|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-257 |
1.59e-180 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 496.03 E-value: 1.59e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDGQLK 80
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 81 VFDKKQLQLLRTRLTMVFQHFNLWSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQR 160
Cdd:PRK10619 81 VADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELF 240
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
250
....*....|....*..
gi 491074476 241 GNPKSPRLQQFLSGALK 257
Cdd:PRK10619 241 GNPQSPRLQQFLKGSLK 257
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-257 |
5.93e-172 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 474.29 E-value: 5.93e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSEN---KLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDG 77
Cdd:COG4598 1 MTDTappALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 78 QLKVFDKKQLQLLRTRLTMVFQHFNLWSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDERaRGKYPVHLSGGQ 157
Cdd:COG4598 81 ELVPADRRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADK-RDAYPAHLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPA 237
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPA 239
|
250 260
....*....|....*....|
gi 491074476 238 ELFGNPKSPRLQQFLSGALK 257
Cdd:COG4598 240 EVFGNPKSERLRQFLSSSLK 259
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-253 |
1.43e-140 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 393.98 E-value: 1.43e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIRMvrdkdgqlkvfDKK 85
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVvviigpsgsgKSTLLRCINLLEEPDSGTITVDGEDLTD-----------SKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQLLRTRLTMVFQHFNLWSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDERArGKYPVHLSGGQQQRVSIAR 165
Cdd:COG1126 71 DINKLRRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKA-DAYPAQLSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKS 245
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
....*...
gi 491074476 246 PRLQQFLS 253
Cdd:COG1126 230 ERTRAFLS 237
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-230 |
7.56e-114 |
|
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: 325.64 E-value: 7.56e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 8 VTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvFDKKQL 87
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-----------DDKKNI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 88 QLLRTRLTMVFQHFNLWSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDERArGKYPVHLSGGQQQRVSIARAL 167
Cdd:cd03262 72 NELRQKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKA-DAYPAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491074476 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLI 230
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-252 |
6.95e-97 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 283.52 E-value: 6.95e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 13 KRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLnnedirmvrdkDGqLKVFDKK-QLQLLR 91
Cdd:PRK09493 9 KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIV-----------DG-LKVNDPKvDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 92 TRLTMVFQHFNLWSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDERArGKYPVHLSGGQQQRVSIARALAMEP 171
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERA-HHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 172 EVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKSPRLQQF 251
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEF 235
|
.
gi 491074476 252 L 252
Cdd:PRK09493 236 L 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
8-253 |
2.66e-91 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 269.70 E-value: 2.66e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 8 VTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDGQlkvfdKKQL 87
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQ-----KGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 88 QLLRTRLTMVFQHFNLWSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDerarGK---YPVHLSGGQQQRVSIA 164
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLA----GKetsYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPK 244
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
....*....
gi 491074476 245 SPRLQQFLS 253
Cdd:PRK11264 237 QPRTRQFLE 245
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
11-253 |
2.86e-85 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 254.17 E-value: 2.86e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 11 LHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkDGQLKVfDKKQLQLL 90
Cdd:COG4161 8 INCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF------DFSQKP-SEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 91 RTRLTMVFQHFNLWSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDERArGKYPVHLSGGQQQRVSIARALAME 170
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKA-DRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 171 PEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGpPAELFGNPKSPRLQQ 250
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQPQTEAFAH 238
|
...
gi 491074476 251 FLS 253
Cdd:COG4161 239 YLS 241
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-253 |
7.97e-85 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 253.01 E-value: 7.97e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 8 VTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDgqlkvfdKKQL 87
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPS-------DKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 88 QLLRTRLTMVFQHFNLWSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDERArGKYPVHLSGGQQQRVSIARAL 167
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYA-DRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGpPAELFGNPKSPR 247
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG-DASCFTQPQTEA 235
|
....*.
gi 491074476 248 LQQFLS 253
Cdd:PRK11124 236 FKNYLS 241
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
13-257 |
1.73e-81 |
|
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: 244.74 E-value: 1.73e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 13 KRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDGQLKVFDKKQLQLLRT 92
Cdd:TIGR03005 8 KRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNGPLVPADEKHLRQMRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 93 RLTMVFQHFNLWSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRVSIARALAMEPE 172
Cdd:TIGR03005 88 KIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKAD-HMPAQLSGGQQQRVAIARALAMRPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 173 VLLFDEPTSALDPELVGEVLRIMQKLAEEGK-TMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKSPRLQQF 251
Cdd:TIGR03005 167 VMLFDEVTSALDPELVGEVLNVIRRLASEHDlTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKEERTREF 246
|
....*.
gi 491074476 252 LSGALK 257
Cdd:TIGR03005 247 LSKVIA 252
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
11-253 |
5.43e-80 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 243.83 E-value: 5.43e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 11 LHKRY----GDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdGQLkvfDKKQ 86
Cdd:COG1135 7 LSKTFptkgGPVTALDDVSLTIEKGEIfgiigysgagKSTLIRCINLLERPTSGSVLVDGVDL-------TAL---SERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 87 LQLLRTRLTMVFQHFNLWSHMTVLENVmEAPVQVLGLSKADAHERAVRYLDKVGIDERArGKYPVHLSGGQQQRVSIARA 166
Cdd:COG1135 77 LRAARRKIGMIFQHFNLLSSRTVAENV-ALPLEIAGVPKAEIRKRVAELLELVGLSDKA-DAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKS 245
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQS 234
|
....*...
gi 491074476 246 PRLQQFLS 253
Cdd:COG1135 235 ELTRRFLP 242
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
11-244 |
1.55e-74 |
|
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: 226.31 E-value: 1.55e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 11 LHKRYGDH----EVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlKVFDKKQ 86
Cdd:cd03258 7 VSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDL----------TLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 87 LQLLRTRLTMVFQHFNLWSHMTVLENVMeAPVQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRVSIARA 166
Cdd:cd03258 77 LRKARRRIGMIFQHFNLLSSRTVFENVA-LPLEIAGVPKAEIEERVLELLELVGLEDKAD-AYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491074476 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPK 244
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-252 |
1.84e-69 |
|
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: 213.69 E-value: 1.84e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdGQLk 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEIlaiiggsgsgKSVLLKLIIGLLRPDSGEILVDGQDI-------TGL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 81 vfDKKQLQLLRTRLTMVFQHFNLWSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDErARGKYPVHLSGGQQQR 160
Cdd:COG1127 73 --SEKELYELRRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPG-AADKMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAEL 239
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
250
....*....|...
gi 491074476 240 FgNPKSPRLQQFL 252
Cdd:COG1127 230 L-ASDDPWVRQFL 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-246 |
9.47e-66 |
|
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: 212.46 E-value: 9.47e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRY-----GDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIRMVRdkdgqlk 80
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETlglvgesgsgKSTLARLLLGLLRPTSGSILFDGKDLTKLS------- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 81 vfdKKQLQLLRTRLTMVFQH----FNlwSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDERARGKYPVHLSGG 156
Cdd:COG1123 334 ---RRSLRELRRRVQMVFQDpyssLN--PRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGP 235
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGP 488
|
250
....*....|.
gi 491074476 236 PAELFGNPKSP 246
Cdd:COG1123 489 TEEVFANPQHP 499
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-233 |
1.08e-65 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 203.74 E-value: 1.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGD----HEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdGQLKv 81
Cdd:COG1136 5 LELRNLTKSYGTgegeVTALRGVSLSIEAGEFvaivgpsgsgKSTLLNILGGLDRPTSGEVLIDGQDI-------SSLS- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 82 fDKKQLQLLRTRLTMVFQHFNLWSHMTVLENVMeAPVQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRV 161
Cdd:COG1136 77 -ERELARLRRRHIGFVFQFFNLLPELTALENVA-LPLLLAGVSRKERRERARELLERVGLGDRLD-HRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491074476 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHvSNHVIFLHKGLIEEQ 233
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
5-254 |
4.33e-65 |
|
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: 202.91 E-value: 4.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 5 KLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEK--PS---EGSISLNNEDIrmvrdkdgql 79
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvPGvriEGKVLFDGQDI---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 80 kvFDKK-QLQLLRTRLTMVFQHFNLWShMTVLENVMEAPvQVLGL-SKADAHERAVRYLDKVGI-DE---RARgKYPVHL 153
Cdd:TIGR00972 71 --YDKKiDVVELRRRVGMVFQKPNPFP-MSIYDNIAYGP-RLHGIkDKKELDEIVEESLKKAALwDEvkdRLH-DSALGL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQ 233
Cdd:TIGR00972 146 SGGQQQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEY 224
|
250 260
....*....|....*....|.
gi 491074476 234 GPPAELFGNPKSPRLQQFLSG 254
Cdd:TIGR00972 225 GPTEQIFTNPKEKRTEDYISG 245
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-230 |
1.79e-64 |
|
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: 200.41 E-value: 1.79e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGD----HEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgQLKv 81
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIS-------KLS- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 82 fDKKQLQLLRTRLTMVFQHFNLWSHMTVLENVMeAPVQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRV 161
Cdd:cd03255 73 -EKELAAFRRRHIGFVFQSFNLLPDLTALENVE-LPLLLAGVPKKERRERAEELLERVGLGDRLN-HYPSELSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSnHVIFLHKGLI 230
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYAD-RIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-228 |
7.49e-64 |
|
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: 197.41 E-value: 7.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDkdgqlkvfdkk 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLED----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQLLRTRLTMVFQHFNLWSHMTVLENVMEApvqvlglskadaheravryldkvgiderargkypvhLSGGQQQRVSIAR 165
Cdd:cd03229 70 ELPPLRRRIGMVFQDFALFPHLTVLENIALG------------------------------------LSGGQQQRVALAR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491074476 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:cd03229 114 ALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-244 |
3.32e-63 |
|
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: 197.55 E-value: 3.32e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRY-GDHEVLKGVSLA-----------AN-AGdvisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIRmv 72
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSiekgefvaiigPNgSG------------KSTLLRLLNGLLKPTSGEVLVDGKDIT-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 73 rdkdgqlkvfdKKQLQLLRTRLTMVFQH-----FNlwshMTVLENVMEAPVQvLGLSKADAHERAVRYLDKVGIDERARg 147
Cdd:COG1122 67 -----------KKNLRELRRKVGLVFQNpddqlFA----PTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLAD- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 148 KYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHK 227
Cdd:COG1122 130 RPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDD 209
|
250
....*....|....*..
gi 491074476 228 GLIEEQGPPAELFGNPK 244
Cdd:COG1122 210 GRIVADGTPREVFSDYE 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-246 |
5.36e-63 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 201.09 E-value: 5.36e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIRMV----RDkd 76
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFvallgpsgcgKTTLLRMIAGFETPDSGRILLDGRDVTGLppekRN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 77 gqlkvfdkkqlqllrtrLTMVFQHFNLWSHMTVLENVmEAPVQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGG 156
Cdd:COG3842 79 -----------------VGMVFQDYALFPHLTVAENV-AFGLRMRGVPKAEIRARVAELLELVGLEGLAD-RYPHQLSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 157 QQQRVSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRIMQKLaeeGKTMVVVTHEME--FArhVSNHVIFLHKGLI 230
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAklreEMREELRRLQREL---GITFIYVTHDQEeaLA--LADRIAVMNDGRI 214
|
250
....*....|....*.
gi 491074476 231 EEQGPPAELFGNPKSP 246
Cdd:COG3842 215 EQVGTPEEIYERPATR 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
11-256 |
5.94e-62 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 198.10 E-value: 5.94e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 11 LHKRY----GDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDirmvrdkdgqLKVFDKKQ 86
Cdd:PRK11153 7 ISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQD----------LTALSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 87 LQLLRTRLTMVFQHFNLWSHMTVLENVmeA-PVQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRVSIAR 165
Cdd:PRK11153 77 LRKARRQIGMIFQHFNLLSSRTVFDNV--AlPLELAGTPKAEIKARVTELLELVGLSDKAD-RYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPK 244
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPK 233
|
250
....*....|..
gi 491074476 245 SPRLQQFLSGAL 256
Cdd:PRK11153 234 HPLTREFIQSTL 245
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-238 |
5.37e-60 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 189.11 E-value: 5.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 13 KRY-GDHEVLKGVSLAAN------------AGdvisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgQL 79
Cdd:COG2884 9 KRYpGGREALSDVSLEIEkgefvfltgpsgAG------------KSTLLKLLYGEERPTSGQVLVNGQDLS-------RL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 80 KvfdKKQLQLLRTRLTMVFQHFNLWSHMTVLENVMeAPVQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQ 159
Cdd:COG2884 70 K---RREIPYLRRRIGVVFQDFRLLPDRTVYENVA-LPLRVTGKSRKEIRRRVREVLDLVGLSDKAK-ALPHELSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491074476 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAE 238
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
11-251 |
2.15e-59 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 188.09 E-value: 2.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 11 LHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkVFDKKQLQLL 90
Cdd:cd03261 6 LTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIS----------GLSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 91 RTRLTMVFQHFNLWSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRVSIARALAME 170
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAED-LYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 171 PEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFgNPKSPRLQ 249
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR-ASDDPLVR 233
|
..
gi 491074476 250 QF 251
Cdd:cd03261 234 QF 235
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-239 |
1.86e-58 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 186.03 E-value: 1.86e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRY-GDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdGQLKvfdK 84
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFvaligpsgagKSTLLRCLNGLVEPTSGEILVDGQDV-------TALR---G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 85 KQLQLLRTRLTMVFQHFNLWSHMTVLENV-------MEAPVQVLGLSKADAHERAVRYLDKVGIDERA--RGKYpvhLSG 155
Cdd:COG3638 73 RALRRLRRRIGMIFQQFNLVPRLSVLTNVlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADKAyqRADQ---LSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQG 234
Cdd:COG3638 150 GQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDG 229
|
....*
gi 491074476 235 PPAEL 239
Cdd:COG3638 230 PPAEL 234
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-239 |
6.42e-58 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 184.11 E-value: 6.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvfdkK 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIfgllgpngagKTTTIRMLLGLLRPTSGEVRVLGEDVA--------------R 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQLLRTRLTMVFQHFNLWSHMTVLENV-MEApvQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRVSIA 164
Cdd:COG1131 67 DPAEVRRRIGYVPQEPALYPDLTVRENLrFFA--RLYGLPRKEARERIDELLELFGLTDAAD-RKVGTLSGGMKQRLGLA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491074476 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAEL 239
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-239 |
5.45e-57 |
|
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: 182.11 E-value: 5.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYG-DHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRdkdgqlkvfdK 84
Cdd:TIGR02315 2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLR----------G 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 85 KQLQLLRTRLTMVFQHFNLWSHMTVLENVMEAPV-------QVLGLSKADAHERAVRYLDKVGIDERA--RGKYpvhLSG 155
Cdd:TIGR02315 72 KKLRKLRRRIGMIFQHYNLIERLTVLENVLHGRLgykptwrSLLGRFSEEDKERALSALERVGLADKAyqRADQ---LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQG 234
Cdd:TIGR02315 149 GQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDG 228
|
....*
gi 491074476 235 PPAEL 239
Cdd:TIGR02315 229 APSEL 233
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-256 |
8.57e-57 |
|
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: 181.54 E-value: 8.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYG----DHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDgqlkv 81
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 82 fdkkqlqlLRTRLTMVFQH----FNlwSHMTVLENVMEaPVQVLGLskADAHERAVRYLDKVGIDERARGKYPVHLSGGQ 157
Cdd:COG1124 77 --------FRRRVQMVFQDpyasLH--PRHTVDRILAE-PLRIHGL--PDREERIAELLEQVGLPPSFLDRYPHQLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPP 236
Cdd:COG1124 144 RQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTV 223
|
250 260
....*....|....*....|
gi 491074476 237 AELFGNPKSPRLQQFLSGAL 256
Cdd:COG1124 224 ADLLAGPKHPYTRELLAASL 243
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-252 |
1.00e-56 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 184.58 E-value: 1.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSenkLAVTELHKRYGDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDirmvrdkdgqlk 80
Cdd:COG1118 1 MS---IEVRNISKRFGSFTLLDDVSLEIASGELvallgpsgsgKTTLLRIIAGLETPDSGRIVLNGRD------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 81 vfdkkqlqlLRTRLT-------MVFQHFNLWSHMTVLENVMEAPvQVLGLSKADAHERAVRYLDKVGIDERArGKYPVHL 153
Cdd:COG1118 66 ---------LFTNLPprerrvgFVFQHYALFPHMTVAENIAFGL-RVRPPSKAEIRARVEELLELVQLEGLA-DRYPSQL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALD----PELVGEVLRImqkLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGL 229
Cdd:COG1118 135 SGGQRQRVALARALAVEPEVLLLDEPFGALDakvrKELRRWLRRL---HDELGGTTVFVTHDQEEALELADRVVVMNQGR 211
|
250 260
....*....|....*....|...
gi 491074476 230 IEEQGPPAELFGNPKSPRLQQFL 252
Cdd:COG1118 212 IEQVGTPDEVYDRPATPFVARFL 234
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-239 |
2.25e-56 |
|
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: 180.46 E-value: 2.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGD-HEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRdkdgqlkvfdK 84
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLK----------G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 85 KQLQLLRTRLTMVFQHFNLWSHMTVLENVMEA------PVQVL--GLSKADaHERAVRYLDKVGIDERA--RGKYpvhLS 154
Cdd:cd03256 71 KALRQLRRQIGMIFQQFNLIERLSVLENVLSGrlgrrsTWRSLfgLFPKEE-KQRALAALERVGLLDKAyqRADQ---LS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLA-EEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQ 233
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFD 226
|
....*.
gi 491074476 234 GPPAEL 239
Cdd:cd03256 227 GPPAEL 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-254 |
1.17e-55 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 179.08 E-value: 1.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 2 SENKLAVTELHKRYGDHEVLKGVSL--AANA----------GdvisiigssgsgKSTFLRCINFL--EKPS---EGSISL 64
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLdiPENKvtaligpsgcG------------KSTLLRCLNRMndLIPGarvEGEILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 65 NNEDIrmvrdkdgqlkvFDKKQ-LQLLRTRLTMVFQHFNLWShMTVLENVmeapvqVLGL------SKADAHERAVRYLD 137
Cdd:COG1117 76 DGEDI------------YDPDVdVVELRRRVGMVFQKPNPFP-KSIYDNV------AYGLrlhgikSKSELDEIVEESLR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 138 KVGI-DE-RAR-GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPelvGEVLRI---MQKLAEEgKTMVVVTHE 211
Cdd:COG1117 137 KAALwDEvKDRlKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDP---ISTAKIeelILELKKD-YTIVIVTHN 212
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 491074476 212 MEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKSPRLQQFLSG 254
Cdd:COG1117 213 MQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYITG 255
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-239 |
1.93e-55 |
|
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: 177.76 E-value: 1.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEK-----PSEGSISLNNEDIRMVRDkdgqlk 80
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 81 vfdkkQLQLLRTRLTMVFQHFNLWsHMTVLENVmEAPVQVLG-LSKADAHERAVRYLDKVGI-DERARGKYPVHLSGGQQ 158
Cdd:cd03260 75 -----DVLELRRRVGMVFQKPNPF-PGSIYDNV-AYGLRLHGiKLKEELDERVEEALRKAALwDEVKDRLHALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAE 238
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 491074476 239 L 239
Cdd:cd03260 227 I 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-234 |
9.07e-55 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 175.40 E-value: 9.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDI--RMVRdkdgqlkvfd 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVtgVPPE---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 84 kkqlqllRTRLTMVFQHFNLWSHMTVLENVmeA-PVQVLGLSKADAHERAVRYLDKVGIDERArGKYPVHLSGGQQQRVS 162
Cdd:cd03259 71 -------RRNIGMVFQDYALFPHLTVAENI--AfGLKLRGVPKAEIRARVRELLELVGLEGLL-NRYPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491074476 163 IARALAMEPEVLLFDEPTSALDP----ELVGEVLRImqkLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQG 234
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAklreELREELKEL---QRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1-254 |
3.90e-54 |
|
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: 175.52 E-value: 3.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDgqlk 80
Cdd:cd03294 20 LLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKE---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 81 vfdkkQLQLLRTRLTMVFQHFNLWSHMTVLENVmEAPVQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQR 160
Cdd:cd03294 96 -----LRELRRKKISMVFQSFALLPHRTVLENV-AFGLEVQGVPRAEREERAAEALELVGLEGWEH-KYPDELSGGMQQR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 161 VSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRIMqklAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPP 236
Cdd:cd03294 169 VGLARALAVDPDILLMDEAFSALDPlirrEMQDELLRLQ---AELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTP 245
|
250
....*....|....*...
gi 491074476 237 AELFGNPKSPRLQQFLSG 254
Cdd:cd03294 246 EEILTNPANDYVREFFRG 263
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
44-243 |
6.19e-54 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 178.37 E-value: 6.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDI-RMvrdkdgqlkvfDKKQLQLLR-TRLTMVFQHFNLWSHMTVLENVmEAPVQVL 121
Cdd:COG4175 66 KSTLVRCLNRLIEPTAGEVLIDGEDItKL-----------SKKELRELRrKKMSMVFQHFALLPHRTVLENV-AFGLEIQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 122 GLSKADAHERAVRYLDKVGIDERArGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRIMQK 197
Cdd:COG4175 134 GVPKAERRERAREALELVGLAGWE-DSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrEMQDELLELQAK 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491074476 198 LaeeGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNP 243
Cdd:COG4175 213 L---KKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNP 255
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
13-252 |
2.92e-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: 174.51 E-value: 2.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 13 KRYGD-HEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvfdKKQLQLLR 91
Cdd:COG1125 9 KRYPDgTVAVDDLSLTIPAGEFtvlvgpsgcgKTTTLRMINRLIEPTSGRILIDGEDIR-------------DLDPVELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 92 TRLTMVFQHFNLWSHMTVLENVMEAPvQVLGLSKADAHERAVRYLDKVGID-ERARGKYPVHLSGGQQQRVSIARALAME 170
Cdd:COG1125 76 RRIGYVIQQIGLFPHMTVAENIATVP-RLLGWDKERIRARVDELLELVGLDpEEYRDRYPHELSGGQQQRVGVARALAAD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 171 PEVLLFDEPTSALDP----ELVGEVLRIMQKLaeeGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKSP 246
Cdd:COG1125 155 PPILLMDEPFGALDPitreQLQDELLRLQREL---GKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPAND 231
|
....*.
gi 491074476 247 RLQQFL 252
Cdd:COG1125 232 FVADFV 237
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-228 |
2.60e-52 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 170.66 E-value: 2.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRY----GDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIRMvrdkd 76
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFvalvgpsgcgKSTLLRLIAGLEKPTSGEVLVDGKPVTG----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 77 gqlkvfdkkqlqlLRTRLTMVFQHFNL--WshMTVLENVMeAPVQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLS 154
Cdd:COG1116 78 -------------PGPDRGVVFQEPALlpW--LTVLDNVA-LGLELRGVPKAERRERARELLELVGLAGFED-AYPHQLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491074476 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRImqkLAEEGKTMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
44-244 |
4.17e-52 |
|
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: 170.71 E-value: 4.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlKVFDKKQLQLLRTRLTMVFQH-----FNLwshmTVLENVMEAPV 118
Cdd:TIGR04521 44 KSTLIQHLNGLLKPTSGTVTIDGRDI----------TAKKKKKLKDLRKKVGLVFQFpehqlFEE----TVYKDIAFGPK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 119 QvLGLSKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL 198
Cdd:TIGR04521 110 N-LGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRL 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491074476 199 A-EEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPK 244
Cdd:TIGR04521 189 HkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-228 |
2.59e-51 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 166.49 E-value: 2.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 8 VTELHKRYGDHE--VLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvfdKK 85
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT-------------KL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQLLRTRLTMVFQH-----FNLwshmTVLENVMEAPVQvLGLSKADAHERAVRYLDKVGIDERaRGKYPVHLSGGQQQR 160
Cdd:cd03225 69 SLKELRRKVGLVFQNpddqfFGP----TVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGL-RDRSPFTLSGGQKQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491074476 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-245 |
3.84e-51 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 170.25 E-value: 3.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSEnkLAVTELHKRYGDHEVLKGVSLAAN------------AGdvisiigssgsgKSTFLRCINFLEKPSEGSISLNNED 68
Cdd:COG3839 1 MAS--LELENVSKSYGGVEALKDIDLDIEdgeflvllgpsgCG------------KSTLLRMIAGLEDPTSGEILIGGRD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 69 IRMVRDKDgqlkvfdkkqlqllRtRLTMVFQHFNLWSHMTVLENvMEAPVQVLGLSKADAHERAVRYLDKVGIDERArGK 148
Cdd:COG3839 67 VTDLPPKD--------------R-NIAMVFQSYALYPHMTVYEN-IAFPLKLRKVPKAEIDRRVREAAELLGLEDLL-DR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 149 YPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRIMQKLaeeGKTMVVVTHE----MEFArhvsN 220
Cdd:COG3839 130 KPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAklrvEMRAEIKRLHRRL---GTTTIYVTHDqveaMTLA----D 202
|
250 260
....*....|....*....|....*
gi 491074476 221 HVIFLHKGLIEEQGPPAELFGNPKS 245
Cdd:COG3839 203 RIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-234 |
8.92e-51 |
|
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: 165.76 E-value: 8.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRY----GDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqLKV 81
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDL---------LKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 82 fDKKQLQLLRTRLTMVFQH----FNlwSHMTVLENVMEAPVQVLGLSKADAHERAVRY-LDKVGIDERARGKYPVHLSGG 156
Cdd:cd03257 73 -SRRLRKIRRKEIQMVFQDpmssLN--PRMTIGEQIAEPLRIHGKLSKKEARKEAVLLlLVGVGLPEEVLNRYPHELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491074476 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQG 234
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-252 |
1.37e-49 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 162.89 E-value: 1.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 8 VTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDGQLKvfdkkql 87
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVG------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 88 qllrtrltMVFQHFNLWSHMTVLENV---MEAPVQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRVSIA 164
Cdd:cd03296 78 --------FVFQHYALFRHMTVFDNVafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLAD-RYPAQLSGGQRQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNP 243
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
....*....
gi 491074476 244 KSPRLQQFL 252
Cdd:cd03296 229 ASPFVYSFL 237
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-240 |
3.95e-49 |
|
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: 162.14 E-value: 3.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDgqlkvfdkk 85
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVtallgpngsgKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 qlqlLRTRLTMVFQHFNLWSHMTVLENVMeapvqvLG----------LSKADaHERAVRYLDKVGIDE-RARgkyPVH-L 153
Cdd:COG1120 73 ----LARRIAYVPQEPPAPFGLTVRELVA------LGryphlglfgrPSAED-REAVEEALERTGLEHlADR---PVDeL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLA-EEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEE 232
Cdd:COG1120 139 SGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
|
....*...
gi 491074476 233 QGPPAELF 240
Cdd:COG1120 219 QGPPEEVL 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-227 |
4.44e-49 |
|
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: 161.10 E-value: 4.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGD----HEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDkdgqlkv 81
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 82 fdkkqlqllrtRLTMVFQHFNLWSHMTVLENVMeAPVQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRV 161
Cdd:cd03293 74 -----------DRGYVFQQDALLPWLTVLDNVA-LGLELQGVPKAEARERAEELLELVGLSGFEN-AYPHQLSGGMRQRV 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 162 SIARALAMEPEVLLFDEPTSALDP----ELVGEVLRImqkLAEEGKTMVVVTHEMEFARHVSNHVIFLHK 227
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDAltreQLQEELLDI---WRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-239 |
4.97e-49 |
|
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: 161.56 E-value: 4.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 8 VTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvfdkKQL 87
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR--------------KEP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 88 QLLRTRLTMVFQHFNLWSHMTVLENV-MEAPVQvlGLSKADAHERAVRYLDKVGIDERARGKYpVHLSGGQQQRVSIARA 166
Cdd:COG4555 70 REARRQIGVLPDERGLYDRLTVRENIrYFAELY--GLFDEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVALARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491074476 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAEL 239
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-252 |
6.08e-49 |
|
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: 161.31 E-value: 6.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 13 KRYGD-HEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMvrdkdgqlkvFDKKQLqllR 91
Cdd:cd03295 8 KRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE----------QDPVEL---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 92 TRLTMVFQHFNLWSHMTVLENVMEAPvQVLGLSKADAHERAVRYLDKVGIDERA-RGKYPVHLSGGQQQRVSIARALAME 170
Cdd:cd03295 75 RKIGYVIQQIGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 171 PEVLLFDEPTSALDP----ELVGEVLRIMQKLaeeGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKSP 246
Cdd:cd03295 154 PPLLLMDEPFGALDPitrdQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAND 230
|
....*.
gi 491074476 247 RLQQFL 252
Cdd:cd03295 231 FVAEFV 236
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-244 |
7.97e-49 |
|
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: 161.07 E-value: 7.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdGQLKVFDKK 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI-------TGLPPHEIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQLLRTrltmvFQHFNLWSHMTVLENVMEAPVQVLGLS---------KADAHERAVRYLDKVGIDERArgKYPVH-LSG 155
Cdd:cd03219 74 RLGIGRT-----FQIPRLFPELTVLENVMVAAQARTGSGlllararreEREARERAEELLERVGLADLA--DRPAGeLSY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGP 235
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
....*....
gi 491074476 236 PAELFGNPK 244
Cdd:cd03219 227 PDEVRNNPR 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-245 |
1.94e-48 |
|
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: 167.00 E-value: 1.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRY--GDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPS---EGSISLNNEDIRMVRDkdgqlk 80
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 81 vfdkkqlQLLRTRLTMVFQH----FNLwshMTVLENVMEAPvQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGG 156
Cdd:COG1123 79 -------ALRGRRIGMVFQDpmtqLNP---VTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLERRLD-RYPHQLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGP 235
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
250
....*....|
gi 491074476 236 PAELFGNPKS 245
Cdd:COG1123 227 PEEILAAPQA 236
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-246 |
3.94e-48 |
|
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: 161.76 E-value: 3.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRY----GDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCI-NFLEKP--SEGSISLNNEDIRMvrdkdgq 78
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETlglvgesgsgKSTLARAIlGLLPPPgiTSGEILFDGEDLLK------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 79 lkvFDKKQLQLLRTR-LTMVFQH----FNlwSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDERAR--GKYPV 151
Cdd:COG0444 75 ---LSEKELRKIRGReIQMIFQDpmtsLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERrlDRYPH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLI 230
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
250
....*....|....*.
gi 491074476 231 EEQGPPAELFGNPKSP 246
Cdd:COG0444 230 VEEGPVEELFENPRHP 245
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-251 |
4.95e-48 |
|
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: 162.51 E-value: 4.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlkvfdkk 85
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDI---------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 qlqllrTRLT-------MVFQHFNLWSHMTVLENVmEAPVQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQ 158
Cdd:TIGR03265 69 ------TRLPpqkrdygIVFQSYALFPNLTVADNI-AYGLKNRGMGRAEVAERVAELLDLVGLPGSER-KYPGQLSGGQQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 159 QRVSIARALAMEPEVLLFDEPTSALDPE----LVGEVLRIMQKLaeeGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQG 234
Cdd:TIGR03265 141 QRVALARALATSPGLLLLDEPLSALDARvrehLRTEIRQLQRRL---GVTTIMVTHDQEEALSMADRIVVMNHGVIEQVG 217
|
250
....*....|....*..
gi 491074476 235 PPAELFGNPKSPRLQQF 251
Cdd:TIGR03265 218 TPQEIYRHPATPFVADF 234
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
11-228 |
1.31e-47 |
|
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: 157.02 E-value: 1.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 11 LHKRY-GDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKdgqlkvfdkkQLQL 89
Cdd:TIGR02673 7 VSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGR----------QLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 90 LRTRLTMVFQHFNLWSHMTVLENVmEAPVQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRVSIARALAM 169
Cdd:TIGR02673 77 LRRRIGVVFQDFRLLPDRTVYENV-ALPLEVRGKKEREIQRRVGAALRQVGLEHKAD-AFPEQLSGGEQQRVAIARAIVN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491074476 170 EPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:TIGR02673 155 SPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-245 |
1.04e-46 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 155.47 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlkvfdkK 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI---------------T 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQLLRTRLTMVFQHFNLWSHMTVLENVMeAPVQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRVSIAR 165
Cdd:cd03300 66 NLPPHKRPVNTVFQNYALFPHLTVFENIA-FGLRLKKLPKAEIKERVAEALDLVQLEGYAN-RKPSQLSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 166 ALAMEPEVLLFDEPTSALDPELVGEV---LRIMQKlaEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGN 242
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMqleLKRLQK--ELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
...
gi 491074476 243 PKS 245
Cdd:cd03300 222 PAN 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6-244 |
7.82e-46 |
|
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: 153.66 E-value: 7.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAAN------------AGdvisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIrmvr 73
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVErgeivgligpngAG------------KTTLFNLITGFYRPTSGRILFDGRDI---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 74 dkdGQLKVFDKKQLQLLRTrltmvFQHFNLWSHMTVLENVMEAPVQVLGLS--------------KADAHERAVRYLDKV 139
Cdd:COG0411 69 ---TGLPPHRIARLGIART-----FQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreEREARERAEELLERV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 140 GIDERArGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMEFARHV 218
Cdd:COG0411 141 GLADRA-DEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGL 219
|
250 260
....*....|....*....|....*..
gi 491074476 219 SNHVIFLHKG-LIEEqGPPAELFGNPK 244
Cdd:COG0411 220 ADRIVVLDFGrVIAE-GTPAEVRADPR 245
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-240 |
2.32e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 152.17 E-value: 2.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDG--- 77
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFvaivgpngagKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGyvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 78 QLKVFDKkqlqllrtrltmvfqHFnlwsHMTVLENVMeapvqvLGL----------SKADaHERAVRYLDKVGIDERArg 147
Cdd:COG1121 82 QRAEVDW---------------DF----PITVRDVVL------MGRygrrglfrrpSRAD-REAVDEALERVGLEDLA-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 148 KYPV-HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLH 226
Cdd:COG1121 134 DRPIgELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLN 213
|
250
....*....|....
gi 491074476 227 KGLIEEqGPPAELF 240
Cdd:COG1121 214 RGLVAH-GPPEEVL 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-230 |
1.87e-44 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 147.54 E-value: 1.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlkvfdKK 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIygllgpngagKTTLIKIILGLLKPDSGEIKVLGKDI--------------KK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQLLRTRLTMVFQHFNLWSHMTVLENVmeapvqvlglskadaheravryldkvgiderargkypvHLSGGQQQRVSIAR 165
Cdd:cd03230 67 EPEEVKRRIGYLPEEPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQ 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491074476 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLI 230
Cdd:cd03230 109 ALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-238 |
2.12e-44 |
|
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: 149.51 E-value: 2.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGDHE----VLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkd 76
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 77 GQLkvfDKKQLQLLRTRLT-MVFQHFNLWSHMTVLENVMeAPVQVLGlsKADAHERAVRYLDKVGIDERArGKYPVHLSG 155
Cdd:COG4181 77 FAL---DEDARARLRARHVgFVFQSFQLLPTLTALENVM-LPLELAG--RRDARARARALLERVGLGHRL-DHYPAQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPElVGEvlRIMQKL----AEEGKTMVVVTHEMEFARHvSNHVIFLHKGLIE 231
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAA-TGE--QIIDLLfelnRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLV 225
|
....*..
gi 491074476 232 EQGPPAE 238
Cdd:COG4181 226 EDTAATA 232
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-228 |
2.38e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 148.43 E-value: 2.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlkvfDKK 85
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-------------SAM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQLLRTRLTMVFQHFNLWsHMTVLENvMEAPVQVLGlsKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIAR 165
Cdd:COG4619 68 PPPEWRRQVAYVPQEPALW-GGTVRDN-LPFPFQLRE--RKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491074476 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:COG4619 144 ALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-225 |
2.50e-43 |
|
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: 145.84 E-value: 2.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 8 VTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqLKVFDKKQL 87
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQET---------PPLNSKKAS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 88 QLLRTRLTMVFQHFNLWSHMTVLENVMEAPVQVlGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRVSIARAL 167
Cdd:TIGR03608 72 KFRREKLGYLFQNFALIENETVEENLDLGLKYK-KLSKKEKREKKKEALEKVGLNLKLK-QKIYELSGGEQQRVALARAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491074476 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARhVSNHVIFL 225
Cdd:TIGR03608 150 LKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAK-QADRVIEL 206
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
44-252 |
5.98e-43 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 145.67 E-value: 5.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDIRMVRDkdGQLKVfdkkqlqllrtrlTMVFQHFNLWSHMTVLENVmeapvqVLGL 123
Cdd:COG3840 38 KSTLLNLIAGFLPPDSGRILWNGQDLTALPP--AERPV-------------SMLFQENNLFPHLTVAQNI------GLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 124 SK-----ADAHERAVRYLDKVGIDERArGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL 198
Cdd:COG3840 97 RPglkltAEQRAQVEQALERVGLAGLL-DRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDEL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491074476 199 AEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKSPRLQQFL 252
Cdd:COG3840 176 CRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
13-253 |
4.14e-42 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 146.77 E-value: 4.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 13 KRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDgqlkvfdkkqlqllrT 92
Cdd:PRK10851 10 KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---------------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 93 RLTMVFQHFNLWSHMTVLENVmeapvqVLGLSKADAHER---------AVRYLDKVGIDERArGKYPVHLSGGQQQRVSI 163
Cdd:PRK10851 75 KVGFVFQHYALFRHMTVFDNI------AFGLTVLPRRERpnaaaikakVTQLLEMVQLAHLA-DRYPAQLSGGQKQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGK-TMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGN 242
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWRE 227
|
250
....*....|.
gi 491074476 243 PKSPRLQQFLS 253
Cdd:PRK10851 228 PATRFVLEFMG 238
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
44-243 |
1.32e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 144.61 E-value: 1.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLnnEDIRMVRDKDGQLKVFDK-----KQLQLLRTRLTMVFQ--HFNLWSHmTVLENVMEA 116
Cdd:PRK13631 65 KSTLVTHFNGLIKSKYGTIQV--GDIYIGDKKNNHELITNPyskkiKNFKELRRRVSMVFQfpEYQLFKD-TIEKDIMFG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 117 PVqVLGLSKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQ 196
Cdd:PRK13631 142 PV-ALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIL 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491074476 197 KLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNP 243
Cdd:PRK13631 221 DAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
44-243 |
2.08e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 143.24 E-value: 2.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDIRMVRDKdgqlkvfdkKQLQLLRTRLTMVFQ--HFNLWSHmTVLENVMEAPvQVL 121
Cdd:PRK13634 46 KSTLLQHLNGLLQPTSGTVTIGERVITAGKKN---------KKLKPLRKKVGIVFQfpEHQLFEE-TVEKDICFGP-MNF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 122 GLSKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AE 200
Cdd:PRK13634 115 GVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKE 194
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491074476 201 EGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNP 243
Cdd:PRK13634 195 KGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-253 |
3.65e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 143.30 E-value: 3.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 20 VLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDGQLKVFDK-----------KQLQ 88
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKlviqktrfkkiKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 89 LLRTRLTMVFQ--HFNLWSHmTVLENVMEAPVQvLGLSKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARA 166
Cdd:PRK13651 102 EIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVS-MGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPK-- 244
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDNKfl 259
|
250
....*....|....*
gi 491074476 245 ------SPRLQQFLS 253
Cdd:PRK13651 260 iennmePPKLLNFVN 274
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
44-253 |
5.27e-41 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 143.33 E-value: 5.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdGQLkvfDKKQLQLLRTRLTMVFQH----FNlwSHMTVLENVMEaPVQ 119
Cdd:COG4608 57 KSTLGRLLLRLEEPTSGEILFDGQDI-------TGL---SGRELRPLRRRMQMVFQDpyasLN--PRMTVGDIIAE-PLR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 120 VLGL-SKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL 198
Cdd:COG4608 124 IHGLaSKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491074476 199 AEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKSPRLQQFLS 253
Cdd:COG4608 204 QDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPYTQALLS 259
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-256 |
2.31e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 139.66 E-value: 2.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 4 NKLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFL-----EKPSEGSISLNNEDIRmvrdkdgq 78
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIF-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 79 lkvfdKKQLQLLRTRLTMVFQHFNLWSHMTVLENVMEAP-VQVLGLSKADAHERAVRYLDKVGIDERARGKYPV---HLS 154
Cdd:PRK14247 74 -----KMDVIELRRRVQMVFQIPNPIPNLSIFENVALGLkLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDApagKLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQG 234
Cdd:PRK14247 149 GGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
250 260
....*....|....*....|..
gi 491074476 235 PPAELFGNPKSPRLQQFLSGAL 256
Cdd:PRK14247 228 PTREVFTNPRHELTEKYVTGRL 249
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
44-257 |
2.52e-40 |
|
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: 145.60 E-value: 2.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEkPSEGSISLNNEDIrmvrdkDGqlkvFDKKQLQLLRTRLTMVFQ----HFNlwSHMTVLENVMEaPVQ 119
Cdd:COG4172 325 KSTLGLALLRLI-PSEGEIRFDGQDL------DG----LSRRALRPLRRRMQVVFQdpfgSLS--PRMTVGQIIAE-GLR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 120 VL--GLSKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQK 197
Cdd:COG4172 391 VHgpGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRD 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491074476 198 L-AEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKSPRLQQFLSGALK 257
Cdd:COG4172 471 LqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPL 531
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
44-242 |
2.79e-40 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 139.87 E-value: 2.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvfDKKQLQLLRTRLTMVFQH-FNLWSHMTV-------LENvme 115
Cdd:TIGR04520 41 KSTLAKLLNGLLLPTSGKVTVDGLDTL------------DEENLWEIRKKVGMVFQNpDNQFVGATVeddvafgLEN--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 116 apvqvLGLSKADAHERAVRYLDKVGIDErARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIM 195
Cdd:TIGR04520 106 -----LGVPREEMRKRVDEALKLVGMED-FRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491074476 196 QKL-AEEGKTMVVVTHEMEFARHvSNHVIFLHKGLIEEQGPPAELFGN 242
Cdd:TIGR04520 180 RKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-228 |
3.35e-40 |
|
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: 136.22 E-value: 3.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 8 VTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvfdKKQL 87
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA-------------KLPL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 88 QLLRTRLTMVFQhfnlwshmtvlenvmeapvqvlglskadaheravryldkvgiderargkypvhLSGGQQQRVSIARAL 167
Cdd:cd00267 69 EELRRRIGYVPQ-----------------------------------------------------LSGGQRQRVALARAL 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491074476 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:cd00267 96 LLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
10-230 |
4.40e-40 |
|
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: 137.92 E-value: 4.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 10 ELHKRY-GDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRdkdgqlkvfdKKQLQ 88
Cdd:cd03292 5 NVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLR----------GRAIP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 89 LLRTRLTMVFQHFNLWSHMTVLENVMeAPVQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRVSIARALA 168
Cdd:cd03292 75 YLRRKIGVVFQDFRLLPDRNVYENVA-FALEVTGVPPREIRKRVPAALELVGLSHKHR-ALPAELSGGEQQRVAIARAIV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491074476 169 MEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLI 230
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-255 |
8.24e-40 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 141.01 E-value: 8.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 13 KRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDI--RMVRDKDgqlkvfdkkqlqll 90
Cdd:PRK11432 14 KRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRD-------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 91 rtrLTMVFQHFNLWSHMTVLENVmEAPVQVLGLSKADAHER---AVRYLDKVGIDERargkYPVHLSGGQQQRVSIARAL 167
Cdd:PRK11432 80 ---ICMVFQSYALFPHMSLGENV-GYGLKMLGVPKEERKQRvkeALELVDLAGFEDR----YVDQISGGQQQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 168 AMEPEVLLFDEPTSALDPEL---VGEVLRIMQKlaEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPK 244
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLrrsMREKIRELQQ--QFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
250
....*....|.
gi 491074476 245 SPRLQQFLSGA 255
Cdd:PRK11432 230 SRFMASFMGDA 240
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-239 |
9.33e-39 |
|
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: 134.48 E-value: 9.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvfDKK 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT------------GLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQLLRTRLTMVFQHFNLWSHMTVLENVMeapVQVLGLSKADAHERavryLDKV-----GIDERaRGKYPVHLSGGQQQR 160
Cdd:cd03224 69 PHERARAGIGYVPEGRRIFPELTVEENLL---LGAYARRRAKRKAR----LERVyelfpRLKER-RKQLAGTLSGGEQQM 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491074476 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAEL 239
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
13-254 |
1.18e-38 |
|
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: 138.06 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 13 KRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrMVRDKDgQLKvfdkkqlQLLRT 92
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENI-MKQSPV-ELR-------EVRRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 93 RLTMVFQHFNLWSHMTVLENVMEAPvQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRVSIARALAMEPE 172
Cdd:TIGR01186 72 KIGMVFQQFALFPHMTILQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEH-RYPDELSGGMQQRVGLARALAAEPD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 173 VLLFDEPTSALDP----ELVGEVLRIMQKLaeeGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKSPRL 248
Cdd:TIGR01186 150 ILLMDEAFSALDPlirdSMQDELKKLQATL---QKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYV 226
|
....*.
gi 491074476 249 QQFLSG 254
Cdd:TIGR01186 227 EEFIGK 232
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-247 |
5.03e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 134.05 E-value: 5.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGD-HEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvFDK 84
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-----------YDK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 85 KQLQLLRTRLTMVFQHFN--LWSHmTVLENVMEAPVQvLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRVS 162
Cdd:PRK13639 71 KSLLEVRKTVGIVFQNPDdqLFAP-TVEEDVAFGPLN-LGLSKEEVEKRVKEALKAVGMEGFEN-KPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGN 242
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
....*
gi 491074476 243 PKSPR 247
Cdd:PRK13639 228 IETIR 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-230 |
7.95e-38 |
|
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: 131.89 E-value: 7.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 14 RYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDG---QLKVFDkkqlqll 90
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGyvpQRRSID------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 91 RTrltmvfqhFNLwshmTVLENVMEAPVQVLGL----SKADAhERAVRYLDKVGIDERArgKYPV-HLSGGQQQRVSIAR 165
Cdd:cd03235 81 RD--------FPI----SVRDVVLMGLYGHKGLfrrlSKADK-AKVDEALERVGLSELA--DRQIgELSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491074476 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLI 230
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
20-228 |
8.00e-38 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 132.15 E-value: 8.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 20 VLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKdgqlkvfdkKQLQLLRTRLTMVFQ 99
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYS---------QKIILRRELIGYIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 100 HFNLWSHMTVLENVmEAPVQVLGLSKADAHERAVRYLDKVGIDERaRGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
Cdd:NF038007 91 SFNLIPHLSIFDNV-ALPLKYRGVAKKERIERVNQVLNLFGIDNR-RNHKPMQLSGGQQQRVAIARAMVSNPALLLADEP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491074476 180 TSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHvSNHVIFLHKG 228
Cdd:NF038007 169 TGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDEASTY-GNRIINMKDG 216
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-234 |
9.24e-38 |
|
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: 131.61 E-value: 9.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 13 KRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDgqlkvfdkkqlqllrT 92
Cdd:cd03301 8 KRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---------------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 93 RLTMVFQHFNLWSHMTVLENvMEAPVQVLGLSKADAHERAVRYLDKVGIDERArGKYPVHLSGGQQQRVSIARALAMEPE 172
Cdd:cd03301 73 DIAMVFQNYALYPHMTVYDN-IAFGLKLRKVPKDEIDERVREVAELLQIEHLL-DRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491074476 173 VLLFDEPTSALDP----ELVGEVLRIMQKLaeeGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQG 234
Cdd:cd03301 151 VFLMDEPLSNLDAklrvQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
44-242 |
9.93e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 133.63 E-value: 9.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvfDKK-QLQLLRTRLTMVFQH--FNLWSHmTVLENVMEAPVQv 120
Cdd:PRK13637 46 KSTLIQHLNGLLKPTSGKIIIDGVDIT------------DKKvKLSDIRKKVGLVFQYpeYQLFEE-TIEKDIAFGPIN- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 121 LGLSKADAHERAVRYLDKVGID-ERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLA 199
Cdd:PRK13637 112 LGLSEEEIENRVKRAMNIVGLDyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELH 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491074476 200 EEGK-TMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGN 242
Cdd:PRK13637 192 KEYNmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-244 |
1.27e-37 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 135.46 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENK--LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDGQ 78
Cdd:PRK09452 8 PSSLSplVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 79 LKVfdkkqlqllrtrltmVFQHFNLWSHMTVLENVMEApvqvLGLSKADAHERAVRYLDK---VGIDERARGKyPVHLSG 155
Cdd:PRK09452 88 VNT---------------VFQSYALFPHMTVFENVAFG----LRMQKTPAAEITPRVMEAlrmVQLEEFAQRK-PHQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEV---LRIMQKlaEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEE 232
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMqneLKALQR--KLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQ 225
|
250
....*....|..
gi 491074476 233 QGPPAELFGNPK 244
Cdd:PRK09452 226 DGTPREIYEEPK 237
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
44-250 |
1.30e-37 |
|
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: 135.23 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDIRmvrdkDGQLKVFdkkqLQLLRTRLTMVFQHFNLWSHMTVLENVMeapvqvLGL 123
Cdd:COG4148 38 KTTLLRAIAGLERPDSGRIRLGGEVLQ-----DSARGIF----LPPHRRRIGYVFQEARLFPHLSVRGNLL------YGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 124 SKADAHERAVRyLDKV----GID---ERargkYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQ 196
Cdd:COG4148 103 KRAPRAERRIS-FDEVvellGIGhllDR----RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491074476 197 KLAEEGKT-MVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKSPRLQQ 250
Cdd:COG4148 178 RLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-254 |
1.79e-37 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 132.21 E-value: 1.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFL-----EKPSEGSISLNNEDIRMVRDK 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 76 DGQLkvfdkkqlqllRTRLTMVFQHFNLWShMTVLENVmeapvqVLGLSKADAHERAVryLDKVgIDERARG-------K 148
Cdd:PRK14239 81 TVDL-----------RKEIGMVFQQPNPFP-MSIYENV------VYGLRLKGIKDKQV--LDEA-VEKSLKGasiwdevK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 149 YPVH-----LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMEFARHVSNHVI 223
Cdd:PRK14239 140 DRLHdsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTG 218
|
250 260 270
....*....|....*....|....*....|.
gi 491074476 224 FLHKGLIEEQGPPAELFGNPKSPRLQQFLSG 254
Cdd:PRK14239 219 FFLDGDLIEYNDTKQMFMNPKHKETEDYISG 249
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-253 |
1.93e-37 |
|
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: 131.69 E-value: 1.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEvLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlkvfdkK 85
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI---------------T 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQLLRTRLTMVFQHFNLWSHMTVLENVmEAPVQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRVSIAR 165
Cdd:cd03299 65 NLPPEKRDISYVPQNYALFPHMTVYKNI-AYGLKKRKVDKKEIERKVLEIAEMLGIDHLLN-RKPETLSGGEQQRVAIAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVV-VTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPK 244
Cdd:cd03299 143 ALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
....*....
gi 491074476 245 SPRLQQFLS 253
Cdd:cd03299 223 NEFVAEFLG 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-256 |
2.69e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 131.89 E-value: 2.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 3 ENKLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLekpsegsISLNnEDIRMvrdkDGQLKVF 82
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRL-------LELN-EEARV----EGEVRLF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 83 DKKQLQL------LRTRLTMVFQHFNLWSHMTVLENV-MEAPVQVLGLSKADAHERAVRYLDKVGIDERARGK---YPVH 152
Cdd:PRK14267 70 GRNIYSPdvdpieVRREVGMVFQYPNPFPHLTIYDNVaIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRlndYPSN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMEFARHVSNHVIFLHKGLIEE 232
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
250 260
....*....|....*....|....
gi 491074476 233 QGPPAELFGNPKSPRLQQFLSGAL 256
Cdd:PRK14267 229 VGPTRKVFENPEHELTEKYVTGAL 252
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-254 |
6.33e-37 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 137.55 E-value: 6.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 19 EVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlKVFDKKQL-QLLRTRLTMV 97
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDV----------ATLDADALaQLRREHFGFI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 98 FQHFNLWSHMTVLENVmEAPVQVLGLSKADAHERAVRYLDKVGIDERArGKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
Cdd:PRK10535 92 FQRYHLLSHLTAAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLEDRV-EYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 178 EPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHvSNHVIFLHKGLI--------EEQGPPAELFGNPKSPRLQ 249
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIvrnppaqeKVNVAGGTEPVVNTASGWR 248
|
....*
gi 491074476 250 QFLSG 254
Cdd:PRK10535 249 QFVSG 253
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
44-253 |
2.19e-36 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 131.24 E-value: 2.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDirmvrdkdgqLKVFDKKQLQLLRTRLTMVFQ--HFNLWSHMTVlENVMEAPVQV- 120
Cdd:PRK11308 54 KSTLARLLTMIETPTGGELYYQGQD----------LLKADPEAQKLLRQKIQIVFQnpYGSLNPRKKV-GQILEEPLLIn 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 121 LGLSKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAE 200
Cdd:PRK11308 123 TSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQ 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491074476 201 E-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKSPRLQQFLS 253
Cdd:PRK11308 203 ElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLS 256
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-239 |
3.57e-36 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 135.73 E-value: 3.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 14 RYGDHE--VLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIRMVRdkdgqlkvfdkkqLQLLR 91
Cdd:COG2274 482 RYPGDSppVLDNISLTIKPGERvaivgrsgsgKSTLLKLLLGLYEPTSGRILIDGIDLRQID-------------PASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 92 TRLTMVFQHFNLWShMTVLENVmeapvqVLGLSKADaHERAVRYLDKVGID---------------ERARGkypvhLSGG 156
Cdd:COG2274 549 RQIGVVLQDVFLFS-GTIRENI------TLGDPDAT-DEEIIEAARLAGLHdfiealpmgydtvvgEGGSN-----LSGG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMEFARHVsNHVIFLHKGLIEEQGPP 236
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDGTH 693
|
...
gi 491074476 237 AEL 239
Cdd:COG2274 694 EEL 696
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-215 |
4.25e-36 |
|
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: 126.77 E-value: 4.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 16 GDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvFDKKQLQLLRTRLT 95
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLD-----------YSRKGLLERRQRVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 96 MVFQHFN--LWShMTVLENVMEAPVQvLGLSKADAHERAVRYLDKVGIDErARGKYPVHLSGGQQQRVSIARALAMEPEV 173
Cdd:TIGR01166 72 LVFQDPDdqLFA-ADVDQDVAFGPLN-LGLSEAEVERRVREALTAVGASG-LRERPTHCLSGGEKKRVAIAGAVAMRPDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491074476 174 LLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFA 215
Cdd:TIGR01166 149 LLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-244 |
7.00e-36 |
|
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: 127.41 E-value: 7.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdGQLKVFdkk 85
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIvallgrngagKTTLLKAISGLLPPRSGSIRFDGEDI-------TGLPPH--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 qlQLLRTRLTMVFQHFNLWSHMTVLENVMeapvqvLGLSKADAHERAVRYLDKVG-----IDERAR---GkypvHLSGGQ 157
Cdd:COG0410 74 --RIARLGIGYVPEGRRIFPSLTVEENLL------LGAYARRDRAEVRADLERVYelfprLKERRRqraG----TLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPA 237
Cdd:COG0410 142 QQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAA 221
|
....*..
gi 491074476 238 ELFGNPK 244
Cdd:COG0410 222 ELLADPE 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-246 |
7.52e-36 |
|
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: 133.27 E-value: 7.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGD----HEVLKGVSLAANAGDVISIIGSSGSGKS-TFLRCINFLEKPS---EGSISLNNEDIrmv 72
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 73 rdkdgqLKvFDKKQLQLLR-TRLTMVFQH----FNlwSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDERAR- 146
Cdd:COG4172 79 ------LG-LSERELRRIRgNRIAMIFQEpmtsLN--PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERr 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 147 -GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMEFARHVSNHVIF 224
Cdd:COG4172 150 lDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAV 229
|
250 260
....*....|....*....|..
gi 491074476 225 LHKGLIEEQGPPAELFGNPKSP 246
Cdd:COG4172 230 MRQGEIVEQGPTAELFAAPQHP 251
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
44-240 |
3.17e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 127.17 E-value: 3.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLN---------NEDIRMVRDKDGQLKVFDKKQLqllrtrltmvFQHfnlwshmTVLENVM 114
Cdd:PRK13649 46 KSTIMQLLNGLHVPTQGSVRVDdtlitstskNKDIKQIRKKVGLVFQFPESQL----------FEE-------TVLKDVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 115 EAPvQVLGLSKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRI 194
Cdd:PRK13649 109 FGP-QNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491074476 195 MQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELF 240
Cdd:PRK13649 188 FKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-239 |
6.43e-35 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 131.44 E-value: 6.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 14 RY-GDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDgqlkvfdkkqlqlLRT 92
Cdd:COG1132 348 SYpGDRPVLKDISLTIPPGETvalvgpsgsgKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES-------------LRR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 93 RLTMVFQHFNLWsHMTVLEN------------VMEApvqvlgLSKADAHERaVRYLDKvGIDER--ARGkypVHLSGGQQ 158
Cdd:COG1132 415 QIGVVPQDTFLF-SGTIRENirygrpdatdeeVEEA------AKAAQAHEF-IEALPD-GYDTVvgERG---VNLSGGQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMEFARHVsNHVIFLHKGLIEEQGPPAE 238
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRNA-DRILVLDDGRIVEQGTHEE 560
|
.
gi 491074476 239 L 239
Cdd:COG1132 561 L 561
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-234 |
1.11e-34 |
|
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: 122.54 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 7 AVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvfDKKQ 86
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA------------SLSP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 87 LQLLRtrltmvfqhfnlwsHMTVLENVMEApVQVLGLSKadaheravRYLDkvgiderargkypvHLSGGQQQRVSIARA 166
Cdd:cd03214 69 KELAR--------------KIAYVPQALEL-LGLAHLAD--------RPFN--------------ELSGGERQRVLLARA 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491074476 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQKLA-EEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQG 234
Cdd:cd03214 112 LAQEPPILLLDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
44-181 |
1.23e-34 |
|
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: 121.60 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvfdKKQLQLLRTRLTMVFQHFNLWSHMTVLENVMEaPVQVLGL 123
Cdd:pfam00005 24 KSTLLKLIAGLLSPTEGTILLDGQDLT-------------DDERKSLRKEIGYVFQDPQLFPRLTVRENLRL-GLLLKGL 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491074476 124 SKADAHERAVRYLDKVGIDERAR---GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTS 181
Cdd:pfam00005 90 SKREKDARAEEALEKLGLGDLADrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
13-239 |
1.60e-34 |
|
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: 125.58 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 13 KRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmVRDKDGqlkvfdkkqlqlLRT 92
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV--VREPRK------------VRR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 93 RLTMVFQHFNLWSHMTVLENvMEAPVQVLGLSKADAHERAVRYLDKVGIDErARGKYPVHLSGGQQQRVSIARALAMEPE 172
Cdd:TIGR01188 67 SIGIVPQYASVDEDLTGREN-LEMMGRLYGLPKDEAEERAEELLELFELGE-AADRPVGTYSGGMRRRLDIAASLIHQPD 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491074476 173 VLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAEL 239
Cdd:TIGR01188 145 VLFLDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
44-245 |
1.67e-34 |
|
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: 126.45 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDIRMVRDKdgqlkvfdkkqlqllRTRLTMVFQHFNLWSHMTVLENVmEAPVQVLGL 123
Cdd:TIGR01187 9 KTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH---------------LRHINMVFQSYALFPHMTVEENV-AFGLKMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 124 SKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVG----EVLRIMQKLa 199
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQLEEFAD-RKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDqmqlELKTIQEQL- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491074476 200 eeGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKS 245
Cdd:TIGR01187 151 --GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPAN 194
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-228 |
2.12e-34 |
|
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: 121.72 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 11 LHKRYGD--HEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIRMVrdkdgqlkvfdkkQLQ 88
Cdd:cd03228 6 VSFSYPGrpKPVLKDVSLTIKPGEKvaivgpsgsgKSTLLKLLLRLYDPTSGEILIDGVDLRDL-------------DLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 89 LLRTRLTMVFQHFNLWShMTVLENVmeapvqvlglskadaheravryldkvgiderargkypvhLSGGQQQRVSIARALA 168
Cdd:cd03228 73 SLRKNIAYVPQDPFLFS-GTIRENI---------------------------------------LSGGQRQRIAIARALL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 169 MEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMEFARHVsNHVIFLHKG 228
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRDA-DRIIVLDDG 170
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-254 |
4.42e-34 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 126.69 E-value: 4.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 21 LKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlKVFDKKQLQLLRTRLTMVFQH 100
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIA---------KISDAELREVRRKKIAMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 101 FNLWSHMTVLENVMEApVQVLGLSKADAHERAVRYLDKVGIDERARGkYPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
Cdd:PRK10070 115 FALMPHMTVLDNTAFG-MELAGINAEERREKALDALRQVGLENYAHS-YPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491074476 181 SALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKSPRLQQFLSG 254
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-239 |
7.11e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 127.44 E-value: 7.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDGQlkvfdkk 85
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVhallgengagKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQ------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 qlqllRTRLTMVFQHFNLWSHMTVLENVM--EAPVQVLGLSKADAHERAVRYLDKVGIDERARGkyPV-HLSGGQQQRVS 162
Cdd:COG1129 78 -----AAGIAIIHQELNLVPNLSVAENIFlgREPRRGGLIDWRAMRRRARELLARLGLDIDPDT--PVgDLSVAQQQLVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491074476 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAEL 239
Cdd:COG1129 151 IARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
44-244 |
4.52e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 121.47 E-value: 4.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDIRMVRDKdgqlkvfdkKQLQLLRTRLTMVFQ--HFNLWSHmTVLENVMEAPVQvL 121
Cdd:PRK13641 46 KSTLMQHFNALLKPSSGTITIAGYHITPETGN---------KNLKKLRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKN-F 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 122 GLSKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE 201
Cdd:PRK13641 115 GFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA 194
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491074476 202 GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPK 244
Cdd:PRK13641 195 GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-228 |
1.36e-32 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 118.44 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 10 ELHKRY-GDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRdkdgqlkvfdKKQLQ 88
Cdd:PRK10908 6 HVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLK----------NREVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 89 LLRTRLTMVFQHFNLWSHMTVLENVmEAPVQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRVSIARALA 168
Cdd:PRK10908 76 FLRRQIGMIFQDHHLLMDRTVYDNV-AIPLIIAGASGDDIRRRVSAALDKVGLLDKAK-NFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 169 MEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-239 |
3.08e-32 |
|
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: 123.71 E-value: 3.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGD-HEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCI-NFLEkPSEGSISLNNEDIRMVRDKDgqlkvfd 83
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLlGFLP-PYSGSILINGVDLSDLDPAS------- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 84 kkqlqlLRTRLTMVFQH---FnlwsHMTVLENvmeapvqvLGLSKADAHERAVRY-LDKVGID---------------ER 144
Cdd:COG4988 409 ------WRRQIAWVPQNpylF----AGTIREN--------LRLGRPDASDEELEAaLEAAGLDefvaalpdgldtplgEG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 145 ARGkypvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMEFARHvSNHVIF 224
Cdd:COG4988 471 GRG-----LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILV 543
|
250
....*....|....*
gi 491074476 225 LHKGLIEEQGPPAEL 239
Cdd:COG4988 544 LDDGRIVEQGTHEEL 558
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
20-256 |
3.83e-32 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 118.75 E-value: 3.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 20 VLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDirmvrdkdgqLKVFDKKQLQLLRTRLTMVFQ 99
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQD----------LYQLDRKQRRAFRRDVQLVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 100 H----FNlwSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
Cdd:TIGR02769 96 DspsaVN--PRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 176 FDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNpKSPRLQQFLSG 254
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF-KHPAGRNLQSA 252
|
..
gi 491074476 255 AL 256
Cdd:TIGR02769 253 VL 254
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-253 |
5.00e-32 |
|
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: 117.24 E-value: 5.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdGQLKVFDkk 85
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDI-------TKLPPHE-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 qlqllRTRLTM--VFQHFNLWSHMTVLENVMeapvqvLGLSKADAHERAvryldkvgIDERARGKYPV----------HL 153
Cdd:TIGR03410 72 -----RARAGIayVPQGREIFPRLTVEENLL------TGLAALPRRSRK--------IPDEIYELFPVlkemlgrrggDL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGK-TMVVVTHEMEFARHVSNHVIFLHKGLIEE 232
Cdd:TIGR03410 133 SGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVA 212
|
250 260
....*....|....*....|.
gi 491074476 233 QGPPAELfgnpKSPRLQQFLS 253
Cdd:TIGR03410 213 SGAGDEL----DEDKVRRYLA 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-240 |
5.08e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 118.80 E-value: 5.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGD-HEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgql 79
Cdd:PRK13636 1 MEDYILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 80 kvFDKKQLQLLRTRLTMVFQH--FNLWShMTVLENVMEAPVQvLGLSKADAHERAVRYLDKVGIdERARGKyPVH-LSGG 156
Cdd:PRK13636 72 --YSRKGLMKLRESVGMVFQDpdNQLFS-ASVYQDVSFGAVN-LKLPEDEVRKRVDNALKRTGI-EHLKDK-PTHcLSFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGP 235
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN 225
|
....*
gi 491074476 236 PAELF 240
Cdd:PRK13636 226 PKEVF 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-239 |
5.81e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 118.67 E-value: 5.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLA-----------AN-AGdvisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIRM-V 72
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTvpkgeifgllgPNgAG------------KTTTIRIILGILAPDSGEVLWDGEPLDPeD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 73 RDKDGQLkvfdkkqlqlLRTRltmvfqhfNLWSHMTVLEnvmeapvQVL------GLSKADAHERAVRYLDKVGIDERAr 146
Cdd:COG4152 70 RRRIGYL----------PEER--------GLYPKMKVGE-------QLVylarlkGLSKAEAKRRADEWLERLGLGDRA- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 147 gKYPVH-LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFL 225
Cdd:COG4152 124 -NKKVEeLSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVII 202
|
250
....*....|....
gi 491074476 226 HKGLIEEQGPPAEL 239
Cdd:COG4152 203 NKGRKVLSGSVDEI 216
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
11-248 |
5.99e-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: 120.22 E-value: 5.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 11 LHKRYGDHEVlkGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdKDGQLKVFdkkqLQLL 90
Cdd:TIGR02142 5 FSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL-----FDSRKGIF----LPPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 91 RTRLTMVFQHFNLWSHMTVLENVmeapvqVLGLSKADAHERAVRY---LDKVGIDERARgKYPVHLSGGQQQRVSIARAL 167
Cdd:TIGR02142 74 KRRIGYVFQEARLFPHLSVRGNL------RYGMKRARPSERRISFervIELLGIGHLLG-RLPGRLSGGEKQRVAIGRAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKSP 246
Cdd:TIGR02142 147 LSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLP 226
|
..
gi 491074476 247 RL 248
Cdd:TIGR02142 227 WL 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-253 |
2.82e-31 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 120.97 E-value: 2.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 11 LHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKST----FLRCINflekpSEGSISLnnedirmvrdkDGQ-LKVFDKK 85
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWF-----------DGQpLHNLNRR 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQLLRTRLTMVFQHFN--LWSHMTVLENVMEA-PVQVLGLSKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQRVS 162
Cdd:PRK15134 356 QLLPVRHRIQVVFQDPNssLNPRLNVLQIIEEGlRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGK-TMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFG 241
Cdd:PRK15134 436 IARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFA 515
|
250
....*....|..
gi 491074476 242 NPKSPRLQQFLS 253
Cdd:PRK15134 516 APQQEYTRQLLA 527
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-238 |
4.44e-31 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 115.60 E-value: 4.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvfDKK 85
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLA------------AWS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQLLRTRLTMVfQHfnlwSHM----TVLENVMeapvqvLGL-----SKADAHERAVRYLDKVGIDERARGKYPvHLSGG 156
Cdd:COG4559 70 PWELARRRAVLP-QH----SSLafpfTVEEVVA------LGRaphgsSAAQDRQIVREALALVGLAHLAGRSYQ-TLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 157 QQQRVSIARALA-------MEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGL 229
Cdd:COG4559 138 EQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGR 217
|
....*....
gi 491074476 230 IEEQGPPAE 238
Cdd:COG4559 218 LVAQGTPEE 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-219 |
5.03e-31 |
|
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: 114.11 E-value: 5.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKdgqlkvfdkk 85
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEAlaltgpngsgKTTLLRILAGLLPPSAGEVLWNGEPIRDARED---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 qlqlLRTRLTMVFQHFNLWSHMTVLENVmEAPVQVLGLSKADAHERAVryLDKVGIDERARgKYPVHLSGGQQQRVSIAR 165
Cdd:COG4133 73 ----YRRRLAYLGHADGLKPELTVRENL-RFWAALYGLRADREAIDEA--LEAVGLAGLAD-LPVRQLSAGQKRRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491074476 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTH---EMEFARHVS 219
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqplELAAARVLD 201
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-234 |
5.33e-31 |
|
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: 114.21 E-value: 5.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVS----------LAAN-AGdvisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIRmvrd 74
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSltlgpgmyglLGPNgAG------------KTTLMRILATLTPPSSGTIRIDGQDVL---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 75 kdgqlkvfdkKQLQLLRTRLTMVFQHFNLWSHMTVLENVmeAPVQVL-GLSKADAHERAVRYLDKVGIDERArGKYPVHL 153
Cdd:cd03264 65 ----------KQPQKLRRRIGYLPQEFGVYPNFTVREFL--DYIAWLkGIPSKEVKARVDEVLELVNLGDRA-KKKIGSL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQ 233
Cdd:cd03264 132 SGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
.
gi 491074476 234 G 234
Cdd:cd03264 211 G 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-244 |
5.85e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 115.60 E-value: 5.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 3 ENKLAVTELHKRYGD-HEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlkv 81
Cdd:PRK13647 2 DNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 82 fDKKQLQLLRTRLTMVFQHFN--LWShMTVLENVMEAPVQvLGLSKADAHERAVRYLDKVGIdERARGKYPVHLSGGQQQ 159
Cdd:PRK13647 70 -NAENEKWVRSKVGLVFQDPDdqVFS-STVWDDVAFGPVN-MGLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPaEL 239
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SL 224
|
....*
gi 491074476 240 FGNPK 244
Cdd:PRK13647 225 LTDED 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-239 |
8.48e-31 |
|
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: 114.00 E-value: 8.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 8 VTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmVRDKDGqlkvfdkkql 87
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV--VREPRE---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 88 qlLRTRLTMVFQHFNLWSHMTVLENV-MEAPVQvlGLSKADAHERAVRYLDKVGIDErARGKYPVHLSGGQQQRVSIARA 166
Cdd:cd03265 71 --VRRRIGIVFQDLSVDDELTGWENLyIHARLY--GVPGAERRERIDELLDFVGLLE-AADRLVKTYSGGMRRRLEIARS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491074476 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAEL 239
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
44-240 |
1.23e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 115.22 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNneDIRMVRDKDgqlkvfdKKQLQLLRTRLTMVFQ--HFNLWSHmTVLENVMEAPvQVL 121
Cdd:PRK13643 45 KSTLLQHLNGLLQPTEGKVTVG--DIVVSSTSK-------QKEIKPVRKKVGVVFQfpESQLFEE-TVLKDVAFGP-QNF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 122 GLSKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE 201
Cdd:PRK13643 114 GIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS 193
|
170 180 190
....*....|....*....|....*....|....*....
gi 491074476 202 GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELF 240
Cdd:PRK13643 194 GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-215 |
1.53e-30 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 114.19 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSEnkLAVTELHKRYG----DHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDI------R 70
Cdd:COG4525 1 MSM--LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgadR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 71 MVrdkdgqlkvfdkkqlqllrtrltmVFQHFNLWSHMTVLENVmEAPVQVLGLSKADAHERAVRYLDKVGIDERARgKYP 150
Cdd:COG4525 79 GV------------------------VFQKDALLPWLNVLDNV-AFGLRLRGVPKAERRARAEELLALVGLADFAR-RRI 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpELVGEVlriMQKL-----AEEGKTMVVVTHEMEFA 215
Cdd:COG4525 133 WQLSGGMRQRVGIARALAADPRFLLMDEPFGALD-ALTREQ---MQELlldvwQRTGKGVFLITHSVEEA 198
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-250 |
2.32e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 114.01 E-value: 2.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDH---------EVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkd 76
Cdd:PRK10419 4 LNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPL------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 77 GQLkvfDKKQLQLLRTRLTMVFQH----FNlwSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDERARGKYPVH 152
Cdd:PRK10419 77 AKL---NRAQRKAFRRDIQMVFQDsisaVN--PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKT-MVVVTHEMEFARHVSNHVIFLHKGLIE 231
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQIV 231
|
250 260
....*....|....*....|.
gi 491074476 232 EQGPPAEL--FGNPKSPRLQQ 250
Cdd:PRK10419 232 ETQPVGDKltFSSPAGRVLQN 252
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-228 |
2.68e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.82 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGDHEVLKGVSLAAN------------AGdvisiigssgsgKSTFLRCINFLEKPSEGSISLNNED 68
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRpgeihallgengAG------------KSTLMKILYGLYQPDSGEILIDGKP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 69 IRMVRDKDGqlkvfdkkqlqlLRTRLTMVFQHFNLWSHMTVLENVM--EAPVQVLGLSKADAHERAVRYLDKVG--IDER 144
Cdd:COG3845 69 VRIRSPRDA------------IALGIGMVHQHFMLVPNLTVAENIVlgLEPTKGGRLDRKAARARIRELSERYGldVDPD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 145 ARgkypVH-LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVI 223
Cdd:COG3845 137 AK----VEdLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVT 212
|
....*
gi 491074476 224 FLHKG 228
Cdd:COG3845 213 VLRRG 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
44-234 |
3.66e-30 |
|
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: 112.00 E-value: 3.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNedirmVRDKDGQLKVFDKKQlqllRTRLTMVFQHFNLWSHMTVLENVmeapvqVLGL 123
Cdd:cd03297 36 KSTLLRCIAGLEKPDGGTIVLNG-----TVLFDSRKKINLPPQ----QRKIGLVFQQYALFPHLNVRENL------AFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 124 SKADAHERAVRY---LDKVGIDERARgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAE 200
Cdd:cd03297 101 KRKRNREDRISVdelLDLLGLDHLLN-RYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....*
gi 491074476 201 E-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQG 234
Cdd:cd03297 180 NlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-232 |
3.79e-30 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 113.23 E-value: 3.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKdgqlkvfdkk 85
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 qlqllrTRltMVFQHFNLWSHMTVLENVMeapvqvLGLsKADAHERAVRYLDKVGIDERArGKYPVHLSGGQQQRVSIAR 165
Cdd:PRK11247 83 ------TR--LMFQDARLLPWKKVIDNVG------LGL-KGQWRDAALQALAAVGLADRA-NEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491074476 166 ALAMEPEVLLFDEPTSALDPelvgeVLRI-MQKLAE-----EGKTMVVVTHEMEFARHVSNHVIflhkgLIEE 232
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDA-----LTRIeMQDLIEslwqqHGFTVLLVTHDVSEAVAMADRVL-----LIEE 209
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-225 |
4.19e-30 |
|
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: 112.14 E-value: 4.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHE-------VLKGVSLAANAGDVISIIGSSGSGKSTFLRCI--NFLekPSEGSISLNNED--IRMVRD 74
Cdd:COG4778 5 LEVENLSKTFTLHLqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYL--PDSGSILVRHDGgwVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 75 KDGQLkvfdkkqLQLLRTRLTMVFQHFNLWSHMTVLENVMEaPVQVLGLSKADAHERAVRYLDKVGIDERARGKYPVHLS 154
Cdd:COG4778 83 SPREI-------LALRRRTIGYVSQFLRVIPRVSALDVVAE-PLLERGVDREEARARARELLARLNLPERLWDLPPATFS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491074476 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFL 225
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
44-234 |
5.72e-30 |
|
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: 111.43 E-value: 5.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdGQLKVFDKKqlqllrtrLTMVFQHFNLWSHMTVLENVMEAPVQVLGL 123
Cdd:cd03298 37 KSTLLNLIAGFETPQSGRVLINGVDV-------TAAPPADRP--------VSMLFQENNLFAHLTVEQNVGLGLSPGLKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 124 SKADaHERAVRYLDKVGIDERARgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEG 202
Cdd:cd03298 102 TAED-RQAIEVALARVGLAGLEK-RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAETK 179
|
170 180 190
....*....|....*....|....*....|..
gi 491074476 203 KTMVVVTHEMEFARHVSNHVIFLHKGLIEEQG 234
Cdd:cd03298 180 MTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-230 |
6.24e-30 |
|
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: 111.19 E-value: 6.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 11 LHKRYGDH-EVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlkvfdkKQLQL 89
Cdd:cd03226 5 ISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---------------KAKER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 90 LRTrLTMVFQH--FNLWSHmTVLENVMeapvqvLGL-SKADAHERAVRYLDKVGIDErARGKYPVHLSGGQQQRVSIARA 166
Cdd:cd03226 70 RKS-IGYVMQDvdYQLFTD-SVREELL------LGLkELDAGNEQAETVLKDLDLYA-LKERHPLSLSGGQKQRLAIAAA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491074476 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLI 230
Cdd:cd03226 141 LLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
44-253 |
9.04e-30 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 113.65 E-value: 9.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdGQlkvfDKKQLQLLRTRLTMVFQH--FNLWSHMTVLENVMEaPVQVL 121
Cdd:PRK15079 60 KSTFARAIIGLVKATDGEVAWLGKDLL------GM----KDDEWRAVRSDIQMIFQDplASLNPRMTIGEIIAE-PLRTY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 122 --GLSKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLA 199
Cdd:PRK15079 129 hpKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQ 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491074476 200 EE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKSPRLQQFLS 253
Cdd:PRK15079 209 REmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMS 263
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-239 |
9.06e-30 |
|
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: 111.06 E-value: 9.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHE--VLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKdgqlkvfd 83
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 84 kkqlqlLRTRLTMVFQHFNLWSHMTVLENVM-EAPVQvlGLSKADAHERAVRYLDKVGI----DERARGkypvhLSGGQQ 158
Cdd:cd03263 73 ------ARQSLGYCPQFDALFDELTVREHLRfYARLK--GLPKSEIKEEVELLLRVLGLtdkaNKRART-----LSGGMK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAE 238
Cdd:cd03263 140 RKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
.
gi 491074476 239 L 239
Cdd:cd03263 219 L 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-228 |
9.63e-30 |
|
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: 109.44 E-value: 9.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDGQlkvfdkk 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDAR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 qlqllRTRLTMVFQhfnlwshmtvlenvmeapvqvlglskadaheravryldkvgiderargkypvhLSGGQQQRVSIAR 165
Cdd:cd03216 74 -----RAGIAMVYQ-----------------------------------------------------LSVGERQMVEIAR 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491074476 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:cd03216 96 ALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-238 |
1.40e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.79 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvfDKK 85
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA------------DWS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQLLRTRLTMVfQHFNLWSHMTVLEnVMEAPVQVLGLSKADAHERAVRYLDKVGIDERARGKYPvHLSGGQQQRVSIAR 165
Cdd:PRK13548 71 PAELARRRAVLP-QHSSLSFPFTVEE-VVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYP-QLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 166 ALA------MEPEVLLFDEPTSALDPELVGEVLRIMQKLA-EEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAE 238
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-239 |
1.46e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 111.33 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 8 VTELHKRYGDHEVLKGVSLA-----------AN-AGdvisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIrmVRDK 75
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTipkggitaligPNgAG------------KSTLLSMISRLLPPDSGEVLVDGLDV--ATTP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 76 DGQLKvfdkKQLQLLRtrltmvfQ--HFNlwSHMTVLENVMeapvqvLG--------LSKADAH--ERAVRYLDKVGIde 143
Cdd:COG4604 70 SRELA----KRLAILR-------QenHIN--SRLTVRELVA------FGrfpyskgrLTAEDREiiDEAIAYLDLEDL-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 144 raRGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHV 222
Cdd:COG4604 129 --ADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHI 206
|
250
....*....|....*..
gi 491074476 223 IFLHKGLIEEQGPPAEL 239
Cdd:COG4604 207 VAMKDGRVVAQGTPEEI 223
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-234 |
2.08e-29 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 110.06 E-value: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIslnnedirmvrdkdgqlkVFDKK 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV------------------LFDGK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQLL-RTRLTMVFQHFNLWSHMTVLENVMEApVQVLGLSKADAHERAVRYLDKVGIDERARGKYPvHLSGGQQQRVSIA 164
Cdd:cd03269 63 PLDIAaRNRIGYLPEERGLYPKMKVIDQLVYL-AQLKGLKKEEARRRIDEWLERLELSEYANKRVE-ELSKGNQQKVQFI 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQG 234
Cdd:cd03269 141 AAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-239 |
4.86e-29 |
|
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: 109.63 E-value: 4.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 15 YGDH-EVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVrdkdgqlkvfdkkQLQLLRTR 93
Cdd:cd03253 10 YDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV-------------TLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 94 LTMVFQHFNLWsHMTVLENVMEA-----PVQVLGLSK-ADAHERAVR----YLDKVGidERArgkypVHLSGGQQQRVSI 163
Cdd:cd03253 77 IGVVPQDTVLF-NDTIGYNIRYGrpdatDEEVIEAAKaAQIHDKIMRfpdgYDTIVG--ERG-----LKLSGGEKQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491074476 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMefaRHVSN--HVIFLHKGLIEEQGPPAEL 239
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRL---STIVNadKIIVLKDGRIVERGTHEEL 222
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-253 |
6.67e-29 |
|
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: 114.48 E-value: 6.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRY--GDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDgqlkvfd 83
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 84 kkqlqlLRTRLTMVFQHFNLWsHMTVLENvmeapvqvLGLSKADA-HERAVRYLDKVGIDERAR----------GKYPVH 152
Cdd:COG4987 407 ------LRRRIAVVPQRPHLF-DTTLREN--------LRLARPDAtDEELWAALERVGLGDWLAalpdgldtwlGEGGRR 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMEFARHVsNHVIFLHKGLIEE 232
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGLERM-DRILVLEDGRIVE 549
|
250 260
....*....|....*....|.
gi 491074476 233 QGPPAELfgNPKSPRLQQFLS 253
Cdd:COG4987 550 QGTHEEL--LAQNGRYRQLYQ 568
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-240 |
8.47e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 110.10 E-value: 8.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGDHE--VLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNedirMVRDKDgq 78
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG----MVLSEE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 79 lKVFDkkqlqlLRTRLTMVFQH-FNLWSHMTV-------LENVmeapvqvlGLSKADAHERAVRYLDKVGIDERARgKYP 150
Cdd:PRK13635 75 -TVWD------VRRQVGMVFQNpDNQFVGATVqddvafgLENI--------GVPREEMVERVDQALRQVGMEDFLN-REP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGK-TMVVVTHEMEFARHvSNHVIFLHKGL 229
Cdd:PRK13635 139 HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGE 217
|
250
....*....|.
gi 491074476 230 IEEQGPPAELF 240
Cdd:PRK13635 218 ILEEGTPEEIF 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-243 |
8.90e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 109.89 E-value: 8.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 12 HKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlkvfDKKQLQLLR 91
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI-------------TKENIREVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 92 TRLTMVFQHFN--LWShMTVLENVMEAPVQvLGLSKADAHERAVRYLDKVGIDErARGKYPVHLSGGQQQRVSIARALAM 169
Cdd:PRK13652 78 KFVGLVFQNPDdqIFS-PTVEQDIAFGPIN-LGLDEETVAHRVSSALHMLGLEE-LRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491074476 170 EPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNP 243
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-244 |
1.17e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.87 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 17 DHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrMVRDKDgqlkvfdkKQLQLLRTRLTM 96
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITI-THKTKD--------KYIRPVRKRIGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 97 VFQHFNLWSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARALAMEPEVLLF 176
Cdd:PRK13646 90 VFQFPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 177 DEPTSALDPELVGEVLRIMQKLA-EEGKTMVVVTHEM-EFARHVSNhVIFLHKGLIEEQGPPAELFGNPK 244
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMnEVARYADE-VIVMKEGSIVSQTSPKELFKDKK 238
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-245 |
1.54e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 111.47 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLnnedirmvrdkDGQlkvfDKK 85
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-----------DGV----DLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQLLRTRLTMVFQHFNLWSHMTVLENVMEAPVQVlGLSKADAHERAVRYLDKVGIDERARGKyPVHLSGGQQQRVSIAR 165
Cdd:PRK11607 85 HVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQD-KLPKAEIASRVNEMLGLVHMQEFAKRK-PHQLSGGQRQRVALAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 166 ALAMEPEVLLFDEPTSALDPELVG----EVLRIMQKLaeeGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFG 241
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKKLRDrmqlEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
....
gi 491074476 242 NPKS 245
Cdd:PRK11607 240 HPTT 243
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-244 |
1.85e-28 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 108.01 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDI-RMVRDKdgqlkvfdk 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMHK--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 85 kqlqllRTRLTMVF--QHFNLWSHMTVLENVMeAPVQVLGLSKADAHERAVRYLDKVGIdERARGKYPVHLSGGQQQRVS 162
Cdd:cd03218 72 ------RARLGIGYlpQEASIFRKLTVEENIL-AVLEIRGLSKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGN 242
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
..
gi 491074476 243 PK 244
Cdd:cd03218 224 EL 225
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-250 |
6.63e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.02 E-value: 6.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 5 KLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKdgqlkvfdk 84
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSR--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 85 kqlQLLRtRLTMVFQHFNLWSHMTVLENVM--EAP-VQVLG-LSKADaHERAVRYLDKVGIDERARgKYPVHLSGGQQQR 160
Cdd:PRK11231 73 ---QLAR-RLALLPQHHLTPEGITVRELVAygRSPwLSLWGrLSAED-NARVNQAMEQTRINHLAD-RRLTDLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELF 240
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
250
....*....|
gi 491074476 241 gnpkSPRLQQ 250
Cdd:PRK11231 227 ----TPGLLR 232
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
14-234 |
9.58e-28 |
|
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: 105.71 E-value: 9.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 14 RYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlkvfdkKQLQLLRTR 93
Cdd:TIGR01277 7 RYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH---------------TGLAPYQRP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 94 LTMVFQHFNLWSHMTVLENVMEAPVQVLGLSkADAHERAVRYLDKVGIDERArGKYPVHLSGGQQQRVSIARALAMEPEV 173
Cdd:TIGR01277 72 VSMLFQENNLFAHLTVRQNIGLGLHPGLKLN-AEQQEKVVDAAQQVGIADYL-DRLPEQLSGGQRQRVALARCLVRPNPI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491074476 174 LLFDEPTSALDPELVGEVLRIMQKLAEEGK-TMVVVTHEMEFARHVSNHVIFLHKGLIEEQG 234
Cdd:TIGR01277 150 LLLDEPFSALDPLLREEMLALVKQLCSERQrTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
15-254 |
9.87e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 106.79 E-value: 9.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 15 YGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEK--PS---EGSISLNNEDIRmvrdkDGQLKVFDkkqlql 89
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLY-----APDVDPVE------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 90 LRTRLTMVFQHFNLWSHmTVLENVMEAPvQVLGLsKADAHERAVRYLDKVGIDERARGKYP---VHLSGGQQQRVSIARA 166
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPK-SIYDNIAYGA-RINGY-KGDMDELVERSLRQAALWDEVKDKLKqsgLSLSGGQQQRLCIARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAEL------- 239
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLvefdrte 244
|
250
....*....|....*..
gi 491074476 240 --FGNPKSPRLQQFLSG 254
Cdd:PRK14243 245 kiFNSPQQQATRDYVSG 261
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
6-246 |
1.32e-27 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 106.46 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDH---------EVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEdirmvrdkd 76
Cdd:COG4167 5 LEVRNLSKTFKYRtglfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 77 gQLKVFDKKQL-QLLRtrltMVFQHFN--LWSHMTVLEnVMEAPVQVL-GLSKADAHERAVRYLDKVGIDERARGKYPVH 152
Cdd:COG4167 76 -KLEYGDYKYRcKHIR----MIFQDPNtsLNPRLNIGQ-ILEEPLRLNtDLTAEEREERIFATLRLVGLLPEHANFYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIE 231
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
250
....*....|....*
gi 491074476 232 EQGPPAELFGNPKSP 246
Cdd:COG4167 230 EYGKTAEVFANPQHE 244
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-232 |
2.27e-27 |
|
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: 104.61 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLnnedirmvrdkDGQLKVFDKK 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF-----------DGKSYQKNIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQllrtRLTMVFQHFNLWSHMTVLENvMEAPVQVLGLSKADAHEravrYLDKVGIDERAR---GKYpvhlSGGQQQRVS 162
Cdd:cd03268 70 ALR----RIGALIEAPGFYPNLTAREN-LRLLARLLGIRKKRIDE----VLDVVGLKDSAKkkvKGF----SLGMKQRLG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491074476 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKG-LIEE 232
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGkLIEE 207
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-254 |
3.40e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 105.95 E-value: 3.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSisLNNEDIRMvrdkdGQLKVFDKK 85
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY--RYSGDVLL-----GGRSIFNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQLLRTRLTMVFQHFNLWShMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDERARGKY---PVHLSGGQQQRVS 162
Cdd:PRK14271 95 DVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGN 242
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
250
....*....|..
gi 491074476 243 PKSPRLQQFLSG 254
Cdd:PRK14271 253 PKHAETARYVAG 264
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-244 |
6.16e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 104.34 E-value: 6.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 5 KLAVTELHKRYGDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlkvfdk 84
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIvgllgpngagKTTTFYMIVGLVKPDSGRIFLDGEDI--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 85 kqlqllrTRLTM----------------VFQHfnlwshMTVLENVMeAPVQVLGLSKADAHERAVRYLDKVGIDERARGK 148
Cdd:COG1137 68 -------THLPMhkrarlgigylpqeasIFRK------LTVEDNIL-AVLELRKLSKKEREERLEELLEEFGITHLRKSK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 149 yPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGktM-VVVT----HEMEfarHVSNHVI 223
Cdd:COG1137 134 -AYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERG--IgVLITdhnvRETL---GICDRAY 207
|
250 260
....*....|....*....|.
gi 491074476 224 FLHKGLIEEQGPPAELFGNPK 244
Cdd:COG1137 208 IISEGKVLAEGTPEEILNNPL 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-228 |
9.76e-27 |
|
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: 103.31 E-value: 9.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 21 LKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDI------RMVrdkdgqlkvfdkkqlqllrtrl 94
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItepgpdRMV---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 95 tmVFQHFNLWSHMTVLENVMEAPVQVL-GLSKADAHERAVRYLDKVGIDErARGKYPVHLSGGQQQRVSIARALAMEPEV 173
Cdd:TIGR01184 59 --VFQNYSLLPWLTVRENIALAVDRVLpDLSKSERRAIVEEHIALVGLTE-AADKRPGQLSGGMKQRVAIARALSIRPKV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491074476 174 LLFDEPTSALDP----ELVGEVLRIMQklaEEGKTMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:TIGR01184 136 LLLDEPFGALDAltrgNLQEELMQIWE---EHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-239 |
1.42e-26 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 103.00 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 17 DHEVLKGVSLAANAGDVISIIGSSGSGKSTflrCINFLEK---PSEGSISLNNEDIRMVrdkdgqlkvfdkkQLQLLRTR 93
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERfydPTSGEILLDGVDIRDL-------------NLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 94 LTMVFQHFNLWShMTVLENVmeapvqvlGLSKADAH----ERAVR--YLDKV------GIDERArGKYPVHLSGGQQQRV 161
Cdd:cd03249 79 IGLVSQEPVLFD-GTIAENI--------RYGKPDATdeevEEAAKkaNIHDFimslpdGYDTLV-GERGSQLSGGQKQRI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491074476 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMEFARHvSNHVIFLHKGLIEEQGPPAEL 239
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDEL 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-252 |
2.43e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 103.19 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFL-----EKPSEGSISLNNEDIRMVRdkdgqlk 80
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERR------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 81 vfdkKQLQLLRTRLTMVFQHFNLWShMTVLENVMEApVQVLG----LSKADAHERAVRYLDKVGIDERARGKYPVHLSGG 156
Cdd:PRK14258 81 ----VNLNRLRRQVSMVHPKPNLFP-MSVYDNVAYG-VKIVGwrpkLEIDDIVESALKDADLWDEIKHKIHKSALDLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGK-TMVVVTHEMEFARHVSNHVIFLHK-----GLI 230
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFFKGnenriGQL 234
|
250 260
....*....|....*....|..
gi 491074476 231 EEQGPPAELFGNPKSPRLQQFL 252
Cdd:PRK14258 235 VEFGLTKKIFNSPHDSRTREYV 256
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-239 |
3.72e-26 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 106.43 E-value: 3.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLE--KPSEGSI----SLNNEDIRMVR-DKDGQ 78
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvALCEKCGYVERpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 79 --------LKVF-------DKKQLQLLRTRLTMVFQH-FNLWSHMTVLENVMEApVQVLGLSKADAHERAVRYLDKVGID 142
Cdd:TIGR03269 81 pcpvcggtLEPEevdfwnlSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEA-LEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 143 ER----ARgkypvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRIMQKlaEEGKTMVVVTHEMEFA 215
Cdd:TIGR03269 160 HRithiAR-----DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtakLVHNALEEAVK--ASGISMVLTSHWPEVI 232
|
250 260
....*....|....*....|....
gi 491074476 216 RHVSNHVIFLHKGLIEEQGPPAEL 239
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
14-242 |
4.81e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 102.76 E-value: 4.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 14 RYGDHE--VLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlkvfDKKQLQLLR 91
Cdd:PRK13632 16 SYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI-------------SKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 92 TRLTMVFQH-FNLWSHMTV-------LENVMEAPvqvlglSKADAheRAVRYLDKVGIDERARgKYPVHLSGGQQQRVSI 163
Cdd:PRK13632 83 KKIGIIFQNpDNQFIGATVeddiafgLENKKVPP------KKMKD--IIDDLAKKVGMEDYLD-KEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEG-KTMVVVTHEMEFARhVSNHVIFLHKGLIEEQGPPAELFGN 242
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
14-240 |
5.55e-26 |
|
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: 101.70 E-value: 5.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 14 RYGDHEVLKGVSLA-----------AN-AGdvisiigssgsgKSTFLRCINFLEKPSEGsislnnEDIRmVRDKD-GQLK 80
Cdd:COG1119 12 RRGGKTILDDISWTvkpgehwailgPNgAG------------KSTLLSLITGDLPPTYG------NDVR-LFGERrGGED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 81 VFDkkqlqlLRTRLTMV--FQHFNLWSHMTVLENVMEAPVQVLGLSK---ADAHERAVRYLDKVGIDERArGKYPVHLSG 155
Cdd:COG1119 73 VWE------LRKRIGLVspALQLRFPRDETVLDVVLSGFFDSIGLYReptDEQRERARELLELLGLAHLA-DRPFGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEG-KTMVVVTHemefarHVS------NHVIFLHKG 228
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTH------HVEeippgiTHVLLLKDG 219
|
250
....*....|..
gi 491074476 229 LIEEQGPPAELF 240
Cdd:COG1119 220 RVVAAGPKEEVL 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-234 |
6.18e-26 |
|
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: 100.91 E-value: 6.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHE----VLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLnnEDIRMVRDKdgqlkv 81
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV--DGFDVVKEP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 82 fdkkqlQLLRTRLTMVFQHFNLWSHMTVLENVmEAPVQVLGLSKADAHERAVRYLDKVGI----DERARGkypvhLSGGQ 157
Cdd:cd03266 74 ------AEARRRLGFVSDSTGLYDRLTARENL-EYFAGLYGLKGDELTARLEELADRLGMeellDRRVGG-----FSTGM 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491074476 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQG 234
Cdd:cd03266 142 RQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
21-243 |
7.46e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 102.37 E-value: 7.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 21 LKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIslnnedirMVRDKDgqlkVFDKKQLQLLRTRLTMVFQH 100
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV--------LVSGID----TGDFSKLQGIRKLVGIVFQN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 101 FNL-WSHMTVLENVMEAPvQVLGLSKADAHERAVRYLDKVGIdERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
Cdd:PRK13644 86 PETqFVGRTVEEDLAFGP-ENLCLPPIEIRKRVDRALAEIGL-EKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491074476 180 TSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEfARHVSNHVIFLHKGLIEEQGPPAELFGNP 243
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-256 |
9.18e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 101.66 E-value: 9.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 2 SENKLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLekpsegsISLNNEDIRMvrdkDGQLKV 81
Cdd:PRK14246 7 AEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRL-------IEIYDSKIKV----DGKVLY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 82 FDKKQLQL----LRTRLTMVFQHFNLWSHMTVLENVmEAPVQVLGLSKADAHERAVRY-LDKVGI--DERARGKYPV-HL 153
Cdd:PRK14246 76 FGKDIFQIdaikLRKEVGMVFQQPNPFPHLSIYDNI-AYPLKSHGIKEKREIKKIVEEcLRKVGLwkEVYDRLNSPAsQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQ 233
Cdd:PRK14246 155 SGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEW 233
|
250 260
....*....|....*....|...
gi 491074476 234 GPPAELFGNPKSPRLQQFLSGAL 256
Cdd:PRK14246 234 GSSNEIFTSPKNELTEKYVIGRI 256
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
11-245 |
9.33e-26 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 103.38 E-value: 9.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 11 LHKRY-GDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMV--RDKDgqlkvfdkkql 87
Cdd:PRK11650 9 VRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELepADRD----------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 88 qllrtrLTMVFQHFNLWSHMTVLENvMEAPVQVLGLSKADAHERavryldkvgIDERAR----GKY----PVHLSGGQQQ 159
Cdd:PRK11650 78 ------IAMVFQNYALYPHMSVREN-MAYGLKIRGMPKAEIEER---------VAEAARilelEPLldrkPRELSGGQRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 160 RVSIARALAMEPEVLLFDEPTSALDPEL-VGEVLRImQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPA 237
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDAKLrVQMRLEI-QRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPV 220
|
....*...
gi 491074476 238 ELFGNPKS 245
Cdd:PRK11650 221 EVYEKPAS 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-242 |
1.45e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 101.70 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 20 VLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvfDKKQLQLLRTRLTMVFQ 99
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS------------DEENLWDIRNKAGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 100 H-FNLWSHMTVLENVMEAPvQVLGLSKADAHERAVRYLDKVGIDERARgkYPVH-LSGGQQQRVSIARALAMEPEVLLFD 177
Cdd:PRK13633 93 NpDNQIVATIVEEDVAFGP-ENLGIPPEEIRERVDESLKKVGMYEYRR--HAPHlLSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491074476 178 EPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMEFARHvSNHVIFLHKGLIEEQGPPAELFGN 242
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-239 |
2.01e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 101.81 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlk 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 81 vfdKKQLQLLRTRLTMVFQHFNLWSHMTVLENVMeAPVQVLGLSKADAHERAVRYLDKVGIDERARGKYPvHLSGGQQQR 160
Cdd:PRK13537 72 ---PSRARHARQRVGVVPQFDNLDPDFTVRENLL-VFGRYFGLSAAAARALVPPLLEFAKLENKADAKVG-ELSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 161 VSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRimqKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPA 237
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQarhLMWERLR---SLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPH 223
|
..
gi 491074476 238 EL 239
Cdd:PRK13537 224 AL 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-243 |
2.79e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 100.06 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvRDKDGQlk 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI---EGLPGH-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 81 vfdkkqlQLLRTRLTMVFQHFNLWSHMTVLENVMEAPVQVL------GL--------SKADAHERAVRYLDKVGIDE--- 143
Cdd:PRK11300 76 -------QIARMGVVRTFQHVRLFREMTVIENLLVAQHQQLktglfsGLlktpafrrAESEALDRAATWLERVGLLEhan 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 144 RARGkypvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHV 222
Cdd:PRK11300 149 RQAG----NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRI 224
|
250 260
....*....|....*....|.
gi 491074476 223 IFLHKGLIEEQGPPAELFGNP 243
Cdd:PRK11300 225 YVVNQGTPLANGTPEEIRNNP 245
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-240 |
4.80e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 100.08 E-value: 4.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvFDKK 85
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-----------YSKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQLLRTRLTMVFQHFNLWSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVgiDERARGKYPVH-LSGGQQQRVSIA 164
Cdd:PRK13638 71 GLLALRQQVATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLV--DAQHFRHQPIQcLSHGQKKRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491074476 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELF 240
Cdd:PRK13638 149 GALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
13-244 |
6.23e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 101.26 E-value: 6.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 13 KRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDgqlkvfdkkqlqllrT 92
Cdd:PRK11000 11 KAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE---------------R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 93 RLTMVFQHFNLWSHMTVLENvMEAPVQVLGLSKADAHER---AVRYLDKVGIDERArgkyPVHLSGGQQQRVSIARALAM 169
Cdd:PRK11000 76 GVGMVFQSYALYPHLSVAEN-MSFGLKLAGAKKEEINQRvnqVAEVLQLAHLLDRK----PKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491074476 170 EPEVLLFDEPTSALDPEL-VG---EVLRIMQKLaeeGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPK 244
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALrVQmriEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
44-253 |
7.32e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 103.01 E-value: 7.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDIRMVRDKdgqlkvfdkkQLQLLRTRLTMVFQ--HFNLWSHMTVLENVMEaPVQVL 121
Cdd:PRK10261 363 KSTTGRALLRLVESQGGEIIFNGQRIDTLSPG----------KLQALRRDIQFIFQdpYASLDPRQTVGDSIME-PLRVH 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 122 GLSKADAHERAVRYL-DKVGIDERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAE 200
Cdd:PRK10261 432 GLLPGKAAAARVAWLlERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQR 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491074476 201 E-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKSPRLQQFLS 253
Cdd:PRK10261 512 DfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMA 565
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
8-228 |
7.99e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 99.32 E-value: 7.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 8 VTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFL---EKPSEGSISLNNEDIRmvrdKDGQLKvfdk 84
Cdd:PRK09984 7 VEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQ----REGRLA---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 85 KQLQLLRTRLTMVFQHFNLWSHMTVLENVMeapVQVLGLS----------KADAHERAVRYLDKVGIDERARGKYPVhLS 154
Cdd:PRK09984 79 RDIRKSRANTGYIFQQFNLVNRLSVLENVL---IGALGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVST-LS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491074476 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRIMQKlaEEGKTMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPEsarIVMDTLRDINQ--NDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
44-239 |
1.06e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.12 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDIRmvRDKDGQLKVfdkkqlqllrtrlTMVFQHFNLWSHMTVLENVmeapvqVLGL 123
Cdd:PRK10771 38 KSTLLNLIAGFLTPASGSLTLNGQDHT--TTPPSRRPV-------------SMLFQENNLFSHLTVAQNI------GLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 124 S-----KADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL 198
Cdd:PRK10771 97 NpglklNAAQREKLHAIARQMGIEDLLA-RLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491074476 199 AEEGK-TMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAEL 239
Cdd:PRK10771 176 CQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
85-242 |
1.07e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 99.31 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 85 KQLQLLRTRLTMVFQ--HFNLWSHmTVLENVMEAPVQvLGLSKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQRVS 162
Cdd:PRK13645 83 KEVKRLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVN-LGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFG 241
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
.
gi 491074476 242 N 242
Cdd:PRK13645 241 N 241
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-222 |
3.05e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 96.81 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGD----HEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdGQLKV 81
Cdd:PRK11629 6 LQCDNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPM-------SKLSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 82 FDKKQLQllRTRLTMVFQHFNLWSHMTVLENVmEAPVQVLGLSKADAHERAVRYLDKVGIDERARGKyPVHLSGGQQQRV 161
Cdd:PRK11629 79 AAKAELR--NQKLGFIYQFHHLLPDFTALENV-AMPLLIGKKKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491074476 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMEFARHVSNHV 222
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
85-246 |
3.43e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 98.64 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 85 KQLQLLRT-RLTMVFQH--FNLWSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDE-RAR-GKYPVHLSGGQQQ 159
Cdd:PRK09473 89 KELNKLRAeQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEaRKRmKMYPHEFSGGMRQ 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKT-MVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAE 238
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
....*...
gi 491074476 239 LFGNPKSP 246
Cdd:PRK09473 249 VFYQPSHP 256
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
44-240 |
3.76e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.51 E-value: 3.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlkvfDKKQLQLLRTRLTMVFQH-FNLWSHMTV-------LENVMe 115
Cdd:PRK13648 48 KSTIAKLMIGIEKVKSGEIFYNNQAI-------------TDDNFEKLRKHIGIVFQNpDNQFVGSIVkydvafgLENHA- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 116 apvqvlgLSKADAHERAVRYLDKVGIDERARGKyPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIM 195
Cdd:PRK13648 114 -------VPYDEMHRRVSEALKQVDMLERADYE-PNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLV 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491074476 196 QKLAEEGK-TMVVVTHEMEFARHvSNHVIFLHKGLIEEQGPPAELF 240
Cdd:PRK13648 186 RKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-254 |
4.13e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 97.53 E-value: 4.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 2 SENKLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlKV 81
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI----------PA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 82 FDKKQLQLLRTRLTMVFQHFNLWSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDERARGKyPVHLSGGQQQRV 161
Cdd:PRK11831 74 MSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLM-PSELSGGMARRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELF 240
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQ 232
|
250
....*....|....
gi 491074476 241 GNPkSPRLQQFLSG 254
Cdd:PRK11831 233 ANP-DPRVRQFLDG 245
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
51-252 |
4.17e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 98.66 E-value: 4.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 51 INFLEKPSEGSISLNNEDIrmvrdkdgqLKVFDKKQLQLLRTRLTMVFQH--FNLWSHMTVLENVMEAPVQVLGLSKADA 128
Cdd:PRK11022 57 IDYPGRVMAEKLEFNGQDL---------QRISEKERRNLVGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 129 HERAVRYLDKVGI-DERAR-GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAE-EGKTM 205
Cdd:PRK11022 128 RQRAIDLLNQVGIpDPASRlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMAL 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491074476 206 VVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKSPRLQQFL 252
Cdd:PRK11022 208 VLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALL 254
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-239 |
6.71e-24 |
|
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: 96.15 E-value: 6.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 14 RYGDHE--VLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVrdkdgqlkvfdkkQLQLLR 91
Cdd:cd03251 9 RYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY-------------TLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 92 TRLTMVFQHFNLWSHmTVLENVM-----EAPVQVLGLSK-ADAHERAVRYLDKVGIDERARGkypVHLSGGQQQRVSIAR 165
Cdd:cd03251 76 RQIGLVSQDVFLFND-TVAENIAygrpgATREEVEEAARaANAHEFIMELPEGYDTVIGERG---VKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491074476 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMEFARHvSNHVIFLHKGLIEEQGPPAEL 239
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-239 |
8.30e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 98.76 E-value: 8.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDGQLKV---- 81
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVasvp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 82 --------FDKKQ-LQLLRTrltmvfQHFNLWSHMTvlenvmeapvqvlglskaDAHERAV-RYLDKVGIDERArgKYPV 151
Cdd:PRK09536 84 qdtslsfeFDVRQvVEMGRT------PHRSRFDTWT------------------ETDRAAVeRAMERTGVAQFA--DRPV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 152 -HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLI 230
Cdd:PRK09536 138 tSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
....*....
gi 491074476 231 EEQGPPAEL 239
Cdd:PRK09536 218 RAAGPPADV 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-228 |
9.15e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 96.31 E-value: 9.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNediRMVRDKDGQLKVfdkk 85
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG---KPVEGPGAERGV---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 qlqllrtrltmVFQHFNLWSHMTVLENVmEAPVQVLGLSKADAHERAVRYLDKVGIDErARGKYPVHLSGGQQQRVSIAR 165
Cdd:PRK11248 75 -----------VFQNEGLLPWRNVQDNV-AFGLQLAGVEKMQRLEIAHQMLKKVGLEG-AEKRYIWQLSGGQRQRVGIAR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491074476 166 ALAMEPEVLLFDEPTSALDP---ELVGEVLriMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALDAftrEQMQTLL--LKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-216 |
1.44e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.22 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 14 RYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSislnnedirmVRDKDGqlkvfdkkqlqllrTR 93
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT----------VRRAGG--------------AR 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 94 LTMVFQHFNL-WSH-MTVLENVMEAPVQVLGLSK---ADAHERAVRYLDKVGIDERArgKYPVH-LSGGQQQRVSIARAL 167
Cdd:NF040873 57 VAYVPQRSEVpDSLpLTVRDLVAMGRWARRGLWRrltRDDRAAVDDALERVGLADLA--GRQLGeLSGGQRQRALLAQGL 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491074476 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFAR 216
Cdd:NF040873 135 AQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVR 183
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-234 |
2.59e-23 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 94.19 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 17 DHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgQLKVFDkkqlqlLRTRLTM 96
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIR-------QLDPAD------LRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 97 VFQHFNLWSHmTVLENVMeapvqvLGLSKADaHERAVRYLDKVGID---------------ERARGkypvhLSGGQQQRV 161
Cdd:cd03245 83 VPQDVTLFYG-TLRDNIT------LGAPLAD-DERILRAAELAGVTdfvnkhpngldlqigERGRG-----LSGGQRQAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491074476 162 SIARALAMEPEVLLFDEPTSALDPElvGEVlRIMQKLAE--EGKTMVVVTHEMEFARHVsNHVIFLHKGLIEEQG 234
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMN--SEE-RLKERLRQllGDKTLIIITHRPSLLDLV-DRIIVMDSGRIVADG 220
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
6-256 |
2.65e-23 |
|
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: 94.90 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLnnedirmvRDKDGQ----LKV 81
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATY--------IMRSGAelelYQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 82 FDKKQLQLLRTRLTMVFQHFNLWSHMTVLE--NVMEAPVQVLGLSKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQ 159
Cdd:TIGR02323 76 SEAERRRLMRTEWGFVHQNPRDGLRMRVSAgaNIGERLMAIGARHYGNIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAE 238
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQ 235
|
250
....*....|....*...
gi 491074476 239 LFGNPKSPRLQQFLSGAL 256
Cdd:TIGR02323 236 VLDDPQHPYTQLLVSSIL 253
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-215 |
2.66e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 94.46 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 2 SENKLAVTELHKRYGDHE----VLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDirmvrdkdg 77
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 78 qLKVFDKKQLQLLRTR-LTMVFQHFNLWSHMTVLENVmEAPVQVLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGG 156
Cdd:PRK10584 74 -LHQMDEEARAKLRAKhVGFVFQSFMLIPTLNALENV-ELPALLRGESSRQSRNGAKALLEQLGLGKRLD-HLPAQLSGG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFA 215
Cdd:PRK10584 151 EQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLA 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-241 |
4.19e-23 |
|
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: 97.57 E-value: 4.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYG--DHEVLK---GVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISlnnedirmVRDKDGQLK 80
Cdd:TIGR03269 280 IKVRNVSKRYIsvDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVN--------VRVGDEWVD 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 81 VFDKKQLqlLRTRLT----MVFQHFNLWSHMTVLENVMEApvqvLGLSKAD--AHERAVRYLDKVGIDE-RARG---KYP 150
Cdd:TIGR03269 352 MTKPGPD--GRGRAKryigILHQEYDLYPHRTVLDNLTEA----IGLELPDelARMKAVITLKMVGFDEeKAEEildKYP 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR-IMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGL 229
Cdd:TIGR03269 426 DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGK 505
|
250
....*....|..
gi 491074476 230 IEEQGPPAELFG 241
Cdd:TIGR03269 506 IVKIGDPEEIVE 517
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-216 |
6.89e-23 |
|
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: 96.97 E-value: 6.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDH-EVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDgqlkvfdk 84
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS-------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 85 kqlqlLRTRLTMVFQHFNLWSHmTVLENVmeapvqvlGLSKADAHERAV-RYLDKVGIDERAR----------GKYPVHL 153
Cdd:TIGR02857 394 -----WRDQIAWVPQHPFLFAG-TIAENI--------RLARPDASDAEIrEALERAGLDEFVAalpqgldtpiGEGGAGL 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491074476 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMEFAR 216
Cdd:TIGR02857 460 SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAA 521
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-228 |
4.64e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 4.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 8 VTELHKRYGDHEVLKGVSLA-----------AN-AGdvisiigssgsgKSTFLRCINFLEKPSEGSISLNNeDIRMvrdk 75
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSinpgdriglvgRNgAG------------KSTLLKILAGELEPDSGEVSIPK-GLRI---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 76 dGQLKvfdkkqlqllrtrltmvfQHFNLWSHMTVLENVMEAPVQVLGLSKA----------------------------- 126
Cdd:COG0488 64 -GYLP------------------QEPPLDDDLTVLDTVLDGDAELRALEAEleeleaklaepdedlerlaelqeefealg 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 127 --DAHERAVRYLDKVGIDERARGKyPV-HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLRimQKLAEEGK 203
Cdd:COG0488 125 gwEAEARAEEILSGLGFPEEDLDR-PVsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESI-EWLE--EFLKNYPG 200
|
250 260
....*....|....*....|....*
gi 491074476 204 TMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:COG0488 201 TVLVVSHDRYFLDRVATRILELDRG 225
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
17-247 |
5.06e-22 |
|
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: 94.93 E-value: 5.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 17 DHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgQLKVFDkkqlqlLRTRLTM 96
Cdd:TIGR03375 477 ETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIR-------QIDPAD------LRRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 97 VFQHFNLWsHMTVLENVMeapvqvLGLSKADaHERAVRYLDKVGIDERARGK-----YPVH-----LSGGQQQRVSIARA 166
Cdd:TIGR03375 544 VPQDPRLF-YGTLRDNIA------LGAPYAD-DEEILRAAELAGVTEFVRRHpdgldMQIGergrsLSGGQRQAVALARA 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMEFARHVsNHVIFLHKGLIEEQGPPAELFGNPKSP 246
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLLDLV-DRIIVMDNGRIVADGPKDQVLEALRKG 693
|
.
gi 491074476 247 R 247
Cdd:TIGR03375 694 R 694
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-222 |
8.38e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.85 E-value: 8.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCIN-FLEKP--SEGSISLNNEDIRMvrdkdgqlkvf 82
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRLTA----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 83 dkkqLQLLRTRLTMVFQHFNLWSHMTVLENVMEA-PVQVlglSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQQRV 161
Cdd:COG4136 71 ----LPAEQRRIGILFQDDLLFPHLSVGENLAFAlPPTI---GRAQRRARVEQALEEAGLAGFAD-RDPATLSGGQRARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491074476 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLR-IMQKLAEEGKTMVVVTHEMEFARHVSNHV 222
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEEDAPAAGRVL 204
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
44-243 |
1.01e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 92.24 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNediRMVRDKDGQLKVFDKKQlqllrtRLTMVFQHFNLWSHMTVLENVMeapvqvLGL 123
Cdd:PRK11144 37 KTSLINAISGLTRPQKGRIVLNG---RVLFDAEKGICLPPEKR------RIGYVFQDARLFPHYKVRGNLR------YGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 124 SKADAHE--RAVRYLdkvGIdERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE 201
Cdd:PRK11144 102 AKSMVAQfdKIVALL---GI-EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLARE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491074476 202 GKT-MVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNP 243
Cdd:PRK11144 178 INIpILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-240 |
1.85e-21 |
|
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: 89.21 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 16 GDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKdgqlkvfdkkqlqLLRTRLT 95
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRK-------------SLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 96 MVFQHFNLWSHmTVLENVM----EAPVQ-VLGLSKADAHERAVRYLDKvGIDERA--RGKYpvhLSGGQQQRVSIARALA 168
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRlgrpNATDEeVIEAAKEAGAHDFIMKLPN-GYDTVLgeNGGN---LSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491074476 169 MEPEVLLFDEPTSALDPELVGEVLRIMQKLaEEGKTMVVVTHEMEFARHvSNHVIFLHKGLIEEQGPPAELF 240
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
44-241 |
1.93e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 90.56 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLnnedirmvrdkDGQL----KVFDKkqlqllRTRLTMVFQH-FNLWSHMTVLENVMEApV 118
Cdd:PRK13650 46 KSTTVRLIDGLLEAESGQIII-----------DGDLlteeNVWDI------RHKIGMVFQNpDNQFVGATVEDDVAFG-L 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 119 QVLGLSKADAHERAVRYLDKVGIDErARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL 198
Cdd:PRK13650 108 ENKGIPHEEMKERVNEALELVGMQD-FKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGI 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491074476 199 AEE-GKTMVVVTHEM-EFArhVSNHVIFLHKGLIEEQGPPAELFG 241
Cdd:PRK13650 187 RDDyQMTVISITHDLdEVA--LSDRVLVMKNGQVESTSTPRELFS 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-239 |
2.49e-21 |
|
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: 89.47 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 14 RYG--DHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVrdkdgqlkvfdkkQLQLLR 91
Cdd:cd03252 9 RYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA-------------DPAWLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 92 TRLTMVFQHfNLWSHMTVLENV--------MEAPVQVLGLskADAHERAVR----YLDKVGidERARGkypvhLSGGQQQ 159
Cdd:cd03252 76 RQVGVVLQE-NVLFNRSIRDNIaladpgmsMERVIEAAKL--AGAHDFISElpegYDTIVG--EQGAG-----LSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMEFARHvSNHVIFLHKGLIEEQGPPAEL 239
Cdd:cd03252 146 RIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-243 |
2.57e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 90.24 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGDHE--VLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGS--------ISLNNEDIR 70
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 71 MVRDKDGqlkvfdkkqlqllrtrltMVFQH-FNLWSHMTVLENVMEApVQVLGLSKADAHERAVRYLDKVGIDERARGKy 149
Cdd:PRK13640 81 DIREKVG------------------IVFQNpDNQFVGATVGDDVAFG-LENRAVPRPEMIKIVRDVLADVGMLDYIDSE- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 150 PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHvSNHVIFLHKG 228
Cdd:PRK13640 141 PANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANM-ADQVLVLDDG 219
|
250
....*....|....*
gi 491074476 229 LIEEQGPPAELFGNP 243
Cdd:PRK13640 220 KLLAQGSPVEIFSKV 234
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
14-239 |
4.04e-21 |
|
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: 91.94 E-value: 4.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 14 RYGDHE--VLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLnnedirmvrdkDGQ-LKVFDKkqlQLL 90
Cdd:TIGR03797 460 RYRPDGplILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFY-----------DGQdLAGLDV---QAV 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 91 RTRLTMVFQHFNLWSHmTVLENVMEAPVqvlgLSKADAHERAVRyldkVGIDERAR----GKYPV------HLSGGQQQR 160
Cdd:TIGR03797 526 RRQLGVVLQNGRLMSG-SIFENIAGGAP----LTLDEAWEAARM----AGLAEDIRampmGMHTVisegggTLSGGQRQR 596
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491074476 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVlriMQKLAEEGKTMVVVTHEMEFARHvSNHVIFLHKGLIEEQGPPAEL 239
Cdd:TIGR03797 597 LLIARALVRKPRILLFDEATSALDNRTQAIV---SESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDEL 671
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
107-230 |
1.31e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.46 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 107 MTVLENVMEAPVQVLG----LSKADAHERAVRYLDKVGIdeRARGKY-PV-HLSGGQQQRVSIARALAMEPEVLLFDEPT 180
Cdd:COG1129 345 LSIRENITLASLDRLSrgglLDRRRERALAEEYIKRLRI--KTPSPEqPVgNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 491074476 181 SALDpelVG---EVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLI 230
Cdd:COG1129 423 RGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
150-228 |
4.07e-20 |
|
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: 84.79 E-value: 4.07e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491074476 150 PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:cd03215 102 SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
13-238 |
4.35e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.90 E-value: 4.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 13 KRYGDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCINFLEKPSEGSISLNNediRMVrdkdgqlkvfdkkqlQLLRt 92
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESvgiigrngagKSTLLKLIAGILEPTSGRVEVNG---RVS---------------ALLE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 93 rLTMVFQhfnlwSHMTVLENV-MEApvQVLGLSKADAHERavryLDKV----GIderarGKY---PV-HLSGGQQQRVSI 163
Cdd:COG1134 95 -LGAGFH-----PELTGRENIyLNG--RLLGLSRKEIDEK----FDEIvefaEL-----GDFidqPVkTYSSGMRARLAF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491074476 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAE 238
Cdd:COG1134 158 AVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
78-253 |
5.38e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 88.76 E-value: 5.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 78 QLKVFDKKQLQLLR-TRLTMVFQH--FNLWSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDERAR--GKYPVH 152
Cdd:PRK10261 89 ELSEQSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTilSRYPHQ 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVV-VTHEMEFARHVSNHVIFLHKGLIE 231
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIfITHDMGVVAEIADRVLVMYQGEAV 248
|
170 180
....*....|....*....|..
gi 491074476 232 EQGPPAELFGNPKSPRLQQFLS 253
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLA 270
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-252 |
8.73e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.22 E-value: 8.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 17 DHEVLKGVSLAANAGDVISIIGSSGSGKS-TFLRCINFLEKPS----EGSISLNNEDIrmvrdkdgqLKVfDKKQLQLLR 91
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESL---------LHA-SEQTLRGVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 92 -TRLTMVFQHfnLWSHMTVLENVMEAPVQVLGLSKADAHERA----VRYLDKVGIDERAR--GKYPVHLSGGQQQRVSIA 164
Cdd:PRK15134 91 gNKIAMIFQE--PMVSLNPLHTLEKQLYEVLSLHRGMRREAArgeiLNCLDRVGIRQAAKrlTDYPHQLSGGERQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNP 243
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAP 248
|
....*....
gi 491074476 244 KSPRLQQFL 252
Cdd:PRK15134 249 THPYTQKLL 257
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-239 |
2.95e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 85.27 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLnnedirmvrdkdgqLK 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV--------------LG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 81 VFDKKQLQLLRTRLTMVFQHFNLWSHMTVLENVMEAPvQVLGLSKADAHERAVRYLDKVGIDERARGKYPvHLSGGQQQR 160
Cdd:PRK13536 103 VPVPARARLARARIGVVPQFDNLDLEFTVRENLLVFG-RYFGMSTREIEAVIPSLLEFARLESKADARVS-DLSGGMKRR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 161 VSIARALAMEPEVLLFDEPTSALDP---ELVGEVLRimqKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPA 237
Cdd:PRK13536 181 LTLARALINDPQLLILDEPTTGLDPharHLIWERLR---SLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPH 257
|
..
gi 491074476 238 EL 239
Cdd:PRK13536 258 AL 259
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-256 |
1.70e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 81.90 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLnnedirmvRDKDGQLK-VFDK 84
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHY--------RMRDGQLRdLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 85 KQLQ---LLRTRLTMVFQHFNLWSHMTVLE--NVMEAPVQVLGLSKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQ 159
Cdd:PRK11701 79 SEAErrrLLRTEWGFVHQHPRDGLRMQVSAggNIGERLMAVGARHYGDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAE 238
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQ 238
|
250
....*....|....*...
gi 491074476 239 LFGNPKSPRLQQFLSGAL 256
Cdd:PRK11701 239 VLDDPQHPYTQLLVSSVL 256
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-210 |
1.81e-18 |
|
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: 84.33 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRY-GDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDgqlkvfdk 84
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE-------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 85 kqlqlLRTRLTMVFQHFNLWsHMTVLENVMeapvqvlgLSKADAHERAV-RYLDKVGIDERARG-----KYPVH-----L 153
Cdd:TIGR02868 407 -----VRRRVSVCAQDAHLF-DTTVRENLR--------LARPDATDEELwAALERVGLADWLRAlpdglDTVLGeggarL 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491074476 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKlAEEGKTMVVVTH 210
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
44-210 |
2.37e-18 |
|
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: 80.29 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCIN--FLEKPSEGSISLNNEDIRmvrdkdgqlkvfdkkqLQLLRTRLTMVFQHFNLWSHMTVLENVMEApvqvl 121
Cdd:cd03213 48 KSTLLNALAgrRTGLGVSGEVLINGRPLD----------------KRSFRKIIGYVPQDDILHPTLTVRETLMFA----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 122 glskadAHERAvryldkvgiderargkypvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE 201
Cdd:cd03213 107 ------AKLRG--------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT 160
|
....*....
gi 491074476 202 GKTMVVVTH 210
Cdd:cd03213 161 GRTIICSIH 169
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-239 |
2.50e-18 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 84.00 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 14 RYG--DHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRdkdgqlkvfdkkqLQLLR 91
Cdd:TIGR02203 339 RYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT-------------LASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 92 TRLTMVFQHFNLWSHmTVLENV-MEAPVQVlglSKADAhERAVR------YLDKV--GIDERArGKYPVHLSGGQQQRVS 162
Cdd:TIGR02203 406 RQVALVSQDVVLFND-TIANNIaYGRTEQA---DRAEI-ERALAaayaqdFVDKLplGLDTPI-GENGVLLSGGQRQRLA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 163 IARALAMEPEVLLFDEPTSALDPE---LVGEVL-RIMQklaeeGKTMVVVTHEMEFARHvSNHVIFLHKGLIEEQGPPAE 238
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNEserLVQAALeRLMQ-----GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNE 553
|
.
gi 491074476 239 L 239
Cdd:TIGR02203 554 L 554
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
137-257 |
4.49e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 83.63 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 137 DKVGIDERArgkypVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFAR 216
Cdd:PLN03130 730 DLTEIGERG-----VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLS 804
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 491074476 217 HVsNHVIFLHKGLIEEQGPPAELFGNpkSPRLQQFLSGALK 257
Cdd:PLN03130 805 QV-DRIILVHEGMIKEEGTYEELSNN--GPLFQKLMENAGK 842
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-239 |
4.77e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.80 E-value: 4.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 15 YGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDgqlkvfdkkqlqlLRTRL 94
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE-------------VARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 95 TMVFQHFNLWSHMTVLENVMEA--PVQVLGLSKADAHERAV-RYLDKVGIDERARGKYPVhLSGGQQQRVSIARALAMEP 171
Cdd:PRK10253 84 GLLAQNATTPGDITVQELVARGryPHQPLFTRWRKEDEEAVtKAMQATGITHLADQSVDT-LSGGQRQRAWIAMVLAQET 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491074476 172 EVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAEL 239
Cdd:PRK10253 163 AIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-243 |
5.74e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.85 E-value: 5.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 17 DHEVLKGVSLAANAGDVISIIGSSGSGKSTflrCINFLE---KPSEGSISLNNEDIRMvrdkdgqlkvFDKKqlqLLRTR 93
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQnlyQPTGGQVLLDGVPLVQ----------YDHH---YLHRQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 94 LTMVFQHFNLWSHmTVLENV--------MEapvQVLGLSK-ADAHERAVRYLDkvGIDERArGKYPVHLSGGQQQRVSIA 164
Cdd:TIGR00958 557 VALVGQEPVLFSG-SVRENIaygltdtpDE---EIMAAAKaANAHDFIMEFPN--GYDTEV-GEKGSQLSGGQKQRIAIA 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 165 RALAMEPEVLLFDEPTSALDpelvGEVLRIMQKLAE-EGKTMVVVTHEMEFARHvSNHVIFLHKGLIEEQGPPAELFGNP 243
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALD----AECEQLLQESRSrASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-228 |
6.02e-18 |
|
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: 78.80 E-value: 6.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGD--HEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRdkdgqlkvfd 83
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 84 kkqLQLLRTRLTMVFQHFNLWSHmTVLENVmeapvqvlglskadaheravryldkvgiderargkypvhLSGGQQQRVSI 163
Cdd:cd03246 71 ---PNELGDHVGYLPQDDELFSG-SIAENI---------------------------------------LSGGQRQRLGL 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491074476 164 ARALAMEPEVLLFDEPTSALDPElvGE--VLRIMQKLAEEGKTMVVVTHEMEFARHVsNHVIFLHKG 228
Cdd:cd03246 108 ARALYGNPRILVLDEPNSHLDVE--GEraLNQAIAALKAAGATRIVIAHRPETLASA-DRILVLEDG 171
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-213 |
6.12e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.65 E-value: 6.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 21 LKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDGqlkvfdkkqlqlLRTRLTMVFQH 100
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAA------------LAAGVAIIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 101 FNLWSHMTVLENVMeapvqvLG--------LSKADAHERAVRYLDKVG--IDERARGKYpvhLSGGQQQRVSIARALAME 170
Cdd:PRK11288 88 LHLVPEMTVAENLY------LGqlphkggiVNRRLLNYEAREQLEHLGvdIDPDTPLKY---LSIGQRQMVEIAKALARN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491074476 171 PEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEME 213
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRME 201
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
153-228 |
1.05e-17 |
|
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: 78.67 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElVGEvlRIMQKL----AEEGKTMVVVTHEMEFARHVsNHVIFLHKG 228
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH-VGR--HIFENCilglLLNNKTRILVTHQLQLLPHA-DQIVVLDNG 203
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-239 |
1.47e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 81.63 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 19 EVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPS---EGSISLNNE--DIRMVRDKDGQLKVFDKkQLQLLRTR 93
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMpiDAKEMRAISAYVQQDDL-FIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 94 LTMVFQ-HFNLWSHMTVLENV--MEAPVQVLGLSKAdAHERavryldkVGIDERARGkypvhLSGGQQQRVSIARALAME 170
Cdd:TIGR00955 118 EHLMFQaHLRMPRRVTKKEKRerVDEVLQALGLRKC-ANTR-------IGVPGRVKG-----LSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491074476 171 PEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHE-----ME-FarhvsNHVIFLHKGLIEEQGPPAEL 239
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpsselFElF-----DKIILMAEGRVAYLGSPDQA 254
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-234 |
1.68e-17 |
|
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: 78.85 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 20 VLKGVSLAANAGDVISIIGSSGSGKSTFLRCINflekpsegsislnnediRMVRDKD---GQLkVFDKKQL--QLLRTRL 94
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAIS-----------------GRVEGGGttsGQI-LFNGQPRkpDQFQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 95 TMVFQHFNLWSHMTVLENVMEAPVQVLGLSKADAHER---AVRYLDKVGiDERARGKYPVHLSGGQQQRVSIARALAMEP 171
Cdd:cd03234 84 AYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKkrvEDVLLRDLA-LTRIGGNLVKGISGGERRRVSIAVQLLWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491074476 172 EVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTH----EMeFarHVSNHVIFLHKGLIEEQG 234
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHqprsDL-F--RLFDRILLLSSGEIVYSG 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-236 |
1.89e-17 |
|
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: 77.95 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLE--KPSEGSISLNNEDIRmvrdkdgQLKVFD 83
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDIT-------DLPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 84 KKqlqllRTRLTMVFQHfnlwshmtvlenvmeaPVQVLGLSKADAheraVRYLDkvgiderargkypVHLSGGQQQRVSI 163
Cdd:cd03217 74 RA-----RLGIFLAFQY----------------PPEIPGVKNADF----LRYVN-------------EGFSGGEKKRNEI 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491074476 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHV-SNHVIFLHKGLIEEQGPP 236
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
119-256 |
2.32e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.97 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 119 QVLGLSKADAheRAVRYLDKVGIDERAR--GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQ 196
Cdd:PRK10418 107 LALGKPADDA--TLTAALEAVGLENAARvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLE 184
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491074476 197 KLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKSPRLQQFLSGAL 256
Cdd:PRK10418 185 SIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSAHL 245
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-230 |
2.62e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.97 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYG-----DHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDI-RMVRDKdgql 79
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtKLPEYK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 80 kvfdkkqlqllRTRL-TMVFQHFNL--WSHMTVLENVMEA--PVQVLGLSKA-DAHERAV--RYLDKVGIDERARGKYPV 151
Cdd:COG1101 78 -----------RAKYiGRVFQDPMMgtAPSMTIEENLALAyrRGKRRGLRRGlTKKRRELfrELLATLGLGLENRLDTKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 152 -HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGK-TMVVVTHEMEFARHVSNHVIFLHKGL 229
Cdd:COG1101 147 gLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
.
gi 491074476 230 I 230
Cdd:COG1101 227 I 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-251 |
3.19e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.64 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGD--HEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlKVFD 83
Cdd:PRK11160 339 LTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI----------ADYS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 84 KKQLqllRTRLTMVFQHFNLWSHmTVLENvmeapvqvLGLSKADAH-ERAVRYLDKVGIDERARGKYPV---------HL 153
Cdd:PRK11160 409 EAAL---RQAISVVSQRVHLFSA-TLRDN--------LLLAAPNASdEALIEVLQQVGLEKLLEDDKGLnawlgeggrQL 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMEFARHVsNHVIFLHKGLIEEQ 233
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQ 554
|
250
....*....|....*...
gi 491074476 234 GPPAELFGnpKSPRLQQF 251
Cdd:PRK11160 555 GTHQELLA--QQGRYYQL 570
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
12-241 |
6.19e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.21 E-value: 6.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 12 HKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlkvfDKKQLQLLR 91
Cdd:PRK13642 14 YEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELL-------------TAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 92 TRLTMVFQHFNLWSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDErARGKYPVHLSGGQQQRVSIARALAMEP 171
Cdd:PRK13642 81 RKIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLD-FKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491074476 172 EVLLFDEPTSALDPELVGEVLRIMQKLAEEGK-TMVVVTHEMEFARHvSNHVIFLHKGLIEEQGPPAELFG 241
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-232 |
6.22e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.72 E-value: 6.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLA-----------AN-AGdvisiigssgsgKSTFLRCINFLEKPSEGSISLnnedirmvr 73
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRidrgdrigligPNgAG------------KSTLLKLLAGELEPDSGTVKL--------- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 74 dkdGQ-LKV--FDKKQLQLLrtrltmvfqhfnlwSHMTVLENVMEApvqvlglsKADAHERAVR-YLDKVGID-ERARGk 148
Cdd:COG0488 375 ---GEtVKIgyFDQHQEELD--------------PDKTVLDELRDG--------APGGTEQEVRgYLGRFLFSgDDAFK- 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 149 yPVH-LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLriMQKLAE-EGkTMVVVTHEMEFARHVSNHVIFLH 226
Cdd:COG0488 429 -PVGvLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETL-EAL--EEALDDfPG-TVLLVSHDRYFLDRVATRILEFE 503
|
....*.
gi 491074476 227 KGLIEE 232
Cdd:COG0488 504 DGGVRE 509
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
19-239 |
9.58e-17 |
|
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: 79.40 E-value: 9.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 19 EVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKdgqlkvfdkkqlqLLRTRLTMVF 98
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPA-------------WLRRQMGVVL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 99 QHFNLWSHmTVLENVmeapvqvlGLSKADAHERAVRYLDKVG-----IDERARG------KYPVHLSGGQQQRVSIARAL 167
Cdd:TIGR01846 538 QENVLFSR-SIRDNI--------ALCNPGAPFEHVIHAAKLAgahdfISELPQGyntevgEKGANLSGGQRQRIAIARAL 608
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491074476 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMEFARHvSNHVIFLHKGLIEEQGPPAEL 239
Cdd:TIGR01846 609 VGNPRILIFDEATSALDYESEALIMRNMREIC-RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEEL 678
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-234 |
1.41e-16 |
|
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: 75.04 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHE--VLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDkdgqlkvfd 83
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 84 kkqlqLLRTRLTMVFQHFNLWShMTVLENVmeapvqvlglskadaheravryldkvgiderarGKypvHLSGGQQQRVSI 163
Cdd:cd03247 72 -----ALSSLISVLNQRPYLFD-TTLRNNL---------------------------------GR---RFSGGERQRLAL 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491074476 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMEFARHVsNHVIFLHKGLIEEQG 234
Cdd:cd03247 110 ARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-250 |
1.99e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.36 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 2 SENKLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdKDGQLKV 81
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL-----ESWSSKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 82 FDKKQLQLLrtrltmvfQHFNLWSHMTVLENVM--EAPVQ-VLGLSKADAHERAVRYLDKVGIDERARgKYPVHLSGGQQ 158
Cdd:PRK10575 83 FARKVAYLP--------QQLPAAEGMTVRELVAigRYPWHgALGRFGAADREKVEEAISLVGLKPLAH-RLVDSLSGGER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPA 237
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPA 233
|
250
....*....|...
gi 491074476 238 ELFgnpKSPRLQQ 250
Cdd:PRK10575 234 ELM---RGETLEQ 243
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
153-238 |
2.22e-16 |
|
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: 78.25 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvGE--VLRIMQKLAEEGKTMVVVTHEMEFARHVsNHVIFLHKGLI 230
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDE--GEaaLAAAIRALKARGATVVVITHRPSLLAAV-DKLLVLRDGRV 544
|
....*...
gi 491074476 231 EEQGPPAE 238
Cdd:COG4618 545 QAFGPRDE 552
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-234 |
4.48e-16 |
|
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: 74.88 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 5 KLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRdkdgqlkvfdk 84
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG----------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 85 kqlqllrtrLTMVFQhfnlwSHMTVLENV-MEApvQVLGLSKADAHERAVRYLDKVGIDERarGKYPV-HLSGGQQQRVS 162
Cdd:cd03220 91 ---------LGGGFN-----PELTGRENIyLNG--RLLGLSRKEIDEKIDEIIEFSELGDF--IDLPVkTYSSGMKARLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491074476 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQG 234
Cdd:cd03220 153 FAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-228 |
5.80e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDG-QL 79
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 80 KVfdkkqlqllrtrlTMVFQHFNLWSHMTVLEN--VMEAPV-QVLGLSKADAHE---RAVRYLDKVGIdERARGKYPVHL 153
Cdd:PRK09700 81 GI-------------GIIYQELSVIDELTVLENlyIGRHLTkKVCGVNIIDWREmrvRAAMMLLRVGL-KVDLDEKVANL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491074476 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:PRK09700 147 SISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
8-230 |
5.83e-16 |
|
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: 74.43 E-value: 5.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 8 VTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTflrCINFLEK---PSEGSISLNNEDIRMVRDKdgqlkvfdk 84
Cdd:cd03248 17 VTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKST---VVALLENfyqPQGGQVLLDGKPISQYEHK--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 85 kqlqLLRTRLTMVFQHFNLWSHmTVLEN------------VMEAPvqvlglSKADAHERAVRYLDkvGIDERArGKYPVH 152
Cdd:cd03248 85 ----YLHSKVSLVGQEPVLFAR-SLQDNiayglqscsfecVKEAA------QKAHAHSFISELAS--GYDTEV-GEKGSQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQKLAE--EGKTMVVVTHEMEFARHvSNHVIFLHKGLI 230
Cdd:cd03248 151 LSGGQKQRVAIARALIRNPQVLILDEATSALDAE---SEQQVQQALYDwpERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
140-242 |
5.91e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 77.32 E-value: 5.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 140 GIDERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVs 219
Cdd:PLN03232 728 GRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM- 806
|
90 100
....*....|....*....|...
gi 491074476 220 NHVIFLHKGLIEEQGPPAELFGN 242
Cdd:PLN03232 807 DRIILVSEGMIKEEGTFAELSKS 829
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
79-246 |
6.16e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 76.10 E-value: 6.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 79 LKVFDKKQLQLLRTRLTMVFQHFN--LWSHMTVLENVMEA-PVQVLGLS----KADAHERAVRYLDKVGI--DERARGKY 149
Cdd:COG4170 76 LKLSPRERRKIIGREIAMIFQEPSscLDPSAKIGDQLIEAiPSWTFKGKwwqrFKWRKKRAIELLHRVGIkdHKDIMNSY 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 150 PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVV-VTHEMEFARHVSNHVIFLHKG 228
Cdd:COG4170 156 PHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILlISHDLESISQWADTITVLYCG 235
|
170
....*....|....*...
gi 491074476 229 LIEEQGPPAELFGNPKSP 246
Cdd:COG4170 236 QTVESGPTEQILKSPHHP 253
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-239 |
1.39e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 75.77 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 21 LKGVSLAANAGDVISIIGSSGSGKSTFlrcINFLEK---PSEGSISLNNEDIRMVrdkdgqlkvfdkkQLQLLRTRLTMV 97
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRvfdPQSGRILIDGTDIRTV-------------TRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 98 FQHFNLWSHmTVLEN------------VMEApvqvlgLSKADAHERAVRYLDKVG--IDERARgkypvHLSGGQQQRVSI 163
Cdd:PRK13657 415 FQDAGLFNR-SIEDNirvgrpdatdeeMRAA------AERAQAHDFIERKPDGYDtvVGERGR-----QLSGGERQRLAI 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491074476 164 ARALAMEPEVLLFDEPTSALDPELvgEVlRIMQKLAE--EGKTMVVVTHEMEFARHvSNHVIFLHKGLIEEQGPPAEL 239
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVET--EA-KVKAALDElmKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDEL 556
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-234 |
1.67e-15 |
|
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: 73.20 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDirmvrdkdgqlkvFDKK 85
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHP-------------WTRK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQllrtRLTMVFQHFNLWSHMTVLENvMEAPVQVLGLSKADAHEravrYLDKVGIdeRARGKYPV-HLSGGQQQRVSIA 164
Cdd:TIGR03740 68 DLH----KIGSLIESPPLYENLTAREN-LKVHTTLLGLPDSRIDE----VLNIVDL--TNTGKKKAkQFSLGMKQRLGIA 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQG 234
Cdd:TIGR03740 137 IALLNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQG 206
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
152-228 |
2.20e-15 |
|
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: 70.94 E-value: 2.20e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491074476 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLRIMqkLAEEGKTMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:cd03221 70 QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI-EALEEA--LKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-248 |
2.81e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.00 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMvrdkdgqLKVFDKK 85
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISL-------LPLHARA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 qlqllRTRLTMVFQHFNLWSHMTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIdERARGKYPVHLSGGQQQRVSIAR 165
Cdd:PRK10895 77 -----RRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKS 245
Cdd:PRK10895 151 ALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
...
gi 491074476 246 PRL 248
Cdd:PRK10895 231 KRV 233
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
129-249 |
3.29e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 73.68 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 129 HERAVRYLDKVGIDER--ARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAE-EGKTM 205
Cdd:PRK15093 133 KRRAIELLHRVGIKDHkdAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTI 212
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 491074476 206 VVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNPKSPRLQ 249
Cdd:PRK15093 213 LLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQ 256
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-232 |
3.81e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.44 E-value: 3.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 17 DHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDGQlkvfdKKQLQLL--RTRL 94
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAV-----KKGMAYIteSRRD 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 95 TMVFQHFNLWSHMTVLENVMEAPVQ-VLGL-SKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARALAMEPE 172
Cdd:PRK09700 350 NGFFPNFSIAQNMAISRSLKDGGYKgAMGLfHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 173 VLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEE 232
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-242 |
5.08e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.22 E-value: 5.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlk 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 81 vfDKKQLQLLRTRLTMVFQHFNLWSHMTVLENVmeapvqVLG---LSKADAHERAVRYLDKVGIDERARGKYPVHLSGGQ 157
Cdd:PRK11614 71 --DWQTAKIMREAVAIVPEGRRVFSRMTVEENL------AMGgffAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPA 237
Cdd:PRK11614 143 QQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGD 222
|
....*
gi 491074476 238 ELFGN 242
Cdd:PRK11614 223 ALLAN 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
123-243 |
5.24e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.51 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 123 LSKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE- 201
Cdd:PRK15112 120 LEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKq 199
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 491074476 202 GKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELFGNP 243
Cdd:PRK15112 200 GISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
44-236 |
9.12e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 73.89 E-value: 9.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlkvfdKKQLQLLRTRLTMVFQHFNLWSHMTVLENVMEApVQVLGL 123
Cdd:TIGR01257 969 KTTTLSILTGLLPPTSGTVLVGGKDI--------------ETNLDAVRQSLGMCPQHNILFHHLTVAEHILFY-AQLKGR 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 124 SKADAHERAVRYLDKVGIDERaRGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLaEEGK 203
Cdd:TIGR01257 1034 SWEEAQLEMEAMLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGR 1111
|
170 180 190
....*....|....*....|....*....|...
gi 491074476 204 TMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPP 236
Cdd:TIGR01257 1112 TIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-228 |
1.52e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.37 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 18 HEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCI--NFLEKPSEGSISLNNEDIrmvrdkdgqlkvfdkkqlqllrtrlt 95
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQF-------------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 96 mvfqhfnlWSHMTVLENVmeapvqvlgLSKADAHErAVRYLDKVGIDE----RARgkyPVHLSGGQQQRVSIARALAMEP 171
Cdd:COG2401 97 --------GREASLIDAI---------GRKGDFKD-AVELLNAVGLSDavlwLRR---FKELSTGQKFRFRLALLLAERP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491074476 172 EVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVS-NHVIFLHKG 228
Cdd:COG2401 156 KLLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATHHYDVIDDLQpDLLIFVGYG 214
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
123-257 |
2.68e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 72.12 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 123 LSKADAHERAVRYLDKVGID---ERARGKypvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGE---VLRIMQ 196
Cdd:COG1245 184 LEKVDERGKLDELAEKLGLEnilDRDISE----LSGGELQRVAIAAALLRDADFYFFDEPSSYLD---IYQrlnVARLIR 256
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491074476 197 KLAEEGKTMVVVTHEMEFARHVSNHVIFLHkglieeqGPPAeLFG---NPKSPR--LQQFLSGALK 257
Cdd:COG1245 257 ELAEEGKYVLVVEHDLAILDYLADYVHILY-------GEPG-VYGvvsKPKSVRvgINQYLDGYLP 314
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-210 |
4.62e-14 |
|
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: 71.22 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 16 GDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMV-RDKDGQLKVFDKKQLQLLRTrl 94
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWdRETFGKHIGYLPQDVELFPG-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 95 tmvfqhfnlwshmTVLENVME-----APVQVLGLSK-ADAHERAVRYLDKVGIDERARGkypVHLSGGQQQRVSIARALA 168
Cdd:TIGR01842 407 -------------TVAENIARfgenaDPEKIIEAAKlAGVHELILRLPDGYDTVIGPGG---ATLSGGQRQRIALARALY 470
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491074476 169 MEPEVLLFDEPTSALDPElvGE--VLRIMQKLAEEGKTMVVVTH 210
Cdd:TIGR01842 471 GDPKLVVLDEPNSNLDEE--GEqaLANAIKALKARGITVVVITH 512
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-210 |
6.06e-14 |
|
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: 68.29 E-value: 6.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDGQLKVFDKK 85
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QlQLLRTRLTmVFQHFNLWSHMTVLENVMEApvqvlglskadaheravryLDKVGIdeRARGKYPVH-LSGGQQQRVSIA 164
Cdd:cd03231 81 A-PGIKTTLS-VLENLRFWHADHSDEQVEEA-------------------LARVGL--NGFEDRPVAqLSAGQQRRVALA 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491074476 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTH 210
Cdd:cd03231 138 RLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
119-239 |
1.09e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 69.76 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 119 QVLGLSKADAHERAVRYLDKVGIDERArGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL 198
Cdd:NF000106 112 R*LDLSRKDARARADELLERFSLTEAA-GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM 190
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 491074476 199 AEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAEL 239
Cdd:NF000106 191 VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
106-239 |
1.21e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.87 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 106 HMTVLENVM-------EAPVQVLgLSKADAHEravrYLDKV--GID----ERARGkypvhLSGGQQQRVSIARALAMEPE 172
Cdd:PRK11174 436 HGTLRDNVLlgnpdasDEQLQQA-LENAWVSE----FLPLLpqGLDtpigDQAAG-----LSVGQAQRLALARALLQPCQ 505
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491074476 173 VLLFDEPTSALDpelVGEVLRIMQKL--AEEGKTMVVVTHEMEFARHVsNHVIFLHKGLIEEQGPPAEL 239
Cdd:PRK11174 506 LLLLDEPTASLD---AHSEQLVMQALnaASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAEL 570
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-225 |
1.78e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.43 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENK--LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDkdgq 78
Cdd:PRK10247 1 MQENSplLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 79 lkvfdkkqlQLLRTRLTMVFQHFNLWSHmTVLENVMeAPVQVLGlsKADAHERAVRYLDKVGIDERARGKYPVHLSGGQQ 158
Cdd:PRK10247 77 ---------EIYRQQVSYCAQTPTLFGD-TVYDNLI-FPWQIRN--QQPDPAIFLDDLERFALPDTILTKNIAELSGGEK 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491074476 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVV-VTHEMEFARHVSNhVIFL 225
Cdd:PRK10247 144 QRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwVTHDKDEINHADK-VITL 210
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-239 |
2.33e-13 |
|
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: 69.08 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 16 GDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCI-NFLEkPSEGSISLNNEDIRMVrdkdgqlkvfdkkQLQLLRTRL 94
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfRFYD-VTSGRILIDGQDIRDV-------------TQASLRAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 95 TMVFQH---FNlwshMTVLENVmeapvqvlGLSKADAHERAVR------------------YLDKVGidERArgkypVHL 153
Cdd:COG5265 435 GIVPQDtvlFN----DTIAYNI--------AYGRPDASEEEVEaaaraaqihdfieslpdgYDTRVG--ERG-----LKL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMEFARHvSNHVIFLHKGLIEEQ 233
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAHRLSTIVD-ADEILVLEAGRIVER 573
|
....*.
gi 491074476 234 GPPAEL 239
Cdd:COG5265 574 GTHAEL 579
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
104-257 |
3.06e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.60 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 104 WSHMTVLENV-MEAPVQVLG-LSKADAHERAV--RYLDKVGIDERaRGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
Cdd:PRK15056 91 WSFPVLVEDVvMMGRYGHMGwLRRAKKRDRQIvtAALARVDMVEF-RHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491074476 180 TSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLhKGLIEEQGPPAELFgnpKSPRLQQFLSGALK 257
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTF---TAENLELAFSGVLR 243
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-210 |
3.10e-13 |
|
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: 66.61 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDkdgqlkvfdkk 85
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 qlqlLRTRLTMVFQHFN-LWSHMTVLENvmeapVQVLGLSKADAHERAVRYLDKVGIDERArgKYPVH-LSGGQQQRVSI 163
Cdd:TIGR01189 70 ----EPHENILYLGHLPgLKPELSALEN-----LHFWAAIHGGAQRTIEDALAAVGLTGFE--DLPAAqLSAGQQRRLAL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491074476 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTH 210
Cdd:TIGR01189 139 ARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-210 |
3.78e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.44 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 4 NKLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvfd 83
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 84 kkqLQLLRTRLTMVfQHFN-LWSHMTVLENVmEAPVQVLGLSKADAHERavryLDKVGIDERA--RGKYpvhLSGGQQQR 160
Cdd:PRK13539 68 ---DPDVAEACHYL-GHRNaMKPALTVAENL-EFWAAFLGGEELDIAAA----LEAVGLAPLAhlPFGY---LSAGQKRR 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491074476 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTH 210
Cdd:PRK13539 136 VALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
153-217 |
6.07e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.91 E-value: 6.07e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGevlRIMQKLAEE--GKTMVVVTHEMEFARH 217
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEA---ALYQLLREElpGTTVISVGHRSTLAAF 549
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
142-240 |
1.02e-12 |
|
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: 67.66 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 142 DERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQKLAEEGKTMVVVTHEMEFARHVs 219
Cdd:TIGR00957 750 DRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhvIGPEGVLKNKTRILVTHGISYLPQV- 828
|
90 100
....*....|....*....|.
gi 491074476 220 NHVIFLHKGLIEEQGPPAELF 240
Cdd:TIGR00957 829 DVIIVMSGGKISEMGSYQELL 849
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
137-217 |
1.40e-12 |
|
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: 65.04 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 137 DKVGIDERArgkypVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQKLAEEGKTMVVVTHEMEF 214
Cdd:cd03290 130 DQTEIGERG-----INLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY 204
|
...
gi 491074476 215 ARH 217
Cdd:cd03290 205 LPH 207
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
15-239 |
1.92e-12 |
|
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: 66.69 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 15 YGDhEVLKGVSLAANAGDVISIIGSSGSGKSTFLRC-INFLEkPSEGSISLNNEDIrmvrdkdgqlKVFDKKQLqllRTR 93
Cdd:TIGR01193 485 YGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLlVGFFQ-ARSGEILLNGFSL----------KDIDRHTL---RQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 94 LTMVFQHFNLWSHmTVLENVMeapvqvLGLSKADAHERAVRYLDKVGIDERARgKYPV-----------HLSGGQQQRVS 162
Cdd:TIGR01193 550 INYLPQEPYIFSG-SILENLL------LGAKENVSQDEIWAACEIAEIKDDIE-NMPLgyqtelseegsSISGGQKQRIA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491074476 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEegKTMVVVTHEMEFARHVSNhVIFLHKGLIEEQGPPAEL 239
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLSVAKQSDK-IIVLDHGKIIEQGSHDEL 695
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-239 |
2.33e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.23 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDI-RMVRDKDGQLKVFdk 84
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCaRLTPAKAHQLGIY-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 85 kqlqllrtrltMVFQHFNLWSHMTVLENVMeapvqvLGLSK-ADAHERAVRYLDKVG----IDERARGkypvhLSGGQQQ 159
Cdd:PRK15439 90 -----------LVPQEPLLFPNLSVKENIL------FGLPKrQASMQKMKQLLAALGcqldLDSSAGS-----LEVADRQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAEL 239
Cdd:PRK15439 148 IVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-239 |
2.56e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 64.70 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVisiigssgsgKSTFLRCI--NFLEKPSEGSISLNNEDIrmvrdkdGQLKVFD 83
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVhaimgpngsgKSTLAKVLmgHPKYEVTSGSILLDGEDI-------LELSPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 84 kkqlqllRTR--LTMVFQH---------FNLWshMTVLENVMEAPvqvlgLSKADAHERAVRYLDKVGIDERARGKY-PV 151
Cdd:COG0396 74 -------RARagIFLAFQYpveipgvsvSNFL--RTALNARRGEE-----LSAREFLKLLKEKMKELGLDEDFLDRYvNE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVS-NHVIFLHKGLI 230
Cdd:COG0396 140 GFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIKpDFVHVLVDGRI 219
|
....*....
gi 491074476 231 EEQGPPaEL 239
Cdd:COG0396 220 VKSGGK-EL 227
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
44-228 |
3.30e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.52 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDGqlkvfdkkqlqlLRTRLTMVFQHFNLWSHMTVLENVM--EAPVQVL 121
Cdd:PRK10982 37 KSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA------------LENGISMVHQELNLVLQRSVMDNMWlgRYPTKGM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 122 GLSKADAHERAVRYLDKVGIDERARGKYpVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE 201
Cdd:PRK10982 105 FVDQDKMYRDTKAIFDELDIDIDPRAKV-ATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER 183
|
170 180
....*....|....*....|....*..
gi 491074476 202 GKTMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:PRK10982 184 GCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
7-243 |
3.89e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 65.50 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 7 AVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRdkdgqlkvfdkkq 86
Cdd:PRK10789 317 NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ------------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 87 LQLLRTRLTMVFQHFNLWSHmTVLENVM-----EAPVQVLGLSK-ADAHERAVR----YLDKVGidERArgkypVHLSGG 156
Cdd:PRK10789 384 LDSWRSRLAVVSQTPFLFSD-TVANNIAlgrpdATQQEIEHVARlASVHDDILRlpqgYDTEVG--ERG-----VMLSGG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEvlrIMQKLAE--EGKTMVVVTHEMEfARHVSNHVIFLHKGLIEEQG 234
Cdd:PRK10789 456 QKQRISIARALLLNAEILILDDALSAVDGRTEHQ---ILHNLRQwgEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRG 531
|
....*....
gi 491074476 235 PPAELFGNP 243
Cdd:PRK10789 532 NHDQLAQQS 540
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-239 |
5.53e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.04 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 17 DHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvfdKKQLQLLRTRLTM 96
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR-------------DYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 97 VFQHFNLWSHmTVLENVMEAPVQVLglSKADAhERAVR------YLDKV--GIDErARGKYPVHLSGGQQQRVSIARALA 168
Cdd:PRK11176 422 VSQNVHLFND-TIANNIAYARTEQY--SREQI-EEAARmayamdFINKMdnGLDT-VIGENGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491074476 169 MEPEVLLFDEPTSALDPElvGEvlRIMQKLAEE---GKTMVVVTHEMEFARHvSNHVIFLHKGLIEEQGPPAEL 239
Cdd:PRK11176 497 RDSPILILDEATSALDTE--SE--RAIQAALDElqkNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAEL 565
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-236 |
6.33e-12 |
|
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: 63.28 E-value: 6.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 14 RYGDHE--VLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRdkdgqlkvfdkkqLQLLR 91
Cdd:cd03244 11 RYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG-------------LHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 92 TRLTMVFQHFNLWSHmTVLENVmeAPvqvlgLSKADAHERaVRYLDKVGIDERARGK-----YPV-----HLSGGQQQRV 161
Cdd:cd03244 78 SRISIIPQDPVLFSG-TIRSNL--DP-----FGEYSDEEL-WQALERVGLKEFVESLpggldTVVeeggeNLSVGQRQLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 162 SIARALAMEPEVLLFDEPTSALDPELVgevlRIMQKLAEE---GKTMVVVTHE----MEFARhvsnhVIFLHKGLIEEQG 234
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETD----ALIQKTIREafkDCTVLTIAHRldtiIDSDR-----ILVLDKGRVVEFD 219
|
..
gi 491074476 235 PP 236
Cdd:cd03244 220 SP 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-228 |
8.56e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 8.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLR--CINFLEKPSEGSISLNNEDIRMVRDKDGQ 78
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKvlSGVYPHGTYEGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 79 lkvfdKKQLQLLRTRLTMVfqhfnlwSHMTVLENV-MEAPVQVLGLSKADA-HERAVRYLDKVGIDERArgKYPV-HLSG 155
Cdd:PRK13549 81 -----RAGIAIIHQELALV-------KELSVLENIfLGNEITPGGIMDYDAmYLRAQKLLAQLKLDINP--ATPVgNLGL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491074476 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
147-243 |
8.81e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.80 E-value: 8.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 147 GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElVGEvlRIMQKL---AEEGKTMVVVTHEMEFARHvSNHVI 223
Cdd:PTZ00243 777 GEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH-VGE--RVVEECflgALAGKTRVLATHQVHVVPR-ADYVV 852
|
90 100
....*....|....*....|
gi 491074476 224 FLHKGLIEEQGPPAELFGNP 243
Cdd:PTZ00243 853 ALGDGRVEFSGSSADFMRTS 872
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
111-257 |
9.22e-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: 63.15 E-value: 9.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 111 ENVMEAPVQVLG-----LSKADAHERAVRYLDKVGID---ERARGkypvHLSGGQQQRVSIARALAMEPEVLLFDEPTSA 182
Cdd:cd03236 94 QYVDLIPKAVKGkvgelLKKKDERGKLDELVDQLELRhvlDRNID----QLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491074476 183 LDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHkglieeqGPPAE--LFGNPKSPR--LQQFLSGALK 257
Cdd:cd03236 170 LDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLY-------GEPGAygVVTLPKSVRegINEFLDGYLP 241
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
153-210 |
1.05e-11 |
|
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: 61.40 E-value: 1.05e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGevlRIMQKLAEEGKTMVVVTH 210
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED---RLYQLLKELGITVISVGH 146
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
152-257 |
1.17e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGE---VLRIMQKLAeEGKTMVVVTHEMEFARHVSN--HVIFlh 226
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD---IRQrlnVARLIRELA-EGKYVLVVEHDLAVLDYLADnvHIAY-- 285
|
90 100 110
....*....|....*....|....*....|....*
gi 491074476 227 kglieeqGPPAE--LFGNPKSPR--LQQFLSGALK 257
Cdd:PRK13409 286 -------GEPGAygVVSKPKGVRvgINEYLKGYLP 313
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-234 |
1.90e-11 |
|
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: 61.96 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 12 HKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEdirmvrdkdgqlkVFDKKQLQLLR 91
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-------------VPWKRRKKFLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 92 tRLTMVF-QHFNLWSHMTVLE--NVMEApvqVLGLSKADAHERAVRYLDKVGIDERArgKYPV-HLSGGQQQRVSIARAL 167
Cdd:cd03267 95 -RIGVVFgQKTQLWWDLPVIDsfYLLAA---IYDLPPARFKKRLDELSELLDLEELL--DTPVrQLSLGQRMRAEIAAAL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 168 AMEPEVLLFDEPTSALD---PELVGEVLRIMQKlaEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQG 234
Cdd:cd03267 169 LHEPEILFLDEPTIGLDvvaQENIRNFLKEYNR--ERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
153-230 |
5.29e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVG---EVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGL 229
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
.
gi 491074476 230 I 230
Cdd:PRK10762 473 I 473
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
152-230 |
5.49e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 5.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVG---EVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
..
gi 491074476 229 LI 230
Cdd:PRK13549 482 KL 483
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
153-228 |
5.77e-11 |
|
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: 62.15 E-value: 5.77e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
87-224 |
6.73e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.35 E-value: 6.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 87 LQLLRTRLTMVFQHFNLWShMTVLENVMeapvqvlgLSKADAHERAVRYLDK-VGIDERAR----------GKYPVHLSG 155
Cdd:PTZ00265 1291 LKDLRNLFSIVSQEPMLFN-MSIYENIK--------FGKEDATREDVKRACKfAAIDEFIEslpnkydtnvGPYGKSLSG 1361
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491074476 156 GQQQRVSIARALAMEPEVLLFDEPTSALDP---ELVGEVLRIMQKLAEegKTMVVVTHEMEFARHVSNHVIF 224
Cdd:PTZ00265 1362 GQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKAD--KTIITIAHRIASIKRSDKIVVF 1431
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-236 |
6.96e-11 |
|
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: 60.12 E-value: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 5 KLAVTELHKRYGDH--EVLKGVSLAANAGDVISIIGSSGSGKSTFLRCI-NFLEkPSEGSISLNNEDIRMVrdkdgqlkv 81
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALfRFLE-AEEGKIEIDGIDISTI--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 82 fdkkQLQLLRTRLTMVFQHFNLWSHmTVLENVmeapvqvlglskadahERAVRYldkvgIDERARGKYPV-----HLSGG 156
Cdd:cd03369 76 ----PLEDLRSSLTIIPQDPTLFSG-TIRSNL----------------DPFDEY-----SDEEIYGALRVsegglNLSQG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEM----EFARhvsnhVIFLHKGLIEE 232
Cdd:cd03369 130 QRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEF-TNSTILTIAHRLrtiiDYDK-----ILVMDAGEVKE 203
|
....
gi 491074476 233 QGPP 236
Cdd:cd03369 204 YDHP 207
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
153-212 |
7.10e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.73 E-value: 7.10e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVG---EVLRIMQKLAEEGKTMVVVTHEM 212
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSEL 464
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
6-215 |
7.23e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.82 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKdgqlkvfdkk 85
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 qlqllrtrltmvFQHFNLW--------SHMTVLENV-MEAPVQvlGLSKADAHERAvryLDKVGIDERARgkYPVH-LSG 155
Cdd:PRK13538 72 ------------YHQDLLYlghqpgikTELTALENLrFYQRLH--GPGDDEALWEA---LAQVGLAGFED--VPVRqLSA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491074476 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKtMVVVT--HEMEFA 215
Cdd:PRK13538 133 GQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGG-MVILTthQDLPVA 193
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
44-223 |
1.01e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 60.11 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDIRMvrdKDGQLKV-FDKKQLQLLRTRLTmvfqhfNLWSHMTVLENVMEaPVQVLG 122
Cdd:cd03237 38 KTTFIKMLAGVLKPDEGDIEIELDTVSY---KPQYIKAdYEGTVRDLLSSITK------DFYTHPYFKTEIAK-PLQIEQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 123 LskadaHERAVRyldkvgiderargkypvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEG 202
Cdd:cd03237 108 I-----LDREVP-----------------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENN 165
|
170 180
....*....|....*....|..
gi 491074476 203 -KTMVVVTHEMEFARHVSNHVI 223
Cdd:cd03237 166 eKTAFVVEHDIIMIDYLADRLI 187
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
153-223 |
2.25e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 2.25e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVI 223
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
119-236 |
2.27e-10 |
|
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: 59.17 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 119 QVLGLSKADAHE---------RAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARALAME---PEVLLFDEPTSALDPE 186
Cdd:cd03271 127 DVLDMTVEEALEffenipkiaRKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFH 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 491074476 187 LVGEVLRIMQKLAEEGKTMVVVTHEMEFARhVSNHVIFL------HKGLIEEQGPP 236
Cdd:cd03271 207 DVKKLLEVLQRLVDKGNTVVVIEHNLDVIK-CADWIIDLgpeggdGGGQVVASGTP 261
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-228 |
2.27e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.22 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 13 KRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLR--CINFLEKPSEGSISLNNEDI--RMVRDKDgqlkvfdkkqlq 88
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKilSGVYPHGTWDGEIYWSGSPLkaSNIRDTE------------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 89 llRTRLTMVFQHFNLWSHMTVLENV-MEAPVQVLGLSKADA--HERAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIAR 165
Cdd:TIGR02633 77 --RAGIVIIHQELTLVPELSVAENIfLGNEITLPGGRMAYNamYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491074476 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKG 228
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-211 |
4.53e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.51 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 20 VLKGVSLAANAGDVISIIGSSGSGKSTFLRCInflekpsEGSISLNNedirmvrdKDGQLKVFDKKQLQLLRTRLTMVFQ 99
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQGNN--------FTGTILANNRKPTKQILKRTGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 100 HFNLWSHMTVLENVMEapVQVLGLSKADAHERAVRYLDKVgIDERARGK---------YPVHLSGGQQQRVSIARALAME 170
Cdd:PLN03211 148 DDILYPHLTVRETLVF--CSLLRLPKSLTKQEKILVAESV-ISELGLTKcentiignsFIRGISGGERKRVSIAHEMLIN 224
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491074476 171 PEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHE 211
Cdd:PLN03211 225 PSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
54-230 |
5.47e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.91 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 54 LEKPSEGSISLNNEDIRMVRDKDgqlkvfdkkqlqllRTRLTMVF-----QHFNLWSHMTVLENVMEAPVQVLGLSKADA 128
Cdd:PRK15439 312 LRPARGGRIMLNGKEINALSTAQ--------------RLARGLVYlpedrQSSGLYLDAPLAWNVCALTHNRRGFWIKPA 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 129 HERAV--RYLDKVGI-----DERARGkypvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE 201
Cdd:PRK15439 378 RENAVleRYRRALNIkfnhaEQAART-----LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ 452
|
170 180
....*....|....*....|....*....
gi 491074476 202 GKTMVVVTHEMEFARHVSNHVIFLHKGLI 230
Cdd:PRK15439 453 NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
146-212 |
6.36e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.97 E-value: 6.36e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491074476 146 RGKYPVH------LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEM 212
Cdd:PRK10982 379 RVKTPGHrtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEM 451
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
130-212 |
6.43e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.77 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 130 ERAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVG---EVLRIMQKLAEEGKTMV 206
Cdd:PRK11288 374 ENADRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID---VGakhEIYNVIYELAAQGVAVL 450
|
....*.
gi 491074476 207 VVTHEM 212
Cdd:PRK11288 451 FVSSDL 456
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
44-240 |
6.53e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 57.93 E-value: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEkPSEGSISLNNEDIRMvrdkdgqlkvFDKKQLQLLRTRLTmvfQHFNLWSHMTVLenvmeapvQVLGL 123
Cdd:COG4138 35 KSTLLARMAGLL-PGQGEILLNGRPLSD----------WSAAELARHRAYLS---QQQSPPFAMPVF--------QYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 124 S-----KADAHERAVRYL-DKVGIDErargKYP---VHLSGGQQQRVSIARAL-----AMEPE--VLLFDEPTSALDPEL 187
Cdd:COG4138 93 HqpagaSSEAVEQLLAQLaEALGLED----KLSrplTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491074476 188 VGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAELF 240
Cdd:COG4138 169 QAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
151-257 |
7.60e-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: 56.43 E-value: 7.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEG-KTMVVVTHEMEFARHVSNHVIflhkgL 229
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHDLAVLDYLSDRIH-----V 144
|
90 100 110
....*....|....*....|....*....|
gi 491074476 230 IEEQGPPAELFGNPKSPR--LQQFLSGALK 257
Cdd:cd03222 145 FEGEPGVYGIASQPKGTRegINRFLRGYLI 174
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
154-226 |
8.50e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.72 E-value: 8.50e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491074476 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLH 226
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLH 415
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
99-239 |
1.34e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.21 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 99 QHFNLWSHMTVLEN-VMEApvQVLGLSKADAHERAVRYLDKVGIDERArGKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
Cdd:NF033858 346 QAFSLYGELTVRQNlELHA--RLFHLPAAEIAARVAEMLERFDLADVA-DALPDSLPLGIRQRLSLAVAVIHKPELLILD 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491074476 178 EPTSALDPELVGEVLRIMQKLA-EEGKTMVVVTHEM-EFAR--HVSnhviFLHKGLIEEQGPPAEL 239
Cdd:NF033858 423 EPTSGVDPVARDMFWRLLIELSrEDGVTIFISTHFMnEAERcdRIS----LMHAGRVLASDTPAAL 484
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
153-223 |
1.41e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.87 E-value: 1.41e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMEFARHVSNHVI 223
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
153-228 |
1.65e-09 |
|
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: 55.71 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHE-----ME-FarhvsNHVIFLH 226
Cdd:cd03232 109 LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQpsasiFEkF-----DRLLLLK 183
|
..
gi 491074476 227 KG 228
Cdd:cd03232 184 RG 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
152-250 |
2.36e-09 |
|
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: 57.25 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGlie 231
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRG--- 234
|
90 100
....*....|....*....|....*
gi 491074476 232 eQGPPAElfGN------PKSPRLQQ 250
Cdd:TIGR03719 235 -RGIPWE--GNysswleQKQKRLEQ 256
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
132-221 |
5.04e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.18 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 132 AVRYLDKVGIDERArGKYPVH-LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKT-MVVVT 209
Cdd:PRK10938 381 AQQWLDILGIDKRT-ADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVS 459
|
90
....*....|..
gi 491074476 210 HEMEFARHVSNH 221
Cdd:PRK10938 460 HHAEDAPACITH 471
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
54-239 |
7.38e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.80 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 54 LEKPSEGSISLNNEDIRM--VRDkdgqlkvfdkkqlqllRTRLTMVF-----QHFNLWSHMTVLENVM-----EAPVQVL 121
Cdd:COG3845 307 LRPPASGSIRLDGEDITGlsPRE----------------RRRLGVAYipedrLGRGLVPDMSVAENLIlgryrRPPFSRG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 122 G-LSKADAHERAVRYLDK-----VGIDERARgkypvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIM 195
Cdd:COG3845 371 GfLDRKAIRAFAEELIEEfdvrtPGPDTPAR-----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLD---VGAIEFIH 442
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491074476 196 QKL---AEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAEL 239
Cdd:COG3845 443 QRLlelRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
128-210 |
1.26e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.80 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 128 AHERAVRYLDKVGIDERargkyPV----HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGK 203
Cdd:NF040905 116 TNRRARELLAKVGLDES-----PDtlvtDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGI 190
|
....*..
gi 491074476 204 TMVVVTH 210
Cdd:NF040905 191 TSIIISH 197
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
119-239 |
1.85e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 54.63 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 119 QVLGLSKADAHE---------RAVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARAL---AMEPEVLLFDEPTSALDPE 186
Cdd:TIGR00630 787 DVLDMTVEEAYEffeavpsisRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFD 866
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 491074476 187 LVGEVLRIMQKLAEEGKTMVVVTHEMEFARhVSNHVIFL------HKGLIEEQGPPAEL 239
Cdd:TIGR00630 867 DIKKLLEVLQRLVDKGNTVVVIEHNLDVIK-TADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
153-228 |
2.33e-08 |
|
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: 52.33 E-value: 2.33e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491074476 153 LSGGQQQRVSIARALAMEPE--VLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHvSNHVIFLHKG 228
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPG 164
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
153-219 |
2.49e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 2.49e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMEFARHVS 219
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLSTIRYAN 647
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-209 |
3.82e-08 |
|
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: 52.26 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGdHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPS---EGSISLNNEDIrmvrdkdg 77
Cdd:cd03233 4 LSWRNISFTTGKGRSK-IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 78 qlkvfdKKQLQLLRTRLTMVFQHFNLWSHMTVLEnVMEAPVQVLGlskadaheravryldkvgiDERARGkypvhLSGGQ 157
Cdd:cd03233 75 ------KEFAEKYPGEIIYVSEEDVHFPTLTVRE-TLDFALRCKG-------------------NEFVRG-----ISGGE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491074476 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVT 209
Cdd:cd03233 124 RKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS 175
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-212 |
5.29e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.08 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIRMVRDKDGQlkvfdkk 85
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQ------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 qlqllRTRLTMVFQHFNLWSHMTVLENVM--EAPVQVLGLSK-ADAHERAVRYLDKVGIDERAR---GKypvhLSGGQQQ 159
Cdd:PRK10762 78 -----EAGIGIIHQELNLIPQLTIAENIFlgREFVNRFGRIDwKKMYAEADKLLARLNLRFSSDklvGE----LSIGEQQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491074476 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEM 212
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRL 201
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
153-228 |
9.30e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 9.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLF-DEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHE------MEFARhvsnhVIFL 225
Cdd:TIGR00956 902 LNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsailfEEFDR-----LLLL 976
|
...
gi 491074476 226 HKG 228
Cdd:TIGR00956 977 QKG 979
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
99-250 |
1.10e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.04 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 99 QHFNLWSHMTVLENVMEApvqvLGLSKADAheravryldKVGiderargkypvHLSGGQQQRVSIARALAMEPEVLLFDE 178
Cdd:PRK11819 134 DAADAWDLDSQLEIAMDA----LRCPPWDA---------KVT-----------KLSGGERRRVALCRLLLEKPDMLLLDE 189
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491074476 179 PTSALDPElvgEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGlieeQGPPAElfGN------PKSPRLQQ 250
Cdd:PRK11819 190 PTNHLDAE---SVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRG----RGIPWE--GNysswleQKAKRLAQ 258
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-210 |
1.81e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.80 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 1 MSENKLAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCInfLEKPS----EGSISLNNEDI-RMVRDK 75
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--AGHPAykilEGDILFKGESIlDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 76 DGQLKVFdkkqlqllrtrltMVFQH---FNLWSHMTVLENVMEAPVQVLGLSKADA---HERAVRYLDKVGIDERARGKY 149
Cdd:CHL00131 81 RAHLGIF-------------LAFQYpieIPGVSNADFLRLAYNSKRKFQGLPELDPlefLEIINEKLKLVGMDPSFLSRN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491074476 150 pVH--LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTH 210
Cdd:CHL00131 148 -VNegFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
110-254 |
2.03e-07 |
|
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: 51.55 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 110 LENVMEAPVQVLGLSkadaheravRYLDKVGiderarGKYpvhlSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVG 189
Cdd:TIGR01257 2047 IEKVANWSIQSLGLS---------LYADRLA------GTY----SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 190 EVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAEL---FGNP-------KSPR---------LQQ 250
Cdd:TIGR01257 2108 MLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLkskFGDGyivtmkiKSPKddllpdlnpVEQ 2187
|
....
gi 491074476 251 FLSG 254
Cdd:TIGR01257 2188 FFQG 2191
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
152-239 |
4.11e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 50.71 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRIMQklaeEGKTMVVVTHE----MEFARhvsnhVIF 224
Cdd:TIGR00957 1421 NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLEtdnLIQSTIRTQF----EDCTVLTIAHRlntiMDYTR-----VIV 1491
|
90
....*....|....*
gi 491074476 225 LHKGLIEEQGPPAEL 239
Cdd:TIGR00957 1492 LDKGEVAEFGAPSNL 1506
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
123-256 |
5.19e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.60 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 123 LSKADAHERaVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARAL---AMEPEVLLFDEPTSALDPELVGEVLRIMQKLA 199
Cdd:PRK00635 781 LDEPSIHEK-IHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLT 859
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491074476 200 EEGKTMVVVTHEMEFARhVSNHVIflhkglieEQGP--------------PAELF--GNPKSPRLQQFLSGAL 256
Cdd:PRK00635 860 HQGHTVVIIEHNMHVVK-VADYVL--------ELGPeggnlggyllascsPEELIhlHTPTAKALRPYLSSPQ 923
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
153-245 |
5.97e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 50.02 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQQRVSIARALAMEPE---VLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARhVSNHVIFL---- 225
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVIK-TADWIIDLgpeg 905
|
90 100
....*....|....*....|..
gi 491074476 226 --HKGLIEEQGPPAELFGNPKS 245
Cdd:COG0178 906 gdGGGEIVAEGTPEEVAKVKAS 927
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
153-239 |
5.98e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.44 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQQRVSIARALAM---------EPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVV-VTHEMEFARHVSNHV 222
Cdd:PRK13547 146 LSGGELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLaIVHDPNLAARHADRI 225
|
90
....*....|....*..
gi 491074476 223 IFLHKGLIEEQGPPAEL 239
Cdd:PRK13547 226 AMLADGAIVAHGAPADV 242
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
153-184 |
9.69e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 9.69e-07
10 20 30
....*....|....*....|....*....|..
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALD 184
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
133-223 |
1.03e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.41 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 133 VRYLDKVGID----ERARGKypvhLSGGQQQRVSIARALAMEPEVLL--FDEPTSALDPELVGEVLRIMQKLAEEGKTMV 206
Cdd:cd03270 118 LGFLVDVGLGyltlSRSAPT----LSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVL 193
|
90
....*....|....*..
gi 491074476 207 VVTHEMEFARHvSNHVI 223
Cdd:cd03270 194 VVEHDEDTIRA-ADHVI 209
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
42-210 |
1.75e-06 |
|
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: 48.64 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 42 SGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlkvfDKKQLQLLRTRLTMVFQHFNLWSHmtvlenvmeapvqVL 121
Cdd:COG4615 369 SGKSTLAKLLTGLYRPESGEILLDGQPV-------------TADNREAYRQLFSAVFSDFHLFDR-------------LL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 122 GLSKADAHERAVRYLDKVGIDERAR---GKY-PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP--------ELVG 189
Cdd:COG4615 423 GLDGEADPARARELLERLELDHKVSvedGRFsTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPefrrvfytELLP 502
|
170 180
....*....|....*....|.
gi 491074476 190 EvlrimqkLAEEGKTMVVVTH 210
Cdd:COG4615 503 E-------LKARGKTVIAISH 516
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
134-229 |
2.22e-06 |
|
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: 46.21 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 134 RYLDKVGIDERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRI------MQKLAEEGKTMVV 207
Cdd:smart00382 42 LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrllLLLKSEKNLTVIL 121
|
90 100
....*....|....*....|....*..
gi 491074476 208 VTHEMEF-----ARHVSNHVIFLHKGL 229
Cdd:smart00382 122 TTNDEKDlgpalLRRRFDRRIVLLLIL 148
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
133-257 |
2.82e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.09 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 133 VRYLDKVGID----ERARGKypvhLSGGQQQRVSIARALAMEPEVLLF--DEPTSALDPELVGEVLRIMQKLAEEGKTMV 206
Cdd:TIGR00630 469 LGFLIDVGLDylslSRAAGT----LSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRDLGNTLI 544
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 491074476 207 VVTHEMEFARHvSNHVIFL------HKGLIEEQGPPAELFGNPKSpRLQQFLSGALK 257
Cdd:TIGR00630 545 VVEHDEDTIRA-ADYVIDIgpgageHGGEVVASGTPEEILANPDS-LTGQYLSGRKK 599
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
122-239 |
2.92e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.20 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 122 GLSKADAHERAVRYLDKVGID---ERARGKypvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP-------ELVGEV 191
Cdd:NF033858 107 GQDAAERRRRIDELLRATGLApfaDRPAGK----LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPlsrrqfwELIDRI 182
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 491074476 192 LRimqklAEEGKTMVVVTHEMEFARHVsNHVIFLHKGLIEEQGPPAEL 239
Cdd:NF033858 183 RA-----ERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAEL 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
151-254 |
3.35e-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: 47.98 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVL-RIMQKLAEEgKTMVVVTHEMEFARHvSNHVIFLHKGL 229
Cdd:TIGR01271 547 ITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFeSCLCKLMSN-KTRILVTSKLEHLKK-ADKILLLHEGV 624
|
90 100
....*....|....*....|....*
gi 491074476 230 IEEQGPPAELFGnpKSPRLQQFLSG 254
Cdd:TIGR01271 625 CYFYGTFSELQA--KRPDFSSLLLG 647
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
153-229 |
4.19e-06 |
|
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: 45.81 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQQRVSIARALA---MEPEVL-LFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHE---MEFARHVSnHVIFL 225
Cdd:cd03227 78 LSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLpelAELADKLI-HIKKV 156
|
....
gi 491074476 226 HKGL 229
Cdd:cd03227 157 ITGV 160
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
153-240 |
4.26e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 47.41 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPelvGEVLRIMQKLAE--EGKTMVVVTHEMEFARHvSNHVIFLHKGLI 230
Cdd:PRK10790 477 LSVGQKQLLALARVLVQTPQILILDEATANIDS---GTEQAIQQALAAvrEHTTLVVIAHRLSTIVE-ADTILVLHRGQA 552
|
90
....*....|
gi 491074476 231 EEQGPPAELF 240
Cdd:PRK10790 553 VEQGTHQQLL 562
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
153-211 |
5.79e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 5.79e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHE 211
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
115-210 |
6.83e-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: 46.23 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 115 EAPVQVLGLSKADAHERAVRYLDKVGIDERARGKYPV---HLSGGQQQ---RVSIARALAMEPEVLLFDEPTSALDPELV 188
Cdd:pfam13304 196 DLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELpafELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLL 275
|
90 100
....*....|....*....|..
gi 491074476 189 GEVLRIMQKLAEEGKTMVVVTH 210
Cdd:pfam13304 276 RRLLELLKELSRNGAQLILTTH 297
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
153-241 |
8.65e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQQRVSIARALAMEPE--VLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEmefarhvsNHVIFLHKGLI 230
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD--------EQMISLADRII 548
|
90
....*....|.
gi 491074476 231 eEQGPPAELFG 241
Cdd:PRK00635 549 -DIGPGAGIFG 558
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
44-244 |
1.45e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.46 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLEKPSEGSISLNNEDIRmvrdkdgqlkvfdKKQLQLLRtRLTMVF-QHFNLWSHMTVLE--NVMEApvqV 120
Cdd:COG4586 61 KSTTIKMLTGILVPTSGEVRVLGYVPF-------------KRRKEFAR-RIGVVFgQRSQLWWDLPAIDsfRLLKA---I 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 121 LGLSKADAHERaVRYLDKV-GIDERArgKYPV-HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP---ELVGEVLRIM 195
Cdd:COG4586 124 YRIPDAEYKKR-LDELVELlDLGELL--DTPVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVvskEAIREFLKEY 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491074476 196 QKlaEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQGPPAEL---FGNPK 244
Cdd:COG4586 201 NR--ERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELkerFGPYK 250
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
107-234 |
1.49e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.65 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 107 MTVLENVmEAPVQVLGLSKADAHERAVRYLDKVGIderarGKY---PVH-LSGGQQQRVSIARALAMEPEVLLFDEPTSA 182
Cdd:PRK13545 100 LTGIENI-ELKGLMMGLTKEKIKEIIPEIIEFADI-----GKFiyqPVKtYSSGMKSRLGFAISVHINPDILVIDEALSV 173
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 491074476 183 LDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLHKGLIEEQG 234
Cdd:PRK13545 174 GDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYG 225
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
6-211 |
1.95e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.17 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 6 LAVTELHKRYGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlkvfdKK 85
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI--------------KK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 86 QLQLLRTRLTMVFQHFNLWSHMTVLENVMeapvqvlglskADAHERAvrylDKVGIDERAR-------GKYPVH-LSGGQ 157
Cdd:PRK13540 68 DLCTYQKQLCFVGHRSGINPYLTLRENCL-----------YDIHFSP----GAVGITELCRlfslehlIDYPCGlLSSGQ 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491074476 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHE 211
Cdd:PRK13540 133 KRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
154-245 |
2.09e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQKLAEEGK--TMVVVTHEMEFARHvSNHVIFLHKGLIE 231
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVD---VRTDALIQKTIREEFKscTMLIIAHRLNTIID-CDRILVLDAGRVV 1451
|
90
....*....|....
gi 491074476 232 EQGPPAELFGNPKS 245
Cdd:PLN03130 1452 EFDTPENLLSNEGS 1465
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
130-208 |
2.21e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 130 ERAVRYLDKVGID---ERaRGKYpvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMV 206
Cdd:PRK10938 114 ARCEQLAQQFGITallDR-RFKY---LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLV 189
|
..
gi 491074476 207 VV 208
Cdd:PRK10938 190 LV 191
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
100-235 |
3.77e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.71 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 100 HFnlwSHMTVLENV-----MEAP-VQVLGLSKAD--AHERAV---------RYLDKVGiDERARGkypvhLSGGQQQRVS 162
Cdd:TIGR00956 149 HF---PHLTVGETLdfaarCKTPqNRPDGVSREEyaKHIADVymatyglshTRNTKVG-NDFVRG-----VSGGERKRVS 219
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491074476 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVT--HEMEFARHVSNHVIFLHKGLIEEQGP 235
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQIYFGP 294
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
136-227 |
3.89e-05 |
|
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: 43.36 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 136 LDKVGIDERARgkypvhLSGGQQQRVSIARALAMEP------EVLLFDEPTSALDPELVGEVL-RIMQK-LAEEGKTMVV 207
Cdd:cd03240 105 SNWPLLDMRGR------CSGGEKVLASLIIRLALAEtfgsncGILALDEPTTNLDEENIEESLaEIIEErKSQKNFQLIV 178
|
90 100
....*....|....*....|
gi 491074476 208 VTHEMEFARHVsNHVIFLHK 227
Cdd:cd03240 179 ITHDEELVDAA-DHIYRVEK 197
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
142-228 |
3.93e-05 |
|
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: 44.08 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 142 DERARGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVL-RIMQKLAEEgKTMVVVTHEMEFARhVSN 220
Cdd:cd03291 149 DNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFeSCVCKLMAN-KTRILVTSKMEHLK-KAD 226
|
....*...
gi 491074476 221 HVIFLHKG 228
Cdd:cd03291 227 KILILHEG 234
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
152-238 |
3.99e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 43.77 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 152 HLSGGQQQRVSIA-------RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIF 224
Cdd:PRK03695 126 QLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWL 205
|
90
....*....|....
gi 491074476 225 LHKGLIEEQGPPAE 238
Cdd:PRK03695 206 LKQGKLLASGRRDE 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
15-184 |
4.10e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 43.56 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 15 YGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIslnnedirmvrDKDGQLKVFDKKQLQLLRTRL 94
Cdd:PRK09544 14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQKLYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 95 TMVFQHFNLWSHMTVLENVMEAPVQVlglskadaheRAVRYLDkvgiderargkYPVH-LSGGQQQRVSIARALAMEPEV 173
Cdd:PRK09544 83 PLTVNRFLRLRPGTKKEDILPALKRV----------QAGHLID-----------APMQkLSGGETQRVLLARALLNRPQL 141
|
170
....*....|.
gi 491074476 174 LLFDEPTSALD 184
Cdd:PRK09544 142 LVLDEPTQGVD 152
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
153-223 |
7.79e-05 |
|
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: 43.39 E-value: 7.79e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPelvgEVLRIMQK-LAEEGKTMVVVTHEMEFARHVSNHVI 223
Cdd:TIGR03719 444 LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV----ETLRALEEaLLNFAGCAVVISHDRWFLDRIATHIL 511
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
153-210 |
8.47e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 43.58 E-value: 8.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGevlRIMQKLAEEGKTMVVVTH 210
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG---YMYRLCREFGITLFSVSH 637
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
153-234 |
1.08e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLRIMQKLAEegKTMVVVTHEMEFARHVSNHVI-FLHKGLIE 231
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESI-ESLNMALEKYE--GTLIFVSHDREFVSSLATRIIeITPDGVVD 515
|
...
gi 491074476 232 EQG 234
Cdd:PRK15064 516 FSG 518
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
153-245 |
1.17e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.04 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQklaEEGK--TMVVVTHEMEFARHVsNHVIFLHKGLI 230
Cdd:PLN03232 1372 FSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR---EEFKscTMLVIAHRLNTIIDC-DKILVLSSGQV 1447
|
90
....*....|....*
gi 491074476 231 EEQGPPAELFGNPKS 245
Cdd:PLN03232 1448 LEYDSPQELLSRDTS 1462
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
15-231 |
1.30e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 15 YGDHEVLKGVSLAANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSISLNnedirmvrdKDGQLKVFDKKQLQLLRTRl 94
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA---------KGIKLGYFAQHQLEFLRAD- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 95 tmvfqhfnlwshmtvlenvmEAPVQVLGLSKADAHERAVR-YL-------DKVgIDERARgkypvhLSGGQQQRVSIARA 166
Cdd:PRK10636 392 --------------------ESPLQHLARLAPQELEQKLRdYLggfgfqgDKV-TEETRR------FSGGEKARLVLALI 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 167 LAMEPEVLLFDEPTSALDpelvgevLRIMQKLAE-----EGkTMVVVTHEMEFARHVSNHVIFLHKGLIE 231
Cdd:PRK10636 445 VWQRPNLLLLDEPTNHLD-------LDMRQALTEalidfEG-ALVVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
44-228 |
2.34e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.91 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 44 KSTFLRCINFLeKPSEGSISLNNEDIRMVRDKDGQLKVFD-----------------------KKQLQLLRTRLTMVFQH 100
Cdd:COG3593 36 KSSILEALRLL-LGPSSSRKFDEEDFYLGDDPDLPEIEIEltfgsllsrllrlllkeedkeelEEALEELNEELKEALKA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 101 FNlwshmTVLENVMEAPVQVLGLSKADAHERAVRYLDKVGIDERARGKYPVHLSG-GQQQRVSIARALAM-------EPE 172
Cdd:COG3593 115 LN-----ELLSEYLKELLDGLDLELELSLDELEDLLKSLSLRIEDGKELPLDRLGsGFQRLILLALLSALaelkrapANP 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491074476 173 VLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVS-NHVIFLHKG 228
Cdd:COG3593 190 ILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVPlENIRRLRRD 246
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
151-234 |
2.67e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.32 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVS-NHVIFLHKGL 229
Cdd:PRK09580 144 VGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGR 223
|
....*
gi 491074476 230 IEEQG 234
Cdd:PRK09580 224 IVKSG 228
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
127-250 |
2.74e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 127 DAHERaVRYLDKVGIDERARGKYPVHLSGGQQQRVSIARALA--MEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKT 204
Cdd:PRK00635 1363 DLLNR-LTFIDKVGLSYITLGQEQDTLSDGEHYRLHLAKKISsnLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNT 1441
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 491074476 205 MVVVTHEMEFARHvSNHVIFLHKGlieeQGPPAELFGNPKSPRLQQ 250
Cdd:PRK00635 1442 VIATDRSGSLAEH-ADHLIHLGPG----SGPQGGYLLSTSALKQSQ 1482
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
153-245 |
2.76e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQQRVSIARALAMEP---EVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFARhVSNHVIFL---- 225
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVIK-TADWIIDLgpeg 909
|
90 100
....*....|....*....|..
gi 491074476 226 --HKGLIEEQGPPAELFGNPKS 245
Cdd:PRK00349 910 gdGGGEIVATGTPEEVAKVEAS 931
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
43-211 |
3.41e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.50 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 43 GKSTFLRCINFLEKPSEGSISLNNEDIrmvrdkdgqlkvfDKKQLQLLRTRLTMVFQHFNLWSHMtvlenvmeapvqvLG 122
Cdd:PRK10522 361 GKSTLAMLLTGLYQPQSGEILLDGKPV-------------TAEQPEDYRKLFSAVFTDFHLFDQL-------------LG 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 123 LSKADAHERAVR-YLDKVGIDERAR---GKYP-VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP----ELVGEVLR 193
Cdd:PRK10522 415 PEGKPANPALVEkWLERLKMAHKLEledGRISnLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPhfrrEFYQVLLP 494
|
170
....*....|....*...
gi 491074476 194 IMQklaEEGKTMVVVTHE 211
Cdd:PRK10522 495 LLQ---EMGKTIFAISHD 509
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
134-257 |
4.22e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 134 RYLDKVGID----ERARGKypvhLSGGQQQRVSIARALAMEpevL---LF--DEPTSALDPELVGEVLRIMQKLAEEGKT 204
Cdd:COG0178 467 GFLVDVGLDyltlDRSAGT----LSGGEAQRIRLATQIGSG---LvgvLYvlDEPSIGLHQRDNDRLIETLKRLRDLGNT 539
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 491074476 205 MVVVTHEMEFARHvSNHVIFL------HKGLIEEQGPPAELFGNPKSPRLqQFLSGALK 257
Cdd:COG0178 540 VIVVEHDEDTIRA-ADYIIDIgpgageHGGEVVAQGTPEEILKNPDSLTG-QYLSGRKR 596
|
|
| Rad50_Sulf |
NF041034 |
DNA double-strand break repair ATPase Rad50; |
153-227 |
5.10e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 468963 [Multi-domain] Cd Length: 872 Bit Score: 41.24 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 153 LSGGQQ------QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFaRHVSNHVIFLH 226
Cdd:NF041034 780 LSGGERisialaLRLAIAKSLMDEIGFMILDEPTVHLDEERKKELIDIIRSSMEIVPQIIVVTHDEEL-KEISDYIISVE 858
|
.
gi 491074476 227 K 227
Cdd:NF041034 859 K 859
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
160-222 |
6.69e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 6.69e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491074476 160 RVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQKLAEEGKTMVVVTHEmefaRHVSNHV 222
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLD---INTIRWLEDVLNERNSTMIIISHD----RHFLNSV 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
144-232 |
9.83e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.32 E-value: 9.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 144 RARgkYPVH-LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLRIMqkLAEEGKTMVVVTHEMEFarhVSNHV 222
Cdd:PRK11147 433 RAM--TPVKaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETL-ELLEEL--LDSYQGTVLLVSHDRQF---VDNTV 504
|
90
....*....|....
gi 491074476 223 ----IFLHKGLIEE 232
Cdd:PRK11147 505 tecwIFEGNGKIGR 518
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
152-210 |
1.06e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 39.06 E-value: 1.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 152 HLSGGQQQRVSIARaLAMEPEVL-LFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTH 210
Cdd:PRK13543 137 QLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
153-213 |
1.22e-03 |
|
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: 39.45 E-value: 1.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPeLVGEVLRIMQKLAEEGKTMVVVTHEME 213
Cdd:cd03289 139 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQVIRKTLKQAFADCTVILSEHRIE 198
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
153-213 |
1.25e-03 |
|
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: 39.89 E-value: 1.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPeLVGEVLRIMQKLAEEGKTMVVVTHEME 213
Cdd:TIGR01271 1354 LSNGHKQLMCLARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
123-215 |
1.38e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 123 LSKADAHERAVRY--LDKVGIDERARGKYPVH-LSGGQQQRVSIARALAMEP----------EVLLFDEPTSALDPELVG 189
Cdd:TIGR00618 918 GRYADSHVNARKYqgLALLVADAYTGSVRPSAtLSGGETFLASLSLALALADllstsggtvlDSLFIDEGFGSLDEDSLD 997
|
90 100
....*....|....*....|....*.
gi 491074476 190 EVLRIMQKLAEEGKTMVVVTHEMEFA 215
Cdd:TIGR00618 998 RAIGILDAIREGSKMIGIISHVPEFR 1023
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
153-186 |
1.44e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.72 E-value: 1.44e-03
10 20 30
....*....|....*....|....*....|....
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE 186
Cdd:PRK11819 446 LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
153-215 |
1.45e-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: 1.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491074476 153 LSGGQQQRVSIARALAMEPEV---------LLF-DEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMEFA 215
Cdd:cd03279 124 LSGGETFLASLSLALALSEVLqnrggarleALFiDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELK 196
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
153-211 |
3.44e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.69 E-value: 3.44e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 491074476 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLriMQKLAEEGKTMVVVTHE 211
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAV-EAL--IQGLVLFQGGVLMVSHD 683
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
154-250 |
3.89e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 38.23 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQKLAEEGKTMVVVTHEMEFARHVSNHVIFLhkglieEQ 233
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHI------EQ 221
|
90
....*....|....*..
gi 491074476 234 GPPAELFGNPKSPRLQQ 250
Cdd:PRK10636 222 QSLFEYTGNYSSFEVQR 238
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
60-246 |
9.06e-03 |
|
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: 36.81 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 60 GSISLNNEDIRMVRDKDGQLkVFD-----KKQLQLLRTRLTMVFQ---------HFNLWSHMTVLENVMEAPVQVLGLsk 125
Cdd:cd03288 59 GKSSLSLAFFRMVDIFDGKI-VIDgidisKLPLHTLRSRLSIILQdpilfsgsiRFNLDPECKCTDDRLWEALEIAQL-- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074476 126 adahERAVRYLDKvGIDERAR--GKypvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpeLVGEvlRIMQKL---AE 200
Cdd:cd03288 136 ----KNMVKSLPG-GLDAVVTegGE---NFSVGQRQLFCLARAFVRKSSILIMDEATASID--MATE--NILQKVvmtAF 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491074476 201 EGKTMVVVTHEMEFARHvSNHVIFLHKGLIEEQGPPAELFGNPKSP 246
Cdd:cd03288 204 ADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGV 248
|
|
| |
