|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-252 |
9.80e-161 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 445.59 E-value: 9.80e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrrLSDK 85
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-----------DSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 ENRQALRDVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:COG1126 71 DINKLRRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPKSP 245
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
....*..
gi 490220552 246 RLQYFLS 252
Cdd:COG1126 231 RTRAFLS 237
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-253 |
5.11e-137 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 386.46 E-value: 5.11e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 4 YAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPlGGEKRRRLS 83
Cdd:COG4598 7 PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKP-DRDGELVPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKENRQALR-DVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAI 162
Cdd:COG4598 86 DRRQLQRIRtRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 163 ARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQP 242
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245
|
250
....*....|.
gi 490220552 243 KSPRLQYFLSS 253
Cdd:COG4598 246 KSERLRQFLSS 256
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-229 |
1.38e-126 |
|
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: 358.38 E-value: 1.38e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrrlSDK 85
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT------------DDK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 ENRQALR-DVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIAR 164
Cdd:cd03262 69 KNINELRqKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490220552 165 ALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCI 229
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-251 |
3.69e-113 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 325.51 E-value: 3.69e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyepLGGEKRRRLSDK 85
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV----NDPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 EnrqalrdVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:PRK09493 78 E-------AGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPKSP 245
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
....*.
gi 490220552 246 RLQYFL 251
Cdd:PRK09493 231 RLQEFL 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-252 |
1.89e-98 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 288.57 E-value: 1.89e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENV-GYEPLGGEKRRRls 83
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 dkenRQALRDVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIA 163
Cdd:PRK11264 81 ----RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 164 RALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPK 243
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
....*....
gi 490220552 244 SPRLQYFLS 252
Cdd:PRK11264 237 QPRTRQFLE 245
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-252 |
3.80e-98 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 288.02 E-value: 3.80e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYePLGGEKRR 80
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINL-VRDKDGQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 RLSDKENRQALRD-VCMVFQQFNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLADKA-DSWPAMLSGGQQQ 158
Cdd:PRK10619 80 KVADKNQLRLLRTrLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 159 RVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQL 238
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
250
....*....|....
gi 490220552 239 FHQPKSPRLQYFLS 252
Cdd:PRK10619 240 FGNPQSPRLQQFLK 253
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-252 |
1.81e-95 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 280.75 E-value: 1.81e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYeplggekRRRLSD 84
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDF-------SQKPSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 KENRQALRDVCMVFQQFNLWPHMTVLDN-VATPLrRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIA 163
Cdd:COG4161 75 KAIRLLRQKVGMVFQQYNLWPHLTVMENlIEAPC-KVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 164 RALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGApAQLFHQPK 243
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQ 232
|
....*....
gi 490220552 244 SPRLQYFLS 252
Cdd:COG4161 233 TEAFAHYLS 241
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
6-253 |
3.08e-93 |
|
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: 275.56 E-value: 3.08e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLGGEKRRRLSDK 85
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNGPLVPADEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 ENRQALRDVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPKS 244
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
....*....
gi 490220552 245 PRLQYFLSS 253
Cdd:TIGR03005 241 ERTREFLSK 249
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-252 |
7.48e-93 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 273.81 E-value: 7.48e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEplggekrRRLSD 84
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFS-------KTPSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 KENRQALRDVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIAR 164
Cdd:PRK11124 75 KAIRELRRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 165 ALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGApAQLFHQPKS 244
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQT 233
|
....*...
gi 490220552 245 PRLQYFLS 252
Cdd:PRK11124 234 EAFKNYLS 241
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-270 |
2.00e-92 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 276.19 E-value: 2.00e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHY----GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrR 81
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLT----------A 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 82 LSDKENRQALRDVCMVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVA 161
Cdd:COG1135 72 LSERELRAARRKIGMIFQHFNLLSSRTVAENVALPLE-IAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 162 IARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFH 240
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230
|
250 260 270
....*....|....*....|....*....|
gi 490220552 241 QPKSPRLQYFLSSwserQSGARLPETALQE 270
Cdd:COG1135 231 NPQSELTRRFLPT----VLNDELPEELLAR 256
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-251 |
2.64e-86 |
|
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: 257.22 E-value: 2.64e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrr 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDIT---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 RLSDKENRQALRDVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRV 160
Cdd:COG1127 71 GLSEKELYELRRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 161 AIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLF 239
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
250
....*....|..
gi 490220552 240 HQPkSPRLQYFL 251
Cdd:COG1127 231 ASD-DPWVRQFL 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-243 |
7.67e-84 |
|
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: 250.58 E-value: 7.67e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGEN----HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrR 81
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLT----------L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 82 LSDKENRQALRDVCMVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVA 161
Cdd:cd03258 72 LSGKELRKARRRIGMIFQHFNLLSSRTVFENVALPLE-IAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 162 IARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFH 240
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
...
gi 490220552 241 QPK 243
Cdd:cd03258 231 NPQ 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-245 |
2.02e-83 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 253.87 E-value: 2.02e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLggEKRr 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP--EKR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 rlsdkenrqalrDVCMVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRV 160
Cdd:COG3842 78 ------------NVGMVFQDYALFPHLTVAENVAFGLR-MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 161 AIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLF 239
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIY 224
|
....*.
gi 490220552 240 HQPKSP 245
Cdd:COG3842 225 ERPATR 230
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-232 |
5.92e-82 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 245.72 E-value: 5.92e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYG----ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrr 80
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIS---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 RLSDKEnRQALR--DVCMVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQ 158
Cdd:COG1136 74 SLSERE-LARLRrrHIGFVFQFFNLLPELTALENVALPLL-LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490220552 159 RVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMgFAAKVSDRVLFLADGCIEEQ 232
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDP-ELAARADRVIRLRDGRIVSD 225
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
5-252 |
2.67e-81 |
|
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: 244.90 E-value: 2.67e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLED-----YSSGSIVVNGENVgYEPlggekr 79
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDI-YDK------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 80 rRLSDKENRqalRDVCMVFQQFNLWPhMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGL----ADKADSWPAMLSGG 155
Cdd:TIGR00972 74 -KIDVVELR---RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 156 QQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDgMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAP 235
Cdd:TIGR00972 149 QQQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPT 227
|
250
....*....|....*..
gi 490220552 236 AQLFHQPKSPRLQYFLS 252
Cdd:TIGR00972 228 EQIFTNPKEKRTEDYIS 244
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-233 |
7.57e-80 |
|
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: 239.73 E-value: 7.57e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLggekrrrlsdk 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 enrqALRDVCMVFQQFNLWPHMTVLDNVATPLRRvKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:cd03259 70 ----ERRNIGMVFQDYALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490220552 166 LTMKPAIMLFDEPTSALDP----ELVGEVLKVIRNLaddGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQG 233
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAklreELREELKELQREL---GITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-227 |
1.93e-78 |
|
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: 236.62 E-value: 1.93e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGEN----HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRR 81
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDI----------SK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 82 LSDKEnRQALR--DVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSREAAyAEAKTQLARVGLADKADSWPAMLSGGQQQR 159
Cdd:cd03255 71 LSEKE-LAAFRrrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERR-ERAEELLERVGLGDRLNHYPSELSGGQQQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490220552 160 VAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKvSDRVLFLADG 227
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDG 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-245 |
2.80e-78 |
|
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: 245.58 E-value: 2.80e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHY-----GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrR 80
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDL----------T 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 RLSDKENRQALRDVCMVFQ----QFNlwPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGL-ADKADSWPAMLSGG 155
Cdd:COG1123 331 KLSRRSLRELRRRVQMVFQdpysSLN--PRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 156 QQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGA 234
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGP 488
|
250
....*....|.
gi 490220552 235 PAQLFHQPKSP 245
Cdd:COG1123 489 TEEVFANPQHP 499
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-238 |
2.88e-78 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 237.26 E-value: 2.88e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHY-GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrRLS 83
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVT----------ALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKENRQALRDVCMVFQQFNLWPHMTVLDNVATP-----------LRRVKKVSREAAYAeaktQLARVGLADKADSWPAML 152
Cdd:COG3638 72 GRALRRLRRRIGMIFQQFNLVPRLSVLTNVLAGrlgrtstwrslLGLFPPEDRERALE----ALERVGLADKAYQRADQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 153 SGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLA-DDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEE 231
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIArEDGITVVVNLHQVDLARRYADRIIGLRDGRVVF 227
|
....*..
gi 490220552 232 QGAPAQL 238
Cdd:COG3638 228 DGPPAEL 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-250 |
2.50e-77 |
|
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: 234.32 E-value: 2.50e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRLSDK 85
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDI----------SGLSEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 ENRQALRDVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:cd03261 71 ELYRLRRRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPkS 244
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-D 229
|
....*.
gi 490220552 245 PRLQYF 250
Cdd:cd03261 230 PLVRQF 235
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-253 |
1.41e-76 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 235.85 E-value: 1.41e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHY----GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrR 81
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLT----------A 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 82 LSDKENRQALRDVCMVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVA 161
Cdd:PRK11153 72 LSEKELRKARRQIGMIFQHFNLLSSRTVFDNVALPLE-LAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 162 IARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFH 240
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFS 230
|
250
....*....|...
gi 490220552 241 QPKSPRLQYFLSS 253
Cdd:PRK11153 231 HPKHPLTREFIQS 243
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-244 |
4.60e-74 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 229.96 E-value: 4.60e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrRLSD 84
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT----------DLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 KEnrqalRDVCMVFQQFNLWPHMTVLDNVATPL--RRVKKVSREAAYAEAktqLARVGLADKADSWPAMLSGGQQQRVAI 162
Cdd:COG3839 73 KD-----RNIAMVFQSYALYPHMTVYENIAFPLklRKVPKAEIDRRVREA---AELLGLEDLLDRKPKQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 163 ARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHE----MGFAakvsDRVLFLADGCIEEQGAPAQ 237
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDqveaMTLA----DRIAVMNDGRIQQVGTPEE 220
|
....*..
gi 490220552 238 LFHQPKS 244
Cdd:COG3839 221 LYDRPAN 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
5-227 |
4.64e-73 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 224.20 E-value: 4.64e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHY----GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrr 80
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 rlsdkenRQALRDVCMVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRV 160
Cdd:COG1116 76 -------TGPGPDRGVVFQEPALLPWLTVLDNVALGLE-LRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490220552 161 AIARALTMKPAIMLFDEPTSALDP----ELVGEVLKVirnLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-227 |
5.90e-72 |
|
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: 218.60 E-value: 5.90e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLGGEKRRrlsdk 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 enrqalRDVCMVFQQFNLWPHMTVLDNVATPlrrvkkvsreaayaeaktqlarvgladkadswpamLSGGQQQRVAIARA 165
Cdd:cd03229 76 ------RRIGMVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARA 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNLAD-DGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:cd03229 115 LAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-243 |
5.94e-72 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 220.28 E-value: 5.94e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHY-GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLggekrrrlsd 84
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNL---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 kenRQALRDVCMVFQQ-----FNlwphMTVLDNVATPLRRvKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQR 159
Cdd:COG1122 71 ---RELRRKVGLVFQNpddqlFA----PTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 160 VAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLF 239
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
....
gi 490220552 240 HQPK 243
Cdd:COG1122 223 SDYE 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-238 |
8.12e-71 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 217.43 E-value: 8.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDY-----SSGSIVVNGENVgyeplggekrr 80
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDI----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 rLSDKENRQALR-DVCMVFQQFNLWPhMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLAD--KADSWPAMLSGGQQ 157
Cdd:cd03260 70 -YDLDVDVLELRrRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 158 QRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDgMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQ 237
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 490220552 238 L 238
Cdd:cd03260 227 I 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-245 |
1.88e-70 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 220.40 E-value: 1.88e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekRRRLSDK 85
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL---------FTNLPPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 EnrqalRDVCMVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:COG1118 74 E-----RRVGFVFQHYALFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPKS 244
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPAT 227
|
.
gi 490220552 245 P 245
Cdd:COG1118 228 P 228
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-238 |
2.17e-69 |
|
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: 214.47 E-value: 2.17e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENH-VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrRLSD 84
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDIT----------KLRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 KENRQALRDVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSR-------EAAYAEAKTQLARVGLADKADSWPAMLSGGQQ 157
Cdd:TIGR02315 72 KKLRKLRRRIGMIFQHYNLIERLTVLENVLHGRLGYKPTWRsllgrfsEEDKERALSALERVGLADKAYQRADQLSGGQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 158 QRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLA-DDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPA 236
Cdd:TIGR02315 152 QRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINkEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPS 231
|
..
gi 490220552 237 QL 238
Cdd:TIGR02315 232 EL 233
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-233 |
3.20e-69 |
|
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: 213.52 E-value: 3.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHY----GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLGGEKRRR 81
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 82 lsdkenrqalRDVCMVFQ--QFNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLAR-VGLADK-ADSWPAMLSGGQQ 157
Cdd:cd03257 82 ----------KEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVgVGLPEEvLNRYPHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490220552 158 QRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQG 233
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-238 |
3.68e-69 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 213.39 E-value: 3.68e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrrlsDK 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV--------------AR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 ENRQALRDVCMVFQQFNLWPHMTVLDNVATpLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:COG1131 67 DPAEVRRRIGYVPQEPALYPDLTVRENLRF-FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQL 238
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-238 |
1.30e-68 |
|
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: 212.43 E-value: 1.30e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGEN-HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRLSD 84
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDI----------NKLKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 KENRQALRDVCMVFQQFNLWPHMTVLDNVATP-----------LRRVKKVSREAAYAeaktQLARVGLADKADSWPAMLS 153
Cdd:cd03256 71 KALRQLRRQIGMIFQQFNLIERLSVLENVLSGrlgrrstwrslFGLFPKEEKQRALA----ALERVGLLDKAYQRADQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 154 GGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLA-DDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQ 232
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFD 226
|
....*.
gi 490220552 233 GAPAQL 238
Cdd:cd03256 227 GPPAEL 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-237 |
2.07e-68 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 211.06 E-value: 2.07e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENH-VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRLSD 84
Cdd:COG2884 2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL----------SRLKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 KENRQALRDVCMVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIAR 164
Cdd:COG2884 72 REIPYLRRRIGVVFQDFRLLPDRTVYENVALPLR-VTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490220552 165 ALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQ 237
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-253 |
2.46e-68 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 211.59 E-value: 2.46e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGE----NHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYeplggekrr 80
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 rlsdKENRQALRDVCMVFQQ----FNlwPHMTVLDNVATPLRRVKKVSREAAYAEAktqLARVGL-ADKADSWPAMLSGG 155
Cdd:COG1124 72 ----RRRKAFRRRVQMVFQDpyasLH--PRHTVDRILAEPLRIHGLPDREERIAEL---LEQVGLpPSFLDRYPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 156 QQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGA 234
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELT 222
|
250
....*....|....*....
gi 490220552 235 PAQLFHQPKSPRLQYFLSS 253
Cdd:COG1124 223 VADLLAGPKHPYTRELLAA 241
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-246 |
2.29e-67 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 209.51 E-value: 2.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 3 DYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLED-----YSSGSIVVNGENVgyeplgge 77
Cdd:COG1117 9 EPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgaRVEGEILLDGEDI-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 78 krrrLSDKENRQALR-DVCMVFQQFNLWPhMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGL----ADKADSwPAM- 151
Cdd:COG1117 81 ----YDPDVDVVELRrRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwdevKDRLKK-SALg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 152 LSGGQQQRVAIARALTMKPAIMLFDEPTSALDP-------ELvgevlkvIRNLADDgMTMMIVTHEMGFAAKVSDRVLFL 224
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPistakieEL-------ILELKKD-YTIVIVTHNMQQAARVSDYTAFF 226
|
250 260
....*....|....*....|..
gi 490220552 225 ADGCIEEQGAPAQLFHQPKSPR 246
Cdd:COG1117 227 YLGELVEFGPTEQIFTNPKDKR 248
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-224 |
5.72e-66 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 204.63 E-value: 5.72e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGEN----HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrr 81
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 82 lsdkenRQALRDVCMVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVA 161
Cdd:cd03293 69 ------TGPGPDRGYVFQQDALLPWLTVLDNVALGLE-LQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490220552 162 IARALTMKPAIMLFDEPTSALDP----ELVGEVLKVIRnlaDDGMTMMIVTHEMGFAAKVSDRVLFL 224
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDAltreQLQEELLDIWR---ETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-251 |
8.67e-65 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 202.29 E-value: 8.67e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHvLRgIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENV-GYEPlggekrrrlsd 84
Cdd:COG3840 2 LRLDDLTYRYGDFP-LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLtALPP----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 kenrqALRDVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSRE--AAYAEAktqLARVGLADKADSWPAMLSGGQQQRVAI 162
Cdd:COG3840 69 -----AERPVSMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEqrAQVEQA---LERVGLAGLLDRLPGQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 163 ARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQ 241
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDG 220
|
250
....*....|
gi 490220552 242 PKSPRLQYFL 251
Cdd:COG3840 221 EPPPALAAYL 230
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-244 |
7.75e-63 |
|
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: 197.07 E-value: 7.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyEPLGGEKRRrlsdk 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 enrqalrdVCMVFQQFNLWPHMTVLDNVATPLRRvKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:cd03300 74 --------VNTVFQNYALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPKS 244
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPAN 224
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
3-242 |
1.80e-62 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 201.10 E-value: 1.80e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 3 DYAIEINNLNKHYGEN----------------------HVLRGIDVS--ISPGEVICVIGGSGSGKSTLLRCINFLEDYS 58
Cdd:COG4175 1 MPKIEVRNLYKIFGKRperalklldqgkskdeilektgQTVGVNDASfdVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 59 SGSIVVNGENVgyeplggekrRRLSDKENRQaLR--DVCMVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQL 136
Cdd:COG4175 81 AGEVLIDGEDI----------TKLSKKELRE-LRrkKMSMVFQHFALLPHRTVLENVAFGLE-IQGVPKAERRERAREAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 137 ARVGLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDP----ELVGEVLKVIRNLaddGMTMMIVTHEMG 212
Cdd:COG4175 149 ELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrEMQDELLELQAKL---KKTIVFITHDLD 225
|
250 260 270
....*....|....*....|....*....|
gi 490220552 213 FAAKVSDRVLFLADGCIEEQGAPAQLFHQP 242
Cdd:COG4175 226 EALRLGDRIAIMKDGRIVQIGTPEEILTNP 255
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-242 |
5.98e-62 |
|
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: 196.33 E-value: 5.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 21 LRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRLSDKENRqALR--DVCMVF 98
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDI----------AAMSRKELR-ELRrkKISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 99 QQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEP 178
Cdd:cd03294 109 QSFALLPHRTVLENVAFGLE-VQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490220552 179 TSALDP----ELVGEVLKVIRNLaddGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQP 242
Cdd:cd03294 188 FSALDPlirrEMQDELLRLQAEL---QKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-245 |
6.58e-62 |
|
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: 197.58 E-value: 6.58e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHY----GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCI-NFLED--YSSGSIVVNGENVgyeplggek 78
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlGLLPPpgITSGEILFDGEDL--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 79 rRRLSDKENRQA-LRDVCMVFQQ----FNlwPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLADK---ADSWPA 150
Cdd:COG0444 73 -LKLSEKELRKIrGREIQMIFQDpmtsLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPerrLDRYPH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 151 MLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCI 229
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
250
....*....|....*.
gi 490220552 230 EEQGAPAQLFHQPKSP 245
Cdd:COG0444 230 VEEGPVEELFENPRHP 245
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-244 |
8.21e-62 |
|
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: 202.83 E-value: 8.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHY--GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYS---SGSIVVNGENVgyeplggekr 79
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDL---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 80 RRLSDKENRqalRDVCMVFQ----QFNLwphMTVLDNVATPLRRvKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGG 155
Cdd:COG1123 74 LELSEALRG---RRIGMVFQdpmtQLNP---VTVGDQIAEALEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 156 QQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGA 234
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
250
....*....|
gi 490220552 235 PAQLFHQPKS 244
Cdd:COG1123 227 PEEILAAPQA 236
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-227 |
9.77e-62 |
|
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: 193.45 E-value: 9.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 7 EINNLNKHY--GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLggekrrrlsd 84
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSL---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 kenRQALRDVCMVFQQ-----FNLwphmTVLDNVATPLRRvKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQR 159
Cdd:cd03225 71 ---KELRRKVGLVFQNpddqfFGP----TVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490220552 160 VAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-236 |
1.20e-60 |
|
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: 191.49 E-value: 1.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHYGEN----HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyePLgg 76
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF--AL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 77 ekrrrlsDKENRQALR--DVCMVFQQFNLWPHMTVLDNVATPLRRVkkvSREAAYAEAKTQLARVGLADKADSWPAMLSG 154
Cdd:COG4181 80 -------DEDARARLRarHVGFVFQSFQLLPTLTALENVMLPLELA---GRRDARARARALLERVGLGHRLDHYPAQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 155 GQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKvSDRVLFLADGCIEEQG 233
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDT 228
|
...
gi 490220552 234 APA 236
Cdd:COG4181 229 AAT 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-239 |
2.38e-60 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 191.41 E-value: 2.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRLSD 84
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL----------ASLSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 KEnrQAlRDVCMVFQQFNLWPHMTVLDNVA-------TPLRRVKKVSREAAyAEAktqLARVGLADKADSWPAMLSGGQQ 157
Cdd:COG1120 71 RE--LA-RRIAYVPQEPPAPFGLTVRELVAlgryphlGLFGRPSAEDREAV-EEA---LERTGLEHLADRPVDELSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 158 QRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPA 236
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
...
gi 490220552 237 QLF 239
Cdd:COG1120 224 EVL 226
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-245 |
4.35e-60 |
|
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: 194.10 E-value: 4.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPlggekrrrlsdk 85
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLP------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 enrQALRDVCMVFQQFNLWPHMTVLDNVATPLRRvKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:TIGR03265 73 ---PQKRDYGIVFQSYALFPNLTVADNIAYGLKN-RGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 166 LTMKPAIMLFDEPTSALDPE----LVGEVLKVIRNLaddGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQ 241
Cdd:TIGR03265 149 LATSPGLLLLDEPLSALDARvrehLRTEIRQLQRRL---GVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRH 225
|
....
gi 490220552 242 PKSP 245
Cdd:TIGR03265 226 PATP 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-252 |
1.74e-59 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 192.61 E-value: 1.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrRLSD 84
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS----------RLHA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 KEnrqalRDVCMVFQQFNLWPHMTVLDNVA---TPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVA 161
Cdd:PRK10851 72 RD-----RKVGFVFQHYALFRHMTVFDNIAfglTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 162 IARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFH 240
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWR 226
|
250
....*....|..
gi 490220552 241 QPKSPRLQYFLS 252
Cdd:PRK10851 227 EPATRFVLEFMG 238
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-251 |
4.35e-59 |
|
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: 187.93 E-value: 4.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 4 YAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrrlS 83
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-------------T 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKENRQalRDVCMVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQ----LARVGLADKADSWPAMLSGGQQQR 159
Cdd:cd03296 68 DVPVQE--RNVGFVFQHYALFRHMTVFDNVAFGLR-VKPRSERPPEAEIRAKvhelLKLVQLDWLADRYPAQLSGGQRQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 160 VAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQL 238
Cdd:cd03296 145 VALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
250
....*....|...
gi 490220552 239 FHQPKSPRLQYFL 251
Cdd:cd03296 225 YDHPASPFVYSFL 237
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-270 |
8.05e-59 |
|
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: 188.02 E-value: 8.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHY--GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrrlS 83
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT-------------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKENRQALRDVC-MVFQ----QFnlwPHMTVLDNVATPL-----------RRVKKVsreaayaeaktqLARVGLADKADS 147
Cdd:TIGR04520 68 DEENLWEIRKKVgMVFQnpdnQF---VGATVEDDVAFGLenlgvpreemrKRVDEA------------LKLVGMEDFRDR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 148 WPAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKvSDRVLFLAD 226
Cdd:TIGR04520 133 EPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVL-ADRVIVMNK 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 490220552 227 GCIEEQGAPAQLFHQ-----------PKSPRLQYFLsswseRQSGARLPETALQE 270
Cdd:TIGR04520 212 GKIVAEGTPREIFSQvellkeigldvPFITELAKAL-----KKRGIPLPPDILTE 261
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-245 |
8.15e-59 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 189.15 E-value: 8.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHV-LRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENV-GYEPLggEKRRRls 83
Cdd:COG1125 2 IEFENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIrDLDPV--ELRRR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 dkenrqalrdvcM--VFQQFNLWPHMTVLDNVAT-PlrRVKKVSREAAYAEAKTQLARVGL--ADKADSWPAMLSGGQQQ 158
Cdd:COG1125 78 ------------IgyVIQQIGLFPHMTVAENIATvP--RLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 159 RVAIARALTMKPAIMLFDEPTSALDP----ELVGEVLKVIRNLaddGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGA 234
Cdd:COG1125 144 RVGVARALAADPPILLMDEPFGALDPitreQLQDELLRLQREL---GKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDT 220
|
250
....*....|.
gi 490220552 235 PAQLFHQPKSP 245
Cdd:COG1125 221 PEEILANPAND 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-238 |
3.61e-58 |
|
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: 185.45 E-value: 3.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPlggekrrrlsdk 85
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 enRQALRDVCMVFQQFNLWPHMTVLDNVA--TPLRRVKKVSREAAYAEAktqLARVGLADKADSWPAMLSGGQQQRVAIA 163
Cdd:COG4555 70 --REARRQIGVLPDERGLYDRLTVRENIRyfAELYGLFDEELKKRIEEL---IELLGLEEFLDRRVGELSTGMKKKVALA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490220552 164 RALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQL 238
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-239 |
2.11e-57 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 183.75 E-value: 2.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggEKRR 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR------RARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 RLSdkenrqalrdvcMVFQQFNL---WPhMTVLDNVAT-------PLRRVKKVSREAAyAEAktqLARVGLADKADSWPA 150
Cdd:COG1121 76 RIG------------YVPQRAEVdwdFP-ITVRDVVLMgrygrrgLFRRPSRADREAV-DEA---LERVGLEDLADRPIG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 151 MLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIE 230
Cdd:COG1121 139 ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVA 218
|
....*....
gi 490220552 231 EqGAPAQLF 239
Cdd:COG1121 219 H-GPPEEVL 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-243 |
3.07e-57 |
|
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: 183.02 E-value: 3.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrrLSDK 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI------------TGLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 ENRQALRDVCMVFQQFNLWPHMTVLDNVATPLRRVKKVS---------REAAYAEAKTQLARVGLADKADSWPAMLSGGQ 156
Cdd:cd03219 69 PHEIARLGIGRTFQIPRLFPELTVLENVMVAAQARTGSGlllararreEREARERAEELLERVGLADLADRPAGELSYGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 157 QQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPA 236
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPD 228
|
....*..
gi 490220552 237 QLFHQPK 243
Cdd:cd03219 229 EVRNNPR 235
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-243 |
3.20e-57 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 187.46 E-value: 3.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPlgGEKRr 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP--AENR- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 rlsdkenrqalrDVCMVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRV 160
Cdd:PRK09452 87 ------------HVNTVFQSYALFPHMTVFENVAFGLR-MQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 161 AIARALTMKPAIMLFDEPTSALDPELVGEV---LKVI-RNLaddGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPA 236
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMqneLKALqRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPR 230
|
....*..
gi 490220552 237 QLFHQPK 243
Cdd:PRK09452 231 EIYEEPK 237
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-229 |
3.58e-57 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 181.94 E-value: 3.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENvgYEPLGGEK-RRRlsd 84
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKP--LSAMPPPEwRRQ--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 kenrqalrdVCMVFQQFNLWPhMTVLDNVATPLR-RVKKVSREaayaEAKTQLARVGLADKADSWPAM-LSGGQQQRVAI 162
Cdd:COG4619 76 ---------VAYVPQEPALWG-GTVRDNLPFPFQlRERKFDRE----RALELLERLGLPPDILDKPVErLSGGERQRLAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490220552 163 ARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHEMGFAAKVSDRVLFLADGCI 229
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-229 |
4.76e-57 |
|
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: 180.29 E-value: 4.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrrlsdK 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK--------------K 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 ENRQALRDVCMVFQQFNLWPHMTVLDNVatplrrvkkvsreaayaeaktqlarvgladkadswpaMLSGGQQQRVAIARA 165
Cdd:cd03230 67 EPEEVKRRIGYLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQA 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCI 229
Cdd:cd03230 110 LLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-238 |
5.16e-57 |
|
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: 181.86 E-value: 5.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekRRRLSDK 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI---------TGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 ENRqalRDVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARvgLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:cd03224 72 RAR---AGIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQL 238
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-251 |
1.33e-55 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 182.61 E-value: 1.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrr 80
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 rlSDKENRQalRDVCMVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRV 160
Cdd:PRK11432 71 --THRSIQQ--RDICMVFQSYALFPHMSLGENVGYGLK-MLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 161 AIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLF 239
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY 225
|
250
....*....|..
gi 490220552 240 HQPKSPRLQYFL 251
Cdd:PRK11432 226 RQPASRFMASFM 237
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-251 |
3.57e-55 |
|
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: 177.88 E-value: 3.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENH-VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENV-GYEPLggEKRRRLS 83
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIrEQDPV--ELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 dkenrqalrdvcMVFQQFNLWPHMTVLDNVATpLRRVKKVSREAAYAEAKTQLARVGLADK--ADSWPAMLSGGQQQRVA 161
Cdd:cd03295 79 ------------YVIQQIGLFPHMTVEENIAL-VPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 162 IARALTMKPAIMLFDEPTSALDP----ELVGEVLKVIRNLaddGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQ 237
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPitrdQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDE 222
|
250
....*....|....
gi 490220552 238 LFHQPKSPRLQYFL 251
Cdd:cd03295 223 ILRSPANDFVAEFV 236
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-227 |
7.44e-54 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 173.59 E-value: 7.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENH-VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRLSD 84
Cdd:TIGR02673 2 IEFHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDV----------NRLRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 KENRQALRDVCMVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIAR 164
Cdd:TIGR02673 72 RQLPLLRRRIGVVFQDFRLLPDRTVYENVALPLE-VRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490220552 165 ALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:TIGR02673 151 AIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-233 |
1.82e-53 |
|
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: 172.44 E-value: 1.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYeplggekrrrLSDK 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD----------LPPK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 EnrqalRDVCMVFQQFNLWPHMTVLDNVATPLrRVKKVSREAAyAEAKTQLARV-GLADKADSWPAMLSGGQQQRVAIAR 164
Cdd:cd03301 71 D-----RDIAMVFQNYALYPHMTVYDNIAFGL-KLRKVPKDEI-DERVREVAELlQIEHLLDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 165 ALTMKPAIMLFDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQG 233
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-227 |
3.77e-52 |
|
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: 167.42 E-value: 3.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 7 EINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrrlSDKE 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI-------------AKLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 87 NRQALRDVCMVFQqfnlwphmtvldnvatplrrvkkvsreaayaeaktqlarvgladkadswpamLSGGQQQRVAIARAL 166
Cdd:cd00267 68 LEELRRRIGYVPQ----------------------------------------------------LSGGQRQRVALARAL 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490220552 167 TMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:cd00267 96 LLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-243 |
5.59e-52 |
|
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: 170.22 E-value: 5.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 3 DYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplgGEKRRRL 82
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT-----GLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 83 sdkenrqALRDVCMVFQQFNLWPHMTVLDNVAT------------PLRRVKKVSRE--AAYAEAKTQLARVGLADKADSW 148
Cdd:COG0411 77 -------ARLGIARTFQNPRLFPELTVLENVLVaaharlgrgllaALLRLPRARREerEARERAEELLERVGLADRADEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 149 PAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFG 229
|
250
....*....|....*.
gi 490220552 228 CIEEQGAPAQLFHQPK 243
Cdd:COG0411 230 RVIAEGTPAEVRADPR 245
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-227 |
9.44e-51 |
|
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: 165.66 E-value: 9.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHV-LRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGEnvgyePLGGEKRRRLSd 84
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQ-----DVSDLRGRAIP- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 kenrQALRDVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSREAAyAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIAR 164
Cdd:cd03292 75 ----YLRRKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIR-KRVPAALELVGLSHKHRALPAELSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490220552 165 ALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-224 |
2.06e-50 |
|
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: 164.71 E-value: 2.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 8 INNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRLSDKEN 87
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQET----------PPLNSKKA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 88 RQALRDVC-MVFQQFNLWPHMTVLDNVATPLRRVKKVSREAAyaEAKTQ-LARVGLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:TIGR03608 71 SKFRREKLgYLFQNFALIENETVEENLDLGLKYKKLSKKEKR--EKKKEaLEKVGLNLKLKQKIYELSGGEQQRVALARA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMgFAAKVSDRVLFL 224
Cdd:TIGR03608 149 ILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
7-243 |
3.73e-50 |
|
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: 164.77 E-value: 3.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 7 EINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyePLGGEKRRRLSdke 86
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT--GLPPHRIARLG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 87 nrqalrdVCMVFQQFNLWPHMTVLDN--VATPLRRVKKVSREAayaeaktqLARVG-----LADKADSWPAMLSGGQQQR 159
Cdd:COG0410 80 -------IGYVPEGRRIFPSLTVEENllLGAYARRDRAEVRAD--------LERVYelfprLKERRRQRAGTLSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 160 VAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLF 239
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
....
gi 490220552 240 HQPK 243
Cdd:COG0410 225 ADPE 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-225 |
7.92e-50 |
|
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: 163.09 E-value: 7.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 7 EINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGEN-------VGYEPlggekR 79
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPlekerkrIGYVP-----Q 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 80 RRLSDKENRQALRD-VCMvfqqfNLWPHMTvldnvatPLRRVKKVSREAAyAEAktqLARVGLADKADSWPAMLSGGQQQ 158
Cdd:cd03235 76 RRSIDRDFPISVRDvVLM-----GLYGHKG-------LFRRLSKADKAKV-DEA---LERVGLSELADRQIGELSGGQQQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490220552 159 RVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLA 225
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-268 |
2.18e-49 |
|
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: 164.16 E-value: 2.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYG-----ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEplggekrr 80
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAK-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 rlsDKENRQALR-DVCMVFQQ-----FNLwphmTVLDNVATPLRRVKkVSREAAYAEAKTQLARVGLADK-ADSWPAMLS 153
Cdd:TIGR04521 73 ---KKKKLKDLRkKVGLVFQFpehqlFEE----TVYKDIAFGPKNLG-LSEEEAEERVKEALELVGLDEEyLERSPFELS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 154 GGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQ 232
Cdd:TIGR04521 145 GGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLD 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490220552 233 GAPAQLFHQ-----------PKSPRLQYFLsswseRQSGARLPETAL 268
Cdd:TIGR04521 225 GTPREVFSDvdelekigldvPEITELARKL-----KEKGLPVPKDPL 266
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
13-251 |
2.77e-49 |
|
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: 166.57 E-value: 2.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 13 KHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrRLSDKENRQALR 92
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIM----------KQSPVELREVRR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 93 -DVCMVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPA 171
Cdd:TIGR01186 71 kKIGMVFQQFALFPHMTILQNTSLGPE-LLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 172 IMLFDEPTSALDP----ELVGEVLKVIRNLaddGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPKSPRL 247
Cdd:TIGR01186 150 ILLMDEAFSALDPlirdSMQDELKKLQATL---QKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYV 226
|
....
gi 490220552 248 QYFL 251
Cdd:TIGR01186 227 EEFI 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-238 |
2.93e-49 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 169.43 E-value: 2.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 3 DYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRL 82
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV----------RFR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 83 SDKENRQAlrDVCMVFQQFNLWPHMTVLDNVA--TPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRV 160
Cdd:COG1129 72 SPRDAQAA--GIAIIHQELNLVPNLSVAENIFlgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490220552 161 AIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQL 238
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-243 |
8.24e-49 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 161.87 E-value: 8.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYS-----SGSIVVNGENVgYEPlg 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNI-YSP-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 76 gekrrRLSDKENRqalRDVCMVFQQFNLWPhMTVLDNVATPLR----RVKKVSREAA---------YAEAKTQLARVGLA 142
Cdd:PRK14239 78 -----RTDTVDLR---KEIGMVFQQPNPFP-MSIYENVVYGLRlkgiKDKQVLDEAVekslkgasiWDEVKDRLHDSALG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 143 dkadswpamLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDgMTMMIVTHEMGFAAKVSDRVL 222
Cdd:PRK14239 149 ---------LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTG 218
|
250 260
....*....|....*....|.
gi 490220552 223 FLADGCIEEQGAPAQLFHQPK 243
Cdd:PRK14239 219 FFLDGDLIEYNDTKQMFMNPK 239
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
8-229 |
8.73e-49 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 162.15 E-value: 8.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 8 INNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVngenvGYEPLGgekrrrlsdken 87
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-----GTAPLA------------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 88 rQALRDVCMVFQQFNLWPHMTVLDNVATPLR-RVKKVSREAayaeaktqLARVGLADKADSWPAMLSGGQQQRVAIARAL 166
Cdd:PRK11247 78 -EAREDTRLMFQDARLLPWKKVIDNVGLGLKgQWRDAALQA--------LAAVGLADRANEWPAALSGGQKQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490220552 167 TMKPAIMLFDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHEMGFAAKVSDRVLFLADGCI 229
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-252 |
1.22e-48 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 160.96 E-value: 1.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHvLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyEPLGGEKRrrlsdk 85
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI--TNLPPEKR------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 enrqalrDVCMVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:cd03299 72 -------DISYVPQNYALFPHMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 166 LTMKPAIMLFDEPTSALDP---ELVGEVLKVIRNLAddGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQP 242
Cdd:cd03299 144 LVVNPKILLLDEPFSALDVrtkEKLREELKKIRKEF--GVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
250
....*....|
gi 490220552 243 KSPRLQYFLS 252
Cdd:cd03299 222 KNEFVAEFLG 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-245 |
1.23e-48 |
|
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: 168.32 E-value: 1.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLN----KHYGENHVLRGIDVSISPGEVICVIGGSGSGKS-TLLRCINFLED---YSSGSIVVNGENVgyeplgge 77
Cdd:COG4172 7 LSVEDLSvafgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDpaaHPSGSILFDGQDL-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 78 krRRLSDKEnRQALR--DVCMVFQQ----FNlwPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLAD---KADSW 148
Cdd:COG4172 79 --LGLSERE-LRRIRgnRIAMIFQEpmtsLN--PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDperRLDAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 149 PAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:COG4172 154 PHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQG 233
|
250
....*....|....*...
gi 490220552 228 CIEEQGAPAQLFHQPKSP 245
Cdd:COG4172 234 EIVEQGPTAELFAAPQHP 251
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
6-227 |
3.00e-48 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 159.50 E-value: 3.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYG----ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyEPLG-GEK-- 78
Cdd:NF038007 2 LNMQNAEKCYItktiKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEV--TNLSySQKii 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 79 -RRRLsdkenrqalrdVCMVFQQFNLWPHMTVLDNVATPL--RRVKKVSREAAYAEAktqLARVGLADKADSWPAMLSGG 155
Cdd:NF038007 80 lRREL-----------IGYIFQSFNLIPHLSIFDNVALPLkyRGVAKKERIERVNQV---LNLFGIDNRRNHKPMQLSGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490220552 156 QQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGfAAKVSDRVLFLADG 227
Cdd:NF038007 146 QQQRVAIARAMVSNPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDG 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-233 |
1.18e-47 |
|
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: 156.44 E-value: 1.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 7 EINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENvgyeplggekrrrLSDKE 86
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKD-------------LASLS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 87 NRQALRDVCMVFQQfnlwphmtvldnvatplrrvkkvsreaayaeaktqLARVGLADKADSWPAMLSGGQQQRVAIARAL 166
Cdd:cd03214 68 PKELARKIAYVPQA-----------------------------------LELLGLAHLADRPFNELSGGERQRVLLARAL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490220552 167 TMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQG 233
Cdd:cd03214 113 AQEPPILLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-243 |
4.01e-47 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 157.70 E-value: 4.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 4 YAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYS-----SGSIVVNGENVgYEPlggek 78
Cdd:PRK14267 3 FAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNI-YSP----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 79 rrrlsDKENRQALRDVCMVFQQFNLWPHMTVLDNVATPLRRVKKV-SREAAYAEAKTQLARVGL----ADKADSWPAMLS 153
Cdd:PRK14267 77 -----DVDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVkSKKELDERVEWALKKAALwdevKDRLNDYPSNLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 154 GGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDgMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQG 233
Cdd:PRK14267 152 GGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
250
....*....|
gi 490220552 234 APAQLFHQPK 243
Cdd:PRK14267 231 PTRKVFENPE 240
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
6-233 |
4.94e-47 |
|
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: 156.11 E-value: 4.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVlrGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPlggekrrrlsdk 85
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 enrQALRDVCMVFQQFNLWPHMTVLDNVA---TPLRRVKKVSREAAyaeaKTQLARVGLADKADSWPAMLSGGQQQRVAI 162
Cdd:cd03298 67 ---PADRPVSMLFQENNLFAHLTVEQNVGlglSPGLKLTAEDRQAI----EVALARVGLAGLEKRLPGELSGGERQRVAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490220552 163 ARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQG 233
Cdd:cd03298 140 ARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-245 |
7.12e-47 |
|
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: 163.70 E-value: 7.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHY-----------GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDySSGSIVVNGENVgyepl 74
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDL----- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 75 ggekrRRLSDKENRQALRDVCMVFQ----QFNlwPHMTVLDNVATPLR----RVKKVSREAAYAEAktqLARVGL-ADKA 145
Cdd:COG4172 350 -----DGLSRRALRPLRRRMQVVFQdpfgSLS--PRMTVGQIIAEGLRvhgpGLSAAERRARVAEA---LEEVGLdPAAR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 146 DSWPAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFL 224
Cdd:COG4172 420 HRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVM 499
|
250 260
....*....|....*....|.
gi 490220552 225 ADGCIEEQGAPAQLFHQPKSP 245
Cdd:COG4172 500 KDGKVVEQGPTEQVFDAPQHP 520
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-244 |
1.02e-46 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 159.62 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHY-GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVG-YEPlggekrrrl 82
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNeLEP--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 83 sdkenrqALRDVCMVFQQFNLWPHMTVLDNVATPL--RRVKKVSREAAYAEAktqlARV-GLADKADSWPAMLSGGQQQR 159
Cdd:PRK11650 74 -------ADRDIAMVFQNYALYPHMSVRENMAYGLkiRGMPKAEIEERVAEA----ARIlELEPLLDRKPRELSGGQRQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 160 VAIARALTMKPAIMLFDEPTSALDPELVG----EVLKVIRNLaddGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAP 235
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDAKLRVqmrlEIQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTP 219
|
....*....
gi 490220552 236 AQLFHQPKS 244
Cdd:PRK11650 220 VEVYEKPAS 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-248 |
1.11e-46 |
|
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: 159.50 E-value: 1.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 24 IDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGEnvgyeplggekrrRLSDKENRQAL----RDVCMVFQ 99
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE-------------VLQDSARGIFLpphrRRIGYVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 100 QFNLWPHMTVLDNVATPLRRVKKVSREAAYAEAktqLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEPT 179
Cdd:COG4148 85 EARLFPHLSVRGNLLYGRKRAPRAERRISFDEV---VELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 180 SALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPKSPRLQ 248
Cdd:COG4148 162 AALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLA 231
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
6-244 |
6.36e-46 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 157.47 E-value: 6.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYG----ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggEKRRR 81
Cdd:NF040933 3 VRVENVTKIFKkgkkEVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVA------SPGKI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 82 LSDKENRqalrDVCMVFQQFNLWPHMTVLDNVATPLrRVKKVSREAAYAEAKtQLARV-GLADKADSWPAMLSGGQQQRV 160
Cdd:NF040933 77 IVPPEDR----NIGMVFQNWALYPNMTVFDNIAFPL-KIKKVPKDEIEKKVK-EVAEIlGISEVLDRYPRELSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 161 AIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLA-DDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLF 239
Cdd:NF040933 151 ALARALVKNPQVLLLDEPFSNLDARIRDSARALVKKIQrELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIY 230
|
....*
gi 490220552 240 HQPKS 244
Cdd:NF040933 231 DNPAN 235
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-253 |
1.44e-45 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 155.66 E-value: 1.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHY-----------GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENV 69
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 70 GyePLGGEKRRRLsdkenRqalRDVCMVFQ--QFNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGL-ADKAD 146
Cdd:COG4608 83 T--GLSGRELRPL-----R---RRMQMVFQdpYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrPEHAD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 147 SWPAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLA 225
Cdd:COG4608 153 RYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMY 232
|
250 260
....*....|....*....|....*...
gi 490220552 226 DGCIEEQGAPAQLFHQPKSPRLQYFLSS 253
Cdd:COG4608 233 LGKIVEIAPRDELYARPLHPYTQALLSA 260
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-244 |
1.55e-45 |
|
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: 155.73 E-value: 1.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 36 VIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPlggekrrrlsdkenrQALRDVCMVFQQFNLWPHMTVLDNVAT 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP---------------PHLRHINMVFQSYALFPHMTVEENVAF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 116 PLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEV-LKVI 194
Cdd:TIGR01187 66 GLK-MRKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMqLELK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490220552 195 RNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPKS 244
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPAN 194
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-227 |
2.05e-45 |
|
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: 150.61 E-value: 2.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENH--VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRLS 83
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL----------RDLD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKENRQAlrdVCMVFQQFNLWpHMTVLDNVatplrrvkkvsreaayaeaktqlarvgladkadswpamLSGGQQQRVAIA 163
Cdd:cd03228 71 LESLRKN---IAYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490220552 164 RALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLAdDGMTMMIVTHEMGfAAKVSDRVLFLADG 227
Cdd:cd03228 109 RALLRDPPILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLS-TIRDADRIIVLDDG 170
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-229 |
4.10e-45 |
|
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: 150.87 E-value: 4.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 7 EINNLNKHYGENH-VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYeplggeKRRRlsdk 85
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA------KERR---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 enrqalRDVCMVFQ--QFNLWphmtvLDNVATPLRRVKKVSrEAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIA 163
Cdd:cd03226 71 ------KSIGYVMQdvDYQLF-----TDSVREELLLGLKEL-DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490220552 164 RALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCI 229
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-238 |
7.24e-45 |
|
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: 160.77 E-value: 7.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENH--VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRL 82
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL----------RQI 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 83 sdkeNRQALRDVC-MVFQQFNLWpHMTVLDNVA-----TPLRRVKKVSREAayaeaktqlarvGLADKADSWP------- 149
Cdd:COG2274 543 ----DPASLRRQIgVVLQDVFLF-SGTIRENITlgdpdATDEEIIEAARLA------------GLHDFIEALPmgydtvv 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 150 ----AMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLAdDGMTMMIVTHEMGFAAKVsDRVLFLA 225
Cdd:COG2274 606 geggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLA-DRIIVLD 683
|
250
....*....|...
gi 490220552 226 DGCIEEQGAPAQL 238
Cdd:COG2274 684 KGRIVEDGTHEEL 696
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-243 |
1.62e-44 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 154.03 E-value: 1.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 10 NLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGEnvgyeplggekrrRLSDKEnrQ 89
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK-------------RMNDVP--P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 90 ALRDVCMVFQQFNLWPHMTVLDNVATPLRRVKkvsreAAYAEAK---TQLARV-GLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:PRK11000 73 AERGVGMVFQSYALYPHLSVAENMSFGLKLAG-----AKKEEINqrvNQVAEVlQLAHLLDRKPKALSGGQRQRVAIGRT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 166 LTMKPAIMLFDEPTSALDPEL-VG---EVLKVIRNLaddGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQ 241
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAALrVQmriEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHY 224
|
..
gi 490220552 242 PK 243
Cdd:PRK11000 225 PA 226
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
7-238 |
1.96e-44 |
|
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: 149.98 E-value: 1.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 7 EINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrrlSDKE 86
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDIT------------KLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 87 NRQALRDVCMVFQQFNLWPHMTVLDN---VATPLRRVKKVSREAAYA---EAKTQLARVGladkadswpAMLSGGQQQRV 160
Cdd:TIGR03410 70 HERARAGIAYVPQGREIFPRLTVEENlltGLAALPRRSRKIPDEIYElfpVLKEMLGRRG---------GDLSGGQQQQL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490220552 161 AIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQL 238
Cdd:TIGR03410 141 AIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-243 |
4.26e-44 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 149.68 E-value: 4.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFL-----EDYSSGSIVVNGENVGYEPLGgEKRR 80
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVI-ELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 RlsdkenrqalrdVCMVFQQFNLWPHMTVLDNVATPLR--RVKKVSRE----AAYAEAKTQLARvGLADKADSWPAMLSG 154
Cdd:PRK14247 83 R------------VQMVFQIPNPIPNLSIFENVALGLKlnRLVKSKKElqerVRWALEKAQLWD-EVKDRLDAPAGKLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 155 GQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDgMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGA 234
Cdd:PRK14247 150 GQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGP 228
|
....*....
gi 490220552 235 PAQLFHQPK 243
Cdd:PRK14247 229 TREVFTNPR 237
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-270 |
1.17e-43 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 149.40 E-value: 1.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGEN--HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGenvgyeplggekrRRLS 83
Cdd:PRK13635 6 IRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-------------MVLS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKENRQALRDVCMVFQ----QFnlwPHMTVLDNVATPLRRvKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQR 159
Cdd:PRK13635 73 EETVWDVRRQVGMVFQnpdnQF---VGATVQDDVAFGLEN-IGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 160 VAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGM-TMMIVTHEMGFAAKvSDRVLFLADGCIEEQGAPAQL 238
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490220552 239 FHQ-----------PKSPRLQYFLsswseRQSGARLPETALQE 270
Cdd:PRK13635 228 FKSghmlqeigldvPFSVKLKELL-----KRNGILLPNTYLTM 265
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-180 |
1.28e-43 |
|
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: 145.10 E-value: 1.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 21 LRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLGGEkRRRLSdkenrqalrdvcMVFQQ 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL-RKEIG------------YVFQD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 101 FNLWPHMTVLDNVATPLrRVKKVSREAAYAEAKTQLARVGLADKAD----SWPAMLSGGQQQRVAIARALTMKPAIMLFD 176
Cdd:pfam00005 68 PQLFPRLTVRENLRLGL-LLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLD 146
|
....
gi 490220552 177 EPTS 180
Cdd:pfam00005 147 EPTA 150
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-227 |
5.16e-43 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 146.17 E-value: 5.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHY-GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrRLSD 84
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDIT----------RLKN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 KENRQALRDVCMVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIAR 164
Cdd:PRK10908 72 REVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLI-IAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490220552 165 ALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-238 |
5.55e-43 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 146.27 E-value: 5.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 25 DVSISPGEVICVIGGSGSGKSTLLRCI-NFLEDySSGSIVVNGENVGYEPlggekrrrlsdkenrQALRDVCMVFQQFNL 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIaGFLTP-ASGSLTLNGQDHTTTP---------------PSRRPVSMLFQENNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 104 WPHMTVLDNVATPLRRVKKVSreaayAEAKTQLA----RVGLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEPT 179
Cdd:PRK10771 83 FSHLTVAQNIGLGLNPGLKLN-----AAQREKLHaiarQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 180 SALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQL 238
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-226 |
7.70e-43 |
|
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: 144.93 E-value: 7.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrrlsDK 85
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI--------------RD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 ENRQALRDVCMVFQQFNLWPHMTVLDNVATpLRRVKKVSREAAYAEAktQLARVGLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:COG4133 69 AREDYRRRLAYLGHADGLKPELTVRENLRF-WAALYGLRADREAIDE--ALEAVGLAGLADLPVRQLSAGQKRRVALARL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTH-EMGFAAkvsDRVLFLAD 226
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqPLELAA---ARVLDLGD 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-238 |
1.44e-42 |
|
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: 144.96 E-value: 1.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYG--ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPlggekrrrls 83
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDR---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 dkenRQALRDVCMVFQQFNLWPHMTVLDNvatpLR---RVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRV 160
Cdd:cd03263 71 ----KAARQSLGYCPQFDALFDELTVREH----LRfyaRLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 161 AIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLAdDGMTMMIVTHEMGFAAKVSDRVLFLADG---CIeeqGAPAQ 237
Cdd:cd03263 143 SLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGklrCI---GSPQE 218
|
.
gi 490220552 238 L 238
Cdd:cd03263 219 L 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-233 |
4.13e-42 |
|
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: 143.59 E-value: 4.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 30 PGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGenvgyeplggekrRRLSDKENRQAL----RDVCMVFQQFNLWP 105
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG-------------TVLFDSRKKINLppqqRKIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 106 HMTVLDNVATPLRRVKKVSREAAYAEaktQLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPE 185
Cdd:cd03297 89 HLNVRENLAFGLKRKRNREDRISVDE---LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490220552 186 LVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQG 233
Cdd:cd03297 166 LRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
6-239 |
8.76e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 144.49 E-value: 8.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYG---ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLGgEKRRRL 82
Cdd:PRK13650 5 IEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVW-DIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 83 SdkenrqalrdvcMVFQQ-FNLWPHMTVLDNVATPLRRvKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVA 161
Cdd:PRK13650 84 G------------MVFQNpDNQFVGATVEDDVAFGLEN-KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490220552 162 IARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAkVSDRVLFLADGCIEEQGAPAQLF 239
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELF 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-241 |
1.21e-41 |
|
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: 150.29 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENH-VLRGIDVSISPGEVICVIGGSGSGKSTLLRCI-NFLEDYSsGSIVVNGENVgyeplggekrRRL 82
Cdd:COG4988 336 SIELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLlGFLPPYS-GSILINGVDL----------SDL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 83 SDKENRQAlrdVCMVFQQfNLWPHMTVLDNvatpLRRVKKVSREAAYAEAktqLARVGLADKADSWP-----------AM 151
Cdd:COG4988 405 DPASWRRQ---IAWVPQN-PYLFAGTIREN----LRLGRPDASDEELEAA---LEAAGLDEFVAALPdgldtplgeggRG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 152 LSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLAdDGMTMMIVTHEMGfAAKVSDRVLFLADGCIEE 231
Cdd:COG4988 474 LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLA-LLAQADRILVLDDGRIVE 551
|
250
....*....|
gi 490220552 232 QGAPAQLFHQ 241
Cdd:COG4988 552 QGTHEELLAK 561
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-242 |
1.27e-41 |
|
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: 150.30 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 2 RDYAIEINNLNKHYGENH--VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekr 79
Cdd:COG4987 330 GGPSLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL---------- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 80 RRLSdkenRQALRD-VCMVFQQfnlwPH---MTVLDN--VATPlrrvkkvsrEAAYAEAKTQLARVGLADKADSWP---- 149
Cdd:COG4987 400 RDLD----EDDLRRrIAVVPQR----PHlfdTTLRENlrLARP---------DATDEELWAALERVGLGDWLAALPdgld 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 150 -------AMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLAdDGMTMMIVTHEMGFAAKVsDRVL 222
Cdd:COG4987 463 twlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGLERM-DRIL 540
|
250 260
....*....|....*....|
gi 490220552 223 FLADGCIEEQGAPAQLFHQP 242
Cdd:COG4987 541 VLEDGRIVEQGTHEELLAQN 560
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-227 |
1.75e-41 |
|
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: 140.26 E-value: 1.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRLSDK 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV----------SFASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 ENRQALrdVCMVFQqfnlwphmtvldnvatplrrvkkvsreaayaeaktqlarvgladkadswpamLSGGQQQRVAIARA 165
Cdd:cd03216 71 DARRAG--IAMVYQ----------------------------------------------------LSVGERQMVEIARA 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:cd03216 97 LARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-225 |
2.60e-41 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 142.69 E-value: 2.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGEN----HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyEPLGGEkrr 80
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV--TGPGAD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 rlsdkenrqalRDVcmVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRV 160
Cdd:COG4525 78 -----------RGV--VFQKDALLPWLNVLDNVAFGLR-LRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490220552 161 AIARALTMKPAIMLFDEPTSALDP-------ELvgeVLKVirnLADDGMTMMIVTHEMgfaakvsDRVLFLA 225
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDAltreqmqEL---LLDV---WQRTGKGVFLITHSV-------EEALFLA 202
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
6-232 |
2.73e-41 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 141.84 E-value: 2.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENH----VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRR 81
Cdd:PRK10584 7 VEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL----------HQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 82 LsDKENRQALR--DVCMVFQQFNLWPHMTVLDNVATP--LR-RVKKVSREaayaEAKTQLARVGLADKADSWPAMLSGGQ 156
Cdd:PRK10584 77 M-DEEARAKLRakHVGFVFQSFMLIPTLNALENVELPalLRgESSRQSRN----GAKALLEQLGLGKRLDHLPAQLSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490220552 157 QQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVsDRVLFLADGCIEEQ 232
Cdd:PRK10584 152 QQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARC-DRRLRLVNGQLQEE 227
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-238 |
5.13e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 148.77 E-value: 5.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 3 DYAIEINNLNKHYGENH-VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRR 81
Cdd:COG1132 337 RGEIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI----------RD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 82 LSdkenRQALRD-VCMVFQQFNLWpHMTVLDNVAtpLRRvKKVSREAAYAEAKtqlaRVGLADKADSWP----------- 149
Cdd:COG1132 407 LT----LESLRRqIGVVPQDTFLF-SGTIRENIR--YGR-PDATDEEVEEAAK----AAQAHEFIEALPdgydtvvgerg 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 150 AMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLAdDGMTMMIVTHEMGfAAKVSDRVLFLADGCI 229
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLS-TIRNADRILVLDDGRI 552
|
....*....
gi 490220552 230 EEQGAPAQL 238
Cdd:COG1132 553 VEQGTHEEL 561
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-256 |
9.89e-41 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 148.72 E-value: 9.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHY--GENH--VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyePLGGEKRRR 81
Cdd:PRK10535 5 LELKDIRRSYpsGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVA--TLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 82 LSDKEnrqalrdVCMVFQQFNLWPHMTVLDNVATPlRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVA 161
Cdd:PRK10535 83 LRREH-------FGFIFQRYHLLSHLTAAQNVEVP-AVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 162 IARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKvSDRVLFLADGCI--------EEQG 233
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIvrnppaqeKVNV 233
|
250 260
....*....|....*....|...
gi 490220552 234 APAQLFHQPKSPRLQYFLSSWSE 256
Cdd:PRK10535 234 AGGTEPVVNTASGWRQFVSGFRE 256
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-233 |
2.25e-40 |
|
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: 138.84 E-value: 2.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 25 DVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRLSDKEnrqalRDVCMVFQQFNLW 104
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH----------TGLAPYQ-----RPVSMLFQENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 105 PHMTVLDNVATPLRRVKKVSreAAYAEAKTQLAR-VGLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALD 183
Cdd:TIGR01277 83 AHLTVRQNIGLGLHPGLKLN--AEQQEKVVDAAQqVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490220552 184 PELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQG 233
Cdd:TIGR01277 161 PLLREEMLALVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-227 |
3.09e-40 |
|
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: 139.14 E-value: 3.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 21 LRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyEPlgGEKRRrlsdkenrqalrdvcMVFQQ 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-EP--GPDRM---------------VVFQN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 101 FNLWPHMTVLDNVATPLRRV-KKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEPT 179
Cdd:TIGR01184 63 YSLLPWLTVRENIALAVDRVlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490220552 180 SALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-237 |
3.24e-40 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 139.91 E-value: 3.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCI-NFLEDYsSGSIVVNGenvgyEPLGGEKRRRLS 83
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGELSPD-SGEVRLNG-----RPLADWSPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 dkENRQALRdvcmvfQQFNLWPHMTVLDNVA---TPLRRVKKVSREAAyAEAktqLARVGLADKAD-SWPAmLSGGQQQR 159
Cdd:PRK13548 76 --RRRAVLP------QHSSLSFPFTVEEVVAmgrAPHGLSRAEDDALV-AAA---LAQVDLAHLAGrDYPQ-LSGGEQQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 160 VAIARALT------MKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQ 232
Cdd:PRK13548 143 VQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVAD 222
|
....*
gi 490220552 233 GAPAQ 237
Cdd:PRK13548 223 GTPAE 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-253 |
8.13e-40 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 140.87 E-value: 8.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHY--------GENHV--LRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVG 70
Cdd:PRK11308 1 SQQPLLQAIDLKKHYpvkrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 71 YEPLGGEKRRRlsdkenrqalRDVCMVFQQ--FNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGL-ADKADS 147
Cdd:PRK11308 81 KADPEAQKLLR----------QKIQIVFQNpyGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 148 WPAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLAD 226
Cdd:PRK11308 151 YPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYL 230
|
250 260
....*....|....*....|....*..
gi 490220552 227 GCIEEQGAPAQLFHQPKSPRLQYFLSS 253
Cdd:PRK11308 231 GRCVEKGTKEQIFNNPRHPYTQALLSA 257
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
6-241 |
8.29e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 139.80 E-value: 8.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYG-----ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggEKRR 80
Cdd:PRK13637 3 IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT------DKKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 RLSDKENRqalrdVCMVFQ--QFNLWPHmTVLDNVATPLRRVKkVSREAAYAEAKTQLARVGLA--DKADSWPAMLSGGQ 156
Cdd:PRK13637 77 KLSDIRKK-----VGLVFQypEYQLFEE-TIEKDIAFGPINLG-LSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 157 QQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAP 235
Cdd:PRK13637 150 KRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
....*.
gi 490220552 236 AQLFHQ 241
Cdd:PRK13637 230 REVFKE 235
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-246 |
1.27e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 138.67 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGEN-HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYeplggekrrrlsD 84
Cdd:PRK13639 2 LETRDLKYSYPDGtEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY------------D 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 KENRQALRD-VCMVFQQFN---LWPhmTVLDNVA-TPLRRvkKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQR 159
Cdd:PRK13639 70 KKSLLEVRKtVGIVFQNPDdqlFAP--TVEEDVAfGPLNL--GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 160 VAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLF 239
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
....*..
gi 490220552 240 HQPKSPR 246
Cdd:PRK13639 226 SDIETIR 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-238 |
1.50e-39 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 138.22 E-value: 1.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFL--EDYSSGSIVvngenvgyEPLGGEKRR--R 81
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGSHI--------ELLGRTVQRegR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 82 LSdKENRQALRDVCMVFQQFNLWPHMTVLDNV------ATPLRR--VKKVSREAAyAEAKTQLARVGLADKADSWPAMLS 153
Cdd:PRK09984 77 LA-RDIRKSRANTGYIFQQFNLVNRLSVLENVligalgSTPFWRtcFSWFTREQK-QRALQALTRVGMVHFAHQRVSTLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 154 GGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQ 232
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
|
....*.
gi 490220552 233 GAPAQL 238
Cdd:PRK09984 235 GSSQQF 240
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-255 |
3.73e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 137.92 E-value: 3.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 10 NLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSivvngENVGYEPLGGekRRRLSDKENRQ 89
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY-----RYSGDVLLGG--RSIFNYRDVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 90 ALRDVCMVFQQFNLWPhMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGL----ADKADSWPAMLSGGQQQRVAIARA 165
Cdd:PRK14271 99 FRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDgMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPKSP 245
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
250
....*....|
gi 490220552 246 RLQYFLSSWS 255
Cdd:PRK14271 257 ETARYVAGLS 266
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-233 |
5.61e-39 |
|
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: 135.04 E-value: 5.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrrlsdk 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 ENRQALRDVCMVFQQFNLWPHMTVLDNVATpLRRVKKVSreaaYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:cd03268 66 KNIEALRRIGALIEAPGFYPNLTARENLRL-LARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQG 233
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
23-253 |
1.24e-38 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 137.92 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 23 GIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRLSDKENRQALRDVCMVFQQ-- 100
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL----------LGMKDDEWRAVRSDIQMIFQDpl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 101 FNLWPHMTVLDNVATPLRRVK-KVSREAAYAEAKTQLARVGL-ADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEP 178
Cdd:PRK15079 109 ASLNPRMTIGEIIAEPLRTYHpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490220552 179 TSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPKSPRLQYFLSS 253
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSA 264
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-237 |
1.65e-38 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 135.24 E-value: 1.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCIN-FLEDYSsGSIVVNGEnvgyePLGGEKRRRLSd 84
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTgELTPSS-GEVRLNGR-----PLAAWSPWELA- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 keNRQAlrdvcmVFQQ-----FNLwphmTVLDNVA---TPLRRVKKVSREAAyAEAktqLARVGLADKAD-SWPAmLSGG 155
Cdd:COG4559 75 --RRRA------VLPQhsslaFPF----TVEEVVAlgrAPHGSSAAQDRQIV-REA---LALVGLAHLAGrSYQT-LSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 156 QQQRVAIARALT-------MKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGC 228
Cdd:COG4559 138 EQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGR 217
|
....*....
gi 490220552 229 IEEQGAPAQ 237
Cdd:COG4559 218 LVAQGTPEE 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-229 |
1.88e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 135.60 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNK--HYG---ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCI--NFLEDysSGSIVVNGENVGYEPlggek 78
Cdd:COG1101 2 LELKNLSKtfNPGtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIagSLPPD--SGSILIDGKDVTKLP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 79 rrrlsdkENRQAlRDVCMVFQ--QFNLWPHMTVLDNVATPLRRVKK------VSReAAYAEAKTQLARV--GLADKADSW 148
Cdd:COG1101 75 -------EYKRA-KYIGRVFQdpMMGTAPSMTIEENLALAYRRGKRrglrrgLTK-KRRELFRELLATLglGLENRLDTK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 149 PAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:COG1101 146 VGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
..
gi 490220552 228 CI 229
Cdd:COG1101 226 RI 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-244 |
2.22e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 135.17 E-value: 2.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 8 INNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYeplgGEKRRRLSDKEN 87
Cdd:PRK14246 13 ISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYF----GKDIFQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 88 RqalRDVCMVFQQFNLWPHMTVLDNVATPL--------RRVKKVSREAayaeaktqLARVGL----ADKADSWPAMLSGG 155
Cdd:PRK14246 89 R---KEVGMVFQQPNPFPHLSIYDNIAYPLkshgikekREIKKIVEEC--------LRKVGLwkevYDRLNSPASQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 156 QQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDgMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAP 235
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
....*....
gi 490220552 236 AQLFHQPKS 244
Cdd:PRK14246 237 NEIFTSPKN 245
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-253 |
2.47e-38 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 138.04 E-value: 2.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPlggekrrrlsdk 85
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP------------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 enrQALRDVCMVFQQFNLWPHMTVLDNVATPLRRvKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:PRK11607 88 ---PYQRPINMMFQSYALFPHMTVEQNIAFGLKQ-DKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEV-LKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPKS 244
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTT 243
|
....*....
gi 490220552 245 PRLQYFLSS 253
Cdd:PRK11607 244 RYSAEFIGS 252
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-238 |
6.35e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 134.85 E-value: 6.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGE--------NVGYEPlgg 76
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEpldpedrrRIGYLP--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 77 EKRRrlsdkenrqalrdvcmvfqqfnLWPHMTVLDnVATPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQ 156
Cdd:COG4152 78 EERG----------------------LYPKMKVGE-QLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 157 QQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPA 236
Cdd:COG4152 135 QQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD 214
|
..
gi 490220552 237 QL 238
Cdd:COG4152 215 EI 216
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-223 |
9.24e-38 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 133.75 E-value: 9.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 3 DYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDY-----SSGSIVVNGENV---GYEPL 74
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyapDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 75 ggEKRRRlsdkenrqalrdVCMVFQQFNLWPHmTVLDNVATPLR----------RVKKVSREAA-YAEAKTQLARVGLAd 143
Cdd:PRK14243 88 --EVRRR------------IGMVFQKPNPFPK-SIYDNIAYGARingykgdmdeLVERSLRQAAlWDEVKDKLKQSGLS- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 144 kadswpamLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDgMTMMIVTHEMGFAAKVSDRVLF 223
Cdd:PRK14243 152 --------LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAF 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
7-226 |
1.58e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 131.45 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 7 EINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCIN-FLE-DYS-SGSIVVNGENVgyEPLGGEKRRrls 83
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSpAFSaSGEVLLNGRRL--TALPAEQRR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 dkenrqalrdVCMVFQQFNLWPHMTVLDNVATPLRRvkKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIA 163
Cdd:COG4136 78 ----------IGILFQDDLLFPHLSVGENLAFALPP--TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490220552 164 RALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSdRVLFLAD 226
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQrGIPALLVTHDEEDAPAAG-RVLDLGN 208
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-227 |
1.80e-37 |
|
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: 131.79 E-value: 1.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYgENH--------VLRGIDVSISPGEVICVIGGSGSGKSTLLRCI--NFLEDysSGSIVVNGENVGYEPLG 75
Cdd:COG4778 5 LEVENLSKTF-TLHlqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYLPD--SGSILVRHDGGWVDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 76 GEKRRRLsdkenrqALR--DVCMVFQQFNLWPHMTVLDNVATPLRRvKKVSREAAYAEAKTQLARVGLADK-ADSWPAML 152
Cdd:COG4778 82 ASPREIL-------ALRrrTIGYVSQFLRVIPRVSALDVVAEPLLE-RGVDREEARARARELLARLNLPERlWDLPPATF 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490220552 153 SGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-238 |
2.02e-37 |
|
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: 131.72 E-value: 2.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPlgGEKRRRLSdk 85
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP--REVRRRIG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 enrqalrdvcMVFQQFNLWPHMTVLDNVATpLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:cd03265 77 ----------IVFQDLSVDDELTGWENLYI-HARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQL 238
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-221 |
3.87e-37 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 137.08 E-value: 3.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrr 80
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 RLSDKenRQALRD-VCMVFQQFNLWPHMTVLDNVA--TPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQ 157
Cdd:COG3845 70 RIRSP--RDAIALgIGMVHQHFMLVPNLTVAENIVlgLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490220552 158 QRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRV 221
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRV 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-239 |
5.04e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 132.04 E-value: 5.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 2 RDYAIEINNLNKHYG--ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekr 79
Cdd:PRK13632 4 KSVMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 80 rrlsDKENRQALRD-VCMVFQ----QFnlwPHMTVLDNVATPLRRvKKVSREAAYAEAKTQLARVGLADKADSWPAMLSG 154
Cdd:PRK13632 74 ----SKENLKEIRKkIGIIFQnpdnQF---IGATVEDDIAFGLEN-KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 155 GQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMI-VTHEMGFAAKvSDRVLFLADGCIEEQG 233
Cdd:PRK13632 146 GQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLIsITHDMDEAIL-ADKVIVFSEGKLIAQG 224
|
....*.
gi 490220552 234 APAQLF 239
Cdd:PRK13632 225 KPKEIL 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-233 |
6.93e-37 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 129.71 E-value: 6.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCIN--FLEDysSGSIVVNGEnvgyePLGGEKRRRLS 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILgiILPD--SGEVLFDGK-----PLDIAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 D-KENRqalrdvcmvfqqfNLWPHMTVLDNVATpLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAI 162
Cdd:cd03269 74 YlPEER-------------GLYPKMKVIDQLVY-LAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490220552 163 ARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQG 233
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-248 |
7.69e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 131.35 E-value: 7.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 20 VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGEnvgyePLGGEKRRrlsdkENRQALRDVCMVFQ 99
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGE-----PLAKLNRA-----QRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 100 Q----FNlwPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLADK-ADSWPAMLSGGQQQRVAIARALTMKPAIML 174
Cdd:PRK10419 97 DsisaVN--PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490220552 175 FDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHEMGFAAKVSDRVLFLADGCI-EEQG-APAQLFHQPKSPRLQ 248
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIvETQPvGDKLTFSSPAGRVLQ 251
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-242 |
1.05e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 131.46 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHY--GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFL---EDYSSGSIVVNGENVGyeplg 75
Cdd:PRK13640 1 MKDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLT----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 76 gekrrrlsdKENRQALRD-VCMVFQQ-FNLWPHMTVLDNVATPLRRvKKVSREAAYAEAKTQLARVGLADKADSWPAMLS 153
Cdd:PRK13640 76 ---------AKTVWDIREkVGIVFQNpDNQFVGATVGDDVAFGLEN-RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 154 GGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLA-DDGMTMMIVTHEMGfAAKVSDRVLFLADGCIEEQ 232
Cdd:PRK13640 146 GGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDID-EANMADQVLVLDDGKLLAQ 224
|
250
....*....|
gi 490220552 233 GAPAQLFHQP 242
Cdd:PRK13640 225 GSPVEIFSKV 234
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
29-247 |
1.08e-36 |
|
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: 133.31 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 29 SPGEVICVI-GGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyepLGGEKRRRLSDKEnrqalRDVCMVFQQFNLWPHM 107
Cdd:TIGR02142 20 LPGQGVTAIfGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL----FDSRKGIFLPPEK-----RRIGYVFQEARLFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 108 TVLDNVATPLRRVKKVSREAAYAEAkTQLarVGLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELV 187
Cdd:TIGR02142 91 SVRGNLRYGMKRARPSERRISFERV-IEL--LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490220552 188 GEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPKSPRL 247
Cdd:TIGR02142 168 YEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWL 228
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
6-245 |
2.21e-36 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 129.96 E-value: 2.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHY---------GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGEnvgyeplgg 76
Cdd:COG4167 5 LEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 77 ekrrRLSDKENRQALRDVCMVFQQFN--LWPHMTV---LDnvaTPLRRVKKVSREAAYAEAKTQLARVGL-ADKADSWPA 150
Cdd:COG4167 76 ----KLEYGDYKYRCKHIRMIFQDPNtsLNPRLNIgqiLE---EPLRLNTDLTAEEREERIFATLRLVGLlPEHANFYPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 151 MLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCI 229
Cdd:COG4167 149 MLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEV 228
|
250
....*....|....*.
gi 490220552 230 EEQGAPAQLFHQPKSP 245
Cdd:COG4167 229 VEYGKTAEVFANPQHE 244
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-232 |
2.56e-36 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 129.17 E-value: 2.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 9 NNLNKHYGE----NHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGEnvgyePLGGEKRRRLSD 84
Cdd:PRK11629 9 DNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ-----PMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 KENRQalrdVCMVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIAR 164
Cdd:PRK11629 84 LRNQK----LGFIYQFHHLLPDFTALENVAMPLL-IGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490220552 165 ALTMKPAIMLFDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHEMGFAAKVSdRVLFLADGCIEEQ 232
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-238 |
3.80e-36 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 129.05 E-value: 3.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPlGGEKRRRLS-- 83
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTP-SRELAKRLAil 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKENRQALRdvCMVFQ--QFNLWPH----MTVLDnvatplrrvkkvsrEAAYAEAktqLARVGLADKADSWPAMLSGGQQ 157
Cdd:COG4604 81 RQENHINSR--LTVRElvAFGRFPYskgrLTAED--------------REIIDEA---IAYLDLEDLADRYLDELSGGQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 158 QRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPA 236
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPE 221
|
..
gi 490220552 237 QL 238
Cdd:COG4604 222 EI 223
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
6-253 |
4.63e-36 |
|
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: 129.18 E-value: 4.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCInfledysSGSIVVNGENVGYEPLGGEKRR--RLS 83
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCL-------AGRLAPDHGTATYIMRSGAELElyQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKENRQALR-DVCMVFQQFNLWPHMTVL--DNVATPLRRVKKVSREAAYAEAKTQLARVGL-ADKADSWPAMLSGGQQQR 159
Cdd:TIGR02323 77 EAERRRLMRtEWGFVHQNPRDGLRMRVSagANIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 160 VAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQL 238
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQV 236
|
250
....*....|....*
gi 490220552 239 FHQPKSPRLQYFLSS 253
Cdd:TIGR02323 237 LDDPQHPYTQLLVSS 251
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-251 |
1.74e-35 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 130.92 E-value: 1.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 26 VSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrRLSDKENRQALRD-VCMVFQQFNLW 104
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIA----------KISDAELREVRRKkIAMVFQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 105 PHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDP 184
Cdd:PRK10070 119 PHMTVLDNTAFGME-LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490220552 185 ELVGEVL-KVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPKSPRLQYFL 251
Cdd:PRK10070 198 LIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-233 |
3.18e-35 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 125.38 E-value: 3.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGeVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrrlsdK 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV---------------L 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 ENRQALRD-VCMVFQQFNLWPHMTVLDNVATpLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIAR 164
Cdd:cd03264 65 KQPQKLRRrIGYLPQEFGVYPNFTVREFLDY-IAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490220552 165 ALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDgMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQG 233
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-239 |
4.31e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 127.27 E-value: 4.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHYGE-NHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLGGEKR 79
Cdd:PRK13636 1 MEDYILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 80 RRlsdkenrqalrDVCMVFQQ--FNLWPHMTVLD------NVATPLRRVKKVSREAayaeaktqLARVGLADKADSWPAM 151
Cdd:PRK13636 81 RE-----------SVGMVFQDpdNQLFSASVYQDvsfgavNLKLPEDEVRKRVDNA--------LKRTGIEHLKDKPTHC 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 152 LSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIE 230
Cdd:PRK13636 142 LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
....*....
gi 490220552 231 EQGAPAQLF 239
Cdd:PRK13636 222 LQGNPKEVF 230
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-214 |
7.93e-35 |
|
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: 124.07 E-value: 7.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 16 GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLGGEKRRRlsdkenrqalrDVC 95
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQ-----------RVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 96 MVFQQFN---LWPhmTVLDNVATPLR-------RVKKVSREAayaeaktqLARVGLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:TIGR01166 72 LVFQDPDdqlFAA--DVDQDVAFGPLnlglseaEVERRVREA--------LTAVGASGLRERPTHCLSGGEKKRVAIAGA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFA 214
Cdd:TIGR01166 142 VAMRPDVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
5-241 |
1.60e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 125.63 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYG-----ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekR 79
Cdd:PRK13649 2 GINLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLI---------T 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 80 RRLSDKENRQALRDVCMVFQ--QFNLWPHmTVLDNVATPLRRVKkVSREAAYAEAKTQLARVGLADKA-DSWPAMLSGGQ 156
Cdd:PRK13649 73 STSKNKDIKQIRKKVGLVFQfpESQLFEE-TVLKDVAFGPQNFG-VSQEEAEALAREKLALVGISESLfEKNPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 157 QQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPA 236
Cdd:PRK13649 151 MRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPK 230
|
....*
gi 490220552 237 QLFHQ 241
Cdd:PRK13649 231 DIFQD 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-238 |
1.83e-34 |
|
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: 124.26 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYG-ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRLSD 84
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI----------REVTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 KENRQAlrdVCMVFQQFNLWpHMTVLDNVA--TPlrrvkKVSREAAYAEAKTqlARVglADKADSWP-----------AM 151
Cdd:cd03253 71 DSLRRA---IGVVPQDTVLF-NDTIGYNIRygRP-----DATDEEVIEAAKA--AQI--HDKIMRFPdgydtivgergLK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 152 LSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLAdDGMTMMIVTHEMGFAAKvSDRVLFLADGCIEE 231
Cdd:cd03253 138 LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVE 215
|
....*..
gi 490220552 232 QGAPAQL 238
Cdd:cd03253 216 RGTHEEL 222
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-251 |
2.24e-34 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 124.88 E-value: 2.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyePlgGEKRRRLSdk 85
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI---P--AMSRSRLY-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 enrQALRDVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:PRK11831 81 ---TVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPkS 244
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-D 236
|
....*..
gi 490220552 245 PRLQYFL 251
Cdd:PRK11831 237 PRVRQFL 243
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-253 |
3.02e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 124.38 E-value: 3.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSS-----GSIVVNGENVgYEplggekr 79
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNI-YE------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 80 RRLSDKENRqalRDVCMVFQQFNLWPhMTVLDNVATPLRRV---KKVS----REAA------YAEAKTQLARVGLAdkad 146
Cdd:PRK14258 79 RRVNLNRLR---RQVSMVHPKPNLFP-MSVYDNVAYGVKIVgwrPKLEiddiVESAlkdadlWDEIKHKIHKSALD---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 147 swpamLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLA-DDGMTMMIVTHEMGFAAKVSDRVLFLA 225
Cdd:PRK14258 151 -----LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFK 225
|
250 260 270
....*....|....*....|....*....|...
gi 490220552 226 D-----GCIEEQGAPAQLFHQPKSPRLQYFLSS 253
Cdd:PRK14258 226 GnenriGQLVEFGLTKKIFNSPHDSRTREYVLS 258
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-233 |
3.24e-34 |
|
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: 123.25 E-value: 3.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGEN----HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPlggekrrr 81
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 82 lsdkenRQALRDVCMVFQQFNLWPHMTVLDNVATpLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVA 161
Cdd:cd03266 74 ------AEARRRLGFVSDSTGLYDRLTARENLEY-FAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490220552 162 IARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQG 233
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-253 |
3.51e-34 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 129.98 E-value: 3.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 8 INNLNKHYGENH----VLRGIDVSISPGEVICVIGGSGSGKS-TLLRCINFLEDyssgsivvNGENVGYEPLGGEKRRR- 81
Cdd:PRK10261 15 VENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ--------AGGLVQCDKMLLRRRSRq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 82 ---LSDKENRQALR----DVCMVFQQ--FNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLADKA---DSWP 149
Cdd:PRK10261 87 vieLSEQSAAQMRHvrgaDMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtilSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 150 AMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGC 228
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250 260
....*....|....*....|....*
gi 490220552 229 IEEQGAPAQLFHQPKSPRLQYFLSS 253
Cdd:PRK10261 247 AVETGSVEQIFHAPQHPYTRALLAA 271
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
13-238 |
3.73e-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: 125.20 E-value: 3.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 13 KHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPlgGEKRRRLSdkenrqalr 92
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREP--RKVRRSIG--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 93 dvcMVFQQFNLWPHMTVLDNVATpLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPAI 172
Cdd:TIGR01188 70 ---IVPQYASVDEDLTGRENLEM-MGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490220552 173 MLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQL 238
Cdd:TIGR01188 146 LFLDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-271 |
4.72e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 124.75 E-value: 4.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 17 ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVnGENVgyepLGGEKRRRlsdkeNRQALRD-VC 95
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERV----ITAGKKNK-----KLKPLRKkVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 96 MVFQ--QFNLWPHmTVLDNVA-TPLRRvkKVSREAAYAEAKTQLARVGL-ADKADSWPAMLSGGQQQRVAIARALTMKPA 171
Cdd:PRK13634 89 IVFQfpEHQLFEE-TVEKDICfGPMNF--GVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 172 IMLFDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQ--------- 241
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADpdeleaigl 245
|
250 260 270
....*....|....*....|....*....|..
gi 490220552 242 --PKSPRLQYFLsswsERQSGARLPETALQES 271
Cdd:PRK13634 246 dlPETVKFKRAL----EEKFGISFPKPCLTLE 273
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-253 |
5.28e-34 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 123.88 E-value: 5.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 8 INNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCInfledysSGSIVVNGENVGYEPLGGEKR--RRLSDK 85
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNAL-------SARLAPDAGEVHYRMRDGQLRdlYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 ENRQALRDVCMVFQQF---NLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGL-ADKADSWPAMLSGGQQQRVA 161
Cdd:PRK11701 82 ERRRLLRTEWGFVHQHprdGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 162 IARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFH 240
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLD 241
|
250
....*....|...
gi 490220552 241 QPKSPRLQYFLSS 253
Cdd:PRK11701 242 DPQHPYTQLLVSS 254
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-242 |
6.29e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 124.96 E-value: 6.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 3 DYAIEINNLNKHYGENH-----VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSI----VVNGENVGYEP 73
Cdd:PRK13631 19 DIILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 74 LGGEKRRRlSDKENRQALRDVCMVFQ--QFNLWPHMTVLDNVATPLrrVKKVSREAAYAEAKTQLARVGLADK-ADSWPA 150
Cdd:PRK13631 99 LITNPYSK-KIKNFKELRRRVSMVFQfpEYQLFKDTIEKDIMFGPV--ALGVKKSEAKKLAKFYLNKMGLDDSyLERSPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 151 MLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIE 230
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
250
....*....|..
gi 490220552 231 EQGAPAQLFHQP 242
Cdd:PRK13631 256 KTGTPYEIFTDQ 267
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-229 |
1.45e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 123.66 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYG-----ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLGGEKRR 80
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 RLSD-----------KENRQALRDVCMVFQ--QFNLWPHMTVLDNVATPlrRVKKVSREAAYAEAKTQLARVGL-ADKAD 146
Cdd:PRK13651 83 VLEKlviqktrfkkiKKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGP--VSMGVSKEEAKKRAAKYIELVGLdESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 147 SWPAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLAD 226
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
...
gi 490220552 227 GCI 229
Cdd:PRK13651 241 GKI 243
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-235 |
8.74e-33 |
|
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: 125.30 E-value: 8.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDY--SSGSIVVN---GENVGYE-------- 72
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYHvalCEKCGYVerpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 73 --PLGGEKRR-------RLSDKENRQALRDVCMVFQQ-FNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTqLARVGLA 142
Cdd:TIGR03269 81 pcPVCGGTLEpeevdfwNLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDL-IEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 143 DKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLA-DDGMTMMIVTHEMGFAAKVSDRV 221
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....
gi 490220552 222 LFLADGCIEEQGAP 235
Cdd:TIGR03269 240 IWLENGEIKEEGTP 253
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-236 |
2.39e-32 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 122.64 E-value: 2.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrrlSDK 85
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV-------------EAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 ENRQALRDVCMVFQQFNLWPHMTVLDNVA---TPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAI 162
Cdd:PRK09536 71 SARAASRRVASVPQDTSLSFEFDVRQVVEmgrTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490220552 163 ARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPA 236
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPA 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-243 |
2.64e-32 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 118.41 E-value: 2.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLggEKRRRLSdk 85
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM--HKRARLG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 enrqalrdVCMVFQQFNLWPHMTVLDNVATPLRRVKKvSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:cd03218 77 --------IGYLPQEASIFRKLTVEENILAVLEIRGL-SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPK 243
Cdd:cd03218 148 LATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-238 |
3.50e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.46 E-value: 3.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 3 DYAIEINNLNKHYGE-NHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrr 81
Cdd:PRK13647 2 DNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 82 lsDKENRQALRD-VCMVFQQ-----FNlwphMTVLDNVA-TPLRrvKKVSREAAYAEAKTQLARVGLADKADSWPAMLSG 154
Cdd:PRK13647 70 --NAENEKWVRSkVGLVFQDpddqvFS----STVWDDVAfGPVN--MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 155 GQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGA 234
Cdd:PRK13647 142 GQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD 221
|
....
gi 490220552 235 PAQL 238
Cdd:PRK13647 222 KSLL 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-238 |
5.15e-32 |
|
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: 118.03 E-value: 5.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHY---GENHVLRGIDVSISPGEVICVIGGSGSGKSTllrCINFLE---DYSSGSIVVNGENVgyeplggekr 79
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLErfyDPTSGEILLDGVDI---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 80 RRLsdkeNRQALRD-VCMVFQQFNLWPhMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLADKADSW----PAMLSG 154
Cdd:cd03249 68 RDL----NLRWLRSqIGLVSQEPVLFD-GTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLvgerGSQLSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 155 GQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLAdDGMTMMIVTHEMGfAAKVSDRVLFLADGCIEEQGA 234
Cdd:cd03249 143 GQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGT 220
|
....
gi 490220552 235 PAQL 238
Cdd:cd03249 221 HDEL 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
6-241 |
8.89e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 118.27 E-value: 8.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENH------VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekr 79
Cdd:PRK13633 5 IKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDT---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 80 rrlSDKENRQALRDVC-MVFQQFNLWPHMTVLD--------NVATPLRRVKKVSREAayaeaktqLARVGLADKADSWPA 150
Cdd:PRK13633 75 ---SDEENLWDIRNKAgMVFQNPDNQIVATIVEedvafgpeNLGIPPEEIRERVDES--------LKKVGMYEYRRHAPH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 151 MLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLAD-DGMTMMIVTHEMGFAAKvSDRVLFLADGCI 229
Cdd:PRK13633 144 LLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
250
....*....|..
gi 490220552 230 EEQGAPAQLFHQ 241
Cdd:PRK13633 223 VMEGTPKEIFKE 234
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-224 |
1.72e-31 |
|
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: 122.01 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHY-GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGenvgyeplggekrRRLS 83
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG-------------VPLA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKENRQALRDVCMVFQQfnlwPHM---TVLDNVAtpLRRvkkvsREAAYAEAKTQLARVGLAD-----------KADSWP 149
Cdd:TIGR02857 388 DADADSWRDQIAWVPQH----PFLfagTIAENIR--LAR-----PDASDAEIREALERAGLDEfvaalpqgldtPIGEGG 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490220552 150 AMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLAdDGMTMMIVTHEMGFAAKVsDRVLFL 224
Cdd:TIGR02857 457 AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-270 |
5.89e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 116.35 E-value: 5.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLN-KHYGENHV--LRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGEnvgyeplggekrrRL 82
Cdd:PRK13642 5 LEVENLVfKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-------------LL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 83 SDKENRQALRDVCMVFQQ-FNLWPHMTVLDNVATPLRRvKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVA 161
Cdd:PRK13642 72 TAENVWNLRRKIGMVFQNpDNQFVGATVEDDVAFGMEN-QGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 162 IARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKvSDRVLFLADGCIEEQGAPAQLFH 240
Cdd:PRK13642 151 VAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 490220552 241 Q-----------PKSPRLQYFLsswseRQSGARLPETALQE 270
Cdd:PRK13642 230 TsedmveigldvPFSSNLMKDL-----RKNGFDLPEKYLSE 265
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-238 |
5.92e-31 |
|
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: 115.28 E-value: 5.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYG--ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrrLS 83
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA-----------LA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKENRQalRDVCMVFQQfNLWPHMTVLDNVAT-----PLRRVKKVSREAAYAEAKTQLaRVGLADKADSWPAMLSGGQQQ 158
Cdd:cd03252 70 DPAWLR--RQVGVVLQE-NVLFNRSIRDNIALadpgmSMERVIEAAKLAGAHDFISEL-PEGYDTIVGEQGAGLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 159 RVAIARALTMKPAIMLFDEPTSALDPElvgEVLKVIRNLAD--DGMTMMIVTHEMGfAAKVSDRVLFLADGCIEEQGAPA 236
Cdd:cd03252 146 RIAIARALIHNPRILIFDEATSALDYE---SEHAIMRNMHDicAGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHD 221
|
..
gi 490220552 237 QL 238
Cdd:cd03252 222 EL 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-227 |
7.01e-31 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 115.57 E-value: 7.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrrlsd 84
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 kENRQALRDVcmVFQQFNLWPHMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIAR 164
Cdd:PRK11248 66 -EGPGAERGV--VFQNEGLLPWRNVQDNVAFGLQ-LAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIAR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490220552 165 ALTMKPAIMLFDEPTSALDP---ELVGEVLkvIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALDAftrEQMQTLL--LKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-223 |
7.10e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 113.48 E-value: 7.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 15 YGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVN-GENVGYEPlggeKRRRLSDkenrqAL-- 91
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAgGARVAYVP----QRSEVPD-----SLpl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 92 --RDVCMVfqqfNLWPHmtvldnvATPLRRVkkvsREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARALTMK 169
Cdd:NF040873 73 tvRDLVAM----GRWAR-------RGLWRRL----TRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490220552 170 PAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLF 223
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-239 |
9.27e-31 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 114.80 E-value: 9.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 3 DYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINflEDY---SSGSIVVNGEnvgyePLGGEK- 78
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLIT--GDLpptYGNDVRLFGE-----RRGGEDv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 79 ---RRRL---SdkenrQALrdvcmvFQQFNlwPHMTVLDNVAT----PLRRVKKVSrEAAYAEAKTQLARVGLADKADSW 148
Cdd:COG1119 74 welRKRIglvS-----PAL------QLRFP--RDETVLDVVLSgffdSIGLYREPT-DEQRERARELLELLGLAHLADRP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 149 PAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMI-VTH---EM--GFaakvsDRVL 222
Cdd:COG1119 140 FGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVlVTHhveEIppGI-----THVL 214
|
250
....*....|....*..
gi 490220552 223 FLADGCIEEQGAPAQLF 239
Cdd:COG1119 215 LLKDGRVVAAGPKEEVL 231
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-227 |
1.25e-30 |
|
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: 113.03 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 20 VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYS--SGSIVVNGENVGyeplggekrrrlsdkenRQALRD-VCM 96
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLD-----------------KRSFRKiIGY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 97 VFQQFNLWPHMTVldnvatplrrvkkvsREAAYAEAKTQlarvgladkadswpaMLSGGQQQRVAIARALTMKPAIMLFD 176
Cdd:cd03213 87 VPQDDILHPTLTV---------------RETLMFAAKLR---------------GLSGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490220552 177 EPTSALDPELVGEVLKVIRNLADDGMTMMIVTH----EMgFaaKVSDRVLFLADG 227
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRRLADTGRTIICSIHqpssEI-F--ELFDKLLLLSQG 188
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-272 |
3.92e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 114.11 E-value: 3.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 17 ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekRRRLSDKENRQALRDVCM 96
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITI---------THKTKDKYIRPVRKRIGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 97 VFQqfnlWPHMTVLD------------NVATPLRRVKkvsreaayAEAKTQLARVGLA-DKADSWPAMLSGGQQQRVAIA 163
Cdd:PRK13646 90 VFQ----FPESQLFEdtvereiifgpkNFKMNLDEVK--------NYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 164 RALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLA-DDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQ- 241
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDk 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 490220552 242 ----------PKSPRLQYFLsswsERQSGARLPETALQESA 272
Cdd:PRK13646 238 kkladwhiglPEIVQLQYDF----EQKYQTKLKDIALTEEE 274
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-238 |
4.63e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 112.82 E-value: 4.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLggEKRRRL--- 82
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPM--HKRARLgig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 83 ------SdkenrqalrdvcmVFQQfnlwphMTVLDNVATPLRrVKKVSREAAYAEAKTQLARVGLADKADSwPAM-LSGG 155
Cdd:COG1137 82 ylpqeaS-------------IFRK------LTVEDNILAVLE-LRKLSKKEREERLEELLEEFGITHLRKS-KAYsLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 156 QQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTH---EMgfaAKVSDRVLFLADGCIEEQ 232
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHnvrET---LGICDRAYIISEGKVLAE 217
|
....*.
gi 490220552 233 GAPAQL 238
Cdd:COG1137 218 GTPEEI 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-252 |
5.19e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 117.88 E-value: 5.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 16 GENHVLRGIDVSISPGEVICVIGGSGSGKST----LLRCINfledySSGSIVVNGEnvgyePLGGEKRRRLSDKENRqal 91
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQ-----PLHNLNRRQLLPVRHR--- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 92 rdVCMVFQQFN--LWPHMTVLDNVATPLR-RVKKVSREAAYAEAKTQLARVGL-ADKADSWPAMLSGGQQQRVAIARALT 167
Cdd:PRK15134 364 --IQVVFQDPNssLNPRLNVLQIIEEGLRvHQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 168 MKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPKSPR 246
Cdd:PRK15134 442 LKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
....*.
gi 490220552 247 LQYFLS 252
Cdd:PRK15134 522 TRQLLA 527
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
6-263 |
5.99e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 114.84 E-value: 5.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYG-ENHVLRGID---VSISPGEVICVIGGSGSGKSTLLRCINFLEDY----SSGSIVVNGENVgyeplgge 77
Cdd:PRK11022 4 LNVDKLSVHFGdESAPFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYpgrvMAEKLEFNGQDL-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 78 krRRLSDKENRQAL-RDVCMVFQQ--FNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLADKA---DSWPAM 151
Cdd:PRK11022 76 --QRISEKERRNLVgAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 152 LSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLAD-DGMTMMIVTHEMGFAAKVSDRVLFLADGCIE 230
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
250 260 270
....*....|....*....|....*....|....
gi 490220552 231 EQGAPAQLFHQPKSPRLQYFLSSWSERQSG-ARL 263
Cdd:PRK11022 234 ETGKAHDIFRAPRHPYTQALLRALPEFAQDkARL 267
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
5-238 |
7.18e-30 |
|
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: 118.14 E-value: 7.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENH--VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrrl 82
Cdd:TIGR03797 451 AIEVDRVTFRYRPDGplILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDL------------- 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 83 sDKENRQALRDVC-MVFQQFNLWPHmTVLDNVA--TPLrrvkkvSREAAYAEAKtqlaRVGLADKADSWP---------- 149
Cdd:TIGR03797 518 -AGLDVQAVRRQLgVVLQNGRLMSG-SIFENIAggAPL------TLDEAWEAAR----MAGLAEDIRAMPmgmhtviseg 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 150 -AMLSGGQQQRVAIARALTMKPAIMLFDEPTSALD---PELVGEVLKVIRnladdgMTMMIVTHEMGfAAKVSDRVLFLA 225
Cdd:TIGR03797 586 gGTLSGGQRQRLLIARALVRKPRILLFDEATSALDnrtQAIVSESLERLK------VTRIVIAHRLS-TIRNADRIYVLD 658
|
250
....*....|...
gi 490220552 226 DGCIEEQGAPAQL 238
Cdd:TIGR03797 659 AGRVVQQGTYDEL 671
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
5-243 |
8.74e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 113.39 E-value: 8.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYG-----ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPlggekr 79
Cdd:PRK13641 2 SIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPET------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 80 rrlSDKENRQALRDVCMVFQqfnlWPHMTVLDNvaTPLRRVK------KVSREAAYAEAKTQLARVGLADK-ADSWPAML 152
Cdd:PRK13641 76 ---GNKNLKKLRKKVSLVFQ----FPEAQLFEN--TVLKDVEfgpknfGFSEDEAKEKALKWLKKVGLSEDlISKSPFEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 153 SGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQ 232
Cdd:PRK13641 147 SGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKH 226
|
250
....*....|.
gi 490220552 233 GAPAQLFHQPK 243
Cdd:PRK13641 227 ASPKEIFSDKE 237
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-241 |
9.92e-30 |
|
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: 111.94 E-value: 9.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYG--ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRLS 83
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV----------RDYT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKENRqalRDVCMVFQQFNLWpHMTVLDNVATPLRRVkkvSREAAYAEAKTQLARVGLADKADSWPAM-------LSGGQ 156
Cdd:cd03251 71 LASLR---RQIGLVSQDVFLF-NDTVAENIAYGRPGA---TREEVEEAARAANAHEFIMELPEGYDTVigergvkLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 157 QQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDgMTMMIVTHEMGfAAKVSDRVLFLADGCIEEQGAPA 236
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKN-RTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHE 221
|
....*
gi 490220552 237 QLFHQ 241
Cdd:cd03251 222 ELLAQ 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
11-268 |
1.97e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 116.49 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 11 LNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrRLSDKENRQA 90
Cdd:PRK10261 330 LNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRID----------TLSPGKLQAL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 91 LRDVCMVFQQ--FNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGL-ADKADSWPAMLSGGQQQRVAIARALT 167
Cdd:PRK10261 400 RRDIQFIFQDpyASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 168 MKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPKSPR 246
Cdd:PRK10261 480 LNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPY 559
|
250 260
....*....|....*....|..
gi 490220552 247 LQYFLSSWSERQSGARLPETAL 268
Cdd:PRK10261 560 TRKLMAAVPVADPSRQRPQRVL 581
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-253 |
2.24e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 115.96 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLN---KHYGENH-VLRGIDVSISPGEVICVIGGSGSGKS-TLLRCINFLED----YSSGSIVVNGENVgyepLGG 76
Cdd:PRK15134 6 LAIENLSvafRQQQTVRtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvvYPSGDIRFHGESL----LHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 77 EKRRRLSDKENRQAlrdvcMVFQQ--FNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGL---ADKADSWPAM 151
Cdd:PRK15134 82 SEQTLRGVRGNKIA-----MIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 152 LSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIE 230
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
250 260
....*....|....*....|...
gi 490220552 231 EQGAPAQLFHQPKSPRLQYFLSS 253
Cdd:PRK15134 237 EQNRAATLFSAPTHPYTQKLLNS 259
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-233 |
3.99e-29 |
|
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: 108.55 E-value: 3.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGEN--HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrrlS 83
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKENrqALRDVCMVFQQfnlWPHM---TVLDNVATPLrrvkkvsreaayaeaktqlarvgladkadswpamlSGGQQQRV 160
Cdd:cd03247 68 DLEK--ALSSLISVLNQ---RPYLfdtTLRNNLGRRF-----------------------------------SGGERQRL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490220552 161 AIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDgMTMMIVTHEMGFAAKVsDRVLFLADGCIEEQG 233
Cdd:cd03247 108 ALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-237 |
5.17e-29 |
|
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: 115.23 E-value: 5.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 16 GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVN------------GENVGYEPlggekrrrls 83
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDgadlsqwdreelGRHIGYLP---------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 dkenrqalrdvcmvfQQFNLWPHmTVLDNVAtplrRVKKVSREAAYAEAKtqLARV-----GLADKADSWP----AMLSG 154
Cdd:COG4618 413 ---------------QDVELFDG-TIAENIA----RFGDADPEKVVAAAK--LAGVhemilRLPDGYDTRIgeggARLSG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 155 GQQQRVAIARALTMKPAIMLFDEPTSALDPElvGE--VLKVIRNLADDGMTMMIVTHEMGfAAKVSDRVLFLADGCIEEQ 232
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNSNLDDE--GEaaLAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAF 547
|
....*
gi 490220552 233 GAPAQ 237
Cdd:COG4618 548 GPRDE 552
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-247 |
8.09e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 110.10 E-value: 8.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGEnvgyePLGGEKRRRLSdk 85
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDK-----PISMLSSRQLA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 enrqalRDVCMVFQQ--------------------FNLWPHMTVLDNvatplRRVKKvsreaayAEAKTQLARvgLADKA 145
Cdd:PRK11231 76 ------RRLALLPQHhltpegitvrelvaygrspwLSLWGRLSAEDN-----ARVNQ-------AMEQTRINH--LADRR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 146 DSwpaMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLA 225
Cdd:PRK11231 136 LT---DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLA 212
|
250 260
....*....|....*....|..
gi 490220552 226 DGCIEEQGAPAQLFhqpkSPRL 247
Cdd:PRK11231 213 NGHVMAQGTPEEVM----TPGL 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-227 |
8.32e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.39 E-value: 8.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 8 INNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVV-NGENVGYeplggekrrrLSdke 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLRIGY----------LP--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 87 nrqalrdvcmvfQQFNLWPHMTVLDNVATPLRRVKKVSRE-------------------------------AAYAEAKTQ 135
Cdd:COG0488 68 ------------QEPPLDDDLTVLDTVLDGDAELRALEAEleeleaklaepdedlerlaelqeefealggwEAEARAEEI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 136 LARVGLADKADSWP-AMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDpelvgevLKVIRNLAD-----DGmTMMIVTH 209
Cdd:COG0488 136 LSGLGFPEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIEWLEEflknyPG-TVLVVSH 207
|
250
....*....|....*...
gi 490220552 210 EMGFAAKVSDRVLFLADG 227
Cdd:COG0488 208 DRYFLDRVATRILELDRG 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-229 |
1.17e-28 |
|
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: 107.30 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENH--VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrrls 83
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKENRQALRD-VCMVFQQFNLWPHmTVLDNVatplrrvkkvsreaayaeaktqlarvgladkadswpamLSGGQQQRVAI 162
Cdd:cd03246 67 SQWDPNELGDhVGYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGL 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490220552 163 ARALTMKPAIMLFDEPTSALDPElvGE--VLKVIRNLADDGMTMMIVTHEMGFAAKVsDRVLFLADGCI 229
Cdd:cd03246 108 ARALYGNPRILVLDEPNSHLDVE--GEraLNQAIAALKAAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-238 |
1.63e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 111.08 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggEKRR 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV-------PARA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 RLsdkenrqALRDVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSREA-AYAEAKTQLARvgLADKADSWPAMLSGGQQQR 159
Cdd:PRK13536 110 RL-------ARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIeAVIPSLLEFAR--LESKADARVSDLSGGMKRR 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490220552 160 VAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQL 238
Cdd:PRK13536 181 LTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-242 |
1.67e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 114.05 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 17 ENHVLRGIDVSISPGEVICVIGGSGSGKSTllrCINFLEDYssgsivvngenvgYEPLGGE---KRRRLSDKENRQALRD 93
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNL-------------YQPTGGQvllDGVPLVQYDHHYLHRQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 94 VCMVFQQFNLWPHmTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLADKADS----WPAMLSGGQQQRVAIARALTMK 169
Cdd:TIGR00958 557 VALVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTevgeKGSQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490220552 170 PAIMLFDEPTSALDPElVGEVLKVIRNLADdgMTMMIVTHEMGFAAKvSDRVLFLADGCIEEQGAPAQLFHQP 242
Cdd:TIGR00958 636 PRVLILDEATSALDAE-CEQLLQESRSRAS--RTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-241 |
2.34e-28 |
|
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: 108.08 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENH-VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRLSD 84
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI----------RDISR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 KENRQAlrdVCMVFQQFNLWPHmTVLDNV--ATPLRRVKKVSREAAYAEAKTQLARV--GLADKADSWPAMLSGGQQQRV 160
Cdd:cd03254 73 KSLRSM---IGVVLQDTFLFSG-TIMENIrlGRPNATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 161 AIARALTMKPAIMLFDEPTSALDPE---LVGEVLKVIRNladdGMTMMIVTHEMGfAAKVSDRVLFLADGCIEEQGAPAQ 237
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTEtekLIQEALEKLMK----GRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDE 223
|
....
gi 490220552 238 LFHQ 241
Cdd:cd03254 224 LLAK 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-239 |
2.98e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 108.69 E-value: 2.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHY--GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggek 78
Cdd:PRK13648 3 DKNSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 79 rrrlsDKENRQALR-DVCMVFQQ-FNLWPHMTVLDNVATPLRRvKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQ 156
Cdd:PRK13648 74 -----TDDNFEKLRkHIGIVFQNpDNQFVGSIVKYDVAFGLEN-HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 157 QQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHEMGFAAKvSDRVLFLADGCIEEQGAP 235
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTP 226
|
....
gi 490220552 236 AQLF 239
Cdd:PRK13648 227 TEIF 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-241 |
3.48e-28 |
|
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: 112.59 E-value: 3.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHY-----GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNgenVGYEPLGGEKRR 80
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR---VGDEWVDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 RLsdkENRQALRDVCMVFQQFNLWPHMTVLDNVATPLRRvkKVSREAAYAEAKTQLARVGLADKA-----DSWPAMLSGG 155
Cdd:TIGR03269 357 PD---GRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGL--ELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 156 QQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGA 234
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
....*..
gi 490220552 235 PAQLFHQ 241
Cdd:TIGR03269 512 PEEIVEE 518
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-242 |
3.49e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 108.74 E-value: 3.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHY-GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrrlsD 84
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI--------------T 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 KEN-RQALRDVCMVFQQ-----FNlwphMTVLDNVA-TPLRRvkKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQ 157
Cdd:PRK13652 70 KENiREVRKFVGLVFQNpddqiFS----PTVEQDIAfGPINL--GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 158 QRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPA 236
Cdd:PRK13652 144 KRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVE 223
|
....*.
gi 490220552 237 QLFHQP 242
Cdd:PRK13652 224 EIFLQP 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-209 |
6.49e-28 |
|
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: 111.68 E-value: 6.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHY-GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgYEPLGGEKRRRlsd 84
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV-SSLDQDEVRRR--- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 kenrqalrdVCMVFQQFNLWpHMTVLDNVAtplrrvkkVSR-EAAYAEAKTQLARVGLADKADSWP-----------AML 152
Cdd:TIGR02868 411 ---------VSVCAQDAHLF-DTTVRENLR--------LARpDATDEELWAALERVGLADWLRALPdgldtvlgeggARL 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490220552 153 SGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNlADDGMTMMIVTH 209
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-231 |
1.42e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.92 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVnGENV--GYeplggekrrrls 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVkiGY------------ 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 dkenrqalrdvcmvFQQFN--LWPHMTVLDNVAtplrrvkKVSREAAYAEAKTQLARVGLA-DKADSWPAMLSGGQQQRV 160
Cdd:COG0488 383 --------------FDQHQeeLDPDKTVLDELR-------DGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490220552 161 AIARALTMKPAIMLFDEPTSALDPELVgEVLkvIRNLAD-DGmTMMIVTHEMGFAAKVSDRVLFLADGCIEE 231
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETL-EAL--EEALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
6-241 |
1.64e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 107.51 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGEN-----HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPlggekrr 80
Cdd:PRK13643 2 IKFEKVNYTYQPNspfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTS------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 rlSDKENRQALRDVCMVFQ--QFNLWPHmTVLDNVATPLRRVKkVSREAAYAEAKTQLARVGLADKA-DSWPAMLSGGQQ 157
Cdd:PRK13643 75 --KQKEIKPVRKKVGVVFQfpESQLFEE-TVLKDVAFGPQNFG-IPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 158 QRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQ 237
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSD 230
|
....
gi 490220552 238 LFHQ 241
Cdd:PRK13643 231 VFQE 234
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
16-238 |
1.81e-27 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 110.91 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 16 GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLrciNFLEDYS------SGSIVVNGENVgyeplggekrrrlsdkeNRQ 89
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFRSpkgvkgSGSVLLNGMPI-----------------DAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 90 ALRDVCMVFQQFNLW-PHMTVLD--NVATPLRRVKKVSREAAYAEAKTQLARVGLADKADS------WPAMLSGGQQQRV 160
Cdd:TIGR00955 96 EMRAISAYVQQDDLFiPTLTVREhlMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 161 AIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMgfAAKVS---DRVLFLADGCIEEQGAPAQ 237
Cdd:TIGR00955 176 AFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQP--SSELFelfDKIILMAEGRVAYLGSPDQ 253
|
.
gi 490220552 238 L 238
Cdd:TIGR00955 254 A 254
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-238 |
2.05e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 107.58 E-value: 2.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrr 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 rlsDKENRQALRDVCMVFQQFNLWPHMTVLDNVATpLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRV 160
Cdd:PRK13537 72 ---PSRARHARQRVGVVPQFDNLDPDFTVRENLLV-FGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490220552 161 AIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQL 238
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-242 |
5.94e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 105.07 E-value: 5.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyEPLGGEKRR 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI--EGLPGHQIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 RLSdkenrqalrdVCMVFQQFNLWPHMTVLDNV-----------------ATP-LRRvkkvSREAAYAEAKTQLARVGLA 142
Cdd:PRK11300 79 RMG----------VVRTFQHVRLFREMTVIENLlvaqhqqlktglfsgllKTPaFRR----AESEALDRAATWLERVGLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 143 DKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRV 221
Cdd:PRK11300 145 EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRI 224
|
250 260
....*....|....*....|.
gi 490220552 222 LFLADGCIEEQGAPAQLFHQP 242
Cdd:PRK11300 225 YVVNQGTPLANGTPEEIRNNP 245
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-229 |
7.19e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.57 E-value: 7.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 7 EINNLNKhygeNHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCInF-LEDYSSGSIVVNGENVgyeplggekrrRLSDk 85
Cdd:COG1129 258 EVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARAL-FgADPADSGEIRLDGKPV-----------RIRS- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 eNRQALRD-VCMV---FQQFNLWPHMTVLDNVATP-LRRVKK---VSREAAYAEAKTQLARVGLadKADSW--PAM-LSG 154
Cdd:COG1129 321 -PRDAIRAgIAYVpedRKGEGLVLDLSIRENITLAsLDRLSRgglLDRRRERALAEEYIKRLRI--KTPSPeqPVGnLSG 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490220552 155 GQQQRVAIARALTMKPAIMLFDEPTSALDpelVG---EVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCI 229
Cdd:COG1129 398 GNQQKVVLAKWLATDPKVLILDEPTRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-227 |
7.61e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 109.13 E-value: 7.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLN-KHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVV-NGENV------GYEPLGg 76
Cdd:COG4178 362 ALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVlflpqrPYLPLG- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 77 ekrrRLsdkenRQALrdvcmvfqqfnLWPHmtvldnvatplrRVKKVSrEAAYAEAktqLARVGLA------DKADSWPA 150
Cdd:COG4178 441 ----TL-----REAL-----------LYPA------------TAEAFS-DAELREA---LEAVGLGhlaerlDEEADWDQ 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490220552 151 MLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNlADDGMTMMIVTHEMGFAAkVSDRVLFLADG 227
Cdd:COG4178 485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLAA-FHDRVLELTGD 559
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-253 |
1.83e-26 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 103.63 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 22 RGIDVSISPGEVICVIGGSGSGKStlLRCINFLE------DYSSGSIVVNGENVGYEPLGGekrrrlsdkenrqalRDVC 95
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPVAPCALRG---------------RKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 96 MVFQQ----FNlwPHMTVLDNVATPLRRVKKVSREAAYAEAktqLARVGLADKA---DSWPAMLSGGQQQRVAIARALTM 168
Cdd:PRK10418 83 TIMQNprsaFN--PLHTMHTHARETCLALGKPADDATLTAA---LEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 169 KPAIMLFDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPKSPRL 247
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVT 237
|
....*.
gi 490220552 248 QYFLSS 253
Cdd:PRK10418 238 RSLVSA 243
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-233 |
2.32e-26 |
|
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: 102.67 E-value: 2.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHY--GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRL 82
Cdd:cd03245 2 RIEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI----------RQL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 83 SDKENRqalRDVCMVFQQFNLWpHMTVLDNVAtplrrvkkVSREAAYAEAKTQLARV-GLADKADSWP-----------A 150
Cdd:cd03245 72 DPADLR---RNIGYVPQDVTLF-YGTLRDNIT--------LGAPLADDERILRAAELaGVTDFVNKHPngldlqigergR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 151 MLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDgMTMMIVTHEMGFAAKVsDRVLFLADGCIE 230
Cdd:cd03245 140 GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD-KTLIIITHRPSLLDLV-DRIIVMDSGRIV 217
|
...
gi 490220552 231 EQG 233
Cdd:cd03245 218 ADG 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-242 |
4.40e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 103.14 E-value: 4.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENH-VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrrlsD 84
Cdd:PRK13644 2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG-------------D 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 KENRQALRD-VCMVFQ----QFnlwPHMTVLDNVA--------TPLRRVKKVSReaayaeaktQLARVGLADKADSWPAM 151
Cdd:PRK13644 69 FSKLQGIRKlVGIVFQnpetQF---VGRTVEEDLAfgpenlclPPIEIRKRVDR---------ALAEIGLEKYRHRSPKT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 152 LSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGfAAKVSDRVLFLADGCIEE 231
Cdd:PRK13644 137 LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVL 215
|
250
....*....|.
gi 490220552 232 QGAPAQLFHQP 242
Cdd:PRK13644 216 EGEPENVLSDV 226
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
5-246 |
5.79e-26 |
|
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: 106.87 E-value: 5.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGEN--HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRL 82
Cdd:TIGR03375 463 EIEFRNVSFAYPGQetPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDI----------RQI 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 83 SDKENRqalRDVCMVFQQFNLWpHMTVLDNVATplrrvkkvsrEAAYAEAKTQLA---RVGLADKADSWP---------- 149
Cdd:TIGR03375 533 DPADLR---RNIGYVPQDPRLF-YGTLRDNIAL----------GAPYADDEEILRaaeLAGVTEFVRRHPdgldmqiger 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 150 -AMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLAdDGMTMMIVTHEMGFAAKVsDRVLFLADGC 228
Cdd:TIGR03375 599 gRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLLDLV-DRIIVMDNGR 676
|
250
....*....|....*...
gi 490220552 229 IEEQGAPAQLFHQPKSPR 246
Cdd:TIGR03375 677 IVADGPKDQVLEALRKGR 694
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-238 |
9.72e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 105.68 E-value: 9.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 4 YAIEINNLNKHY--GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENvgyeplggekrrr 81
Cdd:PRK11160 337 VSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP------------- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 82 LSDKeNRQALRD-VCMVFQQFNLWPHmTVLDNvatpLRRVKKVSREAAYAEAktqLARVGLADKADSWPAM--------- 151
Cdd:PRK11160 404 IADY-SEAALRQaISVVSQRVHLFSA-TLRDN----LLLAAPNASDEALIEV---LQQVGLEKLLEDDKGLnawlgeggr 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 152 -LSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDgMTMMIVTHEMGFAAKVsDRVLFLADGCIE 230
Cdd:PRK11160 475 qLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN-KTVLMITHRLTGLEQF-DRICVMDNGQII 552
|
....*...
gi 490220552 231 EQGAPAQL 238
Cdd:PRK11160 553 EQGTHQEL 560
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
10-247 |
1.05e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 101.51 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 10 NLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLggekrrrlsdkeNRQ 89
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPL------------HAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 90 ALRDVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARALTMK 169
Cdd:PRK10895 76 ARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490220552 170 PAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPKSPRL 247
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRV 233
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
2-241 |
1.19e-25 |
|
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: 105.98 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 2 RDYAIEINNLNKHYGENH--VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekr 79
Cdd:TIGR01846 452 LRGAITFENIRFRYAPDSpeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLA--------- 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 80 rrLSDKENRQalRDVCMVFQQfNLWPHMTVLDNVA-----TPLRRVKKVSREAAYAEAKTQLARvGLADKADSWPAMLSG 154
Cdd:TIGR01846 523 --IADPAWLR--RQMGVVLQE-NVLFSRSIRDNIAlcnpgAPFEHVIHAAKLAGAHDFISELPQ-GYNTEVGEKGANLSG 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 155 GQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLAdDGMTMMIVTHEMGfAAKVSDRVLFLADGCIEEQGA 234
Cdd:TIGR01846 597 GQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREIC-RGRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGR 674
|
....*..
gi 490220552 235 PAQLFHQ 241
Cdd:TIGR01846 675 HEELLAL 681
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-235 |
4.20e-25 |
|
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: 99.11 E-value: 4.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENH--VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGEN---VGYEPLggekRR 80
Cdd:cd03244 3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskIGLHDL----RS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 RLS----DkenrqalrdvCMVFQ---QFNLWPHmtvldNVATplrrvkkvsrEAAYAEAktqLARVGLADKADSWPAML- 152
Cdd:cd03244 79 RISiipqD----------PVLFSgtiRSNLDPF-----GEYS----------DEELWQA---LERVGLKEFVESLPGGLd 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 153 ----------SGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNlADDGMTMMIVTHemgfaaKV----- 217
Cdd:cd03244 131 tvveeggenlSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAH------RLdtiid 203
|
250
....*....|....*...
gi 490220552 218 SDRVLFLADGCIEEQGAP 235
Cdd:cd03244 204 SDRILVLDKGRVVEFDSP 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-227 |
5.26e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 103.47 E-value: 5.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSS--GSIVVNGEnvgyePLggeK 78
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGE-----EL---Q 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 79 RRRLSDKENRqalrDVCMVFQQFNLWPHMTVLDNV--ATPLRRVKKVSREAAYAEAKTQLARVGLADKADSwPAM-LSGG 155
Cdd:PRK13549 73 ASNIRDTERA----GIAIIHQELALVKELSVLENIflGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPAT-PVGnLGLG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490220552 156 QQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:PRK13549 148 QQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-233 |
8.92e-25 |
|
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: 98.63 E-value: 8.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGEnvgyeplggekrrrlsdK 85
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGH-----------------P 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 ENRQALRDVCMVFQQFNLWPHMTVLDN--VATPLRRVKKvsreaayAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIA 163
Cdd:TIGR03740 64 WTRKDLHKIGSLIESPPLYENLTARENlkVHTTLLGLPD-------SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIA 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 164 RALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQG 233
Cdd:TIGR03740 137 IALLNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQG 206
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-241 |
1.59e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 102.40 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHY--GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggeKRRRLS 83
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL--------RDYTLA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DkenrqaLRDVC-MVFQQFNLWpHMTVLDNVATPlrRVKKVSREAAYAEAKTQLArVGLADKADSW--------PAMLSG 154
Cdd:PRK11176 414 S------LRNQVaLVSQNVHLF-NDTIANNIAYA--RTEQYSREQIEEAARMAYA-MDFINKMDNGldtvigenGVLLSG 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 155 GQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDgMTMMIVTHEMGFAAKvSDRVLFLADGCIEEQGA 234
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEK-ADEILVVEDGEIVERGT 561
|
....*..
gi 490220552 235 PAQLFHQ 241
Cdd:PRK11176 562 HAELLAQ 568
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-227 |
3.93e-24 |
|
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: 95.58 E-value: 3.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 20 VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRLSdkeNRQALRD-VCMV- 97
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV----------TRRS---PRDAIRAgIAYVp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 98 --FQQFNLWPHMTVLDNVATPlrrvkkvsreaayaeaktqlarvgladkadswpAMLSGGQQQRVAIARALTMKPAIMLF 175
Cdd:cd03215 82 edRKREGLVLDLSVAENIALS---------------------------------SLLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490220552 176 DEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-227 |
4.44e-24 |
|
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: 96.00 E-value: 4.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENH-----VLRGIDVSISPGEVICVIGGSGSGKSTLLRCInfLEDY--SSGSIVVNGeNVGYEPlggek 78
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELekLSGSVSVPG-SIAYVS----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 79 rrrlsdkenrqalrdvcmvfQQ---FNlwphMTVLDNV--ATPL--RRVKKVSREAAyaeaktqlarvgLADKADSWPA- 150
Cdd:cd03250 73 --------------------QEpwiQN----GTIRENIlfGKPFdeERYEKVIKACA------------LEPDLEILPDg 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 151 ----------MLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPElVGEVL--KVIRNLADDGMTMMIVTHEMGFAAKVs 218
Cdd:cd03250 117 dlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH-VGRHIfeNCILGLLLNNKTRILVTHQLQLLPHA- 194
|
....*....
gi 490220552 219 DRVLFLADG 227
Cdd:cd03250 195 DQIVVLDNG 203
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-229 |
4.56e-24 |
|
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: 96.77 E-value: 4.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 20 VLRGIDVSISPGEVICVIGGSGSGKSTllrCINFLEDYssgsivvngenvgYEPLGGE---KRRRLSDKENRQALRDVCM 96
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKST---VVALLENF-------------YQPQGGQvllDGKPISQYEHKYLHSKVSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 97 VFQQFNLWPHmTVLDNVA-----TPLRRVKKVSrEAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPA 171
Cdd:cd03248 93 VGQEPVLFAR-SLQDNIAyglqsCSFECVKEAA-QKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490220552 172 IMLFDEPTSALDPELVGEVLKVIRNLADDgMTMMIVTHEMGFAAKvSDRVLFLADGCI 229
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
27-245 |
5.36e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 98.64 E-value: 5.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 27 SISPGEVICVIGGSGSGKSTLLRCInfledysSGSIVVNGENVGYEPLGGEKRRRLSDKE-NRQALRDVCMVFQQ--FNL 103
Cdd:PRK09473 38 SLRAGETLGIVGESGSGKSQTAFAL-------MGLLAANGRIGGSATFNGREILNLPEKElNKLRAEQISMIFQDpmTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 104 WPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLAD---KADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEPTS 180
Cdd:PRK09473 111 NPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490220552 181 ALDPELVGEVLKVIRNLADDGMTMMI-VTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLFHQPKSP 245
Cdd:PRK09473 191 ALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHP 256
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-234 |
5.72e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.87 E-value: 5.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrr 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 rlSDKENRQALR-DVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARvgLADKADSWPAMLSGGQQQR 159
Cdd:PRK11614 70 --TDWQTAKIMReAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQM 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490220552 160 VAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCI--EEQGA 234
Cdd:PRK11614 146 LAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVvlEDTGD 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-242 |
1.56e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 96.40 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHY-------GENHV--LRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYeplgG 76
Cdd:PRK15112 5 LEVRNLSKTFryrtgwfRRQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF----G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 77 EKRRRlsdkenRQALRdvcMVFQ--QFNLWPHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGL-ADKADSWPAMLS 153
Cdd:PRK15112 81 DYSYR------SQRIR---MIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 154 GGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQ 232
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVER 231
|
250
....*....|
gi 490220552 233 GAPAQLFHQP 242
Cdd:PRK15112 232 GSTADVLASP 241
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-239 |
1.69e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 96.62 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 17 ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyePLGGEKRrrlsdKENRQALRDVCM 96
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI---PANLKKI-----KEVKRLRKEIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 97 VFQ--QFNLWPHMTVLDNVATPLRRvkKVSREAAYAEAKTQLARVGLA-DKADSWPAMLSGGQQQRVAIARALTMKPAIM 173
Cdd:PRK13645 95 VFQfpEYQLFQETIEKDIAFGPVNL--GENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490220552 174 LFDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLF 239
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-227 |
2.28e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 98.83 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 7 EINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYeplggekrrrlsdKE 86
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRF-------------AS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 87 NRQALR-DVCMVFQQFNLWPHMTVLDNV---ATPLRRvKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAI 162
Cdd:PRK11288 73 TTAALAaGVAIIYQELHLVPEMTVAENLylgQLPHKG-GIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490220552 163 ARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-241 |
2.40e-23 |
|
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: 99.02 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYG--ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENvgyeplggekrrrLS 83
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHD-------------LA 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKENRQALRDVCMVFQQFNLWPHmTVLDNVA------TPLRRVKKVSReAAYAEAKTQLARVGLADKADSWPAMLSGGQQ 157
Cdd:TIGR02203 398 DYTLASLRRQVALVSQDVVLFND-TIANNIAygrteqADRAEIERALA-AAYAQDFVDKLPLGLDTPIGENGVLLSGGQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 158 QRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLAdDGMTMMIVTHEMGFAAKvSDRVLFLADGCIEEQGAPAQ 237
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNE 553
|
....
gi 490220552 238 LFHQ 241
Cdd:TIGR02203 554 LLAR 557
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-233 |
2.47e-23 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 94.65 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 20 VLRGIDVSISPGEVICVIGGSGSGKSTLLRCI-NFLEDYS--SGSIVVNGEnvgyeplggeKRRRlsdkenRQALRDVCM 96
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGGttSGQILFNGQ----------PRKP------DQFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 97 VFQQFNLWPHMTVLDNV--ATPLR-RVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPAIM 173
Cdd:cd03234 86 VRQDDILLPGLTVRETLtyTAILRlPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490220552 174 LFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMG---FaaKVSDRVLFLADGCIEEQG 233
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIVYSG 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
6-241 |
2.95e-23 |
|
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: 99.04 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGEN-HVLRGIDVSISPGEVICVIGGSGSGKSTLLRC-INFLeDYSSGSIVVNGENVgyeplggekrrrls 83
Cdd:TIGR01193 474 IVINDVSYSYGYGsNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLlVGFF-QARSGEILLNGFSL-------------- 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKENRQALRdvcmvfQQFNLWPHM------TVLDNV---ATPLRRVKKVSREAAYAEAKTQLARV--GLADKADSWPAML 152
Cdd:TIGR01193 539 KDIDRHTLR------QFINYLPQEpyifsgSILENLllgAKENVSQDEIWAACEIAEIKDDIENMplGYQTELSEEGSSI 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 153 SGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDgmTMMIVTHEMGFaAKVSDRVLFLADGCIEEQ 232
Cdd:TIGR01193 613 SGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSV-AKQSDKIIVLDHGKIIEQ 689
|
....*....
gi 490220552 233 GAPAQLFHQ 241
Cdd:TIGR01193 690 GSHDELLDR 698
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-238 |
4.50e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 95.05 E-value: 4.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 9 NNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRLSDKEnr 88
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI----------QHYASKE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 89 qALRDVCMVFQQFNLWPHMTVLDNVA------TPLRRVKKVSREAAYAEAktqLARVGLADKADSWPAMLSGGQQQRVAI 162
Cdd:PRK10253 79 -VARRIGLLAQNATTPGDITVQELVArgryphQPLFTRWRKEDEEAVTKA---MQATGITHLADQSVDTLSGGQRQRAWI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490220552 163 ARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQL 238
Cdd:PRK10253 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
7-235 |
4.97e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 94.36 E-value: 4.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 7 EINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDY--SSGSIVVNGENV-GYEPlggEKRrrls 83
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYevTSGSILLDGEDIlELSP---DER---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 dkenrqALRDVCMVFQQ---FnlwPHMTVLD--NVATPLRRVKKVSREAAYAEAKTQLARVGLAdkadswPAML------ 152
Cdd:COG0396 75 ------ARAGIFLAFQYpveI---PGVSVSNflRTALNARRGEELSAREFLKLLKEKMKELGLD------EDFLdryvne 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 153 --SGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTH------EMgfaakVSDRVLFL 224
Cdd:COG0396 140 gfSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHyqrildYI-----KPDFVHVL 214
|
250
....*....|.
gi 490220552 225 ADGCIEEQGAP 235
Cdd:COG0396 215 VDGRIVKSGGK 225
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
5-238 |
6.08e-23 |
|
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: 97.97 E-value: 6.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENH-VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrRRLS 83
Cdd:COG5265 357 EVRFENVSFGYDPERpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI----------RDVT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKENRQAlrdVCMVFQQ---FNlwphMTVLDNVA--TPlrrvkKVSREAAYAEAKtqLARV-----GLADKADSwpaM-- 151
Cdd:COG5265 427 QASLRAA---IGIVPQDtvlFN----DTIAYNIAygRP-----DASEEEVEAAAR--AAQIhdfieSLPDGYDT---Rvg 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 152 -----LSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMI------VTHemgfaakvSDR 220
Cdd:COG5265 490 erglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIahrlstIVD--------ADE 561
|
250
....*....|....*...
gi 490220552 221 VLFLADGCIEEQGAPAQL 238
Cdd:COG5265 562 ILVLEAGRIVERGTHAEL 579
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
18-233 |
6.70e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.10 E-value: 6.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 18 NHVLRgIDVSIsPGEVICVI-GGSGSGKSTLLRCINFLEDYSSGSIVVNGenvgyeplggekrRRLSDKENRQAL----R 92
Cdd:PRK11144 12 DLCLT-VNLTL-PAQGITAIfGRSGAGKTSLINAISGLTRPQKGRIVLNG-------------RVLFDAEKGICLppekR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 93 DVCMVFQQFNLWPHMTVLDNvatpLRR-VKKVSReaAYAEAKTQLarVGLADKADSWPAMLSGGQQQRVAIARALTMKPA 171
Cdd:PRK11144 77 RIGYVFQDARLFPHYKVRGN----LRYgMAKSMV--AQFDKIVAL--LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490220552 172 IMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMI-VTHEMGFAAKVSDRVLFLADGCIEEQG 233
Cdd:PRK11144 149 LLLMDEPLASLDLPRKRELLPYLERLAREINIPILyVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-239 |
7.46e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.69 E-value: 7.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 15 YGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGEnvgyePLGGEKRRRLsdkenrqALRD- 93
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK-----PLDYSKRGLL-------ALRQq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 94 VCMVFQQFNLWPHMTVLD-NVATPLRRVKKVSREAA--YAEAKTQLARVGLADKadswPAM-LSGGQQQRVAIARALTMK 169
Cdd:PRK13638 79 VATVFQDPEQQIFYTDIDsDIAFSLRNLGVPEAEITrrVDEALTLVDAQHFRHQ----PIQcLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 170 PAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLF 239
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
5-237 |
1.07e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 93.22 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHY----------------------GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSI 62
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 63 VVNGenvgyeplggekrrRLSdkenrqALRDVCMVFQqfnlwPHMTVLDNVAtpLR-RVKKVSREaayaEAKTQLARV-- 139
Cdd:COG1134 84 EVNG--------------RVS------ALLELGAGFH-----PELTGRENIY--LNgRLLGLSRK----EIDEKFDEIve 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 140 --GLADKADSwPA-MLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAK 216
Cdd:COG1134 133 faELGDFIDQ-PVkTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRR 211
|
250 260
....*....|....*....|.
gi 490220552 217 VSDRVLFLADGCIEEQGAPAQ 237
Cdd:COG1134 212 LCDRAIWLEKGRLVMDGDPEE 232
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-233 |
1.60e-22 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 91.82 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDY--SSGSIVVNGENvgyeplggekrrrLS 83
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGED-------------IT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKE-NRQALRDVCMVFQQFNLWPHMTVLDNvatpLRRVKkvsreaayaeaktqlarVGLadkadswpamlSGGQQQRVAI 162
Cdd:cd03217 68 DLPpEERARLGIFLAFQYPPEIPGVKNADF----LRYVN-----------------EGF-----------SGGEKKRNEI 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490220552 163 ARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTH-EMGFAAKVSDRVLFLADGCIEEQG 233
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-238 |
1.75e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.27 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENvgYEPLGGEKRRRLSdk 85
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNP--CARLTPAKAHQLG-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 enrqalrdVCMVFQQFNLWPHMTVLDNVATPLRRvkkvsREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARA 165
Cdd:PRK15439 88 --------IYLVPQEPLLFPNLSVKENILFGLPK-----RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490220552 166 LTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQL 238
Cdd:PRK15439 155 LMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-227 |
2.18e-22 |
|
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: 96.05 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSS--GSIVVNGEnvgyePLggeKRRRLS 83
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGS-----PL---KASNIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKENRqalrDVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSR---EAAYAEAKTQLARVGLADKADSWPAM-LSGGQQQR 159
Cdd:TIGR02633 74 DTERA----GIVIIHQELTLVPELSVAENIFLGNEITLPGGRmayNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490220552 160 VAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-209 |
4.38e-22 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 91.17 E-value: 4.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 17 ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCInfledyssgsivvngenvgyepLGGEKRRRLSDkenrqalrdvCM 96
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL----------------------AGALKGTPVAG----------CV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 97 VFQQFNLWPHMTVLDNVAtplrrvkkvsREAAYAEAKTQLARVGLADkADSW---PAMLSGGQQQRVAIARALTMKPAIM 173
Cdd:COG2401 90 DVPDNQFGREASLIDAIG----------RKGDFKDAVELLNAVGLSD-AVLWlrrFKELSTGQKFRFRLALLLAERPKLL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 490220552 174 LFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTH 209
Cdd:COG2401 159 VIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATH 195
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-233 |
5.77e-22 |
|
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: 94.72 E-value: 5.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 16 GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVN------------GENVGYEPlggekrrrls 83
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDgadlkqwdretfGKHIGYLP---------- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 dkenrqalrdvcmvfQQFNLWPHmTVLDNVAtplRRVKKVSREAAYAEAKtqLARV-----GLADKADSW----PAMLSG 154
Cdd:TIGR01842 399 ---------------QDVELFPG-TVAENIA---RFGENADPEKIIEAAK--LAGVhelilRLPDGYDTVigpgGATLSG 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 155 GQQQRVAIARALTMKPAIMLFDEPTSALDPElvGE--VLKVIRNLADDGMTMMIVTHEMGFAAKVsDRVLFLADGCIEEQ 232
Cdd:TIGR01842 458 GQRQRIALARALYGDPKLVVLDEPNSNLDEE--GEqaLANAIKALKARGITVVVITHRPSLLGCV-DKILVLQDGRIARF 534
|
.
gi 490220552 233 G 233
Cdd:TIGR01842 535 G 535
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-242 |
9.74e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 94.14 E-value: 9.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRG-IDVSISPGEVICVIGGSGSGKSTLLRCI-NFLEdYSsGSIVVNGENVgyeplggekrRRLS 83
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALlGFLP-YQ-GSLKINGIEL----------RELD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKENRQALrdvCMVFQQFNLwPHMTVLDNVAtpLRRVkkvsrEAAYAEAKTQLARVGLADKADSWP-----------AML 152
Cdd:PRK11174 418 PESWRKHL---SWVGQNPQL-PHGTLRDNVL--LGNP-----DASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGL 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 153 SGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMiVTHEMGFAAKVsDRVLFLADGCIEEQ 232
Cdd:PRK11174 487 SVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLM-VTHQLEDLAQW-DQIWVMQDGQIVQQ 564
|
250
....*....|
gi 490220552 233 GAPAQLFHQP 242
Cdd:PRK11174 565 GDYAELSQAG 574
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-227 |
1.06e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.08 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENvgYEplggekrrRLSDK 85
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN--YN--------KLDHK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 ENRQAlrDVCMVFQQFNLWPHMTVLDNVAT---PLRRVKKVSReAAYAEAKTQ----LARVGLADKADSWPAMLSGGQQQ 158
Cdd:PRK09700 76 LAAQL--GIGIIYQELSVIDELTVLENLYIgrhLTKKVCGVNI-IDWREMRVRaammLLRVGLKVDLDEKVANLSISHKQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490220552 159 RVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-233 |
2.28e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 89.70 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 12 NKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGEnvgyepLGGEKRRRLsdkenrqaL 91
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL------VPWKRRKKF--------L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 92 RDVCMVFQQFN-LWPHMTVLDNVATpLRRVKKVSreaaYAEAKTQLARvgLADKADSWPAM------LSGGQQQRVAIAR 164
Cdd:cd03267 94 RRIGVVFGQKTqLWWDLPVIDSFYL-LAAIYDLP----PARFKKRLDE--LSELLDLEELLdtpvrqLSLGQRMRAEIAA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 165 ALTMKPAIMLFDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQG 233
Cdd:cd03267 167 ALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-209 |
3.85e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.39 E-value: 3.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 16 GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYePLGGEKRRRLSdkeNRQALRdvc 95
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDD-PDVAEACHYLG---HRNAMK--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 96 mvfqqfnlwPHMTVLDNVATpLRRVKKvSREAAYAEAktqLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLF 175
Cdd:PRK13539 86 ---------PALTVAENLEF-WAAFLG-GEELDIAAA---LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|....*
gi 490220552 176 DEPTSALDPELVGEVLKVIR-NLADDGMtMMIVTH 209
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRaHLAQGGI-VIAATH 185
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-235 |
9.83e-21 |
|
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: 87.47 E-value: 9.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGEN--HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLGgEKRRRLS 83
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE-DLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 dkenrqalrdvcmvfqqfnLWPHMTVL--DNVATPLRRVKKVSREAAYAEAKtqLARVGLAdkadswpamLSGGQQQRVA 161
Cdd:cd03369 86 -------------------IIPQDPTLfsGTIRSNLDPFDEYSDEEIYGALR--VSEGGLN---------LSQGQRQLLC 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490220552 162 IARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGmTMMIVTHEMGFAAKVsDRVLFLADGCIEEQGAP 235
Cdd:cd03369 136 LARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNS-TILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
8-227 |
1.29e-20 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 91.09 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 8 INNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCI-------NFledysSGSIVVNGEnvgyeplggekrr 80
Cdd:PLN03211 71 ISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALagriqgnNF-----TGTILANNR------------- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 rlsdKENRQALRDVCMVFQQFNLWPHMTVLDNV--ATPLRRVKKVSREAAYAEAKTQLARVGLAD-----KADSWPAMLS 153
Cdd:PLN03211 133 ----KPTKQILKRTGFVTQDDILYPHLTVRETLvfCSLLRLPKSLTKQEKILVAESVISELGLTKcentiIGNSFIRGIS 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490220552 154 GGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHE-MGFAAKVSDRVLFLADG 227
Cdd:PLN03211 209 GGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEG 283
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-227 |
2.04e-20 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 84.81 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVN-GENVGYeplggekrrrlsd 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGsTVKIGY------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 kenrqalrdvcmvFQQfnlwphmtvldnvatplrrvkkvsreaayaeaktqlarvgladkadswpamLSGGQQQRVAIAR 164
Cdd:cd03221 68 -------------FEQ---------------------------------------------------LSGGEKMRLALAK 83
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490220552 165 ALTMKPAIMLFDEPTSALDPElvgEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:cd03221 84 LLLENPNLLLLDEPTNHLDLE---SIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-233 |
2.67e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 90.02 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHY-GENHVLRGIDVSISPGEVICVIGGSGSGKSTLlrcINFLE---DYSSGSIVVNGENVgyeplggekrR 80
Cdd:PRK13657 334 AVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQrvfDPQSGRILIDGTDI----------R 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 RLsdkeNRQALR-DVCMVFQQ---FNlwphMTVLDNV------ATP--LRRVKKVSREAAYAEAKTQlarvGLADKADSW 148
Cdd:PRK13657 401 TV----TRASLRrNIAVVFQDaglFN----RSIEDNIrvgrpdATDeeMRAAAERAQAHDFIERKPD----GYDTVVGER 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 149 PAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPEL---VGEVLKVIRNladdGMTMMIVTHEMgfaAKV--SDRVLF 223
Cdd:PRK13657 469 GRQLSGGERQRLAIARALLKDPPILILDEATSALDVETeakVKAALDELMK----GRTTFIIAHRL---STVrnADRILV 541
|
250
....*....|
gi 490220552 224 LADGCIEEQG 233
Cdd:PRK13657 542 FDNGRVVESG 551
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-238 |
3.54e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 87.15 E-value: 3.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 20 VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGEnvgyePLGGEKRRRLSdkenrqalRDVCMVFQ 99
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQ-----PLESWSSKAFA--------RKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 100 QFNLWPHMTVLDNVAT-------PLRRVKKVSREaayaEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPAI 172
Cdd:PRK10575 93 QLPAAEGMTVRELVAIgrypwhgALGRFGAADRE----KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490220552 173 MLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQL 238
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-233 |
5.58e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 85.66 E-value: 5.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHY----------------------GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIV 63
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 64 VNGenvgyeplggekrrRLSdkenrqALRDVCMVFQqfnlwPHMTVLDNVAtpLR-RVKKVSReaayAEAKTQLARV--- 139
Cdd:cd03220 81 VRG--------------RVS------SLLGLGGGFN-----PELTGRENIY--LNgRLLGLSR----KEIDEKIDEIief 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 140 -GLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVS 218
Cdd:cd03220 130 sELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLC 209
|
250
....*....|....*
gi 490220552 219 DRVLFLADGCIEEQG 233
Cdd:cd03220 210 DRALVLEKGKIRFDG 224
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-227 |
9.89e-20 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 88.25 E-value: 9.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 10 NLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYeplggekrrrlsdKENRQ 89
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDF-------------KSSKE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 90 ALRD-VCMVFQQFNLWPHMTVLDNVAtpLRRVKK----VSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIAR 164
Cdd:PRK10982 70 ALENgISMVHQELNLVLQRSVMDNMW--LGRYPTkgmfVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490220552 165 ALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:PRK10982 148 AFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-227 |
1.47e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 87.75 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 21 LRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEplggekrrrlSDKENRQAlrDVCMVFQQ 100
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFN----------GPKSSQEA--GIGIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 101 FNLWPHMTVLDNV---ATPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDE 177
Cdd:PRK10762 88 LNLIPQLTIAENIflgREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490220552 178 PTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:PRK10762 168 PTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
6-215 |
2.90e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 83.31 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrrlsdk 85
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 enrQALRDVcmvFQQFNLW--------PHMTVLDNVATPLRRVKKVSREAAyAEAktqLARVGLADKADSWPAMLSGGQQ 157
Cdd:PRK13538 66 ---RRQRDE---YHQDLLYlghqpgikTELTALENLRFYQRLHGPGDDEAL-WEA---LAQVGLAGFEDVPVRQLSAGQQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490220552 158 QRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVI-RNLADDGMTMMIVTHEMGFAA 215
Cdd:PRK13538 136 RRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLaQHAEQGGMVILTTHQDLPVAS 194
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-236 |
3.23e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 84.49 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 20 VLRGIDVSISPGEVICVIGGSGSGKSTLLRCI--NFLEDYSSGSIVVNGE-NVGYEPLGGEKRRRLSdkenrqALRDVCM 96
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGGGAPRGARVTGDvTLNGEPLAAIDAPRLA------RLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 97 VFQQ--FNLWPHMTVLdnvatpLRRVKKVSREAAYAEAKTQLARVGLAdKADSWP------AMLSGGQQQRVAIARAL-- 166
Cdd:PRK13547 90 QAAQpaFAFSAREIVL------LGRYPHARRAGALTHRDGEIAWQALA-LAGATAlvgrdvTTLSGGELARVQFARVLaq 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490220552 167 -------TMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPA 236
Cdd:PRK13547 163 lwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-272 |
3.90e-19 |
|
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: 86.53 E-value: 3.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 4 YAIEINNLNKHYGEN-HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLE-DYSSGSIVVNGENVGYEPlggekrrr 81
Cdd:TIGR03719 3 YIYTMNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDkDFNGEARPQPGIKVGYLP-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 82 lsdkenrqalrdvcmvfQQFNLWPHMTVLDNVATPLRRVKKVSRE-----AAYAE--------AKTQLARVGLADKADSW 148
Cdd:TIGR03719 75 -----------------QEPQLDPTKTVRENVEEGVAEIKDALDRfneisAKYAEpdadfdklAAEQAELQEIIDAADAW 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 149 P-------AM--------------LSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVG--EvlkviRNLADDGMTMM 205
Cdd:TIGR03719 138 DldsqleiAMdalrcppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAwlE-----RHLQEYPGTVV 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490220552 206 IVTHEMGFAAKVSDRVLFLADG-CIEEQGapaqlfhqpksprlQYflSSWSErQSGARLPETALQESA 272
Cdd:TIGR03719 213 AVTHDRYFLDNVAGWILELDRGrGIPWEG--------------NY--SSWLE-QKQKRLEQEEKEESA 263
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-231 |
9.68e-19 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 84.40 E-value: 9.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKStllrcinfledysSGSIV--VNGENVGYEPLggekrRRL 82
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**-------------RGALPahV*GPDAGRRPW-----RF* 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 83 SDKENRQALRDVCMVFQ--QFNLWPHMTVLDNVATpLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRV 160
Cdd:NF000106 75 TWCANRRALRRTIG*HRpvR*GRRESFSGRENLYM-IGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490220552 161 AIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVS------DRVLFLADGCIEE 231
Cdd:NF000106 154 DLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAheltviDRGRVIADGKVDE 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-210 |
9.95e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.45 E-value: 9.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrRLSDK 85
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIS----------TLKPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 ENRQalrDVCMVFQQFNLWPHmTVLDNVATPLRRVKKVSREAAYAEaktQLARVGLADKADSWP-AMLSGGQQQRVAIAR 164
Cdd:PRK10247 78 IYRQ---QVSYCAQTPTLFGD-TVYDNLIFPWQIRNQQPDPAIFLD---DLERFALPDTILTKNiAELSGGEKQRISLIR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490220552 165 ALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLA-DDGMTMMIVTHE 210
Cdd:PRK10247 151 NLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTHD 197
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-231 |
1.55e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.84 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 2 RDYAIEINNLNKHygENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVG-YEPLGGEKRR 80
Cdd:PRK09700 262 HETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 RLSDKENRqalRDVcmvfqqfNLWPHMTVLDNVATpLRRVKKV-----------SREAAYAEAKTQLarvgLADKADSWP 149
Cdd:PRK09700 340 MAYITESR---RDN-------GFFPNFSIAQNMAI-SRSLKDGgykgamglfheVDEQRTAENQREL----LALKCHSVN 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 150 ---AMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLAD 226
Cdd:PRK09700 405 qniTELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCE 484
|
....*
gi 490220552 227 GCIEE 231
Cdd:PRK09700 485 GRLTQ 489
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-227 |
2.43e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.07 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 25 DVSIS--PGEVICVIGGSGSGKSTLLRCINFLEDYSS--GSIVVNGENVGYeplggekrRRLSDKENRqalrDVCMVFQQ 100
Cdd:NF040905 19 DVNLSvrEGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRF--------KDIRDSEAL----GIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 101 FNLWPHMTVLDNVATPLRRVKK--VSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEP 178
Cdd:NF040905 87 LALIPYLSIAENIFLGNERAKRgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490220552 179 TSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:NF040905 167 TAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
16-239 |
3.31e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.43 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 16 GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYsSGSIVVNGENVGYEPLGGEKRRRlsdkenrqalrdvC 95
Cdd:COG4138 7 AVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHR-------------A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 96 MVFQQFNLWPHMTVLDNVATPLRRvkkVSREAAYAEAKTQLA-RVGLADKAdSWPAM-LSGGQQQRVAIARAL-----TM 168
Cdd:COG4138 73 YLSQQQSPPFAMPVFQYLALHQPA---GASSEAVEQLLAQLAeALGLEDKL-SRPLTqLSGGEWQRVRLAAVLlqvwpTI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490220552 169 KP--AIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLF 239
Cdd:COG4138 149 NPegQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-209 |
4.13e-18 |
|
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: 79.12 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVL-RGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVvngenvgyeplggekrrrlsd 84
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 kenRQALRDVCMVFQQfnlwPHMTV--LdnvatplrrvkkvsREA-AYAeaktqlarvgladkadsWPAMLSGGQQQRVA 161
Cdd:cd03223 60 ---MPEGEDLLFLPQR----PYLPLgtL--------------REQlIYP-----------------WDDVLSGGEQQRLA 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490220552 162 IARALTMKPAIMLFDEPTSALDPELVGEVLKVIRnlaDDGMTMMIVTH 209
Cdd:cd03223 102 FARLLLHKPKFVFLDEATSALDEESEDRLYQLLK---ELGITVISVGH 146
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-229 |
4.21e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 82.06 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHY-------G--------------ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIV 63
Cdd:COG4586 1 IIEVENLSKTYrvyekepGlkgalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 64 VNgenvGYEPLggEKRRRLsdkenrqaLRDVCMVFQQFN-LWPHMTVLDNVATpLRRVKKVSrEAAYAEAKTQLARV-GL 141
Cdd:COG4586 81 VL----GYVPF--KRRKEF--------ARRIGVVFGQRSqLWWDLPAIDSFRL-LKAIYRIP-DAEYKKRLDELVELlDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 142 ADKADSwPA-MLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHEMGFAAKVSD 219
Cdd:COG4586 145 GELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCD 223
|
250
....*....|
gi 490220552 220 RVLFLADGCI 229
Cdd:COG4586 224 RVIVIDHGRI 233
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-209 |
4.90e-18 |
|
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: 79.71 E-value: 4.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 16 GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrrlsdkENRQALRDVC 95
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA---------------EQRDEPHENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 96 MVFQQFN-LWPHMTVLDNvatpLRRVKKVSREAAYAeAKTQLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPAIML 174
Cdd:TIGR01189 76 LYLGHLPgLKPELSALEN----LHFWAAIHGGAQRT-IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190
....*....|....*....|....*....|....*
gi 490220552 175 FDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTH 209
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-237 |
6.56e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.36 E-value: 6.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 27 SISPGEVICVIGGSGSGKSTLLRCINFLEDYsSGSIVVNGENVGYEPLGGEKRRR--LSDKENRQALRDvcmVFQQFNLw 104
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRayLSQQQTPPFAMP---VFQYLTL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 105 pHMTVLDNVATPLRRVKKVSReaayaeaktqlaRVGLADKADSWPAMLSGGQQQRVAIARA-LTMKPAI------MLFDE 177
Cdd:PRK03695 93 -HQPDKTRTEAVASALNEVAE------------ALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 178 PTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQ 237
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-219 |
1.07e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.31 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHYGENHV-LRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekr 79
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTaLRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 80 rrlsdkenRQALRD--VCMVFQQFNL-WPHMTVLDNVATP--------LRRVKKVSREAAYAeaktQLARVGLADKADSW 148
Cdd:PRK15056 72 --------RQALQKnlVAYVPQSEEVdWSFPVLVEDVVMMgryghmgwLRRAKKRDRQIVTA----ALARVDMVEFRHRQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490220552 149 PAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSD 219
Cdd:PRK15056 140 IGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD 210
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-227 |
6.77e-17 |
|
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: 79.87 E-value: 6.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 3 DYAIEINNLNKHYGEN-HVLRGIDVSIS--PGEVICVIGGSGSGKSTLLRCI-NFLEDYSSGSIVVNGenvgyeplggek 78
Cdd:TIGR02633 255 DVILEARNLTCWDVINpHRKRVDDVSFSlrRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFING------------ 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 79 rRRLSDKENRQALR-DVCMV---FQQFNLWPHMTVLDNVA-TPLRRVKKVSREAAYAEAKTQLARVGLADKADSWP---- 149
Cdd:TIGR02633 323 -KPVDIRNPAQAIRaGIAMVpedRKRHGIVPILGVGKNITlSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpi 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490220552 150 AMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-229 |
1.07e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.30 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 7 EINNLN-KHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyePLGGEKRRRL--- 82
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDIT--GLSPRERRRLgva 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 83 ---SDKeNRQALrdvcmVfqqfnlwPHMTVLDNVA------TPLRRVKKVSREAAYAEAKTQLAR-----VGLADKADSw 148
Cdd:COG3845 337 yipEDR-LGRGL-----V-------PDMSVAENLIlgryrrPPFSRGGFLDRKAIRAFAEELIEEfdvrtPGPDTPARS- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 149 pamLSGGQQQRVAIARALTMKPAIMLFDEPTSALDpelVG---EVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLA 225
Cdd:COG3845 403 ---LSGGNQQKVILARELSRDPKLLIAAQPTRGLD---VGaieFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMY 476
|
....
gi 490220552 226 DGCI 229
Cdd:COG3845 477 EGRI 480
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-227 |
1.49e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.82 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 7 EINNLNKHYGEN-HVLRGIDVSIS--PGEVICVIGGSGSGKSTLLRCInF--LEDYSSGSIVVNGenvgyeplggekrRR 81
Cdd:PRK13549 261 EVRNLTAWDPVNpHIKRVDDVSFSlrRGEILGIAGLVGAGRTELVQCL-FgaYPGRWEGEIFIDG-------------KP 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 82 LSDKENRQALRD-VCMVFQ---QFNLWPHMTVLDNVATP-LRRVKKVSREAAYAEAKT---QLARvgLADKADSwP---- 149
Cdd:PRK13549 327 VKIRNPQQAIAQgIAMVPEdrkRDGIVPVMGVGKNITLAaLDRFTGGSRIDDAAELKTileSIQR--LKVKTAS-Pelai 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 150 AMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDpelVG---EVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLAD 226
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHE 480
|
.
gi 490220552 227 G 227
Cdd:PRK13549 481 G 481
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
21-227 |
3.67e-16 |
|
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: 74.99 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 21 LRGIDVSISPGEVICVIGGSGSGKSTLLRCI-NFLEDYSS--GSIVVNGENvgyeplggekrrrlSDKENRQALRDVCMV 97
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNVSveGDIHYNGIP--------------YKEFAEKYPGEIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 98 FQQFNLWPHMTVldnvatplrrvkkvsREAAYAEAKTQlarvgladkADSWPAMLSGGQQQRVAIARALTMKPAIMLFDE 177
Cdd:cd03233 89 SEEDVHFPTLTV---------------RETLDFALRCK---------GNEFVRGISGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490220552 178 PTSALDPELVGEVLKVIRNLADD-GMT-MMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:cd03233 145 STRGLDSSTALEILKCIRTMADVlKTTtFVSLYQASDEIYDLFDKVLVLYEG 196
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-209 |
4.16e-16 |
|
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: 74.84 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGenvgyeplggekrrrlsdk 85
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 enrQALRDVCMVFQQFNLW-PHMTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIAR 164
Cdd:cd03231 62 ---GPLDFQRDSIARGLLYlGHAPGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALAR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490220552 165 ALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTH 209
Cdd:cd03231 139 LLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
5-242 |
4.19e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 77.83 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGEnvgyePLggeKRRRLSD 84
Cdd:PRK10789 315 DVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI-----PL---TKLQLDS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 KENRQAlrdvcmVFQQFNLWPHMTVLDNVAtplrrvkkVSREAAYAEAKTQLARV------------GLADKADSWPAML 152
Cdd:PRK10789 387 WRSRLA------VVSQTPFLFSDTVANNIA--------LGRPDATQQEIEHVARLasvhddilrlpqGYDTEVGERGVML 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 153 SGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLAdDGMTMMIVTHEMGfAAKVSDRVLFLADGCIEEQ 232
Cdd:PRK10789 453 SGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLS-ALTEASEILVMQHGHIAQR 530
|
250
....*....|
gi 490220552 233 GAPAQLFHQP 242
Cdd:PRK10789 531 GNHDQLAQQS 540
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
2-245 |
8.00e-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: 8.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 2 RDYAIEINNLNkhyGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCI-NFLEDyssgSIVVNGENVGyepLGGEKRR 80
Cdd:COG4170 7 RNLTIEIDTPQ---GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcGITKD----NWHVTADRFR---WNGIDLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 RLSDKENRQAL-RDVCMVFQ--QFNLWPHMTVLDNV--ATPLRRVKKV---SREAAYAEAKTQLARVGLADKAD---SWP 149
Cdd:COG4170 77 KLSPRERRKIIgREIAMIFQepSSCLDPSAKIGDQLieAIPSWTFKGKwwqRFKWRKKRAIELLHRVGIKDHKDimnSYP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 150 AMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLAD-DGMTMMIVTHEMGFAAKVSDRVLFLADGC 228
Cdd:COG4170 157 HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQ 236
|
250
....*....|....*..
gi 490220552 229 IEEQGAPAQLFHQPKSP 245
Cdd:COG4170 237 TVESGPTEQILKSPHHP 253
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-222 |
1.10e-15 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 74.37 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 27 SISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPlggekrrrlsdkenrqalrdvcmvfQQFNLWPH 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP-------------------------QYIKADYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 107 MTVLDNVAtplrrvKKVSREAAYAEAKTQLAR-VGLADKADSWPAMLSGGQQQRVAIARALTmKPA-IMLFDEPTSALDP 184
Cdd:cd03237 76 GTVRDLLS------SITKDFYTHPYFKTEIAKpLQIEQILDREVPELSGGELQRVAIAACLS-KDAdIYLLDEPSAYLDV 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 490220552 185 ELVGEVLKVIRNLADDG-MTMMIVTHEMGFAAKVSDRVL 222
Cdd:cd03237 149 EQRLMASKVIRRFAENNeKTAFVVEHDIIMIDYLADRLI 187
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-209 |
1.22e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 76.31 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHYGEN-HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVV-NGENVGYEPlggek 78
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKVGYLP----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 79 rrrlsdkenrqalrdvcmvfQQFNLWPHMTVLDNVATPLRRVKKVSRE-----AAYAEAKTQ----LARVG-LADK---A 145
Cdd:PRK11819 77 --------------------QEPQLDPEKTVRENVEEGVAEVKAALDRfneiyAAYAEPDADfdalAAEQGeLQEIidaA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 146 DSWP-------AM--------------LSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVG--EvlkviRNLADDGM 202
Cdd:PRK11819 137 DAWDldsqleiAMdalrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAwlE-----QFLHDYPG 211
|
....*..
gi 490220552 203 TMMIVTH 209
Cdd:PRK11819 212 TVVAVTH 218
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-241 |
5.46e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.37 E-value: 5.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENH-VLRGIDVSISPGEVICVIGGSGSGKSTLlrcINFLEDY---SSGSIVVNGEnvgyePLGgekrr 80
Cdd:PRK10790 340 RIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTL---ASLLMGYyplTEGEIRLDGR-----PLS----- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 RLSdkenRQALRD-VCMVfQQFNLWPHMTVLDNVAtpLRRvkKVSREAAYAeaktQLARVGLADKADSWPA--------- 150
Cdd:PRK10790 407 SLS----HSVLRQgVAMV-QQDPVVLADTFLANVT--LGR--DISEEQVWQ----ALETVQLAELARSLPDglytplgeq 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 151 --MLSGGQQQRVAIARALTMKPAIMLFDEPTSALDP---ELVGEVLKVIRnladDGMTMMIVTHEMGFAAKvSDRVLFLA 225
Cdd:PRK10790 474 gnNLSVGQKQLLALARVLVQTPQILILDEATANIDSgteQAIQQALAAVR----EHTTLVVIAHRLSTIVE-ADTILVLH 548
|
250
....*....|....*.
gi 490220552 226 DGCIEEQGAPAQLFHQ 241
Cdd:PRK10790 549 RGQAVEQGTHQQLLAA 564
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-222 |
6.68e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.07 E-value: 6.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGEN--HVLRGidvSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNgENVGYEPlggekrrrls 83
Cdd:PRK13409 341 VEYPDLTKKLGDFslEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKP---------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 dkenrQALR-DVCMVFQQFnlwphmtvldnvatpLRRVKKVSREAAYaeaKTQLAR-VGLADKADSWPAMLSGGQQQRVA 161
Cdd:PRK13409 407 -----QYIKpDYDGTVEDL---------------LRSITDDLGSSYY---KSEIIKpLQLERLLDKNVKDLSGGELQRVA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490220552 162 IARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVL 222
Cdd:PRK13409 464 IAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLM 525
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-235 |
1.13e-14 |
|
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: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 15 YGENHVLRgIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrrlsdKENRQALRDV 94
Cdd:TIGR01257 941 SGRPAVDR-LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI---------------ETNLDAVRQS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 95 CMVFQQFN-LWPHMTVLDNVATpLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPAIM 173
Cdd:TIGR01257 1005 LGMCPQHNiLFHHLTVAEHILF-YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490220552 174 LFDEPTSALDP---ELVGEVLKVIRNladdGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAP 235
Cdd:TIGR01257 1084 VLDEPTSGVDPysrRSIWDLLLKYRS----GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-227 |
1.38e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 73.60 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 20 VLRGIDVSISPGEVICVIGGSGSGKSTLLRCinfLEDYSSGSIVVNGEnvgyeplggekrrRLSDKENRQAL--RDVCMV 97
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNV---LAERVTTGVITGGD-------------RLVNGRPLDSSfqRSIGYV 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 98 FQQFNLWPHMTVLDNV--ATPLRRVKKVSREAA--YAEAKTQLarVGLADKADSWPAM----LSGGQQQRVAIARALTMK 169
Cdd:TIGR00956 842 QQQDLHLPTSTVRESLrfSAYLRQPKSVSKSEKmeYVEEVIKL--LEMESYADAVVGVpgegLNVEQRKRLTIGVELVAK 919
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490220552 170 PAIMLF-DEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHE---MGFAAkvSDRVLFLADG 227
Cdd:TIGR00956 920 PKLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsaILFEE--FDRLLLLQKG 979
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
20-224 |
1.55e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 70.65 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 20 VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplGGEKRRRLSDKENRQALRdvcmvfq 99
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT----RGDRSRFMAYLGHLPGLK------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 100 qfnlwPHMTVLDNV----ATPLRRVKKVSREAayaeaktqLARVGLADKADSWPAMLSGGQQQRVAIARaLTMKPA-IML 174
Cdd:PRK13543 95 -----ADLSTLENLhflcGLHGRRAKQMPGSA--------LAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPApLWL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490220552 175 FDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFL 224
Cdd:PRK13543 161 LDEPYANLDLEGITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTL 210
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-239 |
2.26e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.09 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYG---ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRC-INFLEDYSSGSIVVNGeNVGYEP-----LG 75
Cdd:PLN03232 614 AISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVIRG-SVAYVPqvswiFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 76 GEKRRRL---SDKENRQALR--DVCMVFQQFNLWPhmtvldnvatplrrvkkvsreaayAEAKTQLARVGLAdkadswpa 150
Cdd:PLN03232 693 ATVRENIlfgSDFESERYWRaiDVTALQHDLDLLP------------------------GRDLTEIGERGVN-------- 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 151 mLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVsDRVLFLADGCIE 230
Cdd:PLN03232 741 -ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIK 818
|
....*....
gi 490220552 231 EQGAPAQLF 239
Cdd:PLN03232 819 EEGTFAELS 827
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-241 |
4.23e-14 |
|
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: 72.29 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGE--NHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyeplggekrrrls 83
Cdd:TIGR00957 1285 VEFRNYCLRYREdlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA------------- 1351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 dKENRQALRdvcmvfQQFNLWPHMTVLdnVATPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAML----------- 152
Cdd:TIGR00957 1352 -KIGLHDLR------FKITIIPQDPVL--FSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLdhecaeggenl 1422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 153 SGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDgMTMMIVTHEMGFAAKVSdRVLFLADGCIEEQ 232
Cdd:TIGR00957 1423 SVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEF 1500
|
....*....
gi 490220552 233 GAPAQLFHQ 241
Cdd:TIGR00957 1501 GAPSNLLQQ 1509
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
24-253 |
5.87e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 70.60 E-value: 5.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 24 IDVSISPGEVICVIGGSGSGKSTLLRCInfledysSGsivVNGENVgyePLGGEKRR-------RLSDKENRQAL-RDVC 95
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAI-------CG---VTKDNW---RVTADRMRfddidllRLSPRERRKLVgHNVS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 96 MVFQ--QFNLWPHMTVLDNV--ATP--------LRRVKKVSREAAyaeakTQLARVGLADKAD---SWPAMLSGGQQQRV 160
Cdd:PRK15093 93 MIFQepQSCLDPSERVGRQLmqNIPgwtykgrwWQRFGWRKRRAI-----ELLHRVGIKDHKDamrSFPYELTEGECQKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 161 AIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNL-ADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQLF 239
Cdd:PRK15093 168 MIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELV 247
|
250
....*....|....
gi 490220552 240 HQPKSPRLQYFLSS 253
Cdd:PRK15093 248 TTPHHPYTQALIRA 261
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-231 |
1.28e-13 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 70.21 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 24 IDVSISPGEVICVIGGSGSGKSTLLRCINFLedY--SSGSIVVNGENVgyeplggekrrrlsDKENRQALRD-VCMVFQQ 100
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGL--YrpESGEILLDGQPV--------------TADNREAYRQlFSAVFSD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 101 FNLWPHMTVLDNVATPlrrvkkvsreaayAEAKTQLARVGLADKAD------SWPAmLSGGQQQRVA-IARALTMKPaIM 173
Cdd:COG4615 415 FHLFDRLLGLDGEADP-------------ARARELLERLELDHKVSvedgrfSTTD-LSQGQRKRLAlLVALLEDRP-IL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490220552 174 LFDEPTSALDP--------ELVGEvlkvirnLADDGMTMMIVTH-EMGFAakVSDRVLFLADGCIEE 231
Cdd:COG4615 480 VFDEWAADQDPefrrvfytELLPE-------LKARGKTVIAISHdDRYFD--LADRVLKMDYGKLVE 537
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-244 |
1.44e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.58 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 20 VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLgGEKRRRLSdkenrqalrdvcMVFQ 99
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGL-RELRRQFS------------MIPQ 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 100 QFNLWPHmTVLDNVATPLrrvkkvsrEAAYAEAKTQLARVGLADKADSWPA-----MLSG------GQQQRVAIARALTM 168
Cdd:PTZ00243 1392 DPVLFDG-TVRQNVDPFL--------EASSAEVWAALELVGLRERVASESEgidsrVLEGgsnysvGQRQLMCMARALLK 1462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490220552 169 K-PAIMLFDEPTSALDPELVGEVLKVIRNlADDGMTMMIVTHEMGFAAKVsDRVLFLADGCIEEQGAPAQLFHQPKS 244
Cdd:PTZ00243 1463 KgSGFILMDEATANIDPALDRQIQATVMS-AFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQS 1537
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-229 |
1.78e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 25 DVSIS--PGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENV-GYEPLGG---------EKRRR------LSDKE 86
Cdd:PRK10762 270 DVSFTlrKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGlangivyisEDRKRdglvlgMSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 87 NRQ--ALRDVCMVFQQFNlwpH----MTVLD-----NVATPlrrvkkvSREAAyaeaktqlarVGLadkadswpamLSGG 155
Cdd:PRK10762 350 NMSltALRYFSRAGGSLK---HadeqQAVSDfirlfNIKTP-------SMEQA----------IGL----------LSGG 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490220552 156 QQQRVAIARALTMKPAIMLFDEPTSALDpelVG---EVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCI 229
Cdd:PRK10762 400 NQQKVAIARGLMTRPKVLILDEPTRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
5-221 |
1.88e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.81 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNL----NKH----YGEN-HVLRGIDVsISPGEVICVIGGSGSGKSTllrCINFLedysSGSIVVNGENVGYEPLG 75
Cdd:COG1245 65 AISIVNLpeelEEDpvhrYGENgFRLYGLPV-PKKGKVTGILGPNGIGKST---ALKIL----SGELKPNLGDYDEEPSW 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 76 GE--KR----------RRLSDKENRQALRDvcmvfQQFNLWPHmtVLD-NVATPLRRV--KKVSREaaYAEaktqlaRVG 140
Cdd:COG1245 137 DEvlKRfrgtelqdyfKKLANGEIKVAHKP-----QYVDLIPK--VFKgTVRELLEKVdeRGKLDE--LAE------KLG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 141 LADKADSWPAMLSGGQQQRVAIARALtMKPA-IMLFDEPTSALDpelVGE---VLKVIRNLADDGMTMMIVTHEMGFAAK 216
Cdd:COG1245 202 LENILDRDISELSGGELQRVAIAAAL-LRDAdFYFFDEPSSYLD---IYQrlnVARLIRELAEEGKYVLVVEHDLAILDY 277
|
....*
gi 490220552 217 VSDRV 221
Cdd:COG1245 278 LADYV 282
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-233 |
2.46e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.77 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHY---GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRC-INFLEDYSSGSIVVNGeNVGYEPlggekrr 80
Cdd:PLN03130 614 AISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAmLGELPPRSDASVVIRG-TVAYVP------- 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 rlsdkenrqalrDVCMVFqqfnlwpHMTVLDNV--ATPLRRVKkvsreaaYAEAktqLARVGLADKADSWPA-------- 150
Cdd:PLN03130 686 ------------QVSWIF-------NATVRDNIlfGSPFDPER-------YERA---IDVTALQHDLDLLPGgdlteige 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 151 ---MLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVL-KVIRNlADDGMTMMIVTHEMGFAAKVsDRVLFLAD 226
Cdd:PLN03130 737 rgvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdKCIKD-ELRGKTRVLVTNQLHFLSQV-DRIILVHE 814
|
....*..
gi 490220552 227 GCIEEQG 233
Cdd:PLN03130 815 GMIKEEG 821
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-239 |
4.82e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.82 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 4 YAIEINNLNKHY--GENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGeNVGYEPlggekrrr 81
Cdd:TIGR00957 635 NSITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYVP-------- 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 82 lsdkenRQA------LRDVCMVFQQFNLWPHMTVLDNVATplrrvkKVSREAAYAEAKTQLARVGLAdkadswpamLSGG 155
Cdd:TIGR00957 706 ------QQAwiqndsLRENILFGKALNEKYYQQVLEACAL------LPDLEILPSGDRTEIGEKGVN---------LSGG 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 156 QQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIrnLADDGM----TMMIVTHEMGFAAKVsDRVLFLADGCIEE 231
Cdd:TIGR00957 765 QKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHV--IGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISE 841
|
....*...
gi 490220552 232 QGAPAQLF 239
Cdd:TIGR00957 842 MGSYQELL 849
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-251 |
5.35e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.60 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 20 VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSivVNGEnVGYEPLGGEKRRRlsdkenrQALRDVCMVFQ 99
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIG--VEGV-ITYDGITPEEIKK-------HYRGDVVYNAE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 100 QFNLWPHMTV---LDNVA---TPLRRVKKVSREAaYAEAKTQL--ARVGLADKADS-----WPAMLSGGQQQRVAIARAL 166
Cdd:TIGR00956 146 TDVHFPHLTVgetLDFAArckTPQNRPDGVSREE-YAKHIADVymATYGLSHTRNTkvgndFVRGVSGGERKRVSIAEAS 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 167 TMKPAIMLFDEPTSALDPELVGEVLKVIR---NLADDGMTMMIVTHEMGfAAKVSDRVLFLADGcieeqgapAQLFHQPK 243
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDSATALEFIRALKtsaNILDTTPLVAIYQCSQD-AYELFDKVIVLYEG--------YQIYFGPA 295
|
....*...
gi 490220552 244 SPRLQYFL 251
Cdd:TIGR00956 296 DKAKQYFE 303
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-209 |
6.18e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.59 E-value: 6.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 1 MRDYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYS--SGSIVVNGENVGY-EPlggE 77
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDlEP---E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 78 KRRRL------------SDKENRQALRDVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSREAAYaeaktqLAR---VGla 142
Cdd:CHL00131 80 ERAHLgiflafqypieiPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSF------LSRnvnEG-- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490220552 143 dkadswpamLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTH 209
Cdd:CHL00131 152 ---------FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-211 |
6.43e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.52 E-value: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGEN---HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGE--------------- 67
Cdd:PTZ00265 383 IQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrski 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 68 ----------------NVGY--------EPLGGEKRRRLSDKENRQALRDVCMVFQQFNLWPHMTVLDnvATPLRRVKKV 123
Cdd:PTZ00265 463 gvvsqdpllfsnsiknNIKYslyslkdlEALSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTTD--SNELIEMRKN 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 124 SREAAYAEAKTQLARVGLADKADSWP-----------AMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLK 192
Cdd:PTZ00265 541 YQTIKDSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
250 260
....*....|....*....|
gi 490220552 193 VIRNL-ADDGMTMMIVTHEM 211
Cdd:PTZ00265 621 TINNLkGNENRITIIIAHRL 640
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-209 |
8.84e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.35 E-value: 8.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDY--SSGSIVVNGENVgyeplggekrRRLS 83
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDL----------LELS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DKEnrQALRDVCMVFQQFNLWPHMTVLDNVATPLRRVKKVSREAA--------YAEAKTQLARVGLADKADSWPAMLSGG 155
Cdd:PRK09580 72 PED--RAGEGIFMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQEPldrfdfqdLMEEKIALLKMPEDLLTRSVNVGFSGG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490220552 156 QQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTH 209
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-185 |
9.13e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.65 E-value: 9.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 3 DYAIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVnGENV--GYEplggekrr 80
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVklAYV-------- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 81 rlsdKENRQALRDVCMVFQQFNLWPHMTVLDNVATPLRrvkkvsreaAYAEA-----KTQLARVGladkadswpaMLSGG 155
Cdd:TIGR03719 391 ----DQSRDALDPNKTVWEEISGGLDIIKLGKREIPSR---------AYVGRfnfkgSDQQKKVG----------QLSGG 447
|
170 180 190
....*....|....*....|....*....|
gi 490220552 156 QQQRVAIARALTMKPAIMLFDEPTSALDPE 185
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-227 |
1.05e-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: 65.82 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 21 LRGIDVSISPGEVICVIGGSGSGKSTLLRCInfLEDYSSGSIVVNGENVGYEPLGGEKrrrlSDKENRQAlrdVCMVFQQ 100
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQTLEGKVHWSNKNESEPSFEA----TRSRNRYS---VAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 101 FNLWpHMTVLDNV--ATPLRRVK-KVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDE 177
Cdd:cd03290 88 PWLL-NATVEENItfGSPFNKQRyKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490220552 178 PTSALDPELVGEVLK--VIRNLADDGMTMMIVTHEMGFAAKvSDRVLFLADG 227
Cdd:cd03290 167 PFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-227 |
1.32e-12 |
|
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: 64.27 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 19 HVLRGIDVSIsPGEVICVIGG-SGSGKSTLLrcinfledyssgsivvngenvgYEPLGGEKRRRLSDKENRQALRDVCMV 97
Cdd:cd03238 9 HNLQNLDVSI-PLNVLVVVTGvSGSGKSTLV----------------------NEGLYASGKARLISFLPKFSRNKLIFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 98 FQqfnlwphmtvldnvatpLRRVKKVSreaayaeaktqLARVGLADKADSwpamLSGGQQQRVAIARAL--TMKPAIMLF 175
Cdd:cd03238 66 DQ-----------------LQFLIDVG-----------LGYLTLGQKLST----LSGGELQRVKLASELfsEPPGTLFIL 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490220552 176 DEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFaAKVSDRVLFLADG 227
Cdd:cd03238 114 DEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDV-LSSADWIIDFGPG 164
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-242 |
2.00e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.11 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 20 VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVvngenvgyeplggekrrrlsdkenrqALRDVCMVFQ 99
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--------------------------AERSIAYVPQ 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 100 QfnLW-PHMTVLDNV-------ATPLRRVKKVSReaayAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPA 171
Cdd:PTZ00243 729 Q--AWiMNATVRGNIlffdeedAARLADAVRVSQ----LEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRD 802
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490220552 172 IMLFDEPTSALDPElVGEvlKVIRNL---ADDGMTMMIVTHEMGFAAKvSDRVLFLADGCIEEQGAPAQLFHQP 242
Cdd:PTZ00243 803 VYLLDDPLSALDAH-VGE--RVVEECflgALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-238 |
2.44e-12 |
|
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: 66.96 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 26 VSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrrlsdkenrqaLRDVCMVFQQFNLWP 105
Cdd:TIGR01257 1960 VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI---------------------LTNISDVHQNMGYCP 2018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 106 HMTVLDNVATPLR------RVKKVSREAAYAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEPT 179
Cdd:TIGR01257 2019 QFDAIDDLLTGREhlylyaRLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490220552 180 SALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEEQGAPAQL 238
Cdd:TIGR01257 2099 TGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-241 |
2.63e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.69 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 3 DYAIEINNLNKHYGE----NHVlrgiDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyEPLGGEK 78
Cdd:NF033858 264 EPAIEARGLTMRFGDftavDHV----SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV--DAGDIAT 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 79 RRRlsdkenrqalrdVCMVFQQFNLWPHMTVLDNVATPLR--RVKKVSREAAYAEAktqLARVGLADKADSWPAMLSGGQ 156
Cdd:NF033858 338 RRR------------VGYMSQAFSLYGELTVRQNLELHARlfHLPAAEIAARVAEM---LERFDLADVADALPDSLPLGI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 157 QQRVAIARALTMKPAIMLFDEPTSALDP-------ELVGEvlkvirnLA-DDGMTMMIVTHEMGFAAKVsDRVLFLADGC 228
Cdd:NF033858 403 RQRLSLAVAVIHKPELLILDEPTSGVDPvardmfwRLLIE-------LSrEDGVTIFISTHFMNEAERC-DRISLMHAGR 474
|
250
....*....|...
gi 490220552 229 IEEQGAPAQLFHQ 241
Cdd:NF033858 475 VLASDTPAALVAA 487
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-231 |
3.27e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.15 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRG-IDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrrlsD 84
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV--------------T 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 KENRQALRD-VCMVFQQFNLWPHMtvldnvatplrrVKKVSREAAYAEAKTQLARVGLADKA--DSWPAM---LSGGQQQ 158
Cdd:PRK10522 389 AEQPEDYRKlFSAVFTDFHLFDQL------------LGPEGKPANPALVEKWLERLKMAHKLelEDGRISnlkLSKGQKK 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490220552 159 RVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRN-LADDGMTMMIVTHEMGFAAKvSDRVLFLADGCIEE 231
Cdd:PRK10522 457 RLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPlLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-227 |
8.44e-12 |
|
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: 62.65 E-value: 8.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 21 LRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYS--SGSIVVNGEnvgyePLGGEKRRRlsdkenrqalrdVCMVF 98
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGR-----PLDKNFQRS------------TGYVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 99 QQFNLWPHMTVldnvatplrrvkkvsREAAYAEAKTQlarvgladkadswpaMLSGGQQQRVAIARALTMKPAIMLFDEP 178
Cdd:cd03232 86 QQDVHSPNLTV---------------REALRFSALLR---------------GLSVEQRKRLTIGVELAAKPSILFLDEP 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490220552 179 TSALDPELVGEVLKVIRNLADDGMTMMIVTH-------EMgFaakvsDRVLFLADG 227
Cdd:cd03232 136 TSGLDSQAAYNIVRFLKKLADSGQAILCTIHqpsasifEK-F-----DRLLLLKRG 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-227 |
8.68e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.69 E-value: 8.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 22 RGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLGGEKRRRLSD-KENRQA--------LR 92
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYlPEDRQSsglyldapLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 93 -DVC-MVFQQFNLWphmtvldnvatpLRRvkkvSREAAYAEAKTQLARVGLADkADSWPAMLSGGQQQRVAIARALTMKP 170
Cdd:PRK15439 360 wNVCaLTHNRRGFW------------IKP----ARENAVLERYRRALNIKFNH-AEQAARTLSGGNQQKVLIAKCLEASP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490220552 171 AIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:PRK15439 423 QLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-224 |
1.21e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.21 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGE-NVGYEPlggekrrrlsd 84
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlRIGYVP----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 kenrqalrdvcmvfQQFNLWPHMTVLDNVATPLR-RVKKvsreaayAEAKTQLARVGLADKADSWPAMLSGGQQQRVAIA 163
Cdd:PRK09544 74 --------------QKLYLDTTLPLTVNRFLRLRpGTKK-------EDILPALKRVQAGHLIDAPMQKLSGGETQRVLLA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490220552 164 RALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVLFL 224
Cdd:PRK09544 133 RALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
87-222 |
2.99e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.51 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 87 NRQALRDVCMVFQQFNLWPHMTVLDNV------ATpLRRVKKVSREAAYAEAKTQL-----ARVGLADKAdswpamLSGG 155
Cdd:PTZ00265 1290 NLKDLRNLFSIVSQEPMLFNMSIYENIkfgkedAT-REDVKRACKFAAIDEFIESLpnkydTNVGPYGKS------LSGG 1362
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 156 QQQRVAIARALTMKPAIMLFDEPTSALDP---ELVGEVLKVIRNLADDgmTMMIVTHEMGfAAKVSDRVL 222
Cdd:PTZ00265 1363 QKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKADK--TIITIAHRIA-SIKRSDKIV 1429
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-222 |
3.33e-11 |
|
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: 63.26 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGEN--HVLRGidvSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNgENVGYEPlggekrrrls 83
Cdd:COG1245 342 VEYPDLTKSYGGFslEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISYKP---------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 dkenrQALR-DVCMVFQQFnlwphmtvldnvatpLRRVKKVSREAAYAeaKTQLAR-VGLADKADSWPAMLSGGQQQRVA 161
Cdd:COG1245 408 -----QYISpDYDGTVEEF---------------LRSANTDDFGSSYY--KTEIIKpLGLEKLLDKNVKDLSGGELQRVA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490220552 162 IARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADD-GMTMMIVTHEMGFAAKVSDRVL 222
Cdd:COG1245 466 IAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLM 527
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-244 |
4.54e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 20 VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLGgEKRRRLSDKENRQALRDVCMvfq 99
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLT-DLRRVLSIIPQSPVLFSGTV--- 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 100 QFNLWPHMTVLD-NVATPLRR--VKKVSREAAYaeaktqlarvGLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFD 176
Cdd:PLN03232 1327 RFNIDPFSEHNDaDLWEALERahIKDVIDRNPF----------GLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490220552 177 EPTSALDPELVGEVLKVIRNlADDGMTMMIVTHEMGFAAKVsDRVLFLADGCIEEQGAPAQLFHQPKS 244
Cdd:PLN03232 1397 EATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSRDTS 1462
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
6-245 |
8.30e-11 |
|
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: 60.69 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGEN--HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLgGEKRRRLS 83
Cdd:cd03288 20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPL-HTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 dkenrQALRDVcMVFQ---QFNLWPHMTVLDNvatplrrvkKVSREAAYAEAKTQLARV--GLADKADSWPAMLSGGQQQ 158
Cdd:cd03288 99 -----IILQDP-ILFSgsiRFNLDPECKCTDD---------RLWEALEIAQLKNMVKSLpgGLDAVVTEGGENFSVGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 159 RVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDgMTMMIVTHEMGFAAKvSDRVLFLADGCIEEQGAPAQL 238
Cdd:cd03288 164 LFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENL 241
|
....*..
gi 490220552 239 FHQPKSP 245
Cdd:cd03288 242 LAQEDGV 248
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
5-211 |
1.88e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNK-------H-YGEN-HVLRGIDVsISPGEVICVIGGSGSGKSTLLRCInfledysSGSIVVNGENVGYEPLG 75
Cdd:PRK13409 65 AISIVNLPEeleeepvHrYGVNgFKLYGLPI-PKEGKVTGILGPNGIGKTTAVKIL-------SGELIPNLGDYEEEPSW 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 76 GE--KR----------RRLSDKENRQALRDvcmvfQQFNLWPhMTVLDNVATPLRRV--KKVSREaaYAEaktqlaRVGL 141
Cdd:PRK13409 137 DEvlKRfrgtelqnyfKKLYNGEIKVVHKP-----QYVDLIP-KVFKGKVRELLKKVdeRGKLDE--VVE------RLGL 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490220552 142 ADKADSWPAMLSGGQQQRVAIARALtMKPA-IMLFDEPTSALDpelVGE---VLKVIRNLAdDGMTMMIVTHEM 211
Cdd:PRK13409 203 ENILDRDISELSGGELQRVAIAAAL-LRDAdFYFFDEPTSYLD---IRQrlnVARLIRELA-EGKYVLVVEHDL 271
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
143-246 |
2.35e-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: 58.35 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 143 DKADSWPAM----------LSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGM-TMMIVTHEM 211
Cdd:cd03222 53 GDNDEWDGItpvykpqyidLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDL 132
|
90 100 110
....*....|....*....|....*....|....*
gi 490220552 212 GFAAKVSDRVLfladgCIEEQGAPAQLFHQPKSPR 246
Cdd:cd03222 133 AVLDYLSDRIH-----VFEGEPGVYGIASQPKGTR 162
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-202 |
2.82e-10 |
|
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: 57.38 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 30 PGEVICVIGGSGSGKSTLLRCI-NFLEDYSSGSIVVNGENvgyeplggekrrrlsdkenrqalrdvcmvfqqfnlwphmt 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGED---------------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 109 vldnvatplrrvkkvsreaayaeAKTQLARVGLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVG 188
Cdd:smart00382 41 -----------------------ILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEA 97
|
170
....*....|....
gi 490220552 189 EVLKVIRNLADDGM 202
Cdd:smart00382 98 LLLLLEELRLLLLL 111
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-185 |
2.98e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.13 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVnGENVgyeplggekrrRLS-- 83
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-----------KLAyv 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DkENRQALRDVCMVFQQFNLWPHMTVLDNVATPlrrvkkvSReaAYAEA-----KTQLARVGladkadswpaMLSGGQQQ 158
Cdd:PRK11819 393 D-QSRDALDPNKTVWEEISGGLDIIKVGNREIP-------SR--AYVGRfnfkgGDQQKKVG----------VLSGGERN 452
|
170 180
....*....|....*....|....*..
gi 490220552 159 RVAIARALTMKPAIMLFDEPTSALDPE 185
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
15-246 |
3.14e-10 |
|
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: 58.92 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 15 YGENH-VLRGIDVsISPGEVICVIGGSGSGKSTLLRCInfledysSGSIVVNGENVGYEP---------LGGEKRRRLSD 84
Cdd:cd03236 10 YGPNSfKLHRLPV-PREGQVLGLVGPNGIGKSTALKIL-------AGKLKPNLGKFDDPPdwdeildefRGSELQNYFTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 85 KENRQAlrDVCMVFQQFNLWPHmTVLDNVATPLrrvKKVSREAAYAEAKTQLARVGLADKADSwpaMLSGGQQQRVAIAR 164
Cdd:cd03236 82 LLEGDV--KVIVKPQYVDLIPK-AVKGKVGELL---KKKDERGKLDELVDQLELRHVLDRNID---QLSGGELQRVAIAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 165 ALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLadgcieeQGAPAQ--LFHQP 242
Cdd:cd03236 153 ALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL-------YGEPGAygVVTLP 225
|
....
gi 490220552 243 KSPR 246
Cdd:cd03236 226 KSVR 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-229 |
3.37e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.92 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 24 IDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGEnvgyeplggekrrRLSDKENRQALRDVCMVF----Q 99
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK-------------PIDIRSPRDAIRAGIMLCpedrK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 100 QFNLWPHMTVLDNVATPLRR-------VKKVSREAAYAEAKTQLARVGLADkADSWPAMLSGGQQQRVAIARALTMKPAI 172
Cdd:PRK11288 339 AEGIIPVHSVADNINISARRhhlragcLINNRWEAENADRFIRSLNIKTPS-REQLIMNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 173 MLFDEPTSALDpelVG---EVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCI 229
Cdd:PRK11288 418 ILLDEPTRGID---VGakhEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
6-210 |
4.24e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrrlsDK 85
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI--------------KK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 86 ENRQALRDVCMVFQQFNLWPHMTVLDNVATPLrrvkkvsREAAYAEAKTQLARVGLADKADSWP-AMLSGGQQQRVAIAR 164
Cdd:PRK13540 68 DLCTYQKQLCFVGHRSGINPYLTLRENCLYDI-------HFSPGAVGITELCRLFSLEHLIDYPcGLLSSGQKRQVALLR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490220552 165 ALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHE 210
Cdd:PRK13540 141 LWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-233 |
4.50e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCInfLEDYSSGSIVVN-GEN--VGYEPLGGEK--- 78
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL--VGELEPDSGTVKwSENanIGYYAQDHAYdfe 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 79 ---------RRRLSDKENRQALRDVC--MVFQQfnlwphmtvlDNVAtplrrvKKVsreaayaeaktqlaRVgladkads 147
Cdd:PRK15064 397 ndltlfdwmSQWRQEGDDEQAVRGTLgrLLFSQ----------DDIK------KSV--------------KV-------- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 148 wpamLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVgEVLkvirNLADDGM--TMMIVTHEMGFAAKVSDRVL-FL 224
Cdd:PRK15064 439 ----LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESI-ESL----NMALEKYegTLIFVSHDREFVSSLATRIIeIT 509
|
....*....
gi 490220552 225 ADGCIEEQG 233
Cdd:PRK15064 510 PDGVVDFSG 518
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
6-209 |
5.61e-10 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 57.71 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVlrgidvSISPGeVICVIGGSGSGKSTLLRCINFL---EDYSSGSIVVNGENVGYEP--------L 74
Cdd:COG0419 5 LRLENFRSYRDTETI------DFDDG-LNLIVGPNGAGKSTILEAIRYAlygKARSRSKLRSDLINVGSEEasvelefeH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 75 GGEK---RRRLSD-----KENRQALRDvcMVFQQFNLwphmTVLDNVATPLRRVK-KVSREAAYAEAKTQLARVGLADKA 145
Cdd:COG0419 78 GGKRyriERRQGEfaeflEAKPSERKE--ALKRLLGL----EIYEELKERLKELEeALESALEELAELQKLKQEILAQLS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490220552 146 DSWPA-MLSGGQQQRVAIARALTmkpaiMLFDepTSALDPELVGEVLKVIRNLAddgmtmmIVTH 209
Cdd:COG0419 152 GLDPIeTLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-227 |
6.40e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.26 E-value: 6.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLrcinfledyssgSIVVNGENVGYE---PLGGekRRRL 82
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL------------SLITGDHPQGYSndlTLFG--RRRG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 83 SDKENRQALRDVCMVFQQFnlwpHMTVldNVATPLRRV------------KKVSrEAAYAEAKTQLARVGLADK-ADSWP 149
Cdd:PRK10938 327 SGETIWDIKKHIGYVSSSL----HLDY--RVSTSVRNVilsgffdsigiyQAVS-DRQQKLAQQWLDILGIDKRtADAPF 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 150 AMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMI-VTHEMGFAAK-VSDRVLFLADG 227
Cdd:PRK10938 400 HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVSHHAEDAPAcITHRLEFVPDG 479
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-183 |
7.70e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 7.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCIN---FLEDyssGSIVVNGENV------------- 69
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLDD---GRIIYEQDLIvarlqqdpprnve 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 70 ---------GYEPLGGEKRR--RLSDK-------ENRQALRDVCMVFQQFNLWPhmtvLDNvatplrRVKKVsreaayae 131
Cdd:PRK11147 81 gtvydfvaeGIEEQAEYLKRyhDISHLvetdpseKNLNELAKLQEQLDHHNLWQ----LEN------RINEV-------- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490220552 132 aktqLARVGLadKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALD 183
Cdd:PRK11147 143 ----LAQLGL--DPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
19-235 |
8.81e-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: 57.62 E-value: 8.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 19 HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINF--LEDYSSGSIVVNGEN---VGYE-----------PLGGEKR--- 79
Cdd:cd03271 9 NNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYpaLARRLHLKKEQPGNHdriEGLEhidkvividqsPIGRTPRsnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 80 ----------RRL------SDKENRQAL------RDVCMVFQqfnlwphMTVlDNVATPLRRVKKVSReaayaeaKTQ-L 136
Cdd:cd03271 89 atytgvfdeiRELfcevckGKRYNRETLevrykgKSIADVLD-------MTV-EEALEFFENIPKIAR-------KLQtL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 137 ARVGLADKADSWPA-MLSGGQQQRVAIARALTMK---PAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMG 212
Cdd:cd03271 154 CDVGLGYIKLGQPAtTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLD 233
|
250 260
....*....|....*....|....*....
gi 490220552 213 fAAKVSDRVLFL------ADGCIEEQGAP 235
Cdd:cd03271 234 -VIKCADWIIDLgpeggdGGGQVVASGTP 261
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
152-227 |
9.65e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 9.65e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490220552 152 LSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-238 |
1.14e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.60 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 5 AIEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLL------RCINfledysSGSIVVngenvgyepLGGek 78
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKIQ------QGRVEV---------LGG-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 79 rrrlsDKENRQALRDVC-----MvfQQ---FNLWPHMTVLDNV---ATpLRRVKKVSREAAYAEAktqLARVGLADKADS 147
Cdd:NF033858 64 -----DMADARHRRAVCpriayM--PQglgKNLYPTLSVFENLdffGR-LFGQDAAERRRRIDEL---LRATGLAPFADR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 148 wPAM-LSGGQQQRVAIARALTMKPAIMLFDEPTSALDP-------ELVGEvlkvIRNlADDGMTMMIVTHEMGFAAKVsD 219
Cdd:NF033858 133 -PAGkLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPlsrrqfwELIDR----IRA-ERPGMSVLVATAYMEEAERF-D 205
|
250
....*....|....*....
gi 490220552 220 RVLFLADGCIEEQGAPAQL 238
Cdd:NF033858 206 WLVAMDAGRVLATGTPAEL 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-272 |
1.25e-09 |
|
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: 57.56 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGE--NHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCinFLE-DYSSGSIVVNGENVGYEPLggekrrrl 82
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSA--FLRlLNTEGDIQIDGVSWNSVPL-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 83 sdKENRQALRDV---CMVFQ---QFNLWPHMTVLDnvatplRRVKKVSREaayaeaktqlarVGLADKADSWPA------ 150
Cdd:cd03289 73 --QKWRKAFGVIpqkVFIFSgtfRKNLDPYGKWSD------EEIWKVAEE------------VGLKSVIEQFPGqldfvl 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 151 -----MLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNlADDGMTMMIVTHEMGfAAKVSDRVLFLA 225
Cdd:cd03289 133 vdggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIE-AMLECQRFLVIE 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 490220552 226 DGCIEEQGAPAQL------FHQPKSP--RLQYF-LSSWSERQSGARLPETALQESA 272
Cdd:cd03289 211 ENKVRQYDSIQKLlnekshFKQAISPsdRLKLFpRRNSSKSKRKPRPQIQALQEET 266
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
19-215 |
1.72e-09 |
|
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: 55.44 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 19 HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLedyssgsivvngenvgyepLGGEkrrrlsdkenrqalrdvcmvf 98
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLA-------------------LGGA--------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 99 qqfnlwphmtvldNVATPLRRVKKVSREAAYAEAKTQLARVGLadkadswpamlSGGQQQRVAIARAL---TMKPA-IML 174
Cdd:cd03227 49 -------------QSATRRRSGVKAGCIVAAVSAELIFTRLQL-----------SGGEKELSALALILalaSLKPRpLYI 104
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490220552 175 FDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAA 215
Cdd:cd03227 105 LDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAE 145
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-238 |
3.05e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.44 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 20 VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGyePLGgekrrrLSDkenrqaLRDVCMVFQ 99
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS--KFG------LMD------LRKVLGIIP 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 100 Q----------FNLWPHMTVLD-NVATPLRR--VKKVSR------EAAYAEAKTQLarvgladkadswpamlSGGQQQRV 160
Cdd:PLN03130 1320 QapvlfsgtvrFNLDPFNEHNDaDLWESLERahLKDVIRrnslglDAEVSEAGENF----------------SVGQRQLL 1383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490220552 161 AIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNlADDGMTMMIVTHEMGFAAKvSDRVLFLADGCIEEQGAPAQL 238
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE-EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENL 1459
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-272 |
4.11e-09 |
|
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: 57.23 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGE--NHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDySSGSIVVNGenVGYEPLGGEKRRRLS 83
Cdd:TIGR01271 1218 MDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG--VSWNSVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 DkenrqALRDVCMVFQ---QFNLWPHMTVLDnvatplRRVKKVSREaayaeaktqlarVGLADKADSWPA---------- 150
Cdd:TIGR01271 1295 G-----VIPQKVFIFSgtfRKNLDPYEQWSD------EEIWKVAEE------------VGLKSVIEQFPDkldfvlvdgg 1351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 151 -MLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDgMTMMIVTHEMgfAAKVSDRVLFLADGC- 228
Cdd:TIGR01271 1352 yVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN-CTVILSEHRV--EALLECQQFLVIEGSs 1428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 490220552 229 ------IEEQGAPAQLFHQPKSPRLQYFLSSWSERQSGARLPE---TALQESA 272
Cdd:TIGR01271 1429 vkqydsIQKLLNETSLFKQAMSAADRLKLFPLHRRNSSKRKPQpkiTALREEA 1481
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-210 |
5.15e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.78 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 20 VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLED--YSSGSIVVNGEnvgyePLGGEKRRRLSDKENRQALRDvcmv 97
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGF-----PKKQETFARISGYCEQNDIHS---- 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 98 fqqfnlwPHMTVLDNV--ATPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPAM-----LSGGQQQRVAIARALTMKP 170
Cdd:PLN03140 966 -------PQVTVRESLiySAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANP 1038
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490220552 171 AIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHE 210
Cdd:PLN03140 1039 SIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-210 |
2.46e-08 |
|
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: 53.03 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 19 HVLRGIDVSISPGEVICVIGGSGSGKSTLlrcinfledySSGSIVVNGENVGYEPLGGEKRRRLS-----DKENRQALRD 93
Cdd:cd03270 9 HNLKNVDVDIPRNKLVVITGVSGSGKSSL----------AFDTIYAEGQRRYVESLSAYARQFLGqmdkpDVDSIEGLSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 94 VCMVFQQ-FNLWPHMTV------LDNVATPLRRVKKVSREAayaeaktQLARVGLADKADSWPAM-LSGGQQQRVAIARA 165
Cdd:cd03270 79 AIAIDQKtTSRNPRSTVgtvteiYDYLRLLFARVGIRERLG-------FLVDVGLGYLTLSRSAPtLSGGEAQRIRLATQ 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490220552 166 LTMK--PAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHE 210
Cdd:cd03270 152 IGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD 198
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
152-253 |
3.87e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.06 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 152 LSGGQQQRVAIARAL---TMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMgFAAKVSDRVLFLA--- 225
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVADYVLELGpeg 888
|
90 100 110
....*....|....*....|....*....|...
gi 490220552 226 ---DGCIEEQGAPAQLFHQ--PKSPRLQYFLSS 253
Cdd:PRK00635 889 gnlGGYLLASCSPEELIHLhtPTAKALRPYLSS 921
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
136-209 |
1.59e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.06 E-value: 1.59e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490220552 136 LARVGLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGevlKVIRNLADDGMTMMIVTH 209
Cdd:TIGR00954 567 LEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG---YMYRLCREFGITLFSVSH 637
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
152-238 |
1.60e-07 |
|
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: 51.94 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 152 LSGGQQQRVAIARALTMK---PAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGfAAKVSDRVLFL---- 224
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLD-VIKTADYIIDLgpeg 908
|
90
....*....|....*.
gi 490220552 225 --ADGCIEEQGAPAQL 238
Cdd:TIGR00630 909 gdGGGTVVASGTPEEV 924
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
6-224 |
5.72e-07 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 50.00 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLnkhygenhvlRGI-DVSIS-PGEVICVIGGSGSGKSTLLRCINFL-----------EDYSSGS------IVVNG 66
Cdd:COG3593 6 IKIKNF----------RSIkDLSIElSDDLTVLVGENNSGKSSILEALRLLlgpsssrkfdeEDFYLGDdpdlpeIEIEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 67 E------NVGYEPLGGEKRRRLSD--KENRQALRDVcmvFQQFNlwphmTVLDNVATPLRRVKKVSREAAYAEAKTQL-- 136
Cdd:COG3593 76 TfgsllsRLLRLLLKEEDKEELEEalEELNEELKEA---LKALN-----ELLSEYLKELLDGLDLELELSLDELEDLLks 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 137 ARVGLADKADSWPAMLSGGQQQRVAIARALTM-------KPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTH 209
Cdd:COG3593 148 LSLRIEDGKELPLDRLGSGFQRLILLALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
250
....*....|....*.
gi 490220552 210 EMGFAAKVS-DRVLFL 224
Cdd:COG3593 228 SPHLLSEVPlENIRRL 243
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-248 |
8.65e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 8.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 7 EINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCInfLEDY--SSGSIVVNGE-NVGYeplggekrrrls 83
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM--LGQLqaDSGRIHCGTKlEVAY------------ 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 84 dkenrqalrdvcmvFQQF--NLWPHMTVLDNVATPLRRV--KKVSREA-AYAE--------AKTQLarvgladKAdswpa 150
Cdd:PRK11147 387 --------------FDQHraELDPEKTVMDNLAEGKQEVmvNGRPRHVlGYLQdflfhpkrAMTPV-------KA----- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 151 mLSGGQQQRVAIARaLTMKPA-IMLFDEPTSALDPELVgEVLKVIrnLADDGMTMMIVTHEMGFAAK-VSDRVLFLADGC 228
Cdd:PRK11147 441 -LSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETL-ELLEEL--LDSYQGTVLLVSHDRQFVDNtVTECWIFEGNGK 515
|
250 260 270
....*....|....*....|....*....|
gi 490220552 229 IEE----------QGAPAQLFHQPKSPRLQ 248
Cdd:PRK11147 516 IGRyvggyhdarqQQAQYLALKQPAVKKKE 545
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
150-230 |
1.14e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.83 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 150 AMLSGGQQQRVAIARAL--TMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEmgfaakvsDRVLFLADG 227
Cdd:PRK00635 475 ATLSGGEQERTALAKHLgaELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD--------EQMISLADR 546
|
...
gi 490220552 228 CIE 230
Cdd:PRK00635 547 IID 549
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
152-267 |
1.25e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 152 LSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGCIEE 231
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAE 215
|
90 100 110
....*....|....*....|....*....|....*.
gi 490220552 232 QGAPAQLFHQPKSPRLQYflsswSERQSGARLPETA 267
Cdd:PRK10938 216 TGEREEILQQALVAQLAH-----SEQLEGVQLPEPD 246
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
34-227 |
1.85e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 34 ICVIGGSGSGKSTLLRCInfledysSGSIvvngenvgyEPLGGEKRRrlsDKENRQAlrdvcmVFQQFnlwpHMTVLDNV 113
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLI-------SGEL---------QPSSGTVFR---SAKVRMA------VFSQH----HVDGLDLS 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 114 ATPLRRVKKVSREAAYAEAKTQLARVGLADKADSWPA-MLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVgEVLk 192
Cdd:PLN03073 589 SNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAV-EAL- 666
|
170 180 190
....*....|....*....|....*....|....*
gi 490220552 193 vIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADG 227
Cdd:PLN03073 667 -IQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEG 700
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
152-229 |
2.09e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 152 LSGGQQQRVAIARALTMKPAIMLFDEPTSALDpelVG---EVLKVIRNLADDGMTMMIVTHEMGFAAKVSDRVLFLADGC 228
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGR 481
|
.
gi 490220552 229 I 229
Cdd:NF040905 482 I 482
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
7-227 |
2.69e-06 |
|
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: 47.54 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 7 EINNLNKHYGENH------------VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGEnVGYEPl 74
Cdd:cd03291 27 ENNDRKHSSDDNNlffsnlclvgapVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISFSS- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 75 ggekrrrlsdkenrqalrdvcmvfqQFNLWPHMTVLDNVATPLR----RVKKVSRE-------AAYAEA-KTQLARVGLa 142
Cdd:cd03291 105 -------------------------QFSWIMPGTIKENIIFGVSydeyRYKSVVKAcqleediTKFPEKdNTVLGEGGI- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 143 dkadswpaMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLK--VIRNLADDgmTMMIVTHEMGfAAKVSDR 220
Cdd:cd03291 159 --------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEscVCKLMANK--TRILVTSKME-HLKKADK 227
|
....*..
gi 490220552 221 VLFLADG 227
Cdd:cd03291 228 ILILHEG 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-227 |
1.61e-05 |
|
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: 46.06 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 20 VLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGEnVGYEPlggekrrrlsdkenrqalrdvcmvfq 99
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-ISFSP-------------------------- 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 100 QFNLWPHMTVLDNVATPLR----RVKKVSREAAYAEAKTQLArvgladKADSWPAM-----LSGGQQQRVAIARALTMKP 170
Cdd:TIGR01271 494 QTSWIMPGTIKDNIIFGLSydeyRYTSVIKACQLEEDIALFP------EKDKTVLGeggitLSGGQRARISLARAVYKDA 567
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490220552 171 AIMLFDEPTSALDPELVGEVLK--VIRNLADDgmTMMIVTHEMGFAAKvSDRVLFLADG 227
Cdd:TIGR01271 568 DLYLLDSPFTHLDVVTEKEIFEscLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
17-185 |
2.90e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.71 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 17 ENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVgyeplggekrrrlsdkeNRQALRDVCM 96
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNI-----------------NNIAKPYCTY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 97 VFQQFNLWPHMTVLDNvatpLRRVKKVSREAAYAEAKTQLARvgLADKADSWPAMLSGGQQQRVAIARALTMKPAIMLFD 176
Cdd:PRK13541 75 IGHNLGLKLEMTVFEN----LKFWSEIYNSAETLYAAIHYFK--LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLD 148
|
....*....
gi 490220552 177 EPTSALDPE 185
Cdd:PRK13541 149 EVETNLSKE 157
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-224 |
4.38e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 6 IEINNLNKHYGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRcinFLEDYSSGSIVVNGENVGYE-PLGGEKRRRL-- 82
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLR---YMAMHAIDGIPKNCQILHVEqEVVGDDTTALqc 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 83 ---SDKENRQALRDVCMVFQQFNLWPHMTVLDNVATPL-----------------RRVKKVSREAAYAEAKTQLArvGLA 142
Cdd:PLN03073 255 vlnTDIERTQLLEEEAQLVAQQRELEFETETGKGKGANkdgvdkdavsqrleeiyKRLELIDAYTAEARAASILA--GLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 143 DKAD---SWPAMLSGGQQQRVAIARALTMKPAIMLFDEPTSALDpelVGEVLKVIRNLADDGMTMMIVTHEMGFAAKVSD 219
Cdd:PLN03073 333 FTPEmqvKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTVVT 409
|
....*
gi 490220552 220 RVLFL 224
Cdd:PLN03073 410 DILHL 414
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
15-183 |
4.43e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 15 YGENHVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSI-VVNGENVGYeplggekrrrlsdkenrqalrd 93
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGY---------------------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 94 vcmvFQQFNLwphmTVLDNVATPLRRVKKVSREAAYAEAKTQLARVGL-ADKADSWPAMLSGGQQQRVAIARALTMKPAI 172
Cdd:PRK10636 380 ----FAQHQL----EFLRADESPLQHLARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNL 451
|
170
....*....|.
gi 490220552 173 MLFDEPTSALD 183
Cdd:PRK10636 452 LLLDEPTNHLD 462
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
160-209 |
1.08e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.76 E-value: 1.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 490220552 160 VAIARALtMKPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTH 209
Cdd:pfam13304 249 AALLSAL-PKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
152-211 |
1.60e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 1.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490220552 152 LSGGQQQRVAIARALTmKPA----IMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTHEM 211
Cdd:COG0178 827 LSGGEAQRVKLASELS-KRStgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNL 889
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
21-48 |
2.01e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 2.01e-04
10 20
....*....|....*....|....*...
gi 490220552 21 LRGIDVSISPGEVICVIGGSGSGKSTLL 48
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
148-210 |
2.45e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.05 E-value: 2.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490220552 148 WPAM-----LSGGQQQ------RVAIARALTMKPAIMLFDEPTSALDPELVGEVL-KVIRN-LADDGMTMMIVTHE 210
Cdd:cd03240 107 WPLLdmrgrCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLaEIIEErKSQKNFQLIVITHD 182
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
19-47 |
2.90e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 2.90e-04
10 20
....*....|....*....|....*....
gi 490220552 19 HVLRGIDVSISPGEVICVIGGSGSGKSTL 47
Cdd:COG0178 619 NNLKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
152-249 |
6.68e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 152 LSGGQQQRVAIAR----ALTmkPAIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTH--EMGFAAkvsDRVLFLA 225
Cdd:TIGR00630 489 LSGGEAQRIRLATqigsGLT--GVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHdeDTIRAA---DYVIDIG 563
|
90 100 110
....*....|....*....|....*....|
gi 490220552 226 ------DGCIEEQGAPAQLFHQPKSPRLQY 249
Cdd:TIGR00630 564 pgagehGGEVVASGTPEEILANPDSLTGQY 593
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
37-213 |
7.24e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 37 IGGSGSGKSTLLRCInfledysSGSIVVNGENVGYEPlgGEKRRRLsdkenRQalrdvcmvfQQFNlWPHMTVLDNVA-- 114
Cdd:PRK15064 33 IGANGCGKSTFMKIL-------GGDLEPSAGNVSLDP--NERLGKL-----RQ---------DQFA-FEEFTVLDTVImg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 115 -TPLRRVKKvSREAAYA---------------EAK-------TQLAR-------VGLADKADSWPaM--LSGGQQQRVAI 162
Cdd:PRK15064 89 hTELWEVKQ-ERDRIYAlpemseedgmkvadlEVKfaemdgyTAEARagelllgVGIPEEQHYGL-MseVAPGWKLRVLL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490220552 163 ARALTMKPAIMLFDEPTSALDpelvgevLKVIRNLADD----GMTMMIVTHEMGF 213
Cdd:PRK15064 167 AQALFSNPDILLLDEPTNNLD-------INTIRWLEDVlnerNSTMIIISHDRHF 214
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
33-88 |
1.15e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.68 E-value: 1.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 490220552 33 VICVIGGSGSGKSTLLRCINFLEDYSSGSIVVNGENVGYEPLGGEKRRRLSDKENR 88
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKE 56
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
25-62 |
1.22e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.91 E-value: 1.22e-03
10 20 30
....*....|....*....|....*....|....*...
gi 490220552 25 DVSISPGEVICVIGGSGSGKSTLLRCINFLEDYSSGSI 62
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDALRFLSDAARGGL 52
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
19-54 |
1.94e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.65 E-value: 1.94e-03
10 20 30
....*....|....*....|....*....|....*.
gi 490220552 19 HVLRGIDVSISPGEVICVIGGSGSGKSTLLRCINFL 54
Cdd:pfam13555 10 GTFDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTL 45
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
153-232 |
2.39e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.00 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490220552 153 SGGQQQRVAIARALTMKPAIMLFDEPTSALDPELVGEVLKVIRNLADdgmTMMIVTHEMGFAAKVSDRVLFladgcIEEQ 232
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKIIH-----IEQQ 222
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-53 |
2.45e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.25 E-value: 2.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 490220552 6 IEINNLNKHygenhvlRGIDVSISPGeVICVIGGSGSGKSTLLRCINF 53
Cdd:pfam13476 1 LTIENFRSF-------RDQTIDFSKG-LTLITGPNGSGKTTILDAIKL 40
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
152-208 |
2.66e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.40 E-value: 2.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490220552 152 LSGGQQQRVAIARALTMK---PAIM-LFDEPTSALDPELVGEVLKVIRNLADDgmTMMIVT 208
Cdd:cd03272 159 LSGGQKSLVALALIFAIQkcdPAPFyLFDEIDAALDAQYRTAVANMIKELSDG--AQFITT 217
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
152-209 |
3.32e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.90 E-value: 3.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490220552 152 LSGGQQQRVAIARALTMKP---AIMLFDEPTSALDPELVGEVLKVIRNLADDGMTMMIVTH 209
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEH 891
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
19-47 |
6.82e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.69 E-value: 6.82e-03
10 20
....*....|....*....|....*....
gi 490220552 19 HVLRGIDVSISPGEVICVIGGSGSGKSTL 47
Cdd:TIGR00630 10 HNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| |
