFQ----SFNLWshkTVLENVMEApLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLS 160
Cdd:COG1123 78 ---------EALRGrRIGMVFQdpmtQLNPV---TVGDQIAEA-LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 161 GGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRAL-AEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEE 239
Cdd:COG1123 145 GGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVED 224
|
250
....*....|..
gi 752717930 240 GRPQDMFTNAKS 251
Cdd:COG1123 225 GPPEEILAAPQA 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-249 |
1.90e-56 |
|
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: 181.01 E-value: 1.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 12 AITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGEtirmkptgsgksRIADR 91
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGR------------DLASL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 RQVERIRsELGMVFQSFNLWSHKTVLENVM--EAP-LHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAA 168
Cdd:COG1120 69 SRRELAR-RIAYVPQEPPAPFGLTVRELVAlgRYPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 169 IARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALA-EEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFT 247
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
..
gi 752717930 248 NA 249
Cdd:COG1120 228 PE 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-250 |
6.04e-56 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 181.79 E-value: 6.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSF----GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCI-NMLETP--DAGEITVAGETIRMkptgsgk 85
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlGLLPPPgiTSGEILFDGEDLLK------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 86 sriADRRQVERIR-SELGMVFQ----SFNlwSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIADKRNH---YPA 157
Cdd:COG0444 75 ---LSEKELRKIRgREIQMIFQdpmtSLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRldrYPH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 158 HLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAI 236
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
250
....*....|....
gi 752717930 237 EEEGRPQDMFTNAK 250
Cdd:COG0444 230 VEEGPVEELFENPR 243
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
11-251 |
7.65e-56 |
|
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: 182.54 E-value: 7.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 11 AAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTGsgksriad 90
Cdd:TIGR03265 3 PYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 91 rrqveriRSELGMVFQSFNLWSHKTVLENVmEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIA 170
Cdd:TIGR03265 75 -------KRDYGIVFQSYALFPNLTVADNI-AYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 171 RALAMRPKVMLFDEPTSALDPeLVGEVLRV-MRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTN 248
Cdd:TIGR03265 147 RALATSPGLLLLDEPLSALDA-RVREHLRTeIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRH 225
|
...
gi 752717930 249 AKS 251
Cdd:TIGR03265 226 PAT 228
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
11-260 |
1.08e-55 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 183.38 E-value: 1.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 11 AAITVRGLRKSFG--PVEVLKGID----------------------MEAREGEVVSILGSSGSGKSTMLRCINMLETPDA 66
Cdd:COG4175 2 PKIEVRNLYKIFGkrPERALKLLDqgkskdeilektgqtvgvndasFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 67 GEITVAGETIrMKptgsgksriADRRQVERIRSE-LGMVFQSFNLWSHKTVLENVmEAPLHVQKRSRAECLEEAEALLAK 145
Cdd:COG4175 82 GEVLIDGEDI-TK---------LSKKELRELRRKkMSMVFQHFALLPHRTVLENV-AFGLEIQGVPKAERRERAREALEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 146 VGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDP----ELVGEVLRvmraL-AEEGRTMLVVTHEMGF 220
Cdd:COG4175 151 VGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrEMQDELLE----LqAKLKKTIVFITHDLDE 226
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 752717930 221 ARDVSSRVIFLHQGAIEEEGRPQDMFTNAKSERFRKFISG 260
Cdd:COG4175 227 ALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVED 266
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-247 |
8.27e-55 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 176.43 E-value: 8.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 8 PAPAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGetirmKPTGSGKSR 87
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG-----KPPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 88 IA---DRRQVERirselgmvfqSFNLwshkTVLENVM---EAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSG 161
Cdd:COG1121 77 IGyvpQRAEVDW----------DFPI----TVRDVVLmgrYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 162 GQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIeEEGR 241
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGP 221
|
....*.
gi 752717930 242 PQDMFT 247
Cdd:COG1121 222 PEEVLT 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-234 |
8.64e-55 |
|
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: 174.12 E-value: 8.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgksriadRR 92
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI--------------KK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIRSELGMVFQSFNLWSHKTVLENVmeaplhvqkrsraecleeaeallakvgiadkrnhypaHLSGGQQQRAAIARA 172
Cdd:cd03230 67 EPEEVKRRIGYLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQA 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752717930 173 LAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQG 234
Cdd:cd03230 110 LLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
13-236 |
1.06e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 175.00 E-value: 1.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgksriaDRR 92
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-------------SAM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIRSELGMVFQSFNLWsHKTVLENvMEAPLHVQKRSRAEclEEAEALLAKVGIADKRNHYPAH-LSGGQQQRAAIAR 171
Cdd:COG4619 68 PPPEWRRQVAYVPQEPALW-GGTVRDN-LPFPFQLRERKFDR--ERALELLERLGLPPDILDKPVErLSGGERQRLALIR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752717930 172 ALAMRPKVMLFDEPTSALDPELVGEVLRVMRAL-AEEGRTMLVVTHEMGFARDVSSRVIFLHQGAI 236
Cdd:COG4619 144 ALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
13-248 |
1.23e-54 |
|
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: 176.85 E-value: 1.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSF--GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGetirMKPtgsgksriAD 90
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG----LDT--------LD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 91 RRQVERIRSELGMVFQ--------SfnlwshkTV-------LENVMEAPLHVQKRsraecLEEAealLAKVGIADKRNHY 155
Cdd:TIGR04520 69 EENLWEIRKKVGMVFQnpdnqfvgA-------TVeddvafgLENLGVPREEMRKR-----VDEA---LKLVGMEDFRDRE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 156 PAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRAL-AEEGRTMLVVTHEMGFARDvSSRVIFLHQG 234
Cdd:TIGR04520 134 PHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKG 212
|
250
....*....|....
gi 752717930 235 AIEEEGRPQDMFTN 248
Cdd:TIGR04520 213 KIVAEGTPREIFSQ 226
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
23-234 |
2.39e-54 |
|
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: 174.36 E-value: 2.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 23 GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETI-RMKptgsgksriadRRQVERIRSEL 101
Cdd:TIGR02673 13 GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVnRLR-----------GRQLPLLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 102 GMVFQSFNLWSHKTVLENVmEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVML 181
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENV-ALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 752717930 182 FDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQG 234
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-258 |
2.67e-54 |
|
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: 175.18 E-value: 2.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVE-VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPtgsgksriadr 91
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQD----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 rqVERIRSELGMVFQSFNLWSHKTVLENVMEAPlHVQKRSRAECLEEAEALLAKVGIADK--RNHYPAHLSGGQQQRAAI 169
Cdd:cd03295 70 --PVELRRKIGYVIQQIGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 170 ARALAMRPKVMLFDEPTSALDP----ELVGEVLRVMRALaeeGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDM 245
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPitrdQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
250
....*....|...
gi 752717930 246 FTNAKSERFRKFI 258
Cdd:cd03295 224 LRSPANDFVAEFV 236
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
13-246 |
3.11e-53 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 176.68 E-value: 3.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPtgsgksriADRR 92
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP--------AENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVErirselgMVFQSFNLWSHKTVLENVMEApLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARA 172
Cdd:PRK09452 87 HVN-------TVFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 173 LAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMF 246
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIY 233
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
16-238 |
4.13e-53 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 171.38 E-value: 4.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 16 RGLRKSFGP----VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgkSRIADR 91
Cdd:TIGR02211 5 ENLGKRYQEgkldTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSL---------SKLSSN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 RQVERIRSELGMVFQSFNLWSHKTVLENVMeAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIAR 171
Cdd:TIGR02211 76 ERAKLRNKKLGFIYQFHHLLPDFTALENVA-MPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 752717930 172 ALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRT-MLVVTHEMGFARDVsSRVIFLHQGAIEE 238
Cdd:TIGR02211 155 ALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTsFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
13-258 |
4.16e-53 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 171.86 E-value: 4.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGpvEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPtgsgksrIADRr 92
Cdd:COG3840 2 LRLDDLTYRYG--DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-------PAER- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 qverirsELGMVFQSFNLWSHKTVLENVMEApLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARA 172
Cdd:COG3840 72 -------PVSMLFQENNLFPHLTVAQNIGLG-LRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 173 LAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAKS 251
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPP 223
|
....*..
gi 752717930 252 ERFRKFI 258
Cdd:COG3840 224 PALAAYL 230
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
13-258 |
6.21e-53 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 173.74 E-value: 6.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSF-GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIR-MKPtgsgksrIAD 90
Cdd:COG1125 2 IEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRdLDP-------VEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 91 RRQVerirselGMVFQSFNLWSHKTVLENVMEAPlHVQKRSRAECLEEAEALLAKVGI--ADKRNHYPAHLSGGQQQRAA 168
Cdd:COG1125 75 RRRI-------GYVIQQIGLFPHMTVAENIATVP-RLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 169 IARALAMRPKVMLFDEPTSALDP----ELVGEVLRVMRALaeeGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQD 244
Cdd:COG1125 147 VARALAADPPILLMDEPFGALDPitreQLQDELLRLQREL---GKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEE 223
|
250
....*....|....
gi 752717930 245 MFTNAKSERFRKFI 258
Cdd:COG1125 224 ILANPANDFVADFV 237
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-245 |
2.12e-52 |
|
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: 169.54 E-value: 2.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGEtirmkptgsgksRIADRR 92
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGR------------DITGLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIRSELGMVFQSFNLWSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKvgIADKRNHYPAHLSGGQQQRAAIARA 172
Cdd:cd03224 69 PHERARAGIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752717930 173 LAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDM 245
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
15-231 |
3.12e-52 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 168.95 E-value: 3.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 15 VRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmKPTGSGKSRiadrrqv 94
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQET--PPLNSKKAS------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 95 ERIRSELGMVFQSFNLWSHKTVLENvMEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALA 174
Cdd:TIGR03608 72 KFRREKLGYLFQNFALIENETVEEN-LDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 175 MRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFArDVSSRVIFL 231
Cdd:TIGR03608 151 KPPPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-240 |
3.06e-51 |
|
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: 166.66 E-value: 3.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGEtirmkptgsgksRIADRR 92
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR------------DVTDLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERirsELGMVFQSFNLWSHKTVLENvMEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARA 172
Cdd:cd03301 69 PKDR---DIAMVFQNYALYPHMTVYDN-IAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752717930 173 LAMRPKVMLFDEPTSALDPElvgevLRV-MRA-----LAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEG 240
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAK-----LRVqMRAelkrlQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
14-234 |
1.24e-49 |
|
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: 160.49 E-value: 1.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 14 TVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksriadRRQ 93
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA-------------KLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 94 VERIRSELGMVFQsfnlwshktvlenvmeaplhvqkrsraecleeaeallakvgiadkrnhypahLSGGQQQRAAIARAL 173
Cdd:cd00267 68 LEELRRRIGYVPQ----------------------------------------------------LSGGQRQRVALARAL 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 752717930 174 AMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQG 234
Cdd:cd00267 96 LLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
27-234 |
4.92e-49 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 161.04 E-value: 4.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkpTGSGKS-RIADRRQVerirseLGMVF 105
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEV----TNLSYSqKIILRREL------IGYIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 106 QSFNLWSHKTVLENVmEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEP 185
Cdd:NF038007 90 QSFNLIPHLSIFDNV-ALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 752717930 186 TSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGfARDVSSRVIFLHQG 234
Cdd:NF038007 169 TGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDG 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-187 |
1.01e-48 |
|
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: 157.81 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksriadRRQVERIRSELGMVFQS 107
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-------------DDERKSLRKEIGYVFQD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 108 FNLWSHKTVLENVMEaPLHVQKRSRAECLEEAEALLAKVGIADKRNH----YPAHLSGGQQQRAAIARALAMRPKVMLFD 183
Cdd:pfam00005 68 PQLFPRLTVRENLRL-GLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLD 146
|
....
gi 752717930 184 EPTS 187
Cdd:pfam00005 147 EPTA 150
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-254 |
1.24e-48 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 164.10 E-value: 1.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 12 AITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgkSRIADR 91
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---------SRLHAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 -RQVerirselGMVFQSFNLWSHKTVLENVMEApLHVQKR----SRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQR 166
Cdd:PRK10851 73 dRKV-------GFVFQHYALFRHMTVFDNIAFG-LTVLPRrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 167 AAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGR-TMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDM 245
Cdd:PRK10851 145 VALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
....*....
gi 752717930 246 FTNAKSeRF 254
Cdd:PRK10851 225 WREPAT-RF 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
13-259 |
2.69e-48 |
|
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: 159.81 E-value: 2.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEvLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETI-RMKPtgsgksriaDR 91
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDItNLPP---------EK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 RQVerirselGMVFQSFNLWSHKTVLENVmEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIAR 171
Cdd:cd03299 71 RDI-------SYVPQNYALFPHMTVYKNI-AYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 172 ALAMRPKVMLFDEPTSALDPELvGEVLRVM--RALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNA 249
Cdd:cd03299 143 ALVVNPKILLLDEPFSALDVRT-KEKLREElkKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
250
....*....|
gi 752717930 250 KSERFRKFIS 259
Cdd:cd03299 222 KNEFVAEFLG 231
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
28-250 |
3.34e-48 |
|
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: 160.69 E-value: 3.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKptgsgksriaDRRQVERIRSELGMVFQS 107
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAK----------KKKKLKDLRKKVGLVFQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 108 -----FnlwsHKTVLENVMEAPLHVQKrSRAECLEEAEALLAKVGIADK-RNHYPAHLSGGQQQRAAIARALAMRPKVML 181
Cdd:TIGR04521 91 pehqlF----EETVYKDIAFGPKNLGL-SEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAMEPEVLI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 182 FDEPTSALDPELVGEVLRVMRALA-EEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAK 250
Cdd:TIGR04521 166 LDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
6-248 |
7.15e-48 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 161.44 E-value: 7.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 6 NPPAPAAITVRGLRKSF--------GPVEVLK---GIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGE 74
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrgglfgRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 75 TIrmkpTGsgksriADRRQVERIRSELGMVFQ----SFNlwSHKTVLENVMEaPLHVQK-RSRAECLEEAEALLAKVGI- 148
Cdd:COG4608 81 DI----TG------LSGRELRPLRRRMQMVFQdpyaSLN--PRMTVGDIIAE-PLRIHGlASKAERRERVAELLELVGLr 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 149 ADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSR 227
Cdd:COG4608 148 PEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDR 227
|
250 260
....*....|....*....|.
gi 752717930 228 VIFLHQGAIEEEGRPQDMFTN 248
Cdd:COG4608 228 VAVMYLGKIVEIAPRDELYAR 248
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
21-231 |
1.47e-47 |
|
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: 156.92 E-value: 1.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 21 SFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGetirmKPTGSGKSRIA---DRRQVERi 97
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGyvpQRRSIDR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 98 rselgmvfqSFNLwshkTVLENVMEAPLH---VQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALA 174
Cdd:cd03235 82 ---------DFPI----SVRDVVLMGLYGhkgLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 175 MRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFL 231
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-250 |
1.71e-47 |
|
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: 157.45 E-value: 1.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 10 PAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETI-RMKPTgsgksri 88
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItGLPPH------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 89 adrrqvERIRSELGMVFQSFNLWSHKTVLEN-VMEAPLHVQKRSRAECLEEAEAL---LAkvgiaDKRNHYPAHLSGGQQ 164
Cdd:COG0410 74 ------RIARLGIGYVPEGRRIFPSLTVEENlLLGAYARRDRAEVRADLERVYELfprLK-----ERRRQRAGTLSGGEQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 165 QRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQD 244
Cdd:COG0410 143 QMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAE 222
|
....*.
gi 752717930 245 MFTNAK 250
Cdd:COG0410 223 LLADPE 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
16-252 |
4.00e-47 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 159.88 E-value: 4.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 16 RGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgKSRIADRrqve 95
Cdd:PRK11432 10 KNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT-------HRSIQQR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 96 rirsELGMVFQSFNLWSHKTVLENVmEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAM 175
Cdd:PRK11432 79 ----DICMVFQSYALFPHMSLGENV-GYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 176 RPKVMLFDEPTSALDPELvgevLRVMRALAEE-----GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAK 250
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANL----RRSMREKIRElqqqfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
..
gi 752717930 251 SE 252
Cdd:PRK11432 230 SR 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-260 |
2.88e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 155.07 E-value: 2.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 11 AAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINML-----ETPDAGEITVAGETIRMKPTgsgk 85
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 86 srIADRRQVErirselgMVFQSFNLWSHKTVLENVMEAP-LHVQKRSRAECLEEAEALLAKVGIADK---RNHYPA-HLS 160
Cdd:PRK14247 78 --IELRRRVQ-------MVFQIPNPIPNLSIFENVALGLkLNRLVKSKKELQERVRWALEKAQLWDEvkdRLDAPAgKLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 161 GGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEgRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEG 240
Cdd:PRK14247 149 GGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
250 260
....*....|....*....|
gi 752717930 241 RPQDMFTNAKSERFRKFISG 260
Cdd:PRK14247 228 PTREVFTNPRHELTEKYVTG 247
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-252 |
6.51e-46 |
|
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: 160.62 E-value: 6.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 7 PPAPAAITVRGLRKSF-----------GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLEtPDAGEITVAGET 75
Cdd:COG4172 270 PDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 76 IrmkptgSGKSRIADRRqverIRSELGMVFQ----SFN--LwshkTVLENVMEaPLHVQ--KRSRAECLEEAEALLAKVG 147
Cdd:COG4172 349 L------DGLSRRALRP----LRRRMQVVFQdpfgSLSprM----TVGQIIAE-GLRVHgpGLSAAERRARVAEALEEVG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 148 I-ADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRAL-AEEGRTMLVVTHEMGFARDVS 225
Cdd:COG4172 414 LdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALA 493
|
250 260
....*....|....*....|....*..
gi 752717930 226 SRVIFLHQGAIEEEGRPQDMFTNAKSE 252
Cdd:COG4172 494 HRVMVMKDGKVVEQGPTEQVFDAPQHP 520
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-236 |
9.75e-46 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 152.56 E-value: 9.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGP-VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPtgsgksriadR 91
Cdd:cd03292 1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLR----------G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 RQVERIRSELGMVFQSFNLWSHKTVLENVMeAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIAR 171
Cdd:cd03292 71 RAIPYLRRKIGVVFQDFRLLPDRNVYENVA-FALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 172 ALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAI 236
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
20-260 |
3.04e-45 |
|
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: 155.40 E-value: 3.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 20 KSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgkSRIADRRQVERIRS 99
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENI---------MKQSPVELREVRRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 100 ELGMVFQSFNLWSHKTVLENVMEAPlHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKV 179
Cdd:TIGR01186 72 KIGMVFQQFALFPHMTILQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 180 MLFDEPTSALDP----ELVGEVLRVMRALaeeGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAKSERFR 255
Cdd:TIGR01186 151 LLMDEAFSALDPlirdSMQDELKKLQATL---QKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVE 227
|
....*
gi 752717930 256 KFISG 260
Cdd:TIGR01186 228 EFIGK 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-245 |
5.10e-45 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 157.87 E-value: 5.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 9 APAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMK-PTGSGKSR 87
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRsPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 88 IAdrrqverirselgMVFQSFNLWSHKTVLENVMeapLHVQKRS-----RAECLEEAEALLAKVGI---ADKRnhyPAHL 159
Cdd:COG1129 81 IA-------------IIHQELNLVPNLSVAENIF---LGREPRRgglidWRAMRRRARELLARLGLdidPDTP---VGDL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 160 SGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEE 239
Cdd:COG1129 142 SVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGT 221
|
....*.
gi 752717930 240 GRPQDM 245
Cdd:COG1129 222 GPVAEL 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-236 |
1.67e-44 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 147.97 E-value: 1.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 14 TVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETI-RMKPtgsgksriadrR 92
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLaSLSP-----------K 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIRSelgmvfqsfnlwshktVLENVMEAplhvqkrsraecleeaeallakVGIADKRNHYPAHLSGGQQQRAAIARA 172
Cdd:cd03214 70 ELARKIA----------------YVPQALEL----------------------LGLAHLADRPFNELSGGERQRVLLARA 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 173 LAMRPKVMLFDEPTSALDPELVGEVLRVMRALA-EEGRTMLVVTHEMGFARDVSSRVIFLHQGAI 236
Cdd:cd03214 112 LAQEPPILLLDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-260 |
7.55e-44 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 148.84 E-value: 7.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 12 AITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCIN-MLE-TPDA---GEITVAGETI---RMKPTgs 83
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrLLElNEEArveGEVRLFGRNIyspDVDPI-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 84 gksriadrrqveRIRSELGMVFQSFNLWSHKTVLENV-MEAPLHVQKRSRAECLEEAEALLAKVG----IADKRNHYPAH 158
Cdd:PRK14267 82 ------------EVRREVGMVFQYPNPFPHLTIYDNVaIGVKLNGLVKSKKELDERVEWALKKAAlwdeVKDRLNDYPSN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 159 LSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEgRTMLVVTHEMGFARDVSSRVIFLHQGAIEE 238
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
250 260
....*....|....*....|..
gi 752717930 239 EGRPQDMFTNAKSERFRKFISG 260
Cdd:PRK14267 229 VGPTRKVFENPEHELTEKYVTG 250
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
26-253 |
7.97e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 149.46 E-value: 7.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 26 EVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMkptgSGKSRIADRRQVerirselGMVF 105
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY----DKKSLLEVRKTV-------GIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 106 QSFN--LWShKTVLENVMEAPLHVqKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFD 183
Cdd:PRK13639 85 QNPDdqLFA-PTVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 184 EPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAKSER 253
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-238 |
1.86e-43 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 148.09 E-value: 1.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 11 AAITVRGLRKSFG----PVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkpTGSGks 86
Cdd:COG4525 2 SMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV----TGPG-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 87 riADRrqverirselGMVFQSFNLWSHKTVLENVmEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQR 166
Cdd:COG4525 76 --ADR----------GVVFQKDALLPWLNVLDNV-AFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 167 AAIARALAMRPKVMLFDEPTSALDP---ELVGEVLrvMRALAEEGRTMLVVTHEMGFARDVSSRVIFL--HQGAIEE 238
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDAltrEQMQELL--LDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-260 |
1.99e-43 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 156.15 E-value: 1.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 2 TPSTNPPAPAAITVRGLRKSFGP--VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGetirmk 79
Cdd:COG2274 463 SKLSLPRLKGDIELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDG------ 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 80 ptgsgksriADRRQVER--IRSELGMVFQSFNLWShKTVLENVMEAplhvqkRSRAEcLEEAEALLAKVGIADKRNHYP- 156
Cdd:COG2274 537 ---------IDLRQIDPasLRRQIGVVLQDVFLFS-GTIRENITLG------DPDAT-DEEIIEAARLAGLHDFIEALPm 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 157 ----------AHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAeEGRTMLVVTHEMGFARDVsS 226
Cdd:COG2274 600 gydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLA-D 677
|
250 260 270
....*....|....*....|....*....|....
gi 752717930 227 RVIFLHQGAIEEEGRPQDMFtnAKSERFRKFISG 260
Cdd:COG2274 678 RIIVLDKGRIVEDGTHEELL--ARKGLYAELVQQ 709
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-236 |
2.05e-43 |
|
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: 144.88 E-value: 2.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksrIADRR 92
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS----------FASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 qvERIRSELGMVFQsfnlwshktvlenvmeaplhvqkrsraecleeaeallakvgiadkrnhypahLSGGQQQRAAIARA 172
Cdd:cd03216 71 --DARRAGIAMVYQ----------------------------------------------------LSVGERQMVEIARA 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752717930 173 LAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAI 236
Cdd:cd03216 97 LARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
11-260 |
2.76e-43 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 155.27 E-value: 2.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 11 AAITVRGLRKSF----GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMkptgsgks 86
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAT-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 87 riADRRQVERIRSE-LGMVFQSFNLWSHKTVLENVmEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQ 165
Cdd:PRK10535 75 --LDADALAQLRREhFGFIFQRYHLLSHLTAAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 166 RAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDvSSRVIFLHQGAI--------E 237
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIvrnppaqeK 230
|
250 260
....*....|....*....|...
gi 752717930 238 EEGRPQDMFTNAKSERFRKFISG 260
Cdd:PRK10535 231 VNVAGGTEPVVNTASGWRQFVSG 253
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-248 |
4.22e-43 |
|
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: 153.30 E-value: 4.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFG----PVEVLKGIDMEAREGEVVSILGSSGSGKS-TMLRCINMLETPDA---GEITVAGETIRmkptgsg 84
Cdd:COG4172 7 LSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAAhpsGSILFDGQDLL------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 85 ksrIADRRQVERIR-SELGMVFQ----SFNlwSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIADKR---NHYP 156
Cdd:COG4172 80 ---GLSERELRRIRgNRIAMIFQepmtSLN--PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPErrlDAYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 157 AHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRAL-AEEGRTMLVVTHEMGFARDVSSRVIFLHQGA 235
Cdd:COG4172 155 HQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGE 234
|
250
....*....|...
gi 752717930 236 IEEEGRPQDMFTN 248
Cdd:COG4172 235 IVEQGPTAELFAA 247
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-246 |
5.17e-43 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 147.47 E-value: 5.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgksriaDRRQVERIRSELGMVFQS 107
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL-------------SEETVWDVRRQVGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 108 -FNLWSHKTVLENVMEApLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPT 186
Cdd:PRK13635 90 pDNQFVGATVQDDVAFG-LENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 752717930 187 SALDPELVGEVLRVMRALAEEGR-TMLVVTHEMGFARDvSSRVIFLHQGAIEEEGRPQDMF 246
Cdd:PRK13635 169 SMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-260 |
1.06e-42 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 145.69 E-value: 1.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAgEITVAGETIRmkptgSGKSRIADRR 92
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNP-EVTITGSIVY-----NGHNIYSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIRSELGMVFQSFNLWSHkTVLENVMEApLHVQKRSRAECLEEA-EALLAKVGIADK---RNHYPA-HLSGGQQQRA 167
Cdd:PRK14239 80 DTVDLRKEIGMVFQQPNPFPM-SIYENVVYG-LRLKGIKDKQVLDEAvEKSLKGASIWDEvkdRLHDSAlGLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 168 AIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEgRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFT 247
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFM 236
|
250
....*....|...
gi 752717930 248 NAKSERFRKFISG 260
Cdd:PRK14239 237 NPKHKETEDYISG 249
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
31-248 |
2.36e-42 |
|
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: 147.55 E-value: 2.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 31 IDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgSGKSRIadRRQVERIRseLGMVFQSFNL 110
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQ-----DSARGI--FLPPHRRR--IGYVFQEARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 111 WSHKTVLENVMEAPLHVQKRSRAECLEEAEALLakvGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALD 190
Cdd:COG4148 89 FPHLSVRGNLLYGRKRAPRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 191 PELVGEVLRVMRALAEEGRT-MLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTN 248
Cdd:COG4148 166 LARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
14-259 |
5.37e-42 |
|
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: 143.05 E-value: 5.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 14 TVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETI-RMKPTgsgksriadrr 92
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItKLPPH----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 qvERIRSELGMVFQSFNLWSHKTVLENvMEAPLHVQKRSRAECLEEAEALLAKvgIADKRNHYPAHLSGGQQQRAAIARA 172
Cdd:TIGR03410 71 --ERARAGIAYVPQGREIFPRLTVEEN-LLTGLAALPRRSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 173 LAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGR-TMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMftnaKS 251
Cdd:TIGR03410 146 LVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DE 221
|
....*...
gi 752717930 252 ERFRKFIS 259
Cdd:TIGR03410 222 DKVRRYLA 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
11-249 |
1.06e-41 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 143.37 E-value: 1.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 11 AAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETI-RMKPtgsgkSRIA 89
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLaDWSP-----AELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 90 DRRQVERIRSELGMVFqsfnlwshkTVLENV-MEAPLHVQKRSRAECLeeAEALLAKVGIADKRN-HYPAhLSGGQQQRA 167
Cdd:PRK13548 76 RRRAVLPQHSSLSFPF---------TVEEVVaMGRAPHGLSRAEDDAL--VAAALAQVDLAHLAGrDYPQ-LSGGEQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 168 AIARALA------MRPKVMLFDEPTSALDPELVGEVLRVMRALA-EEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEG 240
Cdd:PRK13548 144 QLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
....*....
gi 752717930 241 RPQDMFTNA 249
Cdd:PRK13548 224 TPAEVLTPE 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
13-234 |
1.56e-41 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 140.21 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLrkSF----GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTGSgksri 88
Cdd:cd03228 1 IEFKNV--SFsypgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 89 adrrqverIRSELGMVFQSFNLWShKTVLENVmeaplhvqkrsraecleeaeallakvgiadkrnhypahLSGGQQQRAA 168
Cdd:cd03228 74 --------LRKNIAYVPQDPFLFS-GTIRENI--------------------------------------LSGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752717930 169 IARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAeEGRTMLVVTHEMGFARDVsSRVIFLHQG 234
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRDA-DRIIVLDDG 170
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
11-217 |
3.40e-41 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 140.31 E-value: 3.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 11 AAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksriad 90
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 91 rRQVERIRSELGMVFQSFNLWSHKTVLENV-MEAPLHVQKRSRaeclEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAI 169
Cdd:COG4133 68 -DAREDYRRRLAYLGHADGLKPELTVRENLrFWAALYGLRADR----EAIDEALEAVGLAGLADLPVRQLSAGQKRRVAL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 752717930 170 ARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHE 217
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-244 |
4.46e-41 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 147.10 E-value: 4.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 9 APAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKptgsgKSRI 88
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIR-----SPRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 89 AdrrqverIRSELGMVFQSFNLWSHKTVLENVM--EAPLHVQKRSRAECLEEAEALLAKVGIA---DKRNHypaHLSGGQ 163
Cdd:COG3845 77 A-------IALGIGMVHQHFMLVPNLTVAENIVlgLEPTKGGRLDRKAARARIRELSERYGLDvdpDAKVE---DLSVGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 164 QQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQ 243
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
.
gi 752717930 244 D 244
Cdd:COG3845 227 E 227
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
43-258 |
4.60e-41 |
|
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: 143.40 E-value: 4.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 43 ILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPtgsgksriADRRQVerirselGMVFQSFNLWSHKTVLENVmE 122
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP--------PHLRHI-------NMVFQSYALFPHMTVEENV-A 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 123 APLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMR 202
Cdd:TIGR01187 65 FGLKMRKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 203 ALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAKSERFRKFI 258
Cdd:TIGR01187 145 TIQEQlGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-243 |
8.01e-41 |
|
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: 139.95 E-value: 8.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVE--VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgksriad 90
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 91 RRQVERIRSELGMVFQSFNLWSHKTVLENVMeapLHVQKR--SRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAA 168
Cdd:cd03263 67 RTDRKAARQSLGYCPQFDALFDELTVREHLR---FYARLKglPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 169 IARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAeEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQ 243
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
9-254 |
9.48e-41 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 143.60 E-value: 9.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 9 APAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDA--GEITVAGETIRMKPTgsgks 86
Cdd:TIGR03258 2 ACGGIRIDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGltGRIAIADRDLTHAPP----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 87 riadrrqverIRSELGMVFQSFNLWSHKTVLENVMEApLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQR 166
Cdd:TIGR03258 77 ----------HKRGLALLFQNYALFPHLKVEDNVAFG-LRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 167 AAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE--GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQD 244
Cdd:TIGR03258 146 IAIARAIAIEPDVLLLDEPLSALDANIRANMREEIAALHEElpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQA 225
|
250
....*....|
gi 752717930 245 MFtNAKSERF 254
Cdd:TIGR03258 226 LY-DAPADGF 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
22-234 |
1.19e-40 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 139.62 E-value: 1.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 22 FGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgkSRIADRrQVERIRSEL 101
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDI---------TRLKNR-EVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 102 GMVFQSFNLWSHKTVLENVmEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVML 181
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNV-AIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 752717930 182 FDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQG 234
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
13-250 |
1.27e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 141.76 E-value: 1.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGP-----VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEI------------TVAGET 75
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkkTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 76 IRMKPTgSGKSRIADRRQVERIRSELGMVFQ--SFNLWShKTVLENVMEAPLHVqKRSRAECLEEAEALLAKVGIAD--- 150
Cdd:PRK13651 83 VLEKLV-IQKTRFKKIKKIKEIRRRVGVVFQfaEYQLFE-QTIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLDEsyl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 151 KRNhyPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIF 230
Cdd:PRK13651 160 QRS--PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIF 237
|
250 260
....*....|....*....|
gi 752717930 231 LHQGAIEEEGRPQDMFTNAK 250
Cdd:PRK13651 238 FKDGKIIKDGDTYDILSDNK 257
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
20-245 |
1.94e-40 |
|
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: 141.37 E-value: 1.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 20 KSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksriadrRQVERIRS 99
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV--------------REPRKVRR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 100 ELGMVFQSFNLWSHKTVLEN-VMEAPLHVQKRSRAEclEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPK 178
Cdd:TIGR01188 67 SIGIVPQYASVDEDLTGRENlEMMGRLYGLPKDEAE--ERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPD 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 179 VMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDM 245
Cdd:TIGR01188 145 VLFLDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-249 |
2.90e-40 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 139.48 E-value: 2.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETI-RMKPTgsgksRIADR 91
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLaAWSPW-----ELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 RQVERIRSELgmvfqSFNLwshkTVLENVM--EAPLHvqkRSRAECLEEAEALLAKVGIADKRN-HYPaHLSGGQQQRAA 168
Cdd:COG4559 77 RAVLPQHSSL-----AFPF----TVEEVVAlgRAPHG---SSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 169 IARALA-------MRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGR 241
Cdd:COG4559 144 LARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGT 223
|
....*...
gi 752717930 242 PQDMFTNA 249
Cdd:COG4559 224 PEEVLTDE 231
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-236 |
3.60e-40 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 139.43 E-value: 3.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 2 TPSTNPPAPAAItvRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEItvagetirmkpt 81
Cdd:PRK11247 4 TARLNQGTPLLL--NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 82 gsgksrIADRRQVERIRSELGMVFQSFNLWSHKTVLENVmeaPLHVQKRSRAECLEEAEAllakVGIADKRNHYPAHLSG 161
Cdd:PRK11247 70 ------LAGTAPLAEAREDTRLMFQDARLLPWKKVIDNV---GLGLKGQWRDAALQALAA----VGLADRANEWPAALSG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 162 GQQQRAAIARALAMRPKVMLFDEPTSALDP----ELVGEVLRVMRalaEEGRTMLVVTHEMGFARDVSSRVIFLHQGAI 236
Cdd:PRK11247 137 GQKQRVALARALIHRPGLLLLDEPLGALDAltriEMQDLIESLWQ---QHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
23-221 |
6.43e-40 |
|
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: 136.78 E-value: 6.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 23 GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGEtirmkPTGSGKSRIADRRQverirsELG 102
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGE-----PLDYSRKGLLERRQ------RVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 103 MVFQSFN--LWShKTVLENVMEAPLHVqKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVM 180
Cdd:TIGR01166 72 LVFQDPDdqLFA-ADVDQDVAFGPLNL-GLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 752717930 181 LFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFA 221
Cdd:TIGR01166 150 LLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-245 |
1.05e-39 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 137.12 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTGsgksriadrr 92
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 qverIRSELGMVFQSFNLWSHKTVLENV-MEAPLHVQKRSRAEclEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIAR 171
Cdd:cd03265 71 ----VRRRIGIVFQDLSVDDELTGWENLyIHARLYGVPGAERR--ERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 172 ALAMRPKVMLFDEPTSALDPELVGEVLRVMRAL-AEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDM 245
Cdd:cd03265 145 SLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-246 |
2.75e-39 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 139.78 E-value: 2.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 11 AAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLEtpdagEITvagetirmkptgSGKSRIAD 90
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLE-----DIT------------SGDLFIGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 91 RR--QVERIRSELGMVFQSFNLWSHKTVLENvMEAPLHVQKRSRAEC---LEEAEALLAKVGIADKRnhyPAHLSGGQQQ 165
Cdd:PRK11000 65 KRmnDVPPAERGVGMVFQSYALYPHLSVAEN-MSFGLKLAGAKKEEInqrVNQVAEVLQLAHLLDRK---PKALSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 166 RAAIARALAMRPKVMLFDEPTSALDPelvgeVLRV-MRA----LAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEE 239
Cdd:PRK11000 141 RVAIGRTLVAEPSVFLLDEPLSNLDA-----ALRVqMRIeisrLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQV 215
|
....*..
gi 752717930 240 GRPQDMF 246
Cdd:PRK11000 216 GKPLELY 222
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
13-240 |
4.77e-39 |
|
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: 135.19 E-value: 4.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSF----GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGetirmkptgsgksrI 88
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--------------F 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 89 ADRRQVERIRSELGMVFQSFNLWSHKTVLENVME-APLHVQKRsrAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRA 167
Cdd:cd03266 68 DVVKEPAEARRRLGFVSDSTGLYDRLTARENLEYfAGLYGLKG--DELTARLEELADRLGMEELLDRRVGGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752717930 168 AIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEG 240
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
32-240 |
5.03e-39 |
|
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: 134.93 E-value: 5.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 32 DMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPtgsgksrIADRrqverirsELGMVFQSFNLW 111
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP-------PADR--------PVSMLFQENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 112 SHKTVLENVMEApLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDP 191
Cdd:cd03298 83 AHLTVEQNVGLG-LSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 752717930 192 ELVGEVLRVMRAL-AEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEG 240
Cdd:cd03298 162 ALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-244 |
5.86e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 137.16 E-value: 5.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 12 AITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKptgsgksriaDR 91
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE----------DR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 RQV-----ERirselGmvfqsfnLWSHKTVLENVME-APLHvqKRSRAECLEEAEALLAKVGIADKRNHyPAH-LSGGQQ 164
Cdd:COG4152 71 RRIgylpeER-----G-------LYPKMKVGEQLVYlARLK--GLSKAEAKRRADEWLERLGLGDRANK-KVEeLSKGNQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 165 QRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQD 244
Cdd:COG4152 136 QKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDE 215
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-239 |
6.68e-39 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 136.36 E-value: 6.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 17 GLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgkSRIaDRRQVER 96
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPL---------AKL-NRAQRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 97 IRSELGMVFQ----SFNlwSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVG----IADKRnhyPAHLSGGQQQRAA 168
Cdd:PRK10419 87 FRRDIQMVFQdsisAVN--PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDlddsVLDKR---PPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752717930 169 IARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRT-MLVVTHEMGFARDVSSRVIFLHQGAIEEE 239
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
10-231 |
1.35e-38 |
|
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: 134.48 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 10 PAAITVRGLRKSF-----GPVE--VLKGIDMEAREGEVVSILGSSGSGKSTMLRCI--NMLetPDAGEITVAgetirmkp 80
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYL--PDSGSILVR-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 81 tgSGKSRI----ADRRQVERIR-SELGMVFQSFNLWSHKTVLENVMEaPLHVQKRSRAECLEEAEALLAKVGIADKRNH- 154
Cdd:COG4778 72 --HDGGWVdlaqASPREILALRrRTIGYVSQFLRVIPRVSALDVVAE-PLLERGVDREEARARARELLARLNLPERLWDl 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 155 YPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFL 231
Cdd:COG4778 149 PPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
13-254 |
1.61e-38 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 135.14 E-value: 1.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDA---GEITVAGETIRMKptgsgkSRIA 89
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQRE------GRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 90 drRQVERIRSELGMVFQSFNLWSHKTVLENVMEAPLHVQKRSRAeCL--------EEAEALLAKVGIADKRNHYPAHLSG 161
Cdd:PRK09984 79 --RDIRKSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRT-CFswftreqkQRALQALTRVGMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 162 GQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAE-EGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEG 240
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
250
....*....|....
gi 752717930 241 RPQDmFTNaksERF 254
Cdd:PRK09984 236 SSQQ-FDN---ERF 245
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
26-228 |
4.64e-38 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 133.40 E-value: 4.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 26 EVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmKPTGSGKSRIADRrqverirsELGMVF 105
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMS-KLSSAAKAELRNQ--------KLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 106 QSFNLWSHKTVLENVmEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEP 185
Cdd:PRK11629 94 QFHHLLPDFTALENV-AMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 752717930 186 TSALDP-------ELVGEVLRvmralaEEGRTMLVVTHEMGFARDVSSRV 228
Cdd:PRK11629 173 TGNLDArnadsifQLLGELNR------LQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-250 |
8.85e-38 |
|
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: 132.28 E-value: 8.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPtgsgksriadrr 92
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 qVERiRSELGMVF--QSFNLWSHKTVLENVMeAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIA 170
Cdd:cd03218 69 -MHK-RARLGIGYlpQEASIFRKLTVEENIL-AVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 171 RALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAK 250
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
37-243 |
1.04e-37 |
|
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: 131.65 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 37 EGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGET-------IRMKPTgsgksriaDRRqverirseLGMVFQSFN 109
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkINLPPQ--------QRK--------IGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 110 LWSHKTVLENVMEAplhVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSAL 189
Cdd:cd03297 86 LFPHLNVRENLAFG---LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 190 DPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLhqgaieEEGRPQ 243
Cdd:cd03297 163 DRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVM------EDGRLQ 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
13-234 |
1.19e-37 |
|
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: 131.25 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksrIADRR 92
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----------IAARN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIRSELGmvfqsfnLWSHKTVLENVME-APLHVQKRSRAecLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIAR 171
Cdd:cd03269 71 RIGYLPEERG-------LYPKMKVIDQLVYlAQLKGLKKEEA--RRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752717930 172 ALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQG 234
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-244 |
1.58e-37 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 138.76 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 7 PPAPAAITVRGLrkSF---GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgs 83
Cdd:COG1132 334 PPVRGEIEFENV--SFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR------ 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 84 gksriaDRRQvERIRSELGMVFQSFNLWsHKTVLENV----MEAplhvqkrSRAEcLEEAealLAKVGIADKRNHYP--- 156
Cdd:COG1132 406 ------DLTL-ESLRRQIGVVPQDTFLF-SGTIRENIrygrPDA-------TDEE-VEEA---AKAAQAHEFIEALPdgy 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 157 --------AHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAeEGRTMLVVTHEMGFARDVsSRV 228
Cdd:COG1132 467 dtvvgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRNA-DRI 544
|
250
....*....|....*.
gi 752717930 229 IFLHQGAIEEEGRPQD 244
Cdd:COG1132 545 LVLDDGRIVEQGTHEE 560
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-257 |
1.88e-37 |
|
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: 138.36 E-value: 1.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 7 PPAPAAITVRGLRKSF--GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsg 84
Cdd:COG4987 328 APGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 85 ksriadRRQVERIRSELGMVFQSFNLWSHkTVLENVMEAplhvqkRSRAEcLEEAEALLAKVGIADKRNHYP-------- 156
Cdd:COG4987 401 ------DLDEDDLRRRIAVVPQRPHLFDT-TLRENLRLA------RPDAT-DEELWAALERVGLGDWLAALPdgldtwlg 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 157 ---AHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAeEGRTMLVVTHEMGFARDVsSRVIFLHQ 233
Cdd:COG4987 467 eggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGLERM-DRILVLED 544
|
250 260
....*....|....*....|....
gi 752717930 234 GAIEEEGRPQDmfTNAKSERFRKF 257
Cdd:COG4987 545 GRIVEQGTHEE--LLAQNGRYRQL 566
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
27-250 |
2.23e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 132.90 E-value: 2.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAG-ETirmkptgsgksriADRRQVERIRSELGMVF 105
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDT-------------SDEENLWDIRNKAGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 106 QS-FNLWSHKTVLENVMEAP--LHVQKRSRAECLEEAealLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLF 182
Cdd:PRK13633 92 QNpDNQIVATIVEEDVAFGPenLGIPPEEIRERVDES---LKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 183 DEPTSALDPELVGEVLRVMRAL-AEEGRTMLVVTHEMGFARDvSSRVIFLHQGAIEEEGRPQDMFTNAK 250
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVE 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
10-257 |
2.49e-37 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 131.30 E-value: 2.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 10 PAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPtgsgksria 89
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 90 drrqVERiRSELGM--------VFQsfNLwshkTVLENVMeAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSG 161
Cdd:COG1137 72 ----MHK-RARLGIgylpqeasIFR--KL----TVEDNIL-AVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 162 GQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEG----------RTMLVVTHemgfardvssRVIFL 231
Cdd:COG1137 140 GERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGigvlitdhnvRETLGICD----------RAYII 209
|
250 260
....*....|....*....|....*.
gi 752717930 232 HQGAIEEEGRPQDMftnAKSERFRKF 257
Cdd:COG1137 210 SEGKVLAEGTPEEI---LNNPLVRKV 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-250 |
3.00e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 132.04 E-value: 3.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 11 AAITVRGLRKSFGPVE--VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgksri 88
Cdd:PRK13632 6 VMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 89 aDRRQVERIRSELGMVFQS-FNLWSHKTV-------LENVMEAPlhvqKRSRAECLEEAEallaKVGIADKRNHYPAHLS 160
Cdd:PRK13632 74 -SKENLKEIRKKIGIIFQNpDNQFIGATVeddiafgLENKKVPP----KKMKDIIDDLAK----KVGMEDYLDKEPQNLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 161 GGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEG-RTMLVVTHEMGFARdVSSRVIFLHQGAIEEE 239
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI-LADKVIVFSEGKLIAQ 223
|
250
....*....|.
gi 752717930 240 GRPQDMFTNAK 250
Cdd:PRK13632 224 GKPKEILNNKE 234
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
11-246 |
3.60e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 134.20 E-value: 3.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 11 AAITVRGLRKSF-GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETI-RMKPtgsgksri 88
Cdd:PRK11650 2 AGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnELEP-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 89 ADRrqverirsELGMVFQSFNLWSHKTVLENvMEAPLHVQKRSRAEC---LEEAEALLAKVGIADKRnhyPAHLSGGQQQ 165
Cdd:PRK11650 74 ADR--------DIAMVFQNYALYPHMSVREN-MAYGLKIRGMPKAEIeerVAEAARILELEPLLDRK---PRELSGGQRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 166 RAAIARALAMRPKVMLFDEPTSALDPELVG----EVLRVMRALaeeGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGR 241
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDAKLRVqmrlEIQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGT 218
|
....*
gi 752717930 242 PQDMF 246
Cdd:PRK11650 219 PVEVY 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
26-236 |
4.17e-37 |
|
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: 129.68 E-value: 4.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 26 EVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKptgsgksriadrrqvERIRSeLGMVF 105
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK---------------ERRKS-IGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 106 QS--FNLWShKTVLENvmeapLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFD 183
Cdd:cd03226 78 QDvdYQLFT-DSVREE-----LLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 752717930 184 EPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAI 236
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-244 |
5.59e-37 |
|
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: 136.81 E-value: 5.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 2 TPSTNPPAPAAITVRGLRKSFGP-VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIR-MK 79
Cdd:COG4988 326 TAPLPAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSdLD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 80 PtgsgksriadrrqvERIRSELGMVFQS---FnlwsHKTVLENVMEAplhvqkRSRAEcLEEAEALLAKVGIADKRNHYP 156
Cdd:COG4988 406 P--------------ASWRRQIAWVPQNpylF----AGTIRENLRLG------RPDAS-DEELEAALEAAGLDEFVAALP 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 157 -----------AHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAeEGRTMLVVTHEMGFARDvS 225
Cdd:COG4988 461 dgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-A 538
|
250
....*....|....*....
gi 752717930 226 SRVIFLHQGAIEEEGRPQD 244
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEE 557
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
26-243 |
7.51e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 131.40 E-value: 7.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 26 EVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgksriaDRRQVERIRSELGMVF 105
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV-------------NAENEKWVRSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 106 QSFN--LWShKTVLENVMEAPLHvQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFD 183
Cdd:PRK13647 86 QDPDdqVFS-STVWDDVAFGPVN-MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 184 EPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQ 243
Cdd:PRK13647 164 EPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
28-250 |
1.36e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 131.10 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKpTGSgksriadrRQVERIRSELGMVFQ- 106
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPE-TGN--------KNLKKLRKKVSLVFQf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 107 SFNLWSHKTVLENVMEAPLHVqKRSRAECLEEAEALLAKVGIADK-RNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEP 185
Cdd:PRK13641 94 PEAQLFENTVLKDVEFGPKNF-GFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 186 TSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAK 250
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-248 |
1.43e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 131.90 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 20 KSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTGSGKSRIADRRQVE---R 96
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSKKIKnfkE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 97 IRSELGMVFQ--SFNLWShKTVLENVMEAPLHVqKRSRAECLEEAEALLAKVGIAD---KRNhyPAHLSGGQQQRAAIAR 171
Cdd:PRK13631 114 LRRRVSMVFQfpEYQLFK-DTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDsylERS--PFGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 172 ALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTN 248
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTD 266
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
32-240 |
1.77e-36 |
|
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: 128.44 E-value: 1.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 32 DMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkpTGSGKSRiadrRQVErirselgMVFQSFNLW 111
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH----TGLAPYQ----RPVS-------MLFQENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 112 SHKTVLENVMEApLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDP 191
Cdd:TIGR01277 83 AHLTVRQNIGLG-LHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 752717930 192 ELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEG 240
Cdd:TIGR01277 162 LLREEMLALVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-258 |
3.56e-36 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 131.88 E-value: 3.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 2 TPSTNPPAPAAIT----VRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGEtir 77
Cdd:PRK11607 5 IPRPQAKTRKALTplleIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 78 mkptgsgksriaDRRQVERIRSELGMVFQSFNLWSHKTVLENVMEApLHVQKRSRAECLEEAEALLAKVGIADKRNHYPA 157
Cdd:PRK11607 82 ------------DLSHVPPYQRPINMMFQSYALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 158 HLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEV-LRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAI 236
Cdd:PRK11607 149 QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
|
250 260
....*....|....*....|..
gi 752717930 237 EEEGRPQDMFTNAKSERFRKFI 258
Cdd:PRK11607 229 VQIGEPEEIYEHPTTRYSAEFI 250
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
28-249 |
4.22e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 129.75 E-value: 4.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgSGKsriaDRRQVERIRSELGMVFQ- 106
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVIT-----AGK----KNKKLKPLRKKVGIVFQf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 107 -SFNLWsHKTVLENVMEAPLHVQKrSRAECLEEAEALLAKVGI-ADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDE 184
Cdd:PRK13634 94 pEHQLF-EETVEKDICFGPMNFGV-SEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752717930 185 PTSALDPELVGEVLRVMRAL-AEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNA 249
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-248 |
5.73e-36 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 130.08 E-value: 5.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 16 RGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkpTGSGKSRIADRRQve 95
Cdd:PRK11308 19 RGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL----LKADPEAQKLLRQ-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 96 rirsELGMVFQ----SFNlwSHKTVlENVMEAPLHVQ-KRSRAECLEEAEALLAKVGIadKRNH---YPAHLSGGQQQRA 167
Cdd:PRK11308 93 ----KIQIVFQnpygSLN--PRKKV-GQILEEPLLINtSLSAAERREKALAMMAKVGL--RPEHydrYPHMFSGGQRQRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 168 AIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMF 246
Cdd:PRK11308 164 AIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIF 243
|
..
gi 752717930 247 TN 248
Cdd:PRK11308 244 NN 245
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
28-246 |
9.83e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 128.31 E-value: 9.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKptgsgksriadrrQVERIRSELGMVFQS 107
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEE-------------NVWDIRHKIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 108 -FNLWSHKTVLENVMEApLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPT 186
Cdd:PRK13650 90 pDNQFVGATVEDDVAFG-LENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 752717930 187 SALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARdVSSRVIFLHQGAIEEEGRPQDMF 246
Cdd:PRK13650 169 SMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELF 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
26-256 |
2.25e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 127.66 E-value: 2.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 26 EVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKptgsgksriadRRQVERIRSELGMVF 105
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYS-----------RKGLMKLRESVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 106 QS--FNLWShKTVLENVMEAPLHVQkRSRAECLEEAEALLAKVGIADKRnHYPAH-LSGGQQQRAAIARALAMRPKVMLF 182
Cdd:PRK13636 89 QDpdNQLFS-ASVYQDVSFGAVNLK-LPEDEVRKRVDNALKRTGIEHLK-DKPTHcLSFGQKKRVAIAGVLVMEPKVLVL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 183 DEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFtnAKSERFRK 256
Cdd:PRK13636 166 DEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF--AEKEMLRK 238
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-240 |
2.46e-35 |
|
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: 125.41 E-value: 2.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETirMKPTGSGKSRIadrr 92
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS--YQKNIEALRRI---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 qverirselGMVFQSFNLWSHKTVLENVMEAPLHVQKRSraeclEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARA 172
Cdd:cd03268 75 ---------GALIEAPGFYPNLTARENLRLLARLLGIRK-----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 752717930 173 LAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEG 240
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-252 |
2.96e-35 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 125.85 E-value: 2.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 32 DMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPtgsgksriADRRQVErirselgMVFQSFNLW 111
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP--------PSRRPVS-------MLFQENNLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 112 SHKTVLENVMEApLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDP 191
Cdd:PRK10771 84 SHLTVAQNIGLG-LNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752717930 192 ELVGEVLRVMRALAEEGR-TMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAKSE 252
Cdd:PRK10771 163 ALRQEMLTLVSQVCQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASA 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-234 |
8.48e-35 |
|
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: 124.50 E-value: 8.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkpTGSGKSRIadrrqverirselgMVFQS 107
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI----TEPGPDRM--------------VVFQN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 108 FNLWSHKTVLENVMEAPLHVQK-RSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPT 186
Cdd:TIGR01184 63 YSLLPWLTVRENIALAVDRVLPdLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 752717930 187 SALDPELVGEVL-RVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQG 234
Cdd:TIGR01184 143 GALDALTRGNLQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
28-246 |
2.20e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 124.86 E-value: 2.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkpTGSGKSRiadrrQVERIRSELGMVFQ- 106
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLI----TSTSKNK-----DIKQIRKKVGLVFQf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 107 SFNLWSHKTVLENVMEAPLH--VQKrsraeclEEAEAL----LAKVGIADK-RNHYPAHLSGGQQQRAAIARALAMRPKV 179
Cdd:PRK13649 94 PESQLFEETVLKDVAFGPQNfgVSQ-------EEAEALarekLALVGISESlFEKNPFELSGGQMRRVAIAGILAMEPKI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 180 MLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMF 246
Cdd:PRK13649 167 LVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
28-260 |
3.49e-34 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 127.07 E-value: 3.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgkSRIADRRQVERIRSELGMVFQS 107
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI---------AKISDAELREVRRKKIAMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 108 FNLWSHKTVLENVMEApLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTS 187
Cdd:PRK10070 115 FALMPHMTVLDNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752717930 188 ALDPELVGEVL-RVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAKSERFRKFISG 260
Cdd:PRK10070 194 ALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-245 |
4.65e-34 |
|
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: 128.38 E-value: 4.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKST---MLRCINMLEtPDAGEI----------------TVAG 73
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVlmhVLRGMDQYE-PTSGRIiyhvalcekcgyverpSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 74 ETIRmKPTGSGKSRIAD-----RRQVERIRSELGMVFQ-SFNLWSHKTVLENVMEApLHVQKRSRAECLEEAEALLAKVG 147
Cdd:TIGR03269 80 EPCP-VCGGTLEPEEVDfwnlsDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEA-LEEIGYEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 148 IADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPE---LVGEVLRvmRALAEEGRTMLVVTHEMGFARDV 224
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtakLVHNALE--EAVKASGISMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|.
gi 752717930 225 SSRVIFLHQGAIEEEGRPQDM 245
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEV 256
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
13-247 |
7.27e-34 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 126.11 E-value: 7.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgSGKSRIADRR 92
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV------EALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIRSELGMVFQsfnlWSHKTVLEnvMEAPLHVQKRSRAECLEEA--EALLAKVGIADKRNHYPAHLSGGQQQRAAIA 170
Cdd:PRK09536 78 RVASVPQDTSLSFE----FDVRQVVE--MGRTPHRSRFDTWTETDRAavERAMERTGVAQFADRPVTSLSGGERQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 171 RALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFT 247
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLT 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-258 |
8.11e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 122.84 E-value: 8.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 12 AITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDaGEITVAGetirmKPTGSGKSRIADR 91
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEG-----RVEFFNQNIYERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 RQVERIRSELGMVFQSFNLWShKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIADKRNH----YPAHLSGGQQQRA 167
Cdd:PRK14258 81 VNLNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHkihkSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 168 AIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGR-TMLVVTHEMGFARDVSSRVIFLHQ-----GAIEEEGR 241
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGL 239
|
250
....*....|....*..
gi 752717930 242 PQDMFTNAKSERFRKFI 258
Cdd:PRK14258 240 TKKIFNSPHDSRTREYV 256
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
10-240 |
1.29e-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: 122.25 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 10 PAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAG------ETIRMKPtgs 83
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgaelELYQLSE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 84 gksriADRRQVerIRSELGMVFQSFNLWSHKTVLE--NVMEAPLHVQKRSRAECLEEAEALLAKVGI-ADKRNHYPAHLS 160
Cdd:TIGR02323 78 -----AERRRL--MRTEWGFVHQNPRDGLRMRVSAgaNIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 161 GGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEE 239
Cdd:TIGR02323 151 GGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVES 230
|
.
gi 752717930 240 G 240
Cdd:TIGR02323 231 G 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
8-239 |
2.18e-33 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 121.04 E-value: 2.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 8 PAPAAITVRGLRKSFGPVE----VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETI-RMkptg 82
Cdd:PRK10584 2 PAENIVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhQM---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 83 sgksriaDRRQVERIRSE-LGMVFQSFNLWSHKTVLENVmEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSG 161
Cdd:PRK10584 78 -------DEEARAKLRAKhVGFVFQSFMLIPTLNALENV-ELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 162 GQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRvIFLHQGAIEEE 239
Cdd:PRK10584 150 GEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRR-LRLVNGQLQEE 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
13-240 |
2.40e-33 |
|
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: 120.38 E-value: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGeVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksriadrR 92
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL--------------K 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIRSELGMVFQSFNLWSHKTVLENV-MEAPLH--VQKRSRAECleeaEALLAKVGIADKRNHYPAHLSGGQQQRAAI 169
Cdd:cd03264 66 QPQKLRRRIGYLPQEFGVYPNFTVREFLdYIAWLKgiPSKEVKARV----DEVLELVNLGDRAKKKIGSLSGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752717930 170 ARALAMRPKVMLFDEPTSALDPElvgEVLRVMRALAE--EGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEG 240
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPE---ERIRFRNLLSElgEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
13-249 |
2.64e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 121.34 E-value: 2.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTGSGKSRIADRR 92
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIRSELgmvfqsfnlwshkTVLENVM--EAPlHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIA 170
Cdd:COG4604 82 QENHINSRL-------------TVRELVAfgRFP-YSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 171 RALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNA 249
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPE 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-260 |
3.75e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 121.74 E-value: 3.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 8 PAPAAITvrgLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGeITVAGETIRmkptgsGKSR 87
Cdd:PRK14271 20 PAMAAVN---LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLL------GGRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 88 IADRRQVERIRSELGMVFQSFNLWShKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVG----IADKRNHYPAHLSGGQ 163
Cdd:PRK14271 90 IFNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGlwdaVKDRLSDSPFRLSGGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 164 QQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEgRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQ 243
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTE 247
|
250
....*....|....*..
gi 752717930 244 DMFTNAKSERFRKFISG 260
Cdd:PRK14271 248 QLFSSPKHAETARYVAG 264
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-236 |
6.66e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 120.58 E-value: 6.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGP-----VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTgsgksr 87
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 88 iadrrqVERIRSeLGMVFQ------SFNLwshkTVLENVMEAPLHVQKRS-----RAECLEEAEALLAKVGIA-DKRNHY 155
Cdd:COG1101 76 ------YKRAKY-IGRVFQdpmmgtAPSM----TIEENLALAYRRGKRRGlrrglTKKRRELFRELLATLGLGlENRLDT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 156 PA-HLSGGQQQraaiARALAM----RPKVMLFDEPTSALDPELVGEVLRV-MRALAEEGRTMLVVTHEMGFARDVSSRVI 229
Cdd:COG1101 145 KVgLLSGGQRQ----ALSLLMatltKPKLLLLDEHTAALDPKTAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLI 220
|
....*..
gi 752717930 230 FLHQGAI 236
Cdd:COG1101 221 MMHEGRI 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-245 |
1.13e-32 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 122.14 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 31 IDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgSGKSRI---ADRRQVerirselGMVFQS 107
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF-----DSRKGIflpPEKRRI-------GYVFQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 108 FNLWSHKTVLENVmeapLHVQKRSRAECLEEA-EALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPT 186
Cdd:TIGR02142 84 ARLFPHLSVRGNL----RYGMKRARPSERRISfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 187 SALDPELVGEVLRVMRALAEEGRT-MLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDM 245
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-260 |
1.18e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 119.77 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMkptgsGKsriaDRRQVE--RIRSELGMV 104
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYF-----GK----DIFQIDaiKLRKEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 105 FQSFNLWSHKTVLENVmEAPLHV----QKRSRAECLEEAealLAKVG----IADKRNHYPAHLSGGQQQRAAIARALAMR 176
Cdd:PRK14246 96 FQQPNPFPHLSIYDNI-AYPLKShgikEKREIKKIVEEC---LRKVGlwkeVYDRLNSPASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 177 PKVMLFDEPTSALDPELVGEVLRVMRALAEEgRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAKSERFRK 256
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
....
gi 752717930 257 FISG 260
Cdd:PRK14246 251 YVIG 254
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
13-248 |
1.57e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 119.32 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTgsgksriadrR 92
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG----------H 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERirseLGMV--FQSFNLWSHKTVLENVMEAP-LHVQ-------------KRSRAECLEEAEALLAKVGIADKRNHYP 156
Cdd:PRK11300 76 QIAR----MGVVrtFQHVRLFREMTVIENLLVAQhQQLKtglfsgllktpafRRAESEALDRAATWLERVGLLEHANRQA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 157 AHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGA 235
Cdd:PRK11300 152 GNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
250
....*....|...
gi 752717930 236 IEEEGRPQDMFTN 248
Cdd:PRK11300 232 PLANGTPEEIRNN 244
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
12-248 |
1.63e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 120.29 E-value: 1.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 12 AITVRGLRKSF--GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGE---ITVAGETIRMKptgsgks 86
Cdd:PRK13640 5 IVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAK------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 87 riadrrQVERIRSELGMVFQS-FNLWSHKTVLENVMEApLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQ 165
Cdd:PRK13640 78 ------TVWDIREKVGIVFQNpDNQFVGATVGDDVAFG-LENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 166 RAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFArDVSSRVIFLHQGAIEEEGRPQD 244
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVE 229
|
....
gi 752717930 245 MFTN 248
Cdd:PRK13640 230 IFSK 233
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
14-240 |
1.96e-32 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 119.26 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 14 TVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTGSGKSriADRRQ 93
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSE--AERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 94 VerIRSELGMVFQSF--NLWSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIADKR-NHYPAHLSGGQQQRAAIA 170
Cdd:PRK11701 86 L--LRTEWGFVHQHPrdGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAARiDDLPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 752717930 171 RALAMRPKVMLFDEPTSALDPELVGEVLRVMRAL-AEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEG 240
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
28-249 |
2.70e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.77 E-value: 2.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKptgsgKSRIADrrqverIRSELGMVFQ- 106
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDK-----KVKLSD------IRKKVGLVFQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 107 -SFNLWsHKTVLENVMEAPLHVqKRSRAECLEEAEALLAKVGIA--DKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFD 183
Cdd:PRK13637 92 pEYQLF-EETIEKDIAFGPINL-GLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 184 EPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNA 249
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEV 236
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
14-231 |
4.06e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 117.20 E-value: 4.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 14 TVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDA---GEITVAGETIRMKPTgsgksriaD 90
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTALPA--------E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 91 RRQVerirselGMVFQSFNLWSHKTVLENVMEA-PLHVQKRSRAECLEEAealLAKVGIADKRNHYPAHLSGGQQQRAAI 169
Cdd:COG4136 75 QRRI-------GILFQDDLLFPHLSVGENLAFAlPPTIGRAQRRARVEQA---LEEAGLAGFADRDPATLSGGQRARVAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752717930 170 ARALAMRPKVMLFDEPTSALDPELVGEVLR-VMRALAEEGRTMLVVTHEMGFARDVsSRVIFL 231
Cdd:COG4136 145 LRALLAEPRALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEEDAPAA-GRVLDL 206
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-247 |
5.72e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 118.37 E-value: 5.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSF-GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgksriaDR 91
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI-------------TK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 RQVERIRSELGMVFQSFN--LWShKTVLENVMEAP--LHVQKRSRAECLEEAealLAKVGIADKRNHYPAHLSGGQQQRA 167
Cdd:PRK13652 71 ENIREVRKFVGLVFQNPDdqIFS-PTVEQDIAFGPinLGLDEETVAHRVSSA---LHMLGLEELRDRVPHHLSGGEKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 168 AIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMF 246
Cdd:PRK13652 147 AIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIF 226
|
.
gi 752717930 247 T 247
Cdd:PRK13652 227 L 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-245 |
9.25e-32 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 116.82 E-value: 9.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGP--VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksrIAD 90
Cdd:cd03252 1 ITFEHVRFRYKPdgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA----------LAD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 91 RrqvERIRSELGMVFQSfNLWSHKTVLENVmeaPLHVQKRSRAECLEEAEALLAKVGIADKRNHYP-------AHLSGGQ 163
Cdd:cd03252 71 P---AWLRRQVGVVLQE-NVLFNRSIRDNI---ALADPGMSMERVIEAAKLAGAHDFISELPEGYDtivgeqgAGLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 164 QQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAeEGRTMLVVTHEMGFARDvSSRVIFLHQGAIEEEGRPQ 243
Cdd:cd03252 144 RQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHD 221
|
..
gi 752717930 244 DM 245
Cdd:cd03252 222 EL 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-254 |
1.09e-31 |
|
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: 117.11 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 10 PAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAG-EITVAGETIrmkptgsGKSRI 88
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERR-------GGEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 89 ADrrqverIRSELGMVFQSFNLW--SHKTVLENVM---EAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQ 163
Cdd:COG1119 74 WE------LRKRIGLVSPALQLRfpRDETVLDVVLsgfFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 164 QQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEG-RTMLVVTH---EM--GFardvsSRVIFLHQGAIE 237
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhveEIppGI-----THVLLLKDGRVV 222
|
250
....*....|....*..
gi 752717930 238 EEGRPQDMFTNAKSERF 254
Cdd:COG1119 223 AAGPKEEVLTSENLSEA 239
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
25-258 |
1.59e-31 |
|
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: 116.10 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 25 VEVLKGIDMEAREGEVVSILGSSGSGKSTmlrCINMLE---TPDAGEITVAGETIRmkptgsgksriadRRQVERIRSEL 101
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLErfyDPTSGEILLDGVDIR-------------DLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 102 GMVFQSFNLWShKTVLENVMEAplhvqkRSRAEcLEEAEALLAKVGIADKRNHYP-----------AHLSGGQQQRAAIA 170
Cdd:cd03249 80 GLVSQEPVLFD-GTIAENIRYG------KPDAT-DEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 171 RALAMRPKVMLFDEPTSALDPE---LVGEVL-RVMRalaeeGRTMLVVTHEMGFARDvSSRVIFLHQGAIEEEGRPQDMF 246
Cdd:cd03249 152 RALLRNPKILLLDEATSALDAEsekLVQEALdRAMK-----GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELM 225
|
250
....*....|..
gi 752717930 247 tnAKSERFRKFI 258
Cdd:cd03249 226 --AQKGVYAKLV 235
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
28-248 |
2.52e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 116.63 E-value: 2.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGetirmkptgsgkSRIADRRQVERIRSELGMVFQS 107
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG------------IDTGDFSKLQGIRKLVGIVFQN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 108 FNL-WSHKTVLE-------NVMEAPLHVQKRsraecleeAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKV 179
Cdd:PRK13644 86 PETqFVGRTVEEdlafgpeNLCLPPIEIRKR--------VDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 180 MLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDvSSRVIFLHQGAIEEEGRPQDMFTN 248
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-259 |
3.81e-31 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 120.58 E-value: 3.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 8 PAPAAITVRGLRKSF-----------GPVEVLKGIDMEAREGEVVSILGSSGSGKST----MLRCINmletpDAGEITVA 72
Cdd:PRK15134 271 PASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 73 GETIRMkptgsgksriADRRQVERIRSELGMVFQSFN--LWSHKTVLENVMEA-PLHVQKRSRAECLEEAEALLAKVGI- 148
Cdd:PRK15134 346 GQPLHN----------LNRRQLLPVRHRIQVVFQDPNssLNPRLNVLQIIEEGlRVHQPTLSAAQREQQVIAVMEEVGLd 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 149 ADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGR-TMLVVTHEMGFARDVSSR 227
Cdd:PRK15134 416 PETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQ 495
|
250 260 270
....*....|....*....|....*....|..
gi 752717930 228 VIFLHQGAIEEEGRPQDMFTNAKSERFRKFIS 259
Cdd:PRK15134 496 VIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-236 |
7.72e-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: 112.91 E-value: 7.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 9 APAAITVRGLRKSfgpvEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTGsgksri 88
Cdd:cd03215 1 GEPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPR------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 89 adrrqvERIRSELGMV---------FQSFnlwshkTVLENVmeaplhvqkrsraecleeaeALlakvgiadkrnhyPAHL 159
Cdd:cd03215 71 ------DAIRAGIAYVpedrkreglVLDL------SVAENI--------------------AL-------------SSLL 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 160 SGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAI 236
Cdd:cd03215 106 SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
26-250 |
7.84e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 115.65 E-value: 7.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 26 EVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKptgsgksriADRRQVERIRSELGMVF 105
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHK---------TKDKYIRPVRKRIGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 106 QsfnlWSHKTVLENVMEAPLHVQKRSRAECLEEAEA----LLAKVGIA-DKRNHYPAHLSGGQQQRAAIARALAMRPKVM 180
Cdd:PRK13646 92 Q----FPESQLFEDTVEREIIFGPKNFKMNLDEVKNyahrLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDII 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 752717930 181 LFDEPTSALDPELVGEVLRVMRAL-AEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAK 250
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-236 |
8.08e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 119.35 E-value: 8.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 3 PSTNPPAPAAITVRGLRKSfgpvEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMK-PT 81
Cdd:COG1129 247 KRAAAPGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRsPR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 82 GSGKSRIA----DRRqverirsELGMVfqsfnlwSHKTVLENVMEAPLHVQKR----SRAECLEEAEALLAKVGIADKRN 153
Cdd:COG1129 323 DAIRAGIAyvpeDRK-------GEGLV-------LDLSIRENITLASLDRLSRggllDRRRERALAEEYIKRLRIKTPSP 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 154 HYPA-HLSGGQQQRAAIARALAMRPKVMLFDEPTSALDpelVG---EVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVI 229
Cdd:COG1129 389 EQPVgNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRIL 465
|
....*..
gi 752717930 230 FLHQGAI 236
Cdd:COG1129 466 VMREGRI 472
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-242 |
9.46e-31 |
|
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: 114.25 E-value: 9.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGP-VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksriadR 91
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIR-------------E 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 RQVERIRSELGMVFQSFNLWsHKTVLENVMEAPLHVQKrsraeclEEAEALLAKVGIADKRNHYP-----------AHLS 160
Cdd:cd03253 68 VTLDSLRRAIGVVPQDTVLF-NDTIGYNIRYGRPDATD-------EEVIEAAKAAQIHDKIMRFPdgydtivgergLKLS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 161 GGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAeEGRTMLVVTHEMGFARDvSSRVIFLHQGAIEEEG 240
Cdd:cd03253 140 GGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
..
gi 752717930 241 RP 242
Cdd:cd03253 218 TH 219
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
31-246 |
1.01e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 115.60 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 31 IDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgkSRIADRRQVERIRSELGMVFQ-SFN 109
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVV---------SSTSKQKEIKPVRKKVGVVFQfPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 110 LWSHKTVLENVMEAPLHVQKrSRAECLEEAEALLAKVGIADK-RNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSA 188
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNFGI-PKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 752717930 189 LDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMF 246
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-245 |
1.13e-30 |
|
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: 119.14 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSF-----GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITV--AGETIRM-KPTGSG 84
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvGDEWVDMtKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 85 KSRIadrrqveriRSELGMVFQSFNLWSHKTVLENVMEA-----PLHVQKRsraecleEAEALLAKVGIADKR-----NH 154
Cdd:TIGR03269 360 RGRA---------KRYIGILHQEYDLYPHRTVLDNLTEAiglelPDELARM-------KAVITLKMVGFDEEKaeeilDK 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 155 YPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLR-VMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQ 233
Cdd:TIGR03269 424 YPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRD 503
|
250
....*....|..
gi 752717930 234 GAIEEEGRPQDM 245
Cdd:TIGR03269 504 GKIVKIGDPEEI 515
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-245 |
1.74e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 116.08 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 1 MTPSTNPPAPAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkp 80
Cdd:PRK13536 30 KASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 81 tgSGKSRIAdrrqveriRSELGMVFQSFNLWSHKTVLENVMEAPLHVQKRSRaECLEEAEALLAKVGIADKRNHYPAHLS 160
Cdd:PRK13536 106 --PARARLA--------RARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTR-EIEAVIPSLLEFARLESKADARVSDLS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 161 GGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEG 240
Cdd:PRK13536 175 GGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
....*
gi 752717930 241 RPQDM 245
Cdd:PRK13536 255 RPHAL 259
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
29-250 |
1.91e-30 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 115.57 E-value: 1.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 29 KGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgKSRIADRRQVeriRSELGMVFQ-- 106
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLL-------GMKDDEWRAV---RSDIQMIFQdp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 107 --SFNlwSHKTVLENVMEaPLHV--QKRSRAECLEEAEALLAKVGI-ADKRNHYPAHLSGGQQQRAAIARALAMRPKVML 181
Cdd:PRK15079 108 laSLN--PRMTIGEIIAE-PLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 182 FDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAK 250
Cdd:PRK15079 185 CDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
13-260 |
2.48e-30 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 114.09 E-value: 2.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkPTGSgksriadRR 92
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI---PAMS-------RS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIRSELGMVFQSFNLWSHKTVLENVmEAPLHVQKRSRAECLEEAEAL-LAKVGIADKRNHYPAHLSGGQQQRAAIAR 171
Cdd:PRK11831 78 RLYTVRKRMSMLFQSGALFTDMNVFDNV-AYPLREHTQLPAPLLHSTVMMkLEAVGLRGAAKLMPSELSGGMARRAALAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 172 ALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNaK 250
Cdd:PRK11831 157 AIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAN-P 235
|
250
....*....|
gi 752717930 251 SERFRKFISG 260
Cdd:PRK11831 236 DPRVRQFLDG 245
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
28-248 |
2.81e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 114.33 E-value: 2.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkPTGsgksrIADRRQVERIRSELGMVFQ- 106
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI---PAN-----LKKIKEVKRLRKEIGLVFQf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 107 -SFNLWsHKTVLENVMEAPLHVQKrSRAECLEEAEALLAKVGIA-DKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDE 184
Cdd:PRK13645 99 pEYQLF-QETIEKDIAFGPVNLGE-NKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 185 PTSALDPELVGEVLRVMRAL-AEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTN 248
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-245 |
5.42e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 114.13 E-value: 5.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 7 PPAPAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgSGKS 86
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV------PSRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 87 RIAdrrqveriRSELGMVFQSFNLWSHKTVLENvmeapLHVQKR----SRAECLEEAEALLAKVGIADKRNHYPAHLSGG 162
Cdd:PRK13537 76 RHA--------RQRVGVVPQFDNLDPDFTVREN-----LLVFGRyfglSAAAARALVPPLLEFAKLENKADAKVGELSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 163 QQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRP 242
Cdd:PRK13537 143 MKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAP 222
|
...
gi 752717930 243 QDM 245
Cdd:PRK13537 223 HAL 225
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
28-251 |
6.45e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 112.92 E-value: 6.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgksriaDRRQVERIRSELGMVFQS 107
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI-------------TDDNFEKLRKHIGIVFQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 108 -FNLWSHKTV-------LENVMeAPLHVQKRSRAECLEEaeallakVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKV 179
Cdd:PRK13648 92 pDNQFVGSIVkydvafgLENHA-VPYDEMHRRVSEALKQ-------VDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752717930 180 MLFDEPTSALDPELVGEVLRVMRALAEEGR-TMLVVTHEMGFARDvSSRVIFLHQGAIEEEGRPQDMFTNAKS 251
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
12-218 |
1.19e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 111.72 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 12 AITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkpTGSGKSRiadr 91
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV----EGPGAER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 rqverirselGMVFQSFNLWSHKTVLENVmEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIAR 171
Cdd:PRK11248 73 ----------GVVFQNEGLLPWRNVQDNV-AFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIAR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 752717930 172 ALAMRPKVMLFDEPTSALDP---ELVGEVLrvMRALAEEGRTMLVVTHEM 218
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALDAftrEQMQTLL--LKLWQETGKQVLLITHDI 189
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
23-245 |
1.48e-29 |
|
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: 116.59 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 23 GPVeVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgksriaDRRQVERIRSELG 102
Cdd:TIGR03797 465 GPL-ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDL-------------AGLDVQAVRRQLG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 103 MVFQSFNLWShKTVLENVM-EAPLhvqkrsraeCLEEAEALLAKVGIADKRNHYP-----------AHLSGGQQQRAAIA 170
Cdd:TIGR03797 531 VVLQNGRLMS-GSIFENIAgGAPL---------TLDEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIA 600
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 752717930 171 RALAMRPKVMLFDEPTSALD---PELVGEVLRVMRAlaeegrTMLVVTHEMGFARDvSSRVIFLHQGAIEEEGRPQDM 245
Cdd:TIGR03797 601 RALVRKPRILLFDEATSALDnrtQAIVSESLERLKV------TRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDEL 671
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-260 |
2.86e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 111.03 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 22 FGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETpdageiTVAGETIRMKPTGSGKSRIADRRQVERIRSEL 101
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLND------LIPGFRVEGKVTFHGKNLYAPDVDPVEVRRRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 102 GMVFQSFNLWShKTVLENVMEAP-LHVQKRSRAECLEEA---EALLAKVgiADKRNHYPAHLSGGQQQRAAIARALAMRP 177
Cdd:PRK14243 94 GMVFQKPNPFP-KSIYDNIAYGArINGYKGDMDELVERSlrqAALWDEV--KDKLKQSGLSLSGGQQQRLCIARAIAVQP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 178 KVMLFDEPTSALDPELVGEVLRVMRALAEEgRTMLVVTHEMGFARDVSSRVIFLH---------QGAIEEEGRPQDMFTN 248
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNS 249
|
250
....*....|..
gi 752717930 249 AKSERFRKFISG 260
Cdd:PRK14243 250 PQQQATRDYVSG 261
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
26-234 |
3.79e-29 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 108.79 E-value: 3.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 26 EVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINML--ETPDAGEITVAGETIRMKptgsgksriadrrqveRIRSELGM 103
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKR----------------SFRKIIGY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 104 VFQSFNLWSHKTVLENVMEAplhvqkrsrAECleeaeallakvgiadkRNhypahLSGGQQQRAAIARALAMRPKVMLFD 183
Cdd:cd03213 87 VPQDDILHPTLTVRETLMFA---------AKL----------------RG-----LSGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 184 EPTSALDPELVGEVLRVMRALAEEGRTMLVVTH----EMGFARDvssRVIFLHQG 234
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRRLADTGRTIICSIHqpssEIFELFD---KLLLLSQG 188
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
27-246 |
5.23e-29 |
|
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: 109.62 E-value: 5.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgksriadrRQVERI--RSELGMV 104
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI---------------RDISRKslRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 105 FQSFNLWShKTVLENVmeaplhvqKRSRAECLEEAEALLAK-VGIADKRNHYP-----------AHLSGGQQQRAAIARA 172
Cdd:cd03254 83 LQDTFLFS-GTIMENI--------RLGRPNATDEEVIEAAKeAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 173 LAMRPKVMLFDEPTSALDPE---LVGEVLRVMRalaeEGRTMLVVTHEMGFARDvSSRVIFLHQGAIEEEGRPQDMF 246
Cdd:cd03254 154 MLRDPKILILDEATSNIDTEtekLIQEALEKLM----KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-230 |
1.45e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 107.32 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 21 SFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGetirmkptgsgKSRIADRRQveriRSE 100
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQ----RSE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 101 LGmvfQSFNLwshkTVLENVME---APLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRP 177
Cdd:NF040873 66 VP---DSLPL----TVRDLVAMgrwARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 752717930 178 KVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIF 230
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
25-250 |
2.14e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 109.03 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 25 VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKptgsgksriadrrQVERIRSELGMV 104
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAE-------------NVWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 105 FQSFNLWSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDE 184
Cdd:PRK13642 87 FQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 185 PTSALDPELVGEVLRVMRALAEEGR-TMLVVTHEMGFARDvSSRVIFLHQGAIEEEGRPQDMFTNAK 250
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
11-253 |
3.09e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 107.67 E-value: 3.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 11 AAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTGsgksriad 90
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 91 rrqvERIRSELGMVFQSFNLWSHKTVLENVMeAPLHVQKRSRAECLEE-AEALLAKVGIADKRNHYPAHLSGGQQQRAAI 169
Cdd:PRK10895 74 ----ARARRGIGYLPQEASIFRRLSVYDNLM-AVLQIRDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 170 ARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNA 249
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
....
gi 752717930 250 KSER 253
Cdd:PRK10895 229 HVKR 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
24-245 |
4.93e-28 |
|
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: 106.93 E-value: 4.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 24 PVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTGSgksriadrrqverIRSELGM 103
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS-------------LRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 104 VFQSFNLWShKTVLENVMEAPLHVqkrSRAECLEEAEALLAKVGIADKRNHYPA-------HLSGGQQQRAAIARALAMR 176
Cdd:cd03251 81 VSQDVFLFN-DTVAENIAYGRPGA---TREEVEEAARAANAHEFIMELPEGYDTvigergvKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 177 PKVMLFDEPTSALDPELVGEVLRVMRALAeEGRTMLVVTHEMGFARDvSSRVIFLHQGAIEEEGRPQDM 245
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-216 |
5.40e-28 |
|
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: 111.61 E-value: 5.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 2 TPSTNPPAPAaITVRGLRKSF-GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkp 80
Cdd:TIGR02857 312 APVTAAPASS-LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA--- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 81 tgsGKSRIADRRQVerirselGMVFQSFNLWShKTVLENVMEA-----PLHVQKRSRAECLEEAEALLAKvGIADKRNHY 155
Cdd:TIGR02857 388 ---DADADSWRDQI-------AWVPQHPFLFA-GTIAENIRLArpdasDAEIREALERAGLDEFVAALPQ-GLDTPIGEG 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 752717930 156 PAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAeEGRTMLVVTH 216
Cdd:TIGR02857 456 GAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTH 515
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
5-241 |
6.12e-28 |
|
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: 112.14 E-value: 6.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 5 TNPPAPAAITVRGLRKSFGP--VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptg 82
Cdd:TIGR01846 448 ALPELRGAITFENIRFRYAPdsPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLA----- 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 83 sgksrIAD----RRQVerirselGMVFQSFNLWShKTVLENV--------MEAPLHVQKRSRAE--CLEEAEALLAKVGi 148
Cdd:TIGR01846 523 -----IADpawlRRQM-------GVVLQENVLFS-RSIRDNIalcnpgapFEHVIHAAKLAGAHdfISELPQGYNTEVG- 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 149 adkrnHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAeEGRTMLVVTHEMGFARDvSSRV 228
Cdd:TIGR01846 589 -----EKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREIC-RGRTVIIIAHRLSTVRA-CDRI 661
|
250
....*....|...
gi 752717930 229 IFLHQGAIEEEGR 241
Cdd:TIGR01846 662 IVLEKGQIAESGR 674
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-244 |
8.21e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 106.70 E-value: 8.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 15 VRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGetirmkptgsgksriadrrqv 94
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--------------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 95 eRIRS--ELGMVFQSfNLwshkTVLENVmeaplhvqkRSRAECL----EEAEALLAKV----GIADKRN----HYpahlS 160
Cdd:COG1134 88 -RVSAllELGAGFHP-EL----TGRENI---------YLNGRLLglsrKEIDEKFDEIvefaELGDFIDqpvkTY----S 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 161 GGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEG 240
Cdd:COG1134 149 SGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDG 228
|
....
gi 752717930 241 RPQD 244
Cdd:COG1134 229 DPEE 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-216 |
2.66e-27 |
|
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: 109.76 E-value: 2.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 2 TPSTNPPAPAAITVRGLRKSF-GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKP 80
Cdd:TIGR02868 324 AAGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 81 TGSGKSRIadrrqverirselGMVFQSFNLWsHKTVLENVMEAplhvqkrsRAECL-EEAEALLAKVGIADKRNHYP--- 156
Cdd:TIGR02868 404 QDEVRRRV-------------SVCAQDAHLF-DTTVRENLRLA--------RPDATdEELWAALERVGLADWLRALPdgl 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 752717930 157 --------AHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRAlAEEGRTMLVVTH 216
Cdd:TIGR02868 462 dtvlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
11-246 |
4.01e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 106.75 E-value: 4.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 11 AAITVRGLRKSFG----PVEVLKGIDMEAREGEVVSILGSSGSGKS-TMLRCINMLETPDageiTVAGETIRMKptGSGK 85
Cdd:PRK11022 2 ALLNVDKLSVHFGdesaPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPG----RVMAEKLEFN--GQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 86 SRIADRRQVERIRSELGMVFQ----SFNlwSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIADKRNH---YPAH 158
Cdd:PRK11022 76 QRISEKERRNLVGAEVAMIFQdpmtSLN--PCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 159 LSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAE-EGRTMLVVTHEMGFARDVSSRVIFLHQGAIE 237
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
....*....
gi 752717930 238 EEGRPQDMF 246
Cdd:PRK11022 234 ETGKAHDIF 242
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
25-236 |
5.04e-27 |
|
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: 104.28 E-value: 5.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 25 VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCI-NMLETPDA--GEITVAGETIrmkptgsgksriaDRRQVeriRSEL 101
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGGTtsGQILFNGQPR-------------KPDQF---QKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 102 GMVFQSFNLWSHKTVLENVMEAP---LHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPK 178
Cdd:cd03234 84 AYVRQDDILLPGLTVRETLTYTAilrLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 752717930 179 VMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMG---FarDVSSRVIFLHQGAI 236
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEI 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-246 |
1.67e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 108.02 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 1 MTPSTNPPAPAAITVRGLRKSF----GPVEVLKGIDMEAREGEVVSILGSSGSGKS-TMLRCINMLETPdAGEITVAGET 75
Cdd:PRK10261 1 MPHSDELDARDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQA-GGLVQCDKML 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 76 IRMKPTGSGKSRIADRRQVERIR-SELGMVFQS--FNLWSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIADKR 152
Cdd:PRK10261 80 LRRRSRQVIELSEQSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 153 ---NHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRV 228
Cdd:PRK10261 160 tilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRV 239
|
250
....*....|....*...
gi 752717930 229 IFLHQGAIEEEGRPQDMF 246
Cdd:PRK10261 240 LVMYQGEAVETGSVEQIF 257
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-236 |
3.57e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.30 E-value: 3.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 15 VRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETirmkptgsgksRIadrrqv 94
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RI------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 95 erirselGMVFQSFNLWSHKTVLENVMEA--PLHVQKRSRAECLE-----------------------------EAEALL 143
Cdd:COG0488 64 -------GYLPQEPPLDDDLTVLDTVLDGdaELRALEAELEELEAklaepdedlerlaelqeefealggweaeaRAEEIL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 144 AKVGIADKRNHYP-AHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVgEVLRvmRALAEEGRTMLVVTHEMGFAR 222
Cdd:COG0488 137 SGLGFPEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESI-EWLE--EFLKNYPGTVLVVSHDRYFLD 213
|
250
....*....|....
gi 752717930 223 DVSSRVIFLHQGAI 236
Cdd:COG0488 214 RVATRILELDRGKL 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-235 |
4.48e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 106.02 E-value: 4.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETI-RMKPTGSGKSRIadr 91
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnKLDHKLAAQLGI--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 rqverirselGMVFQSFNLWSHKTVLENVMEAPLHVQKR------SRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQ 165
Cdd:PRK09700 83 ----------GIIYQELSVIDELTVLENLYIGRHLTKKVcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 166 RAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGA 235
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGS 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-236 |
7.06e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 105.52 E-value: 7.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 3 PSTNPPAPAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETI-RMKPT 81
Cdd:PRK15439 2 QTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCaRLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 82 GSGKsriadrrqverirseLG--MVFQSFNLWSHKTVLENVMeapLHVQKRSRAEclEEAEALLAKVGIADKRNHYPAHL 159
Cdd:PRK15439 82 KAHQ---------------LGiyLVPQEPLLFPNLSVKENIL---FGLPKRQASM--QKMKQLLAALGCQLDLDSSAGSL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 160 SGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAI 236
Cdd:PRK15439 142 EVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
15-260 |
1.17e-25 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 101.79 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 15 VRGLRKSF---------GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGEtirmkPTGSGK 85
Cdd:PRK15112 7 VRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH-----PLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 86 SRIadRRQveRIRselgMVFQ-SFNLWSHKTVLENVMEAPLHVQKRSRAECLEEA-EALLAKVGI-ADKRNHYPAHLSGG 162
Cdd:PRK15112 82 YSY--RSQ--RIR----MIFQdPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQiIETLRQVGLlPDHASYYPHMLAPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 163 QQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGR 241
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
250
....*....|....*....
gi 752717930 242 PQDMFTNAKSERFRKFISG 260
Cdd:PRK15112 234 TADVLASPLHELTKRLIAG 252
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
27-236 |
1.36e-25 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 98.83 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMkptgsgksriADRRQverIRSELGMVFQ 106
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ----------WDPNE---LGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 107 SFNLWShKTVLENVmeaplhvqkrsraecleeaeallakvgiadkrnhypahLSGGQQQRAAIARALAMRPKVMLFDEPT 186
Cdd:cd03246 84 DDELFS-GSIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 752717930 187 SALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVsSRVIFLHQGAI 236
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-246 |
1.48e-25 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 102.50 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 1 MTPSTNPPAPAAITVRGLRKSF----GPVEVLKGIDMEAREGEVVSILGSSGSGKS-TMLRCINMLETPD--AGEITVAG 73
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGriGGSATFNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 74 ETIRMKPTgsgksriadrRQVERIRSE-LGMVFQ----SFNlwSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGI 148
Cdd:PRK09473 81 REILNLPE----------KELNKLRAEqISMIFQdpmtSLN--PYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 149 --ADKR-NHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRT-MLVVTHEMGFARDV 224
Cdd:PRK09473 149 peARKRmKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGI 228
|
250 260
....*....|....*....|..
gi 752717930 225 SSRVIFLHQGAIEEEGRPQDMF 246
Cdd:PRK09473 229 CDKVLVMYAGRTMEYGNARDVF 250
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
24-236 |
1.61e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 99.97 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 24 PVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGetirmkptgsgksriADRRQVER--IRSEL 101
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG---------------TDIRQLDPadLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 102 GMVFQSFNLWShKTVLENV-MEAPLHvqkrSRAECLEEAEALlakvGIADKRNHYP-----------AHLSGGQQQRAAI 169
Cdd:cd03245 81 GYVPQDVTLFY-GTLRDNItLGAPLA----DDERILRAAELA----GVTDFVNKHPngldlqigergRGLSGGQRQAVAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 170 ARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAeEGRTMLVVTHEMGFArDVSSRVIFLHQGAI 236
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLL-DLVDRIIVMDSGRI 216
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-247 |
8.43e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.93 E-value: 8.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIR--------------- 77
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISmlssrqlarrlallp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 78 ---MKPTGsgksrIADRRQVERIRSELgmvfqsFNLWSHktvlenvmeapLHVQKRSRaecLEEAealLAKVGIADKRNH 154
Cdd:PRK11231 83 qhhLTPEG-----ITVRELVAYGRSPW------LSLWGR-----------LSAEDNAR---VNQA---MEQTRINHLADR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 155 YPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQG 234
Cdd:PRK11231 135 RLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANG 214
|
250
....*....|...
gi 752717930 235 AIEEEGRPQDMFT 247
Cdd:PRK11231 215 HVMAQGTPEEVMT 227
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
27-236 |
1.04e-24 |
|
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: 102.64 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGetirmkptgsgksriADRRQVER--IRSELGMV 104
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDG---------------VDIRQIDPadLRRNIGYV 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 105 FQSFNLWsHKTVLENVMEAPLHVqkrSRAECLEEAEAllakVGIADKRNHYP-----------AHLSGGQQQRAAIARAL 173
Cdd:TIGR03375 545 PQDPRLF-YGTLRDNIALGAPYA---DDEEILRAAEL----AGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARAL 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752717930 174 AMRPKVMLFDEPTSALDPELVGEVLRVMRALAeEGRTMLVVTHEMGFARDVsSRVIFLHQGAI 236
Cdd:TIGR03375 617 LRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLLDLV-DRIIVMDNGRI 677
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-248 |
1.74e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.11 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 25 VEVLKGIDMEAREGEVVSILGSSGSGKSTmlrCINMLET---PDAGEITVAGETIRmkptgsgksriadrrQVER--IRS 99
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNlyqPTGGQVLLDGVPLV---------------QYDHhyLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 100 ELGMVFQSFNLWShKTVLENVMEAplhVQKRSRAECLEEAEALLAKVGIADKRNHYP-------AHLSGGQQQRAAIARA 172
Cdd:TIGR00958 556 QVALVGQEPVLFS-GSVRENIAYG---LTDTPDEEIMAAAKAANAHDFIMEFPNGYDtevgekgSQLSGGQKQRIAIARA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 173 LAMRPKVMLFDEPTSALDPElvgevlrVMRALAE----EGRTMLVVTHEMGFARDvSSRVIFLHQGAIEEEGRPQDMFTN 248
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDAE-------CEQLLQEsrsrASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMED 703
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
13-240 |
3.25e-24 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 100.95 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGP--VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgKSRIAD 90
Cdd:TIGR02203 331 VEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA-------DYTLAS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 91 rrqverIRSELGMVFQSFNLWShKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYP-----AHLSGGQQQ 165
Cdd:TIGR02203 404 ------LRRQVALVSQDVVLFN-DTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPigengVLLSGGQRQ 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 166 RAAIARALAMRPKVMLFDEPTSALDPE---LVGEVL-RVMRalaeeGRTMLVVTHEMGFARDvSSRVIFLHQGAIEEEG 240
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNEserLVQAALeRLMQ-----GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERG 549
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
25-259 |
4.37e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 100.70 E-value: 4.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 25 VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTGsgksriadrrQVERIRSELGMV 104
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPG----------KLQALRRDIQFI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 105 FQS--FNLWSHKTVLENVMEaPLHVQKRSRAECLEEAEA-LLAKVGIADKRN-HYPAHLSGGQQQRAAIARALAMRPKVM 180
Cdd:PRK10261 407 FQDpyASLDPRQTVGDSIME-PLRVHGLLPGKAAAARVAwLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 181 LFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAKSERFRKFIS 259
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMA 565
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-253 |
4.91e-24 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 97.36 E-value: 4.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 15 VRG--LRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksRIADRR 92
Cdd:PRK10253 8 LRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ---------HYASKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIrselGMVFQSFNLWSHKTVLENVMEA-----PLHVqkRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRA 167
Cdd:PRK10253 79 VARRI----GLLAQNATTPGDITVQELVARGryphqPLFT--RWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 168 AIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRAL-AEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMF 246
Cdd:PRK10253 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
....*..
gi 752717930 247 TNAKSER 253
Cdd:PRK10253 233 TAELIER 239
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
12-242 |
5.69e-24 |
|
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: 100.86 E-value: 5.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 12 AITVRGLRKSFGPV--EVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMkptgsgksria 89
Cdd:TIGR01257 928 GVCVKNLVKIFEPSgrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----------- 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 90 drrQVERIRSELGMVFQSFNLWSHKTVLENVMEAPlHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAI 169
Cdd:TIGR01257 997 ---NLDAVRQSLGMCPQHNILFHHLTVAEHILFYA-QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSV 1072
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752717930 170 ARALAMRPKVMLFDEPTSALDP---ELVGEVLRVMRAlaeeGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRP 242
Cdd:TIGR01257 1073 AIAFVGDAKVVVLDEPTSGVDPysrRSIWDLLLKYRS----GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
28-257 |
6.04e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 100.42 E-value: 6.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMlrcINMLE---TPDAGEITVAGETIRmkptgsGKSRIADRRQverirseLGMV 104
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQrvfDPQSGRILIDGTDIR------TVTRASLRRN-------IAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 105 FQS---FNlwshKTVLENvmeapLHVQKR--SRAECLEEAEALLAKVGIADKRNHYPAH-------LSGGQQQRAAIARA 172
Cdd:PRK13657 415 FQDaglFN----RSIEDN-----IRVGRPdaTDEEMRAAAERAQAHDFIERKPDGYDTVvgergrqLSGGERQRLAIARA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 173 LAMRPKVMLFDEPTSALDPELvgEVlRVMRALAE--EGRTMLVVTHEMGFARDvSSRVIFLHQGAIEEEGRPQDMFtnAK 250
Cdd:PRK13657 486 LLKDPPILILDEATSALDVET--EA-KVKAALDElmKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELV--AR 559
|
....*..
gi 752717930 251 SERFRKF 257
Cdd:PRK13657 560 GGRFAAL 566
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-218 |
6.76e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 99.99 E-value: 6.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 9 APAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTgsgksri 88
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAST------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 89 adrrqVERIRSELGMVFQSFNLWSHKTVLENVMEAPLHvQKR---SRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQ 165
Cdd:PRK11288 74 -----TAALAAGVAIIYQELHLVPEMTVAENLYLGQLP-HKGgivNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 752717930 166 RAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEM 218
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRM 200
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-240 |
8.65e-24 |
|
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: 94.30 E-value: 8.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVE--VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGetirmKPTGSGKsriad 90
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG-----VPVSDLE----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 91 rrqvERIRSELGMVFQSFNLWShKTVLENVMEaplhvqkrsraecleeaeallakvgiadkrnhypaHLSGGQQQRAAIA 170
Cdd:cd03247 71 ----KALSSLISVLNQRPYLFD-TTLRNNLGR-----------------------------------RFSGGERQRLALA 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 752717930 171 RALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEgRTMLVVTHEM-GFARdvSSRVIFLHQGAIEEEG 240
Cdd:cd03247 111 RILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLtGIEH--MDKILFLENGKIIMQG 178
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
26-247 |
1.87e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.62 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 26 EVLKGIDMEAREGEVVSILGSSGSGKS-TMLRCINMLETPDA----GEITVAGETIRMkptgsgksriADRRQVERIR-S 99
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESLLH----------ASEQTLRGVRgN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 100 ELGMVFQ----SFNlwshktvlenvmeaPLHVQKRSRAECLE----------EAEAL--LAKVGI--ADKR-NHYPAHLS 160
Cdd:PRK15134 93 KIAMIFQepmvSLN--------------PLHTLEKQLYEVLSlhrgmrreaaRGEILncLDRVGIrqAAKRlTDYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 161 GGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEE 239
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQ 238
|
....*...
gi 752717930 240 GRPQDMFT 247
Cdd:PRK15134 239 NRAATLFS 246
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
27-241 |
3.34e-23 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 93.87 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCI--NMLETPDAGEITVAGETIrmkptgsgksriadrrqverirselgmv 104
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQF---------------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 105 fqsfnlWSHKTVLENVmeaplhvqkrSRAECLEEAEALLAKVGIAD----KRNhyPAHLSGGQQQRAAIARALAMRPKVM 180
Cdd:COG2401 97 ------GREASLIDAI----------GRKGDFKDAVELLNAVGLSDavlwLRR--FKELSTGQKFRFRLALLLAERPKLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752717930 181 LFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVS-SRVIFLHQG-AIEEEGR 241
Cdd:COG2401 159 VIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATHHYDVIDDLQpDLLIFVGYGgVPEEKRR 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-238 |
3.38e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 3.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVaGETIrmkptgsgksRIA--- 89
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGyfd 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 90 -DRRQVErirselgmvfqsfnlwSHKTVLENVMEA-----PLHVqkRSRAEC-LEEAEALLAKVGiadkrnhypaHLSGG 162
Cdd:COG0488 385 qHQEELD----------------PDKTVLDELRDGapggtEQEV--RGYLGRfLFSGDDAFKPVG----------VLSGG 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 163 QQQRAAIARALAMRPKVMLFDEPTSALDPELVgEVLrvMRALAE-EGrTMLVVTHEMGFARDVSSRVIFLHQGAIEE 238
Cdd:COG0488 437 EKARLALAKLLLSPPNVLLLDEPTNHLDIETL-EAL--EEALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-240 |
3.59e-23 |
|
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: 93.75 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 16 RGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGetirmkptgsgksriadrrqve 95
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 96 RIRS--ELGMVFQSfNLwshkTVLENV-MEAPLHVQKRSRAECLEEAEALLAKVGiadKRNHYP-AHLSGGQQQRAAIAR 171
Cdd:cd03220 84 RVSSllGLGGGFNP-EL----TGRENIyLNGRLLGLSRKEIDEKIDEIIEFSELG---DFIDLPvKTYSSGMKARLAFAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 172 ALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEG 240
Cdd:cd03220 156 ATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
15-216 |
7.57e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.59 E-value: 7.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 15 VRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCI--NMLETPDAGEITVAGETI-RMKPTgsgksriadr 91
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDIlELSPD---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 rqvERIRSELGMVFQS---------FNLWshKTVLENVMEAPLhvqkrSRAECLEEAEALLAKVGIAD---KR--NhypA 157
Cdd:COG0396 73 ---ERARAGIFLAFQYpveipgvsvSNFL--RTALNARRGEEL-----SAREFLKLLKEKMKELGLDEdflDRyvN---E 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 158 HLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTH 216
Cdd:COG0396 140 GFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH 198
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
26-250 |
1.64e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 93.15 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 26 EVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKptgsgksriadRRQVERIRSELGMVF 105
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYS-----------KRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 106 QSFNLWSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGiADKRNHYPAH-LSGGQQQRAAIARALAMRPKVMLFDE 184
Cdd:PRK13638 84 QDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752717930 185 PTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNAK 250
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTE 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
13-242 |
3.49e-22 |
|
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: 90.66 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCI--NMLETPDAGEITVAGETI-RMKPTgsgksria 89
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDItDLPPE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 90 drrqvERIRSELGMVFQSfnlwshktvlenvmeaPLHVQKRSRAECLEEAEallakVGiadkrnhypahLSGGQQQRAAI 169
Cdd:cd03217 73 -----ERARLGIFLAFQY----------------PPEIPGVKNADFLRYVN-----EG-----------FSGGEKKRNEI 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752717930 170 ARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTH-EMGFARDVSSRVIFLHQGAIEEEGRP 242
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDK 189
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-243 |
3.51e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.11 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 26 EVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPD---AGEITVAGETIrmkptgsgksriaDRRQVERIRselG 102
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI-------------DAKEMRAIS---A 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 103 MVFQSFNLWSHKTVLENVM-EAPLHVQKR-SRAECLEEAEALLAKVGIADKRN------HYPAHLSGGQQQRAAIARALA 174
Cdd:TIGR00955 103 YVQQDDLFIPTLTVREHLMfQAHLRMPRRvTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752717930 175 MRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEmgfardVSSR-------VIFLHQGAIEEEGRPQ 243
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQ------PSSElfelfdkIILMAEGRVAYLGSPD 252
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-236 |
5.83e-22 |
|
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: 90.85 E-value: 5.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSF---------------------GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITV 71
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 72 AGETirmkptgSGKSRIADRRQverirseLGMVF-QSFNLWSHKTVLE--NVMEAPLHVQKRSRAECLEEAEALLAKVGI 148
Cdd:cd03267 81 AGLV-------PWKRRKKFLRR-------IGVVFgQKTQLWWDLPVIDsfYLLAAIYDLPPARFKKRLDELSELLDLEEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 149 ADK--RNhypahLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRAL-AEEGRTMLVVTHEMGFARDVS 225
Cdd:cd03267 147 LDTpvRQ-----LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALA 221
|
250
....*....|.
gi 752717930 226 SRVIFLHQGAI 236
Cdd:cd03267 222 RRVLVIDKGRL 232
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
15-241 |
8.76e-22 |
|
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: 90.15 E-value: 8.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 15 VRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGetirmkptgsgksRIADRRQV 94
Cdd:TIGR03740 3 TKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDG-------------HPWTRKDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 95 ERIrselGMVFQSFNLWSHKTVLEN--VMEAPLHVQKrsraeclEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARA 172
Cdd:TIGR03740 70 HKI----GSLIESPPLYENLTARENlkVHTTLLGLPD-------SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 173 LAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGR 241
Cdd:TIGR03740 139 LLNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGK 207
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
26-241 |
1.52e-21 |
|
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: 93.35 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 26 EVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksriaDRRQvERIRSELGMVF 105
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIR------------DVTQ-ASLRAAIGIVP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 106 QS---FNlwshKTVLENVM----EAplhvqkrSRAECLEEAEAllakvgiadkrnhypAH-------------------- 158
Cdd:COG5265 439 QDtvlFN----DTIAYNIAygrpDA-------SEEEVEAAARA---------------AQihdfieslpdgydtrvgerg 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 159 --LSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAeEGRTMLVVTHEMGFARDvSSRVIFLHQGAI 236
Cdd:COG5265 493 lkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAHRLSTIVD-ADEILVLEAGRI 570
|
....*
gi 752717930 237 EEEGR 241
Cdd:COG5265 571 VERGT 575
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-216 |
3.43e-21 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 88.18 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEItvagetiRMKPTGSGKSRIADRR 92
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV-------RWNGTPLAEQRDEPHE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIRSELGMvfqsfnlwshK---TVLENvmeapLHVQKRSRAECLEEAEALLAKVGIADkRNHYPAH-LSGGQQQRAA 168
Cdd:TIGR01189 74 NILYLGHLPGL----------KpelSALEN-----LHFWAAIHGGAQRTIEDALAAVGLTG-FEDLPAAqLSAGQQRRLA 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 752717930 169 IARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTH 216
Cdd:TIGR01189 138 LARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-245 |
3.85e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.01 E-value: 3.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 7 PPAPAAITVRGLR-KSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPtgsgk 85
Cdd:COG3845 252 EPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS----- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 86 srIADRRQ--VERI---RSELGMVfQSFNLWSHkTVLENVMEAPLhvQKR---SRAECLEEAEALLAKVGIADKRNHYPA 157
Cdd:COG3845 327 --PRERRRlgVAYIpedRLGRGLV-PDMSVAEN-LILGRYRRPPF--SRGgflDRKAIRAFAEELIEEFDVRTPGPDTPA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 158 -HLSGGQQQRAAIARALAMRPKVMLFDEPTSALDpelVG---EVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQ 233
Cdd:COG3845 401 rSLSGGNQQKVILARELSRDPKLLIAAQPTRGLD---VGaieFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYE 477
|
250
....*....|..
gi 752717930 234 GAIEEEGRPQDM 245
Cdd:COG3845 478 GRIVGEVPAAEA 489
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-258 |
9.10e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.04 E-value: 9.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 4 STNPPAPAAITVRGLrkSFG----PVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGEtirmk 79
Cdd:PRK11160 330 STAAADQVSLTLNNV--SFTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQ----- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 80 ptgsgksRIADRRQvERIRSELGMVFQSFNLWSHkTVLENVMEAplhvQKRSRAECLEEAealLAKVGIA-----DK--- 151
Cdd:PRK11160 403 -------PIADYSE-AALRQAISVVSQRVHLFSA-TLRDNLLLA----APNASDEALIEV---LQQVGLEklledDKgln 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 152 -------RnhypaHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAeEGRTMLVVTHEMgFARDV 224
Cdd:PRK11160 467 awlgeggR-----QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRL-TGLEQ 539
|
250 260 270
....*....|....*....|....*....|....
gi 752717930 225 SSRVIFLHQGAIEEEGRPQDMFtnAKSERFRKFI 258
Cdd:PRK11160 540 FDRICVMDNGQIIEQGTHQELL--AQQGRYYQLK 571
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
22-249 |
1.27e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 87.63 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 22 FGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTgsgkSRIadrrqverIRSEL 101
Cdd:PRK11614 15 YGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQT----AKI--------MREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 102 GMVFQSFNLWSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKvgIADKRNHYPAHLSGGQQQRAAIARALAMRPKVML 181
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 752717930 182 FDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNA 249
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANE 228
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
9-247 |
1.47e-20 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 89.41 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 9 APAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINmLETPDAGE------ITVAGETIRMKPTG 82
Cdd:NF000106 10 ARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAH-V*GPDAGRrpwrf*TWCANRRALRRTIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 83 SGKSRIADRRQVERIRSELGMVFQSFNLwshktvlenvmeaplhvqkrSRAECLEEAEALLAKVGIADKRNHYPAHLSGG 162
Cdd:NF000106 89 *HRPVR*GRRESFSGRENLYMIGR*LDL--------------------SRKDARARADELLERFSLTEAAGRAAAKYSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 163 QQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRP 242
Cdd:NF000106 149 MRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV 228
|
....*
gi 752717930 243 QDMFT 247
Cdd:NF000106 229 DELKT 233
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
27-234 |
1.86e-20 |
|
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: 85.98 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCInmletpdageitvAGETIRMKPTGSGKSRIADRRQVERIRSElgmvfq 106
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-------------LGELEKLSGSVSVPGSIAYVSQEPWIQNG------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 107 sfnlwshkTVLEN-VMEAPLHVQKRS---RAECLEEAEALLAK-----V---GIAdkrnhypahLSGGQQQRAAIARALA 174
Cdd:cd03250 81 --------TIRENiLFGKPFDEERYEkviKACALEPDLEILPDgdlteIgekGIN---------LSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752717930 175 MRPKVMLFDEPTSALDPElVGEVL--RVMRALAEEGRTMLVVTHEMGFARDVsSRVIFLHQG 234
Cdd:cd03250 144 SDADIYLLDDPLSAVDAH-VGRHIfeNCILGLLLNNKTRILVTHQLQLLPHA-DQIVVLDNG 203
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
8-246 |
2.38e-20 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 89.81 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 8 PAPAA-ITVRGLrkSFGP----VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGetirmkptg 82
Cdd:COG4618 325 PRPKGrLSVENL--TVVPpgskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG--------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 83 sgksriADRRQVERirSELGMVF----QSFNLWShKTVLENV--MEAPlhvqkrsRAECLEEAeALLAKVG--IADKRNH 154
Cdd:COG4618 394 ------ADLSQWDR--EELGRHIgylpQDVELFD-GTIAENIarFGDA-------DPEKVVAA-AKLAGVHemILRLPDG 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 155 Y-------PAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPElvGE--VLRVMRALAEEGRTMLVVTHEMGFARDVs 225
Cdd:COG4618 457 YdtrigegGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDE--GEaaLAAAIRALKARGATVVVITHRPSLLAAV- 533
|
250 260
....*....|....*....|.
gi 752717930 226 SRVIFLHQGAIEEEGRPQDMF 246
Cdd:COG4618 534 DKLLVLRDGRVQAFGPRDEVL 554
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-234 |
2.42e-20 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 89.88 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDA--GEITVAGETIRMKPTgsgksRIAD 90
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNI-----RDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 91 RRQVERIRSELGMVfqsfnlwSHKTVLENVM---EAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYP-AHLSGGQQQR 166
Cdd:TIGR02633 77 RAGIVIIHQELTLV-------PELSVAENIFlgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 752717930 167 AAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQG 234
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
40-241 |
2.72e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 88.39 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 40 VVSILGSSGSGKSTMLRCINMLETPDAGEITVAGET-------IRMKPTgsgKSRIadrrqverirselGMVFQSFNLWS 112
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgICLPPE---KRRI-------------GYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 113 HKTVLENVmeapLHVQKRSRAECLEEAEALLakvGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPE 192
Cdd:PRK11144 90 HYKVRGNL----RYGMAKSMVAQFDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 752717930 193 LVGEVLRVMRALAEEGRT-MLVVTHEMGFARDVSSRVIFLHQGAIEEEGR 241
Cdd:PRK11144 163 RKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
25-236 |
3.58e-20 |
|
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: 85.99 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 25 VEVLKGIDMEAREGEVVSILGSSGSGKSTmlrCINMLET---PDAGEITVAGETIRMkptgsgksriadrRQVERIRSEL 101
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKST---VVALLENfyqPQGGQVLLDGKPISQ-------------YEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 102 GMVFQSFNLWShKTVLENVMEAplhVQKRSRAECLEEAEALLAKVGIADKRNHYP-------AHLSGGQQQRAAIARALA 174
Cdd:cd03248 91 SLVGQEPVLFA-RSLQDNIAYG---LQSCSFECVKEAAQKAHAHSFISELASGYDtevgekgSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752717930 175 MRPKVMLFDEPTSALDPElvgEVLRVMRALAE--EGRTMLVVTHEMGFARDvSSRVIFLHQGAI 236
Cdd:cd03248 167 RNPQVLILDEATSALDAE---SEQQVQQALYDwpERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
15-216 |
7.03e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 84.47 E-value: 7.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 15 VRGLRKSFgpvevlKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksriadrRQV 94
Cdd:PRK13538 10 ERDERILF------SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR--------------RQR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 95 ERIRSELgmvfqsfnLW-SHK-------TVLENV-MEAPLHvQKRSRAECLeeaeALLAKVGIAdKRNHYPAH-LSGGQQ 164
Cdd:PRK13538 70 DEYHQDL--------LYlGHQpgiktelTALENLrFYQRLH-GPGDDEALW----EALAQVGLA-GFEDVPVRqLSAGQQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 752717930 165 QRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTH 216
Cdd:PRK13538 136 RRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-216 |
7.27e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.45 E-value: 7.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 9 APAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLE---TPDaGEITVAGETIRMKptgsgk 85
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphgTYE-GEIIFEGEELQAS------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 86 sRIAD--RRQVERIRSELGMVfqsfnlwSHKTVLENVM--EAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSG 161
Cdd:PRK13549 75 -NIRDteRAGIAIIHQELALV-------KELSVLENIFlgNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 162 GQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTH 216
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISH 201
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
23-248 |
9.41e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 86.50 E-value: 9.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 23 GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCInMLETPDAGEITVAgetiRMKPTGSG--KSRIADRRQVerIRSE 100
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAI-CGITKDNWHVTAD----RFRWNGIDllKLSPRERRKI--IGRE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 101 LGMVFQ--SFNLWSHKTVLENVMEA-PLHVQKRS----RAECLEEAEALLAKVGIADKR---NHYPAHLSGGQQQRAAIA 170
Cdd:COG4170 91 IAMIFQepSSCLDPSAKIGDQLIEAiPSWTFKGKwwqrFKWRKKRAIELLHRVGIKDHKdimNSYPHELTEGECQKVMIA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 171 RALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAE-EGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTN 248
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
13-234 |
1.15e-19 |
|
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: 82.50 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVagetirmkptgsgksriadrr 92
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 qverirselgmvfqsfnlwsHKTVlenvmeaplhvqkrsraecleeaeallaKVGiadkrnhYPAHLSGGQQQRAAIARA 172
Cdd:cd03221 60 --------------------GSTV----------------------------KIG-------YFEQLSGGEKMRLALAKL 84
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752717930 173 LAMRPKVMLFDEPTSALDPELVgEVLRvmRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQG 234
Cdd:cd03221 85 LLENPNLLLLDEPTNHLDLESI-EALE--EALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
38-253 |
1.21e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 85.70 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 38 GEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkpTGSGKSRIADRRQVERIRselgmvfqsfnlWSHKTVL 117
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR---QALQKNLVAYVPQSEEVD------------WSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 118 ENV--MEAPLHVQ--KRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPEL 193
Cdd:PRK15056 98 EDVvmMGRYGHMGwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 194 VGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLhQGAIEEEGRPQDMFTNAKSER 253
Cdd:PRK15056 178 EARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTFTAENLEL 236
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
13-216 |
2.20e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.38 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgksriadrr 92
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 qverirsELGMVFQSFNLWSHK-------TVLENvmeapLHVQKRSRAECLEEAEALLAKVGIADKrNHYPA-HLSGGQQ 164
Cdd:PRK13539 67 -------DDPDVAEACHYLGHRnamkpalTVAEN-----LEFWAAFLGGEELDIAAALEAVGLAPL-AHLPFgYLSAGQK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 752717930 165 QRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTH 216
Cdd:PRK13539 134 RRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-236 |
2.29e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.52 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 12 AITVRGLRKSF-----GP----------------VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEIT 70
Cdd:COG4586 1 IIEVENLSKTYrvyekEPglkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 71 VAGETirmkPTgsgKSRIADRRQVerirselGMVF-QSFNLWSHKTVLENVMeapLH-----VQKRSRAECLEEAEALLa 144
Cdd:COG4586 81 VLGYV----PF---KRRKEFARRI-------GVVFgQRSQLWWDLPAIDSFR---LLkaiyrIPDAEYKKRLDELVELL- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 145 kvGIADK-----RNhypahLSGGQQQRAAIARALAMRPKVMLFDEPTSALDP---ELVGEVLRVMRalAEEGRTMLVVTH 216
Cdd:COG4586 143 --DLGELldtpvRQ-----LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVvskEAIREFLKEYN--RERGTTILLTSH 213
|
250 260
....*....|....*....|...
gi 752717930 217 EMGfarDV---SSRVIFLHQGAI 236
Cdd:COG4586 214 DMD---DIealCDRVIVIDHGRI 233
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-218 |
2.52e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.60 E-value: 2.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 17 GLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMK-PTGSGKSRIadrrqve 95
Cdd:PRK10762 9 GIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgPKSSQEAGI------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 96 rirselGMVFQSFNLWSHKTVLENVMeapLHVQKRSR------AECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAI 169
Cdd:PRK10762 82 ------GIIHQELNLIPQLTIAENIF---LGREFVNRfgridwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 752717930 170 ARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEM 218
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRL 201
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-216 |
5.30e-19 |
|
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: 82.16 E-value: 5.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 15 VRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEItvagetiRMKPTGSGKSRIADRRQV 94
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV-------LLNGGPLDFQRDSIARGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 95 ERIRSELGMvfqsfnlwshKTVL---ENV-MEAPLHvqkrSRAECLEEaealLAKVGIAdKRNHYPAH-LSGGQQQRAAI 169
Cdd:cd03231 76 LYLGHAPGI----------KTTLsvlENLrFWHADH----SDEQVEEA----LARVGLN-GFEDRPVAqLSAGQQRRVAL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 752717930 170 ARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTH 216
Cdd:cd03231 137 ARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
27-242 |
6.08e-19 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 82.54 E-value: 6.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgkSRIAdrrqVERIRSELGMVFQ 106
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI---------SKIG----LHDLRSRISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 107 SFNLWShKTVLENVmeAPLHvqKRSRAE---CLEEA---EALLAKVGIADKR-NHYPAHLSGGQQQRAAIARALAMRPKV 179
Cdd:cd03244 86 DPVLFS-GTIRSNL--DPFG--EYSDEElwqALERVglkEFVESLPGGLDTVvEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752717930 180 MLFDEPTSALDPE---LVGEVLRVMRAlaeeGRTMLVVTHEMGFARDvSSRVIFLHQGAIEEEGRP 242
Cdd:cd03244 161 LVLDEATASVDPEtdaLIQKTIREAFK----DCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-241 |
1.24e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 84.93 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCInmletpdAGEITVAGETirmkptgsGKSRIADRRQVERIRSELGMVFQ 106
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQGNNFT--------GTILANNRKPTKQILKRTGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 107 SFNLWSHKTVLENVMEAPLHVQKRS--RAECLEEAEALLAKVGIADKRN-----HYPAHLSGGQQQRAAIARALAMRPKV 179
Cdd:PLN03211 148 DDILYPHLTVRETLVFCSLLRLPKSltKQEKILVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752717930 180 MLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEmgfardVSSRVI-FLHQGAIEEEGR 241
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ------PSSRVYqMFDSVLVLSEGR 284
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
27-247 |
3.66e-18 |
|
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: 83.55 E-value: 3.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGetirmkptgsgksriADRRQVER--IRSELGMV 104
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG---------------ADLKQWDRetFGKHIGYL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 105 FQSFNLWShKTVLENV--MEAPLHVQKRSRAECLEEAEALLAK--------VGIADkrnhypAHLSGGQQQRAAIARALA 174
Cdd:TIGR01842 398 PQDVELFP-GTVAENIarFGENADPEKIIEAAKLAGVHELILRlpdgydtvIGPGG------ATLSGGQRQRIALARALY 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 175 MRPKVMLFDEPTSALDPElvGE--VLRVMRALAEEGRTMLVVTHEMGfARDVSSRVIFLHQGAIEEEGRPQDMFT 247
Cdd:TIGR01842 471 GDPKLVVLDEPNSNLDEE--GEqaLANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
10-259 |
3.81e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 80.90 E-value: 3.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 10 PAAITVRGLRKSfGPVEVLKGIDMEAREGEVVSILGSSGSGKStmLRCINMLETPDAGEITVAGE-TIRMKPTGSGKSR- 87
Cdd:PRK10418 2 PQQIELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRvLLDGKPVAPCALRg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 88 --IADRRQVERirselgmvfQSFNlwSHKTVLENVMEAPLHVQKRSRAECLEEAealLAKVGIADKR---NHYPAHLSGG 162
Cdd:PRK10418 79 rkIATIMQNPR---------SAFN--PLHTMHTHARETCLALGKPADDATLTAA---LEAVGLENAArvlKLYPFEMSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 163 QQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLR-VMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGR 241
Cdd:PRK10418 145 MLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDlLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGD 224
|
250
....*....|....*...
gi 752717930 242 PQDMFTNAKSERFRKFIS 259
Cdd:PRK10418 225 VETLFNAPKHAVTRSLVS 242
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-239 |
9.13e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.14 E-value: 9.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 1 MTPSTNPPAPAAI-TVRGL-RKSFGPVevlKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRM 78
Cdd:PRK09700 253 MKENVSNLAHETVfEVRNVtSRDRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 79 K-PTGSGKSRIAdrrQVERIRSELGMvFQSFNLWSHKTVLENVMEAPLH-----VQKRSRAECLEEAEALLAKVGIADKR 152
Cdd:PRK09700 330 RsPLDAVKKGMA---YITESRRDNGF-FPNFSIAQNMAISRSLKDGGYKgamglFHEVDEQRTAENQRELLALKCHSVNQ 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 153 NhyPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLH 232
Cdd:PRK09700 406 N--ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFC 483
|
....*..
gi 752717930 233 QGAIEEE 239
Cdd:PRK09700 484 EGRLTQI 490
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
38-245 |
2.04e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.45 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 38 GEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGEtirmkPTGSGKSRiADRRQVERIRSEL----GMvfqsfnlwsh 113
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQ-----PLESWSSK-AFARKVAYLPQQLpaaeGM---------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 114 kTVLENVM--EAPLH-VQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALD 190
Cdd:PRK10575 101 -TVRELVAigRYPWHgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 752717930 191 PELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDM 245
Cdd:PRK10575 180 IAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-218 |
2.94e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 80.54 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 16 RGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKptgSGKsriadrrqvE 95
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFK---SSK---------E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 96 RIRSELGMVFQSFNLWSHKTVLENVM--EAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARAL 173
Cdd:PRK10982 70 ALENGISMVHQELNLVLQRSVMDNMWlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAF 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 752717930 174 AMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEM 218
Cdd:PRK10982 150 SYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKM 194
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-229 |
3.02e-17 |
|
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: 78.60 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 36 REGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPtgsgKSRIADrrQVERIRSELGMVFQSFnlWSHKT 115
Cdd:cd03237 23 SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP----QYIKAD--YEGTVRDLLSSITKDF--YTHPY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 116 VLENVMEaPLHVQKRSRAECLEeaeallakvgiadkrnhypahLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVG 195
Cdd:cd03237 95 FKTEIAK-PLQIEQILDREVPE---------------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRL 152
|
170 180 190
....*....|....*....|....*....|....*
gi 752717930 196 EVLRVMRALAEEG-RTMLVVTHEMGFARDVSSRVI 229
Cdd:cd03237 153 MASKVIRRFAENNeKTAFVVEHDIIMIDYLADRLI 187
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
7-216 |
3.06e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 80.62 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 7 PPAPAAITVRGLRKSFGPVEVL-KGIDMEAREGEVVSILGSSGSGKSTMLRCInmletpdageitvAGetirMKPTGSGk 85
Cdd:COG4178 357 TSEDGALALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAI-------------AG----LWPYGSG- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 86 sRIAdRRQVERI-----RSELgmvfqsfnlwshktVLENVMEA---PLHVQKRSRAECleeaEALLAKVGIA------DK 151
Cdd:COG4178 419 -RIA-RPAGARVlflpqRPYL--------------PLGTLREAllyPATAEAFSDAEL----REALEAVGLGhlaerlDE 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 152 RNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRAlAEEGRTMLVVTH 216
Cdd:COG4178 479 EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
8-242 |
3.32e-17 |
|
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: 77.45 E-value: 3.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 8 PAPAAITVRGLRKSFGP--VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPtgsgk 85
Cdd:cd03369 2 PEHGEIEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 86 sriadrrqVERIRSELGMVFQSFNLWShKTVLENvmeapLHVQKRSRAEclEEAEALLAKVGiadkrnhyPAHLSGGQQQ 165
Cdd:cd03369 77 --------LEDLRSSLTIIPQDPTLFS-GTIRSN-----LDPFDEYSDE--EIYGALRVSEG--------GLNLSQGQRQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 166 RAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRalaEE--GRTMLVVTHEMGFARDVsSRVIFLHQGAIEEEGRP 242
Cdd:cd03369 133 LLCLARALLKRPRVLVLDEATASIDYATDALIQKTIR---EEftNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-236 |
4.05e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.34 E-value: 4.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 7 PPAPAAITVRGLRksfGPvEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMK-PTGSGK 85
Cdd:PRK11288 252 PLGEVRLRLDGLK---GP-GLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRsPRDAIR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 86 SRIA----DRRQverirseLGMVfqsfnlwSHKTVLENV-MEAPLHvqkRSRAECL--EEAEALLAKVGIADKRNHYPAH 158
Cdd:PRK11288 328 AGIMlcpeDRKA-------EGII-------PVHSVADNInISARRH---HLRAGCLinNRWEAENADRFIRSLNIKTPSR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 159 ------LSGGQQQRAAIARALAMRPKVMLFDEPTSALDpelVG---EVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVI 229
Cdd:PRK11288 391 eqlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGID---VGakhEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIV 467
|
....*..
gi 752717930 230 FLHQGAI 236
Cdd:PRK11288 468 VMREGRI 474
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-247 |
7.13e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.57 E-value: 7.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLeTPDAGEITVAGETIRMKPTgsgksriadrRQVERIRSEL------ 101
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSA----------AELARHRAYLsqqqsp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 102 --GM-VFQsfnlwshktVLEnvmeapLHVQKRSRAECLEEA-EALLAKVGIADKRNHYPAHLSGGQQQRAAIARAL---- 173
Cdd:COG4138 81 pfAMpVFQ---------YLA------LHQPAGASSEAVEQLlAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvw 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 174 -AMRP--KVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFT 247
Cdd:COG4138 146 pTINPegQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
27-224 |
1.58e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.91 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETI-RMKPtgsgksriadrrqvERIRSELGMVF 105
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIsTLKP--------------EIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 106 QSFNLWShKTVLENVMeapLHVQKRSRAECLEEAEALLAKVGIADKRNHYP-AHLSGGQQQRAAIARALAMRPKVMLFDE 184
Cdd:PRK10247 88 QTPTLFG-DTVYDNLI---FPWQIRNQQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 752717930 185 PTSALDP---ELVGEVlrVMRALAEEGRTMLVVTH---EMGFARDV 224
Cdd:PRK10247 164 ITSALDEsnkHNVNEI--IHRYVREQNIAVLWVTHdkdEINHADKV 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
36-234 |
1.62e-16 |
|
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: 78.71 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 36 REGEVVSILGSSGSGKSTMLRCI-NMLETPDAGEITVAGETIRMK-PTGSGKSRIA---DRRQVERIRSELGmvfqsfnl 110
Cdd:TIGR02633 284 RRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRnPAQAIRAGIAmvpEDRKRHGIVPILG-------- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 111 wshktVLENVMEAPLH-VQKRSRAECLEEAEALLAKVGIADKRNHYP----AHLSGGQQQRAAIARALAMRPKVMLFDEP 185
Cdd:TIGR02633 356 -----VGKNITLSVLKsFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 752717930 186 TSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQG 234
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
28-216 |
1.05e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.21 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgksriadRRQVERIRSELGMVFQS 107
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR-------------DYTLASLRNQVALVSQN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 108 FNLWShKTVLENVMEAplHVQKRSRAECLEEAEALLAkVGIADKRNH--------YPAHLSGGQQQRAAIARALAMRPKV 179
Cdd:PRK11176 426 VHLFN-DTIANNIAYA--RTEQYSREQIEEAARMAYA-MDFINKMDNgldtvigeNGVLLSGGQRQRIAIARALLRDSPI 501
|
170 180 190
....*....|....*....|....*....|....*....
gi 752717930 180 MLFDEPTSALDPElvgEVLRVMRALAE--EGRTMLVVTH 216
Cdd:PRK11176 502 LILDEATSALDTE---SERAIQAALDElqKNRTSLVIAH 537
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-245 |
1.25e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.00 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 3 PSTNPPAPAAITVRGLRKSFG--PVEVLKGidmEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAgETIRMKP 80
Cdd:PRK13409 331 PRDESERETLVEYPDLTKKLGdfSLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 81 tgsgkSRIADRrQVERIRSELGMVFQSF--NLWSHKTV----LENVMEAPLhvqkrsraecleeaeallakvgiadkrnh 154
Cdd:PRK13409 407 -----QYIKPD-YDGTVEDLLRSITDDLgsSYYKSEIIkplqLERLLDKNV----------------------------- 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 155 ypAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVI-FLH 232
Cdd:PRK13409 452 --KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLMvFEG 529
|
250
....*....|....
gi 752717930 233 QGAIEEEGR-PQDM 245
Cdd:PRK13409 530 EPGKHGHASgPMDM 543
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
23-247 |
1.46e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 74.84 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 23 GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLeTPDAGEITVAgetiRMKPTGSGKSRIADRRQVERIRSELG 102
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTAD----RMRFDDIDLLRLSPRERRKLVGHNVS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 103 MVFQSFN--LWSHKTVLENVMEA------------PLHVQKRSRAEcleeaeaLLAKVGIADKRN---HYPAHLSGGQQQ 165
Cdd:PRK15093 93 MIFQEPQscLDPSERVGRQLMQNipgwtykgrwwqRFGWRKRRAIE-------LLHRVGIKDHKDamrSFPYELTEGECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 166 RAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAE-EGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQD 244
Cdd:PRK15093 166 KVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKE 245
|
...
gi 752717930 245 MFT 247
Cdd:PRK15093 246 LVT 248
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
31-240 |
7.11e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 73.73 E-value: 7.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 31 IDMEAREGEVVSILGSSGSGKSTMLrciNMLE--TPDAGEITVAGETIRmkptgsgksriadRRQVERIRSELGMVFQSF 108
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLL---NALLgfLPYQGSLKINGIELR-------------ELDPESWRKHLSWVGQNP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 109 NLWsHKTVLENVMEAPLHVQKrsraeclEEAEALLAKVGIADKRNHYP-----------AHLSGGQQQRAAIARALAMRP 177
Cdd:PRK11174 433 QLP-HGTLRDNVLLGNPDASD-------EQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPC 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 178 KVMLFDEPTSALDpeLVGEVlRVMRAL--AEEGRTMLVVTHEMGFARDVsSRVIFLHQGAIEEEG 240
Cdd:PRK11174 505 QLLLLDEPTASLD--AHSEQ-LVMQALnaASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQG 565
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
26-240 |
8.08e-15 |
|
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: 73.62 E-value: 8.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 26 EVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgkSRIaDRRQverIRSELGMVF 105
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL---------KDI-DRHT---LRQFINYLP 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 106 QSFNLWShKTVLENvmeapLHVQKRSRAEcLEEAEALLAKVGIADKRNHYP-----------AHLSGGQQQRAAIARALA 174
Cdd:TIGR01193 555 QEPYIFS-GSILEN-----LLLGAKENVS-QDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALL 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752717930 175 MRPKVMLFDEPTSALDpeLVGEVLRVMRALAEEGRTMLVVTHEMGFARDvSSRVIFLHQGAIEEEG 240
Cdd:TIGR01193 628 TDSKVLILDESTSNLD--TITEKKIVNNLLNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQG 690
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-235 |
1.02e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.29 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 16 RGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLrciNMLE------TPDaGEITVAGETIRMKptgsgksria 89
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLM---KVLSgvyphgSYE-GEILFDGEVCRFK---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 90 DRRQVER-----IRSELGMVfqsfnlwSHKTVLENVMEAplHVQKR----SRAECLEEAEALLAKVGIADKRNHYPAHLS 160
Cdd:NF040905 71 DIRDSEAlgiviIHQELALI-------PYLSIAENIFLG--NERAKrgviDWNETNRRARELLAKVGLDESPDTLVTDIG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 161 GGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGA 235
Cdd:NF040905 142 VGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-245 |
1.12e-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: 73.28 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 2 TPSTNPPAPAAITVRGLRKSFG--PVEVLKGidmEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITvAGETIRMK 79
Cdd:COG1245 331 APRREKEEETLVEYPDLTKSYGgfSLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKISYK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 80 PtgsgkSRI---ADRRQVERIRSELGMVFQSfNLWSHKTV----LENVMEAPLhvqkrsraecleeaeallakvgiadkr 152
Cdd:COG1245 407 P-----QYIspdYDGTVEEFLRSANTDDFGS-SYYKTEIIkplgLEKLLDKNV--------------------------- 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 153 nhypAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEE-GRTMLVVTHEMGFARDVSSRVI-F 230
Cdd:COG1245 454 ----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLMvF 529
|
250
....*....|....*.
gi 752717930 231 LHQGAIEEEG-RPQDM 245
Cdd:COG1245 530 EGEPGVHGHAsGPMDM 545
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-234 |
1.32e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.05 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 14 TVRGLRKSFGP-VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVA-GETIrmkptgsgksriadr 91
Cdd:TIGR03719 6 TMNRVSKVVPPkKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKV--------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 rqverirselGMVFQSFNLWSHKTVLENVMEA---PLHVQKR------SRAECLEEAEALLAKVG-IADKRNHYPAH--- 158
Cdd:TIGR03719 71 ----------GYLPQEPQLDPTKTVRENVEEGvaeIKDALDRfneisaKYAEPDADFDKLAAEQAeLQEIIDAADAWdld 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 159 ---------------------LSGGQQQRAAIARALAMRPKVMLFDEPTSALDPElvgEVLRVMRALAEEGRTMLVVTHE 217
Cdd:TIGR03719 141 sqleiamdalrcppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQEYPGTVVAVTHD 217
|
250
....*....|....*..
gi 752717930 218 MGFARDVSSRVIFLHQG 234
Cdd:TIGR03719 218 RYFLDNVAGWILELDRG 234
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
34-247 |
1.90e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.73 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 34 EAREGEVVSILGSSGSGKSTMLRCINMLeTPDAGEITVAGETIRMKPTgsgkSRIADRRQ--VERIRSELGM-VFQSFNL 110
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSA----AELARHRAylSQQQTPPFAMpVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 111 wshktvlenvmeaplHVQKRSRAECLEEA-EALLAKVGIADKRNHYPAHLSGGQQQR---AA----IARALAMRPKVMLF 182
Cdd:PRK03695 93 ---------------HQPDKTRTEAVASAlNEVAEALGLDDKLGRSVNQLSGGEWQRvrlAAvvlqVWPDINPAGQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 183 DEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFT 247
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-220 |
2.53e-14 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 70.05 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 21 SFGP-VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCInmletpdAGEItvagETIRMKPTGSGKSRIADRRQVERIRS 99
Cdd:cd03290 9 SWGSgLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAI-------LGEM----QTLEGKVHWSNKNESEPSFEATRSRN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 100 ELGMVFQSFNLWS-HKTVLENV-MEAPLHVQkRSRA---ECLEEAEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALA 174
Cdd:cd03290 78 RYSVAYAAQKPWLlNATVEENItFGSPFNKQ-RYKAvtdACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 752717930 175 MRPKVMLFDEPTSALDPELVGEVLR--VMRALAEEGRTMLVVTHEMGF 220
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY 204
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
27-253 |
4.69e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.86 E-value: 4.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCI-NMLETPDA-------GEITVAGETIRMKPTgsgkSRIADRRQVERIR 98
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGAprgarvtGDVTLNGEPLAAIDA----PRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 99 SELGMVFqsfnlwshkTVLENVMEAPLHVQKRSRAECLEE---AEALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAM 175
Cdd:PRK13547 92 AQPAFAF---------SAREIVLLGRYPHARRAGALTHRDgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 176 ---------RPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRT-MLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDM 245
Cdd:PRK13547 163 lwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
....*...
gi 752717930 246 FTNAKSER 253
Cdd:PRK13547 243 LTPAHIAR 250
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-243 |
7.27e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.92 E-value: 7.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 6 NPPAPAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPtgsgk 85
Cdd:NF033858 260 DDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD----- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 86 srIADRRQVerirselGMVFQSFNLWSHKTVLEN-VMEAPL-HVQKRSRAECLEEaeaLLAKVGIADKRNHYPAHLSGGQ 163
Cdd:NF033858 335 --IATRRRV-------GYMSQAFSLYGELTVRQNlELHARLfHLPAAEIAARVAE---MLERFDLADVADALPDSLPLGI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 164 QQRAAIARALAMRPKVMLFDEPTSALDP-------ELVGEVLRvmralaEEGRTMLVVTHEMGFA-R-DvssRVIFLHQG 234
Cdd:NF033858 403 RQRLSLAVAVIHKPELLILDEPTSGVDPvardmfwRLLIELSR------EDGVTIFISTHFMNEAeRcD---RISLMHAG 473
|
....*....
gi 752717930 235 AIEEEGRPQ 243
Cdd:NF033858 474 RVLASDTPA 482
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-243 |
1.09e-13 |
|
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: 70.21 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 2 TPSTNPPAPAAITVRGLRKSFGPVE-----VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETI 76
Cdd:COG4615 317 AAPPAPADFQTLELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 77 rmkptgsgksriaDRRQVERIRSELGMVFQSFNLWSHktvLENVMEAPLHvqkrsraeclEEAEALLAKVGIADK---RN 153
Cdd:COG4615 397 -------------TADNREAYRQLFSAVFSDFHLFDR---LLGLDGEADP----------ARARELLERLELDHKvsvED 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 154 HY--PAHLSGGQQQRAAIARALAM-RPkVMLFDEPTSALDP--------ELVGEvlrvMRAlaeEGRTMLVVTH-EMGFa 221
Cdd:COG4615 451 GRfsTTDLSQGQRKRLALLVALLEdRP-ILVFDEWAADQDPefrrvfytELLPE----LKA---RGKTVIAISHdDRYF- 521
|
250 260
....*....|....*....|..
gi 752717930 222 rDVSSRVIFLHQGAIEEEGRPQ 243
Cdd:COG4615 522 -DLADRVLKMDYGKLVELTGPA 542
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
36-218 |
1.22e-13 |
|
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: 70.20 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 36 REGEVVSILGSSGSGKSTmlrCINMLetpdAGEItvagetirmKPTGSGKSRIADRRQV-ERIR-SELGMVFQsfNLW-- 111
Cdd:COG1245 97 KKGKVTGILGPNGIGKST---ALKIL----SGEL---------KPNLGDYDEEPSWDEVlKRFRgTELQDYFK--KLAng 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 112 ----SHKTvlENVMEAPLHVQKRSRaECLEEA------EALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVML 181
Cdd:COG1245 159 eikvAHKP--QYVDLIPKVFKGTVR-ELLEKVdergklDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 752717930 182 FDEPTSALDpelVGE---VLRVMRALAEEGRTMLVVTHEM 218
Cdd:COG1245 236 FDEPSSYLD---IYQrlnVARLIRELAEEGKYVLVVEHDL 272
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-251 |
1.45e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.15 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgKSRIADRRQVerirseLGMVFQ 106
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS-------KFGLMDLRKV------LGIIPQ 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 107 SFNLWShKTVLENVMEAPLHvqkrSRAECLEEAEALLAKVGIadKRNHYP---------AHLSGGQQQRAAIARALAMRP 177
Cdd:PLN03130 1321 APVLFS-GTVRFNLDPFNEH----NDADLWESLERAHLKDVI--RRNSLGldaevseagENFSVGQRQLLSLARALLRRS 1393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752717930 178 KVMLFDEPTSALDpelVGEVLRVMRALAEEGR--TMLVVTHEMGFARDvSSRVIFLHQGAIEEEGRPQDMFTNAKS 251
Cdd:PLN03130 1394 KILVLDEATAAVD---VRTDALIQKTIREEFKscTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNEGS 1465
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-250 |
1.94e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.77 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMLRCinMLetpdaGEItvagetirmkPTGSGKSRIadrrqverIRSELGMVFQS 107
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISA--ML-----GEL----------PPRSDASVV--------IRGTVAYVPQV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 108 ---FNlwshKTVLENVM-EAPLHVQKRSRA---ECLEEAEALLAKvGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVM 180
Cdd:PLN03130 688 swiFN----ATVRDNILfGSPFDPERYERAidvTALQHDLDLLPG-GDLTEIGERGVNISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752717930 181 LFDEPTSALDPELVGEVLRvmRALAEE--GRTMLVVTHEMGFARDVsSRVIFLHQGAIEEEGRPQDMFTNAK 250
Cdd:PLN03130 763 IFDDPLSALDAHVGRQVFD--KCIKDElrGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNNGP 831
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-217 |
2.31e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 69.75 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINmlETPDAGEITVAGETIRMKPTGSGKSRIADRRQVERIRSELGMVFQ 106
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 107 SFNLWSHktvlenvMEAPLHVQKRSRAECLEE----------AEALLAKVGIAdkrnhypahLSGGQQQRAAIARALAMR 176
Cdd:TIGR00956 856 SLRFSAY-------LRQPKSVSKSEKMEYVEEvikllemesyADAVVGVPGEG---------LNVEQRKRLTIGVELVAK 919
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 752717930 177 PKVMLF-DEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHE 217
Cdd:TIGR00956 920 PKLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-206 |
2.54e-13 |
|
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: 69.19 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 7 PPAP----AAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVaGETIRmkptg 82
Cdd:TIGR03719 313 PPGPrlgdKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 83 sgksriadrrqverirseLGMVFQSF-NLWSHKTVLENVMEAP--LHVQKR---SRAECLE---EAEALLAKVGIadkrn 153
Cdd:TIGR03719 387 ------------------LAYVDQSRdALDPNKTVWEEISGGLdiIKLGKReipSRAYVGRfnfKGSDQQKKVGQ----- 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 752717930 154 hypahLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPElvgevlrVMRALAE 206
Cdd:TIGR03719 444 -----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE-------TLRALEE 484
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-249 |
3.80e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.54 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 26 EVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTgsgksriadrrqveRIRSELGMVF 105
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST--------------AQRLARGLVY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 106 -----QSFNL-------WSHKTVLENVMeaPLHVQKRSRAECLEEAEALLakvGIadKRNH--YPAH-LSGGQQQRAAIA 170
Cdd:PRK15439 343 lpedrQSSGLyldaplaWNVCALTHNRR--GFWIKPARENAVLERYRRAL---NI--KFNHaeQAARtLSGGNQQKVLIA 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 171 RALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTNA 249
Cdd:PRK15439 416 KCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDT 494
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-255 |
4.36e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.85 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 18 LRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsGKSRIADRRQVeri 97
Cdd:PLN03232 1242 LRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV-------AKFGLTDLRRV--- 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 98 rseLGMVFQSFNLWShKTVLENVMEAPLHvQKRSRAECLEEAEallakvgIADKRNHYPAHL-----------SGGQQQR 166
Cdd:PLN03232 1312 ---LSIIPQSPVLFS-GTVRFNIDPFSEH-NDADLWEALERAH-------IKDVIDRNPFGLdaevseggenfSVGQRQL 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 167 AAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRalaEEGR--TMLVVTHEMGFARDVsSRVIFLHQGAIEEEGRPQD 244
Cdd:PLN03232 1380 LSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR---EEFKscTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQE 1455
|
250
....*....|.
gi 752717930 245 MFTNAKSERFR 255
Cdd:PLN03232 1456 LLSRDTSAFFR 1466
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-245 |
5.48e-13 |
|
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: 68.43 E-value: 5.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTGSGKSRIADRRQVERIRS-ELGMVF 105
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSgSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 106 QSFNLWSHKTVLENVMEAPLHVQKRSRA-----ECLEEAEallakvgiadkrnhypaHLSGGQQQRAAIARALAMRPKVM 180
Cdd:TIGR00957 1381 DPFSQYSDEEVWWALELAHLKTFVSALPdkldhECAEGGE-----------------NLSVGQRQLVCLARALLRKTKIL 1443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 181 LFDEPTSALDPELVGEVLRVMRALAEEGrTMLVVTHEMGFARDVsSRVIFLHQGAIEEEGRPQDM 245
Cdd:TIGR00957 1444 VLDEATAAVDLETDNLIQSTIRTQFEDC-TVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
157-236 |
5.60e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 157 AHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDpelVG---EVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQ 233
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHE 480
|
...
gi 752717930 234 GAI 236
Cdd:PRK13549 481 GKL 483
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-235 |
6.10e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.03 E-value: 6.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 3 PSTNPPAPAAitvRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETirmkptg 82
Cdd:PRK13543 5 LHTAPPLLAA---HALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 83 sgkSRIADRRQVERIRSELGMVFQSFnlwshkTVLENV-MEAPLHVQKRSRAecleeAEALLAKVGIADKRNHYPAHLSG 161
Cdd:PRK13543 75 ---ATRGDRSRFMAYLGHLPGLKADL------STLENLhFLCGLHGRRAKQM-----PGSALAIVGLAGYEDTLVRQLSA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752717930 162 GQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGA 235
Cdd:PRK13543 141 GQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTLEAAA 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-258 |
9.27e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.69 E-value: 9.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 3 PSTNPPAPAAITVRGL----RKSFGPVevLKGIDMEAREGEVVSILGSSGSGKSTMLRCinMLetpdaGEITVAgETIRM 78
Cdd:PLN03232 606 PPLQPGAPAISIKNGYfswdSKTSKPT--LSDINLEIPVGSLVAIVGGTGEGKTSLISA--ML-----GELSHA-ETSSV 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 79 KPTGSgksrIADRRQVERIrselgmvfqsFNlwshKTVLENVM-EAPLHVQKRSRAEcleEAEALLAKVGIADKRN---- 153
Cdd:PLN03232 676 VIRGS----VAYVPQVSWI----------FN----ATVRENILfGSDFESERYWRAI---DVTALQHDLDLLPGRDltei 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 154 -HYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVsSRVIFLH 232
Cdd:PLN03232 735 gERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVS 813
|
250 260
....*....|....*....|....*.
gi 752717930 233 QGAIEEEGRPQDMFTNakSERFRKFI 258
Cdd:PLN03232 814 EGMIKEEGTFAELSKS--GSLFKKLM 837
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
159-239 |
2.05e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 159 LSGGQQQRAAIARALAMRPKVMLFDEPTSALDpelVG---EVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGA 235
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
....
gi 752717930 236 IEEE 239
Cdd:PRK10762 473 ISGE 476
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-218 |
4.28e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 64.31 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 36 REGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGE--TIRMKPTGS-----------GKSRIADRRQ-VERIRsel 101
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDwdEILDEFRGSelqnyftklleGDVKVIVKPQyVDLIP--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 102 gmvfqsfnlwshKTVLENVMEAplhVQKRSRAECLEEaeaLLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVML 181
Cdd:cd03236 101 ------------KAVKGKVGEL---LKKKDERGKLDE---LVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYF 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 752717930 182 FDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEM 218
Cdd:cd03236 163 FDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
155-216 |
4.87e-12 |
|
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: 62.56 E-value: 4.87e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752717930 155 YPAH--LSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGevlRVMRALAEEGRTMLVVTH 216
Cdd:cd03223 86 YPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED---RLYQLLKELGITVISVGH 146
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
25-222 |
5.30e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.44 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 25 VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITvagetirmkptgsgksrIADRRQVERI-----RS 99
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDII-----------------INDSHNLKDInlkwwRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 100 ELGMVFQ-------------SFNLWSHKTV----------------------------------LENVMEAPLHVQKRSR 132
Cdd:PTZ00265 461 KIGVVSQdpllfsnsiknniKYSLYSLKDLealsnyynedgndsqenknkrnscrakcagdlndMSNTTDSNELIEMRKN 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 133 AECLEEAEAL--LAKVGIADKRNHYP-----------AHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLR 199
Cdd:PTZ00265 541 YQTIKDSEVVdvSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
250 260
....*....|....*....|....
gi 752717930 200 VMRAL-AEEGRTMLVVTHEMGFAR 222
Cdd:PTZ00265 621 TINNLkGNENRITIIIAHRLSTIR 644
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
27-243 |
8.28e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 64.73 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgkSRIadrrQVERIRSELGMVFQ 106
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL---------TKL----QLDSWRSRLAVVSQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 107 SFNLWShKTVLENV-MEAPLHVQkrsraECLEEAeALLAKV---------GIADKRNHYPAHLSGGQQQRAAIARALAMR 176
Cdd:PRK10789 397 TPFLFS-DTVANNIaLGRPDATQ-----QEIEHV-ARLASVhddilrlpqGYDTEVGERGVMLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752717930 177 PKVMLFDEPTSALDPELVGEVLRVMRALAeEGRTMLVVTHEMGfARDVSSRVIFLHQGAIEEEGRPQ 243
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHD 534
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-218 |
8.37e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 8.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 36 REGEVVSILGSSGSGKSTMLRCInmletpdageitvAGEtirMKPTGSGKSRIADRRQV-ERIR-SELGMVFQSFNLWSH 113
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKIL-------------SGE---LIPNLGDYEEEPSWDEVlKRFRgTELQNYFKKLYNGEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 114 KTVLEN--VMEAPLHVQKRSRaECLEEA------EALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEP 185
Cdd:PRK13409 161 KVVHKPqyVDLIPKVFKGKVR-ELLKKVdergklDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....*
gi 752717930 186 TSALDpelVGEVLRVMRALAE--EGRTMLVVTHEM 218
Cdd:PRK13409 240 TSYLD---IRQRLNVARLIRElaEGKYVLVVEHDL 271
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-216 |
1.02e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.37 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 14 TVRGLRKSFGP-VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVA-GETIrmkptgsgksriadr 91
Cdd:PRK11819 8 TMNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKV--------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 rqverirselGMVFQSFNLWSHKTVLENVMEAPLHV-QKRSR--------AECLEEAEALLAKVG----IADKRNHY--- 155
Cdd:PRK11819 73 ----------GYLPQEPQLDPEKTVRENVEEGVAEVkAALDRfneiyaayAEPDADFDALAAEQGelqeIIDAADAWdld 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 156 ------------P------AHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPElvgEVLRVMRALAEEGRTMLVVTH 216
Cdd:PRK11819 143 sqleiamdalrcPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLEQFLHDYPGTVVAVTH 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
36-245 |
1.14e-11 |
|
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: 64.65 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 36 REGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgkSRIADrrqverirselgmVFQSFNLWSHKT 115
Cdd:TIGR01257 1963 RPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL--------TNISD-------------VHQNMGYCPQFD 2021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 116 VLENVMEAP--LHVQKRSRAECLEEAEAL----LAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSAL 189
Cdd:TIGR01257 2022 AIDDLLTGRehLYLYARLRGVPAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 752717930 190 DPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDM 245
Cdd:TIGR01257 2102 DPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-208 |
1.76e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 7 PPAP----AAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVaGETIRmkptg 82
Cdd:PRK11819 315 PPGPrlgdKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK----- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 83 sgksriadrrqverirseLGMVFQSF-NLWSHKTVLENVMEAP--LHVQKR---SRAECleeaeallA-----------K 145
Cdd:PRK11819 389 ------------------LAYVDQSRdALDPNKTVWEEISGGLdiIKVGNReipSRAYV--------GrfnfkggdqqkK 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752717930 146 VGIadkrnhypahLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPElvgevlrVMRALaEEG 208
Cdd:PRK11819 443 VGV----------LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVE-------TLRAL-EEA 487
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
26-217 |
2.93e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 60.72 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 26 EVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETpdAGEITvagetirmkptgsGKSRIADRRQVERIRSELGMVF 105
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKT--AGVIT-------------GEILINGRPLDKNFQRSTGYVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 106 QsfnlwshktvlenvmeAPLHVQKRSRAECLEEAEALLAkvgiadkrnhypahLSGGQQQRAAIARALAMRPKVMLFDEP 185
Cdd:cd03232 86 Q----------------QDVHSPNLTVREALRFSALLRG--------------LSVEQRKRLTIGVELAAKPSILFLDEP 135
|
170 180 190
....*....|....*....|....*....|..
gi 752717930 186 TSALDPELVGEVLRVMRALAEEGRTMLVVTHE 217
Cdd:cd03232 136 TSGLDSQAAYNIVRFLKKLADSGQAILCTIHQ 167
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-215 |
6.50e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.97 E-value: 6.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 10 PAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINmletpdageitvagetirmkptgsgkSRIA 89
Cdd:cd03233 5 SWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA--------------------------NRTE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 90 DRRQVERIRSELGMVFQSFNLWSHKTVLENVME----APLHVQK--RSRAECleeaeallakvgiadKRNHYPAHLSGGQ 163
Cdd:cd03233 59 GNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEdvhfPTLTVREtlDFALRC---------------KGNEFVRGISGGE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 752717930 164 QQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVT 215
Cdd:cd03233 124 RKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS 175
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-234 |
7.99e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 7.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 11 AAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETI--RMK---P---TG 82
Cdd:PRK11147 2 SLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIvaRLQqdpPrnvEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 83 SGKSRIADRRQverirsELGMVFQSFNLWSHKtVLENVMEAPL----HVQkrsraECLEEAEA---------LLAKVGI- 148
Cdd:PRK11147 82 TVYDFVAEGIE------EQAEYLKRYHDISHL-VETDPSEKNLnelaKLQ-----EQLDHHNLwqlenrineVLAQLGLd 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 149 ADKRnhyPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVgEVLRVMraLAEEGRTMLVVTHEMGFARDVSSRV 228
Cdd:PRK11147 150 PDAA---LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETI-EWLEGF--LKTFQGSIIFISHDRSFIRNMATRI 223
|
....*.
gi 752717930 229 IFLHQG 234
Cdd:PRK11147 224 VDLDRG 229
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
34-229 |
2.38e-10 |
|
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: 57.97 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 34 EAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPtgsgksriadrrqverirselgmvfqsfnlwsh 113
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP--------------------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 114 ktvlenvmeaplhvQKRSraecleeaeallakvgiadkrnhypahLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPEL 193
Cdd:cd03222 68 --------------QYID---------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQ 106
|
170 180 190
....*....|....*....|....*....|....*..
gi 752717930 194 VGEVLRVMRALAEEG-RTMLVVTHEMGFARDVSSRVI 229
Cdd:cd03222 107 RLNAARAIRRLSEEGkKTALVVEHDLAVLDYLSDRIH 143
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
13-190 |
3.11e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.97 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEItvagetirmkptgsgksriaDRR 92
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------------------KRN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 93 QVERIrselGMVFQSFNLwshKTVLenvmeaPLHVQKRSRAE-CLEEAEAL--LAKVGIADKRNHYPAHLSGGQQQRAAI 169
Cdd:PRK09544 65 GKLRI----GYVPQKLYL---DTTL------PLTVNRFLRLRpGTKKEDILpaLKRVQAGHLIDAPMQKLSGGETQRVLL 131
|
170 180
....*....|....*....|.
gi 752717930 170 ARALAMRPKVMLFDEPTSALD 190
Cdd:PRK09544 132 ARALLNRPQLLVLDEPTQGVD 152
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-258 |
3.54e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.96 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 4 STNPPAPAAITVRGLRKSFGPVE--VLKGIDMEAREGEVVSILGSSGSGKSTMLRCInmletpdageitvAGETIRMKPT 81
Cdd:TIGR00957 628 TIKPGEGNSITVHNATFTWARDLppTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-------------LAEMDKVEGH 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 82 GSGKSRIADRRQVERIRSElgmvfqsfnlwshkTVLENVMEAPLHVQKRSRAecLEEAEALLAKVGI---ADKRN--HYP 156
Cdd:TIGR00957 695 VHMKGSVAYVPQQAWIQND--------------SLRENILFGKALNEKYYQQ--VLEACALLPDLEIlpsGDRTEigEKG 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 157 AHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPElVGE-----VLRVMRALAeeGRTMLVVTHEMGFARDVSSrVIFL 231
Cdd:TIGR00957 759 VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH-VGKhifehVIGPEGVLK--NKTRILVTHGISYLPQVDV-IIVM 834
|
250 260
....*....|....*....|....*..
gi 752717930 232 HQGAIEEEGRPQDMFtnAKSERFRKFI 258
Cdd:TIGR00957 835 SGGKISEMGSYQELL--QRDGAFAEFL 859
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
28-238 |
6.11e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.22 E-value: 6.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkptgsgksriaDRRQVERIRSELGMVFQS 107
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV-------------TAEQPEDYRKLFSAVFTD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 108 FNLWSHktVLENVMEAPLHVQKRSRAECLEEAEallaKVGIADKR--NhypAHLSGGQQQRAAIARALAMRPKVMLFDEP 185
Cdd:PRK10522 406 FHLFDQ--LLGPEGKPANPALVEKWLERLKMAH----KLELEDGRisN---LKLSKGQKKRLALLLALAEERDILLLDEW 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 752717930 186 TSALDPELVGEVLRV-MRALAEEGRTMLVVTHEMGFArDVSSRVIFLHQGAIEE 238
Cdd:PRK10522 477 AADQDPHFRREFYQVlLPLLQEMGKTIFAISHDDHYF-IHADRLLEMRNGQLSE 529
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
7-236 |
8.54e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 8.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 7 PPAPAAITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCInmleTPD-----AGEITVAGetirmKPT 81
Cdd:PRK10938 255 PANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI----TGDhpqgySNDLTLFG-----RRR 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 82 GSGKSrIADrrqverIRSELGMVFQSFNL-WSHKTVLENVMEAPLH--------VQKRSRaeclEEAEALLAKVGIADKR 152
Cdd:PRK10938 326 GSGET-IWD------IKKHIGYVSSSLHLdYRVSTSVRNVILSGFFdsigiyqaVSDRQQ----KLAQQWLDILGIDKRT 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 153 NHYPAH-LSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRT-MLVVTHEmgfARD----VSS 226
Cdd:PRK10938 395 ADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSHH---AEDapacITH 471
|
250
....*....|
gi 752717930 227 RVIFLHQGAI 236
Cdd:PRK10938 472 RLEFVPDGDI 481
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
13-216 |
1.05e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.34 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCI------NMLEtpdaGEITVAGETI-RMKPTgsgk 85
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpayKILE----GDILFKGESIlDLEPE---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 86 sriadrrqverIRSELGmVFQSFNL------WSHKTVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPAH- 158
Cdd:CHL00131 80 -----------ERAHLG-IFLAFQYpieipgVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRn 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752717930 159 ----LSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTH 216
Cdd:CHL00131 148 vnegFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-234 |
2.10e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 3 PSTNPPAPAAITVRGLRKSFGPVevLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIR----M 78
Cdd:PRK10982 241 DKENKPGEVILEVRNLTSLRQPS--IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnhnaN 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 79 KPTGSGKSRIADRRQVERIRSELGMVFQSF--NLWSHKT---VLENvmeaplhvqKRSRAECLEEAEALLAKVgiadkrn 153
Cdd:PRK10982 319 EAINHGFALVTEERRSTGIYAYLDIGFNSLisNIRNYKNkvgLLDN---------SRMKSDTQWVIDSMRVKT------- 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 154 hyPAH------LSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSR 227
Cdd:PRK10982 383 --PGHrtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDR 460
|
....*..
gi 752717930 228 VIFLHQG 234
Cdd:PRK10982 461 ILVMSNG 467
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-229 |
2.63e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 12 AITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVA----------------GET 75
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenanigyyaqdhaydfEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 76 IRMKPTGSGKSRIADRRQVerIRSELG-MVFQSFNLwshktvlenvmeaplhvqKRSraecleeaeallAKVgiadkrnh 154
Cdd:PRK15064 399 LTLFDWMSQWRQEGDDEQA--VRGTLGrLLFSQDDI------------------KKS------------VKV-------- 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 155 ypahLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVgEVLRVmrALAEEGRTMLVVTHEMGFARDVSSRVI 229
Cdd:PRK15064 439 ----LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESI-ESLNM--ALEKYEGTLIFVSHDREFVSSLATRII 506
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-246 |
4.44e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 56.65 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 3 PSTNPPAPAAITVRGLRKSFGPVE-VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIrmkpt 81
Cdd:PRK10790 331 NDDRPLQSGRIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL----- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 82 gSGKSRIADRRQVERIRSE-------------LGMVFQSFNLWshkTVLENVMEAPLhvqKRSRAECLEeaeALLAKVGi 148
Cdd:PRK10790 406 -SSLSHSVLRQGVAMVQQDpvvladtflanvtLGRDISEEQVW---QALETVQLAEL---ARSLPDGLY---TPLGEQG- 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 149 adkrnhypAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPelvGEVLRVMRALAE--EGRTMLVVTHEMGFARDVSS 226
Cdd:PRK10790 475 --------NNLSVGQKQLLALARVLVQTPQILILDEATANIDS---GTEQAIQQALAAvrEHTTLVVIAHRLSTIVEADT 543
|
250 260
....*....|....*....|
gi 752717930 227 rVIFLHQGAIEEEGRPQDMF 246
Cdd:PRK10790 544 -ILVLHRGQAVEQGTHQQLL 562
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
28-248 |
7.02e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.05 E-value: 7.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGeTIRMKPTGSGKSriADRRQVERIrsELGMVFQS 107
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-SAALIAISSGLN--GQLTGIENI--ELKGLMMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 108 FNLWSHKTVLENVMEaplhvqkrsraecleeaealLAKVGiadKRNHYPAH-LSGGQQQRAAIARALAMRPKVMLFDEPT 186
Cdd:PRK13545 115 LTKEKIKEIIPEIIE--------------------FADIG---KFIYQPVKtYSSGMKSRLGFAISVHINPDILVIDEAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752717930 187 SALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFTN 248
Cdd:PRK13545 172 SVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
155-230 |
8.98e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 8.98e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 155 YPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDP---ELVGEVLRVMRALAEegRTMLVVTHEMGFARDVSSRVIF 230
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKAD--KTIITIAHRIASIKRSDKIVVF 1431
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
13-216 |
1.12e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.41 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTmlrcinmLETPDAG--EITVAGETIRMKptgsGKSRIAD 90
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKST-------LSATLAGreDYEVTGGTVEFK----GKDLLEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 91 RRQvERIRSELGMVFQ-------SFNLWSHKTVLENVME----APLhvQKRSRAECLEEAEALLakvgiadkrnHYPAHL 159
Cdd:PRK09580 71 SPE-DRAGEGIFMAFQypveipgVSNQFFLQTALNAVRSyrgqEPL--DRFDFQDLMEEKIALL----------KMPEDL 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752717930 160 ---------SGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTH 216
Cdd:PRK09580 138 ltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-215 |
3.89e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 4 STNPPAPAAITVRGLRKSFGP-----VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRcinmletpdageiTVAGETIRM 78
Cdd:TIGR00956 48 PTFPNALLKILTRGFRKLKKFrdtktFDILKPMDGLIKPGELTVVLGRPGSGCSTLLK-------------TIASNTDGF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 79 KPTGSGKSR---IADRRQVERIRSELGMVFQSFNLWSHKTVLENVMEA---------PLHVQKRSRAEclEEAEALLAKV 146
Cdd:TIGR00956 115 HIGVEGVITydgITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAarcktpqnrPDGVSREEYAK--HIADVYMATY 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752717930 147 GIADKR-----NHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVT 215
Cdd:TIGR00956 193 GLSHTRntkvgNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVA 266
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
27-217 |
4.41e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.87 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRmkptgsgKSRIADRRQverirseLGMVFQ 106
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-------KDLCTYQKQ-------LCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 107 SFNLWSHKTVLENVMeapLHVQKRSRAECLEEAEALLAKVGIADkrnhYPAH-LSGGQQQRAAIARALAMRPKVMLFDEP 185
Cdd:PRK13540 82 RSGINPYLTLRENCL---YDIHFSPGAVGITELCRLFSLEHLID----YPCGlLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 752717930 186 TSALDPELVGEVLRVMRALAEEGRTMLVVTHE 217
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
38-234 |
8.59e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.45 E-value: 8.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 38 GEVVSILGSSGSGKSTMLRCI-NMLETPDAGEITVAGETIRmkptgsgksriadrrqverirselgmvfqsfnlwshktv 116
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDIL--------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 117 lenvmeaplhvqkrsraecleeaeALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGE 196
Cdd:smart00382 43 ------------------------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAL 98
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 752717930 197 VLR------VMRALAEEGRTMLVVTHEMGF-----ARDVSSRVIFLHQG 234
Cdd:smart00382 99 LLLleelrlLLLLKSEKNLTVILTTNDEKDlgpalLRRRFDRRIVLLLI 147
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
160-255 |
9.02e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.55 E-value: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 160 SGGQQQRAAIARALAMRPKVMLFDEPTSALDpelVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEE 239
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTY 422
|
90
....*....|....*.
gi 752717930 240 GRPQDMFTNAKSERFR 255
Cdd:PLN03073 423 KGDYDTFERTREEQLK 438
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
37-235 |
1.06e-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: 50.44 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 37 EGEVVSILGSSGSGKSTMLRCINMLETpdageitvagetirmkptgsGKSRIADRRQVERIRSElgmvfqsfnlwshktv 116
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIGLALG--------------------GAQSATRRRSGVKAGCI---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 117 lenvmeaplhvqkrsraECLEEAEALLAKVGiadkrnhypahLSGGQQQRAAIARALAM-----RPKVmLFDEPTSALDP 191
Cdd:cd03227 64 -----------------VAAVSAELIFTRLQ-----------LSGGEKELSALALILALaslkpRPLY-ILDEIDRGLDP 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 752717930 192 ELVGEVLRVMRALAEEGRTMLVVTHEMGFAR--DVSSRVIFLHQGA 235
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQVIVITHLPELAElaDKLIHIKKVITGV 160
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
27-235 |
1.57e-07 |
|
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: 51.01 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGetirmkptgsgksRIADRRQVERIRS---ELGM 103
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPgtiKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 104 VFQ-SFNLWSHKTVL------ENVMEAPlhvqkrsraeclEEAEALLAKVGIAdkrnhypahLSGGQQQRAAIARALAMR 176
Cdd:cd03291 119 IFGvSYDEYRYKSVVkacqleEDITKFP------------EKDNTVLGEGGIT---------LSGGQRARISLARAVYKD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 752717930 177 PKVMLFDEPTSALDPELVGEVLR--VMRALAEegRTMLVVTHEMGFARdVSSRVIFLHQGA 235
Cdd:cd03291 178 ADLYLLDSPFGYLDVFTEKEIFEscVCKLMAN--KTRILVTSKMEHLK-KADKILILHEGS 235
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
25-217 |
1.68e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.16 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 25 VEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPD--AGEITVAGETIRMKPTgsgkSRIADRRQVERIRSELG 102
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQETF----ARISGYCEQNDIHSPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 103 MVFQSFnlwshktVLENVMEAPLHVQKRSRAECLEEAEALLAKVGIADKRNHYPA--HLSGGQQQRAAIARALAMRPKVM 180
Cdd:PLN03140 969 TVRESL-------IYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSII 1041
|
170 180 190
....*....|....*....|....*....|....*..
gi 752717930 181 LFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHE 217
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
159-218 |
1.71e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 51.08 E-value: 1.71e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752717930 159 LSGGQQQRAAIARALAMR---PKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEM 218
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL 232
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
159-235 |
1.72e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.01 E-value: 1.72e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 159 LSGGQQQRAAIARALAMRPK--VMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFArDVSSRVIFLHQGA 235
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVL-SSADWIIDFGPGS 165
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
27-234 |
3.15e-07 |
|
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: 51.06 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGetirmkptgsgksRIADRRQVERIRSelgmvfq 106
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMP------- 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 107 sfnlwshKTVLENVMEAPLHVQKRSRA---EC-LEEAEALLA---KVGIADKrnhyPAHLSGGQQQRAAIARALAMRPKV 179
Cdd:TIGR01271 501 -------GTIKDNIIFGLSYDEYRYTSvikACqLEEDIALFPekdKTVLGEG----GITLSGGQRARISLARAVYKDADL 569
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 180 MLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDvSSRVIFLHQG 234
Cdd:TIGR01271 570 YLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-191 |
1.49e-06 |
|
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: 49.14 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 8 PAPAAITVRGLRKSF--GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDaGEITVAGETirmkptgsgk 85
Cdd:TIGR01271 1213 PSGGQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVS---------- 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 86 sriADRRQVERIRSELGMVFQSFNLWShKTVLENVmeAPLhvQKRSRAECLEEAEallaKVGIADKRNHYPAHL------ 159
Cdd:TIGR01271 1282 ---WNSVTLQTWRKAFGVIPQKVFIFS-GTFRKNL--DPY--EQWSDEEIWKVAE----EVGLKSVIEQFPDKLdfvlvd 1349
|
170 180 190
....*....|....*....|....*....|....*..
gi 752717930 160 -----SGGQQQRAAIARALAMRPKVMLFDEPTSALDP 191
Cdd:TIGR01271 1350 ggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHLDP 1386
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-218 |
2.01e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 24 PVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCInmletpdAGEITVAgetirmkptgSGksriadrrqveRIRSELGM 103
Cdd:PTZ00243 672 PKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSL-------LSQFEIS----------EG-----------RVWAERSI 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 104 VFQSFNLW-SHKTVLENVM----EAPLHVQKRSRAECLEEAEALLAKvGIADKRNHYPAHLSGGQQQRAAIARALAMRPK 178
Cdd:PTZ00243 724 AYVPQQAWiMNATVRGNILffdeEDAARLADAVRVSQLEADLAQLGG-GLETEIGEKGVNLSGGQKARVSLARAVYANRD 802
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 752717930 179 VMLFDEPTSALDPElVGEvlRVMR-----ALAeeGRTMLVVTHEM 218
Cdd:PTZ00243 803 VYLLDDPLSALDAH-VGE--RVVEecflgALA--GKTRVLATHQV 842
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-251 |
2.28e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTMLRC-INMLETPdAGEITVAGETIrmkptGSGKSRiadrrqveRIRSELGMVF 105
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTfMRMVEVC-GGEIRVNGREI-----GAYGLR--------ELRRQFSMIP 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 106 QSFNLWShKTVLENV---MEAplhvqkrSRAECLEEAE--ALLAKV-----GIADKRNHYPAHLSGGQQQRAAIARALAM 175
Cdd:PTZ00243 1391 QDPVLFD-GTVRQNVdpfLEA-------SSAEVWAALElvGLRERVaseseGIDSRVLEGGSNYSVGQRQLMCMARALLK 1462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 176 R-PKVMLFDEPTSALDPELVGEV-LRVMRALAeeGRTMLVVTHEMgfaRDVSS--RVIFLHQGAIEEEGRPQDMFTNAKS 251
Cdd:PTZ00243 1463 KgSGFILMDEATANIDPALDRQIqATVMSAFS--AYTVITIAHRL---HTVAQydKIIVMDHGAVAEMGSPRELVMNRQS 1537
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
27-251 |
2.57e-06 |
|
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: 47.60 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKSTM-LRCINMLETPDaGEITVAGETIRMKPtgsgksriadrrqVERIRSELGMVF 105
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFD-GKIVIDGIDISKLP-------------LHTLRSRLSIIL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 106 QS---------FNLWSHKTVLENVMEAPLHV-QKRSRAECLEEA-EALLAKVGiadkrnhypAHLSGGQQQRAAIARALA 174
Cdd:cd03288 102 QDpilfsgsirFNLDPECKCTDDRLWEALEIaQLKNMVKSLPGGlDAVVTEGG---------ENFSVGQRQLFCLARAFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 175 MRPKVMLFDEPTSALD---PELVGEVlrVMRALAEegRTMLVVTHEMGFARDvSSRVIFLHQGAIEEEGRPQDMFTNAKS 251
Cdd:cd03288 173 RKSSILIMDEATASIDmatENILQKV--VMTAFAD--RTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDG 247
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
159-216 |
2.73e-06 |
|
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: 48.21 E-value: 2.73e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 752717930 159 LSGGQQQRAAIARALAMRPKVMLFDEPTSALDPELVGevlRVMRALAEEGRTMLVVTH 216
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG---YMYRLCREFGITLFSVSH 637
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-218 |
2.76e-06 |
|
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: 47.54 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRKSF--GPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRC-INMLETpdAGEITVAGETIRMKPtgsgksria 89
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAfLRLLNT--EGDIQIDGVSWNSVP--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 90 drrqVERIRSELGMVFQSFNLWShKTVLENVmeAPLhvQKRSRAECLEEAEallaKVGIADKRNHYPAH----------- 158
Cdd:cd03289 72 ----LQKWRKAFGVIPQKVFIFS-GTFRKNL--DPY--GKWSDEEIWKVAE----EVGLKSVIEQFPGQldfvlvdggcv 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 159 LSGGQQQRAAIARALAMRPKVMLFDEPTSALDPeLVGEVLRVMRALAEEGRTMLVVTHEM 218
Cdd:cd03289 139 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQVIRKTLKQAFADCTVILSEHRI 197
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
22-237 |
3.10e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 22 FGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAgETIRMKPTGsgksriadRRQVERIRSEl 101
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA-KGIKLGYFA--------QHQLEFLRAD- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 102 gmvfqsfnlwshktvlenvmEAPL-HVQKRSRAECLEEAEALLAKVGI-ADKRNHYPAHLSGGQQQRAAIARALAMRPKV 179
Cdd:PRK10636 392 --------------------ESPLqHLARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752717930 180 MLFDEPTSALDpelvgevLRVMRALAE-----EGrTMLVVTHEMGFARDVSSRVIFLHQGAIE 237
Cdd:PRK10636 452 LLLDEPTNHLD-------LDMRQALTEalidfEG-ALVVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
150-216 |
3.22e-06 |
|
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: 47.38 E-value: 3.22e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 150 DKRNHYPAHLSGGQQQ---RAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTH 216
Cdd:pfam13304 228 GGGELPAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-236 |
3.58e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.48 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 27 VLKGIDMEAREGEVVSILGSSGSGKsTML----------RCInmletpdAGEITVAGETIRMKPTGSG-KSRIA----DR 91
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGR-TELamsvfgrsygRNI-------SGTVFKDGKEVDVSTVSDAiDAGLAyvteDR 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 RQ-----VERIR-----SELGMVfqsfnlwSHKTVLENVMEapLHVQKRSRAECLEEAEALLAKVGiadkrnhypaHLSG 161
Cdd:NF040905 347 KGyglnlIDDIKrnitlANLGKV-------SRRGVIDENEE--IKVAEEYRKKMNIKTPSVFQKVG----------NLSG 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 752717930 162 GQQQRAAIARALAMRPKVMLFDEPTSALDpelVG---EVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAI 236
Cdd:NF040905 408 GNQQKVVLSKWLFTDPDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
157-251 |
4.43e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 157 AHLSGGQQQRAAIARALA--MRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHE---MGFArdvsSRVIFL 231
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGaeLIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLA----DRIIDI 550
|
90 100
....*....|....*....|....*.
gi 752717930 232 HQGA------IEEEGRPQDMFTNAKS 251
Cdd:PRK00635 551 GPGAgifggeVLFNGSPREFLAKSDS 576
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
28-256 |
8.04e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.96 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 28 LKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGETIRMKPTGSGKSRIADrrqVERIrsELGMVFQS 107
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTG---IENI--EFKMLCMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 108 FNLWSHKTVLENVMEAPlhvqkrsraeclEEAEALLAKVgiadkrnhypAHLSGGQQQRAAIARALAMRPKVMLFDEPTS 187
Cdd:PRK13546 115 FKRKEIKAMTPKIIEFS------------ELGEFIYQPV----------KKYSSGMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 188 ALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFARDVSSRVIFLHQGAIEEEGRPQDMFtnAKSERFRK 256
Cdd:PRK13546 173 VGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL--PKYEAFLN 239
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
159-218 |
1.37e-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: 46.16 E-value: 1.37e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752717930 159 LSGGQQQRAAIARALAMR---PKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEM 218
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
159-224 |
3.22e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.02 E-value: 3.22e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717930 159 LSGGQQQRAAIARALAMRPK---VMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMgfarDV 224
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNL----DV 891
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
30-217 |
4.27e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 30 GIDMEARegevVSILGSSGSGKSTMLRCInmletpdAGEIT-VAGETIRmkptgSGKSRIAdrrqverirselgmVFQSf 108
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLI-------SGELQpSSGTVFR-----SAKVRMA--------------VFSQ- 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 109 nlwsHKTVLENVMEAPLHVQKRSRAECLEEA-EALLAKVGIADKRNHYPAH-LSGGQQQRAAIARALAMRPKVMLFDEPT 186
Cdd:PLN03073 580 ----HHVDGLDLSSNPLLYMMRCFPGVPEQKlRAHLGSFGVTGNLALQPMYtLSGGQKSRVAFAKITFKKPHILLLDEPS 655
|
170 180 190
....*....|....*....|....*....|.
gi 752717930 187 SALDPELVgEVLRVMRALAEEGrtMLVVTHE 217
Cdd:PLN03073 656 NHLDLDAV-EALIQGLVLFQGG--VLMVSHD 683
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
13-258 |
5.34e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 43.84 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRkSFGPVEvlkgIDMEareGEVVSILGSSGSGKSTMLRCINML-------------------ETPDAGEITVA- 72
Cdd:COG3593 6 IKIKNFR-SIKDLS----IELS---DDLTVLVGENNSGKSSILEALRLLlgpsssrkfdeedfylgddPDLPEIEIELTf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 73 GETIR--MKPTGSGKSRIADRRQVERIRSELGMVFQSFNlwshkTVLENVMEAPLHVQKRSRAECLEEAEALL--AKVGI 148
Cdd:COG3593 78 GSLLSrlLRLLLKEEDKEELEEALEELNEELKEALKALN-----ELLSEYLKELLDGLDLELELSLDELEDLLksLSLRI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 149 ADKRNHYPAHLSGGQQQRAAIA--RALAM-----RPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEMGFA 221
Cdd:COG3593 153 EDGKELPLDRLGSGFQRLILLAllSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLL 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 752717930 222 RDVS-SRVIFLHQGAIEEEGRPQDMFTNAKSERFRKFI 258
Cdd:COG3593 233 SEVPlENIRRLRRDSGGTTSTKLIDLDDEDLRKLLRYL 270
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
43-216 |
1.53e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.53 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 43 ILGSSGSGKSTMLRCINM-LETPDAGEITVAGETIRMKPTGS---------GKSRIADRRQVERIR------SELG-MVF 105
Cdd:COG0419 28 IVGPNGAGKSTILEAIRYaLYGKARSRSKLRSDLINVGSEEAsvelefehgGKRYRIERRQGEFAEfleakpSERKeALK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 106 QSFNLWSHKTVLENVME--APLHVQKRSRAECLEEAEALLAKVGIADKrnhyPAHLSGGQQQRAAIARALAmrpkvMLFD 183
Cdd:COG0419 108 RLLGLEIYEELKERLKEleEALESALEELAELQKLKQEILAQLSGLDP----IETLSGGERLRLALADLLS-----LILD 178
|
170 180 190
....*....|....*....|....*....|...
gi 752717930 184 epTSALDPELVGEVLRVMRALAeegrtmlVVTH 216
Cdd:COG0419 179 --FGSLDEERLERLLDALEELA-------IITH 202
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
43-217 |
1.59e-04 |
|
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: 41.44 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 43 ILGSSGSGKSTMLRCINMLETPDageitvagetirMKPTGSGKSRIADRRQVERIRSELGMVFQSFNlwSHKTVLENVME 122
Cdd:cd03240 27 IVGQNGAGKTTIIEALKYALTGE------------LPPNSKGGAHDPKLIREGEVRAQVKLAFENAN--GKKYTITRSLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 123 APLHV----QKRSRAECLEEAEALlakvgiadkrnhypahlSGGQQQ------RAAIARALAMRPKVMLFDEPTSALDPE 192
Cdd:cd03240 93 ILENVifchQGESNWPLLDMRGRC-----------------SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEE 155
|
170 180
....*....|....*....|....*..
gi 752717930 193 LVGEVL-RVMRA-LAEEGRTMLVVTHE 217
Cdd:cd03240 156 NIEESLaEIIEErKSQKNFQLIVITHD 182
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
159-218 |
1.59e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752717930 159 LSGGQQQRAAIARAL---AMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHEM 218
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM 872
|
|
| Rad50_Sulf |
NF041034 |
DNA double-strand break repair ATPase Rad50; |
159-217 |
1.96e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 468963 [Multi-domain] Cd Length: 872 Bit Score: 42.39 E-value: 1.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 159 LSGGQQ------QRAAIARALAMRPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHE 217
Cdd:NF041034 780 LSGGERisialaLRLAIAKSLMDEIGFMILDEPTVHLDEERKKELIDIIRSSMEIVPQIIVVTHD 844
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
13-217 |
2.39e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.09 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 13 ITVRGLRksfgpVEVLKGIDMEAREGEVVSILGSSGSGKSTML---------------------RCINMLETPDAGEITV 71
Cdd:cd03270 1 IIVRGAR-----EHNLKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSIEG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 72 AGETIRMKPTGSGKSRIADRRQVERIRSELGMVFQSFNLwshKTVLENVMEAPLHVQKRSRAEcleeaeallakvgiadk 151
Cdd:cd03270 76 LSPAIAIDQKTTSRNPRSTVGTVTEIYDYLRLLFARVGI---RERLGFLVDVGLGYLTLSRSA----------------- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 752717930 152 rnhypAHLSGGQQQRAAIARALAMRPKVML--FDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTHE 217
Cdd:cd03270 136 -----PTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD 198
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-214 |
3.02e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 32 DMEAREGEVVSILGSSGSGKSTMLRCInmletpdAGEIT-VAGETIrmkptgSGKSRIAdRRQVERIRSELGMVFQSFN- 109
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARAL-------AGELPlLSGERQ------SQFSHIT-RLSFEQLQKLVSDEWQRNNt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 110 -LWSH------KTVLENVMEaplHVQKRSRaeCLEEAEALlakvGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLF 182
Cdd:PRK10938 89 dMLSPgeddtgRTTAEIIQD---EVKDPAR--CEQLAQQF----GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLIL 159
|
170 180 190
....*....|....*....|....*....|..
gi 752717930 183 DEPTSALDPELVGEVLRVMRALAEEGRTMLVV 214
Cdd:PRK10938 160 DEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
38-238 |
1.28e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.93 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 38 GEVVSILGSSGSGKSTMLRCinMLE--TPDAGEITVagetirmkptGSgKSRIADRRQVeriRSELGmvfqsfnlwSHKT 115
Cdd:PRK11147 345 GDKIALIGPNGCGKTTLLKL--MLGqlQADSGRIHC----------GT-KLEVAYFDQH---RAELD---------PEKT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 116 VLENVMEAP--LHVQKRSRaecleEAEALLAKVGIADKRNHYPAH-LSGGQQQRAAIARaLAMRPKVML-FDEPTSALDP 191
Cdd:PRK11147 400 VMDNLAEGKqeVMVNGRPR-----HVLGYLQDFLFHPKRAMTPVKaLSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLDV 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 752717930 192 ELVgEVLRVMraLAEEGRTMLVVTHEMGFARD-VSSRVIFLHQGAIEE 238
Cdd:PRK11147 474 ETL-ELLEEL--LDSYQGTVLLVSHDRQFVDNtVTECWIFEGNGKIGR 518
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
20-216 |
1.36e-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: 38.79 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 20 KSFGPVEVLKGIDMEAREG-EVVSILGSSGSGKSTMLrcinmletpDAgeITVA--GETIRMKPTGSGKSRIAD------ 90
Cdd:cd03279 9 KNFGPFREEQVIDFTGLDNnGLFLICGPTGAGKSTIL---------DA--ITYAlyGKTPRYGRQENLRSVFAPgedtae 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 91 -------RRQVERIRSELGMVFQSFnlwshktvlenvmeaplhvqKRSraecleeaeALLAKvGIADK--RNHYpAHLSG 161
Cdd:cd03279 78 vsftfqlGGKKYRVERSRGLDYDQF--------------------TRI---------VLLPQ-GEFDRflARPV-STLSG 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752717930 162 GQQQRAAIARALAM----------RPKVMLFDEPTSALDPELVGEVLRVMRALAEEGRTMLVVTH 216
Cdd:cd03279 127 GETFLASLSLALALsevlqnrggaRLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISH 191
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
139-238 |
1.37e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.77 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 139 AEALLAKVGIADKRNHYP-AHLSGGQQQRAAIARALAMRPKVMLFDEPTSALDpelVGEVLRVMRALAEEGRTMLVVTHE 217
Cdd:PRK10636 129 AASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILISHD 205
|
90 100
....*....|....*....|.
gi 752717930 218 MGFARDVSSRVIFLHQGAIEE 238
Cdd:PRK10636 206 RDFLDPIVDKIIHIEQQSLFE 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-191 |
2.38e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 38.95 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 12 AITVRGLRKSFGPVEVLKGIDMEAREGEVVSILGSSGSGKSTMLRCINMLETPDAGEITVAGetirmkptGSgksrIADR 91
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG--------GD----MADA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 92 RQVERIRSE-------LGMvfqsfNLWSHKTVLENV-MEAPLHVQkrSRAECLEEAEALLAKVGIADKRNHyPA-HLSGG 162
Cdd:NF033858 69 RHRRAVCPRiaympqgLGK-----NLYPTLSVFENLdFFGRLFGQ--DAAERRRRIDELLRATGLAPFADR-PAgKLSGG 140
|
170 180
....*....|....*....|....*....
gi 752717930 163 QQQRAAIARALAMRPKVMLFDEPTSALDP 191
Cdd:NF033858 141 MKQKLGLCCALIHDPDLLILDEPTTGVDP 169
|
|
| DUF87 |
pfam01935 |
Helicase HerA, central domain; This entry represents the central domain found in archaeal ... |
41-190 |
9.47e-03 |
|
Helicase HerA, central domain; This entry represents the central domain found in archaeal proteins such as DNA double-strand break repair helicase HerA (EC:3.6.4.12). HerA is a helicase which is able to utilize either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding. It forms a complex with NurA nuclease, this complex has the 5'-3' DNA end resection activity and is essential for cell viability in the crenarchaeon Sulfolobus islandicus. This domain includes the the central RecA-like catalytic core and a flanking four-helix bundle. The function of this prokaryotic domain is unknown. It contains several conserved aspartates and histidines that could be metal ligands.
Pssm-ID: 376671 [Multi-domain] Cd Length: 220 Bit Score: 36.57 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 41 VSILGSSGSGKSTMLRCI--NMLETPDAGEITV--AGETIRMKPTGSgksriADRRQVERIRSELGMVFQSFNLWSHKTV 116
Cdd:pfam01935 26 FAILGSTGSGKSNTVAVLleELLEKKGATVLIFdpHGEYGTLFRDLG-----AENVNVITPDPELKINPWLLSPEDLADL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752717930 117 LENVMEAPLHVQKRSRAECLEEA----------EALLAKVGIADKRNHYPAHLSGGQQQRAAIARALAMRPKVMLFDEPT 186
Cdd:pfam01935 101 LEELNLPNAEVQRSILEEALDQLkseelgklsiDELIEKILEELLTEAAELNKLSNDAIRRVLDKLERLLRSGGLILTST 180
|
....
gi 752717930 187 SALD 190
Cdd:pfam01935 181 DIIK 184
|
|
| |
