|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-257 |
2.05e-176 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 485.63 E-value: 2.05e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDGQLK 80
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 81 VADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQR 160
Cdd:PRK10619 81 VADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVL 240
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
250
....*....|....*..
gi 527036387 241 ANPQSPRLQQFLKGSLK 257
Cdd:PRK10619 241 GNPQSPRLQQFLKGSLK 257
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
5-257 |
7.89e-169 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 466.20 E-value: 7.89e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 5 KLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDGQLKVADK 84
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 85 NQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIA 164
Cdd:COG4598 88 RQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRD-AYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQ 244
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPK 246
|
250
....*....|...
gi 527036387 245 SPRLQQFLKGSLK 257
Cdd:COG4598 247 SERLRQFLSSSLK 259
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-253 |
5.12e-140 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 392.43 E-value: 5.12e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkvADKN 85
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVvviigpsgsgKSTLLRCINLLEEPDSGTITVDGEDLT-----------DSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIAR 165
Cdd:COG1126 71 DINKLRRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKAD-AYPAQLSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQS 245
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
....*...
gi 527036387 246 PRLQQFLK 253
Cdd:COG1126 230 ERTRAFLS 237
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-230 |
2.73e-117 |
|
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: 334.11 E-value: 2.73e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkvADKN 85
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-----------DDKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIAR 165
Cdd:cd03262 70 NINELRQKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKAD-AYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527036387 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKI 230
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-253 |
1.20e-101 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 295.46 E-value: 1.20e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkvADKNQLRLLRT 92
Cdd:PRK09493 9 KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN-----------DPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 93 RLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALAMEPE 172
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAH-HYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 173 VLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQSPRLQQFL 252
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
.
gi 527036387 253 K 253
Cdd:PRK09493 237 Q 237
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
8-256 |
7.58e-92 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 271.24 E-value: 7.58e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 8 VIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDGQlkvadKNQL 87
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQ-----KGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 88 RLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARAL 167
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKET-SYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQSPR 247
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPR 239
|
....*....
gi 527036387 248 LQQFLKGSL 256
Cdd:PRK11264 240 TRQFLEKFL 248
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
8-253 |
5.27e-86 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 256.09 E-value: 5.27e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 8 VIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDkdgqlkvADKNQL 87
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQK-------PSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 88 RLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARAL 167
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKAD-RFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPdEVLANPQSPR 247
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQTEA 235
|
....*.
gi 527036387 248 LQQFLK 253
Cdd:COG4161 236 FAHYLS 241
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
11-253 |
1.91e-83 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 249.55 E-value: 1.91e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDkdgqlkvADKNQLRLL 90
Cdd:PRK11124 8 INCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKT-------PSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 91 RTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALAME 170
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYAD-RFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 171 PEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEvLANPQSPRLQQ 250
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAFKN 238
|
...
gi 527036387 251 FLK 253
Cdd:PRK11124 239 YLS 241
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
10-253 |
7.89e-83 |
|
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: 248.21 E-value: 7.89e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDGQLKVADKNQLRL 89
Cdd:TIGR03005 5 DVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNGPLVPADEKHLRQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 90 LRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALAM 169
Cdd:TIGR03005 85 MRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKAD-HMPAQLSGGQQQRVAIARALAM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 170 EPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGK-TMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQSPRL 248
Cdd:TIGR03005 164 RPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDlTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKEERT 243
|
....*
gi 527036387 249 QQFLK 253
Cdd:TIGR03005 244 REFLS 248
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-253 |
2.51e-79 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 242.29 E-value: 2.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 8 VIDLHKRY----GEHEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgQLkvaD 83
Cdd:COG1135 4 LENLSKTFptkgGPVTALDDVSLTIEKGEIfgiigysgagKSTLIRCINLLERPTSGSVLVDGVDLT-------AL---S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 84 KNQLRLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSI 163
Cdd:COG1135 74 ERELRAARRKIGMIFQHFNLLSSRTVAENV-ALPLEIAGVPKAEIRKRVAELLELVGLSDKAD-AYPSQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLAN 242
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFAN 231
|
250
....*....|.
gi 527036387 243 PQSPRLQQFLK 253
Cdd:COG1135 232 PQSELTRRFLP 242
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
10-244 |
5.06e-73 |
|
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: 222.46 E-value: 5.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRYGEH----EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKdgqlkvadkn 85
Cdd:cd03258 6 NVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGK---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIAR 165
Cdd:cd03258 76 ELRKARRRIGMIFQHFNLLSSRTVFENVA-LPLEIAGVPKAEIEERVLELLELVGLEDKAD-AYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQ 244
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-252 |
1.66e-70 |
|
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: 216.38 E-value: 1.66e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAENKLNVIDLHKRYGEHEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlk 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEIlaiiggsgsgKSVLLKLIIGLLRPDSGEILVDGQDIT---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 81 VADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQR 160
Cdd:COG1127 71 GLSEKELYELRRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAAD-KMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEV 239
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
250
....*....|...
gi 527036387 240 LANPqSPRLQQFL 252
Cdd:COG1127 230 LASD-DPWVRQFL 241
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-229 |
8.52e-66 |
|
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: 202.42 E-value: 8.52e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDkdgqlkvadkn 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLED----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEApiqvlglskqdardravkylakvgiderqqmkypvhLSGGQQQRVSIAR 165
Cdd:cd03229 70 ELPPLRRRIGMVFQDFALFPHLTVLENIALG------------------------------------LSGGQQQRVALAR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527036387 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGK 229
Cdd:cd03229 114 ALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-235 |
2.82e-65 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 202.58 E-value: 2.82e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYG----EHEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdGQLKV 81
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFvaivgpsgsgKSTLLNILGGLDRPTSGEVLIDGQDI-------SSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 82 ADKNQLRllRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRV 161
Cdd:COG1136 78 RELARLR--RRHIGFVFQFFNLLPELTALENVA-LPLLLAGVSRKERRERARELLERVGLGDRLD-HRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527036387 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARnVSNHVIFLHQGKIEEQGH 235
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAA-RADRVIRLRDGRIVSDER 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-246 |
6.12e-64 |
|
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: 207.83 E-value: 6.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRY-----GEHEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDgqlk 80
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETlglvgesgsgKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRS---- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 81 vadknqLRLLRTRLTMVFQH----FNlwSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQMKYPVHLSGG 156
Cdd:COG1123 337 ------LRELRRRVQMVFQDpyssLN--PRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGH 235
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGP 488
|
250
....*....|.
gi 527036387 236 PDEVLANPQSP 246
Cdd:COG1123 489 TEEVFANPQHP 499
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
5-254 |
1.56e-63 |
|
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: 199.06 E-value: 1.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 5 KLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEK--PS---EGSIVVSGQNINlvrdkdgql 79
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvPGvriEGKVLFDGQDIY--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 80 kvADKNQLRLLRTRLTMVFQHFNLWShMTVLENVMEAPiQVLGL-SKQDARDRAVKYLAKVGI-DERQQM--KYPVHLSG 155
Cdd:TIGR00972 72 --DKKIDVVELRRRVGMVFQKPNPFP-MSIYDNIAYGP-RLHGIkDKKELDEIVEESLKKAALwDEVKDRlhDSALGLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGH 235
Cdd:TIGR00972 148 GQQQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGP 226
|
250
....*....|....*....
gi 527036387 236 PDEVLANPQSPRLQQFLKG 254
Cdd:TIGR00972 227 TEQIFTNPKEKRTEDYISG 245
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-244 |
1.73e-63 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 198.33 E-value: 1.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRY-GEHEVLKGVSLQ-----------AN-AGdvisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINlv 72
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSiekgefvaiigPNgSG------------KSTLLRLLNGLLKPTSGEVLVDGKDIT-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 73 rdkdgqlkvadKNQLRLLRTRLTMVFQH-----FNlwshMTVLENVMEAPIQvLGLSKQDARDRAVKYLAKVGIDERQQm 147
Cdd:COG1122 67 -----------KKNLRELRRKVGLVFQNpddqlFA----PTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLAD- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 148 KYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQ 227
Cdd:COG1122 130 RPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDD 209
|
250
....*....|....*..
gi 527036387 228 GKIEEQGHPDEVLANPQ 244
Cdd:COG1122 210 GRIVADGTPREVFSDYE 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-251 |
3.41e-63 |
|
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: 197.72 E-value: 3.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 8 VIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdGQLKVADknqL 87
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDI-------SGLSEAE---L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 88 RLLRTRLTMVFQHFNLWSHMTVLENVMeAPI-QVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARA 166
Cdd:cd03261 73 YRLRRRMGMLFQSGALFDSLTVFENVA-FPLrEHTRLSEEEIREIVLEKLEAVGLRGAED-LYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANpQS 245
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS-DD 229
|
....*.
gi 527036387 246 PRLQQF 251
Cdd:cd03261 230 PLVRQF 235
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
10-230 |
1.40e-62 |
|
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: 195.40 E-value: 1.40e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRYG----EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlKVADKN 85
Cdd:cd03255 5 NLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIS---------KLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIAR 165
Cdd:cd03255 76 LAAFRRRHIGFVFQSFNLLPDLTALENVE-LPLLLAGVPKKERRERAEELLERVGLGDRLN-HYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527036387 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSnHVIFLHQGKI 230
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYAD-RIIELRDGKI 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
10-256 |
7.70e-62 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 197.72 E-value: 7.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRY----GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgQLkvaDKN 85
Cdd:PRK11153 6 NISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLT-------AL---SEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVmeA-PIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIA 164
Cdd:PRK11153 76 ELRKARRQIGMIFQHFNLLSSRTVFDNV--AlPLELAGTPKAEIKARVTELLELVGLSDKAD-RYPAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANP 243
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
250
....*....|...
gi 527036387 244 QSPRLQQFLKGSL 256
Cdd:PRK11153 233 KHPLTREFIQSTL 245
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-246 |
2.59e-61 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 196.47 E-value: 2.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAENKLNVIDLHKRYGEHEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINLV----RDkd 76
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFvallgpsgcgKTTLLRMIAGFETPDSGRILLDGRDVTGLppekRN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 77 gqlkvadknqlrllrtrLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGG 156
Cdd:COG3842 79 -----------------VGMVFQDYALFPHLTVAENV-AFGLRMRGVPKAEIRARVAELLELVGLEGLAD-RYPHQLSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 157 QQQRVSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRIMQKLaeeGKTMVVVTHEMGFARNVSNHVIFLHQGKIEE 232
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAklreEMREELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRIEQ 216
|
250
....*....|....
gi 527036387 233 QGHPDEVLANPQSP 246
Cdd:COG3842 217 VGTPEEIYERPATR 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
10-235 |
3.09e-60 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 189.49 E-value: 3.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRY-GEHEVLKGVSLQAN------------AGdvisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKd 76
Cdd:COG2884 6 NVSKRYpGGREALSDVSLEIEkgefvfltgpsgAG------------KSTLLKLLYGEERPTSGQVLVNGQDLSRLKRR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 77 gqlkvadknQLRLLRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGG 156
Cdd:COG2884 73 ---------EIPYLRRRIGVVFQDFRLLPDRTVYENVA-LPLRVTGKSRKEIRRRVREVLDLVGLSDKAK-ALPHELSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGH 235
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-239 |
2.17e-57 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 183.33 E-value: 2.17e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRY-GEHEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKdgqlkvadk 84
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFvaligpsgagKSTLLRCLNGLVEPTSGEILVDGQDVTALRGR--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 85 nQLRLLRTRLTMVFQHFNLWSHMTVLENVM------EAPIQ-VLGLSKQDARDRAVKYLAKVGIDERQQMKypVH-LSGG 156
Cdd:COG3638 74 -ALRRLRRRIGMIFQQFNLVPRLSVLTNVLagrlgrTSTWRsLLGLFPPEDRERALEALERVGLADKAYQR--ADqLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGH 235
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGP 230
|
....
gi 527036387 236 PDEV 239
Cdd:COG3638 231 PAEL 234
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-241 |
4.49e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 179.49 E-value: 4.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdgqlkvadKN 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIfgllgpngagKTTTIRMLLGLLRPTSGEVRVLGEDV--------------AR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLRTRLTMVFQHFNLWSHMTVLENV-MEAPIQvlGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIA 164
Cdd:COG1131 67 DPAEVRRRIGYVPQEPALYPDLTVRENLrFFARLY--GLPRKEARERIDELLELFGLTDAAD-RKVGTLSGGMKQRLGLA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527036387 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLA 241
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
44-254 |
4.80e-56 |
|
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: 180.53 E-value: 4.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDgqlkvadknqLRLLR-TRLTMVFQHFNLWSHMTVLENVmEAPIQVLG 122
Cdd:cd03294 63 KSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKE----------LRELRrKKISMVFQSFALLPHRTVLENV-AFGLEVQG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 123 LSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRIMqkl 198
Cdd:cd03294 132 VPRAEREERAAEALELVGLEGWEH-KYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPlirrEMQDELLRLQ--- 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 527036387 199 AEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQSPRLQQFLKG 254
Cdd:cd03294 208 AELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRG 263
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-252 |
9.59e-55 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 179.57 E-value: 9.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQ--NINL-VRDKdgqlKVA 82
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELvallgpsgsgKTTLLRIIAGLETPDSGRIVLNGRdlFTNLpPRER----RVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 83 dknqlrllrtrltMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVS 162
Cdd:COG1118 79 -------------FVFQHYALFPHMTVAENIAFGL-RVRPPSKAEIRARVEELLELVQLEGLAD-RYPSQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 163 IARALAMEPEVLLFDEPTSALD----PELVGEVLRImqkLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDE 238
Cdd:COG1118 144 LARALAVEPEVLLLDEPFGALDakvrKELRRWLRRL---HDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDE 220
|
250
....*....|....
gi 527036387 239 VLANPQSPRLQQFL 252
Cdd:COG1118 221 VYDRPATPFVARFL 234
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-239 |
1.67e-54 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 175.45 E-value: 1.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDgqlkvadk 84
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 85 nqLRLLRTRLTMVFQHFNLWSHMTVLENVMEA------PIQVL--GLSKQDaRDRAVKYLAKVGIDER--QQMKYpvhLS 154
Cdd:cd03256 73 --LRQLRRQIGMIFQQFNLIERLSVLENVLSGrlgrrsTWRSLfgLFPKEE-KQRALAALERVGLLDKayQRADQ---LS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLA-EEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQ 233
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFD 226
|
....*.
gi 527036387 234 GHPDEV 239
Cdd:cd03256 227 GPPAEL 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-234 |
2.27e-54 |
|
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: 175.00 E-value: 2.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRY----GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKdgqlkv 81
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRR------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 82 adknQLRLLRTRLTMVFQH----FNlwSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLA-KVGIDERQQMKYPVHLSGG 156
Cdd:cd03257 76 ----LRKIRRKEIQMVFQDpmssLN--PRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLvGVGLPEEVLNRYPHELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQG 234
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-234 |
2.28e-54 |
|
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: 174.24 E-value: 2.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkvadkn 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVmeA-PIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIA 164
Cdd:cd03259 66 GVPPERRNIGMVFQDYALFPHLTVAENI--AfGLKLRGVPKAEIRARVRELLELVGLEGLLN-RYPHELSGGQQQRVALA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036387 165 RALAMEPEVLLFDEPTSALDP----ELVGEVLRImqkLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQG 234
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAklreELREELKEL---QRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
44-243 |
2.50e-54 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 179.53 E-value: 2.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkVADKNQLRLLR-TRLTMVFQHFNLWSHMTVLENVmEAPIQVLG 122
Cdd:COG4175 66 KSTLVRCLNRLIEPTAGEVLIDGEDIT----------KLSKKELRELRrKKMSMVFQHFALLPHRTVLENV-AFGLEIQG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 123 LSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRIMQKL 198
Cdd:COG4175 135 VPKAERRERAREALELVGLAGWED-SYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrEMQDELLELQAKL 213
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 527036387 199 aeeGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANP 243
Cdd:COG4175 214 ---KKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNP 255
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-256 |
2.57e-54 |
|
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: 175.38 E-value: 2.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGE----HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDgqlkv 81
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 82 adknqlrlLRTRLTMVFQH----FNlwSHMTVLENVMEaPIQVLGLskQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQ 157
Cdd:COG1124 77 --------FRRRVQMVFQDpyasLH--PRHTVDRILAE-PLRIHGL--PDREERIAELLEQVGLPPSFLDRYPHQLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHP 236
Cdd:COG1124 144 RQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTV 223
|
250 260
....*....|....*....|
gi 527036387 237 DEVLANPQSPRLQQFLKGSL 256
Cdd:COG1124 224 ADLLAGPKHPYTRELLAASL 243
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-239 |
4.92e-54 |
|
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: 173.91 E-value: 4.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEK-----PSEGSIVVSGQNINlvrdkdgqlk 80
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIY---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 81 vADKNQLRLLRTRLTMVFQHFNLWsHMTVLENVmEAPIQVLGLSKQDARDRAVKY-LAKVGI-DERQQMKYPVHLSGGQQ 158
Cdd:cd03260 71 -DLDVDVLELRRRVGMVFQKPNPF-PGSIYDNV-AYGLRLHGIKLKEELDERVEEaLRKAALwDEVKDRLHALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDE 238
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 527036387 239 V 239
Cdd:cd03260 227 I 227
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-239 |
1.55e-53 |
|
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: 173.25 E-value: 1.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDgqlkvadk 84
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKK-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 85 nqLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPI-------QVLGLSKQDARDRAVKYLAKVGIDER--QQMKYpvhLSG 155
Cdd:TIGR02315 74 --LRKLRRRIGMIFQHYNLIERLTVLENVLHGRLgykptwrSLLGRFSEEDKERALSALERVGLADKayQRADQ---LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQG 234
Cdd:TIGR02315 149 GQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDG 228
|
....*
gi 527036387 235 HPDEV 239
Cdd:TIGR02315 229 APSEL 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-244 |
1.10e-52 |
|
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: 170.70 E-value: 1.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVIsiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgQLKVADKN 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHgligpngagKTTLFNLISGFLRPTSGSVLFDGEDIT-------GLPPHEIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLRTrltmvFQHFNLWSHMTVLENVMEAPIQVLGLS---------KQDARDRAVKYLAKVGIDERqqMKYPVH-LSG 155
Cdd:cd03219 74 RLGIGRT-----FQIPRLFPELTVLENVMVAAQARTGSGlllararreEREARERAEELLERVGLADL--ADRPAGeLSY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGH 235
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
....*....
gi 527036387 236 PDEVLANPQ 244
Cdd:cd03219 227 PDEVRNNPR 235
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
10-252 |
6.98e-52 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 171.04 E-value: 6.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRYGE-HEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNInlvRDKDgqlkvadknqLR 88
Cdd:COG1125 6 NVTKRYPDgTVAVDDLSLTIPAGEFtvlvgpsgcgKTTTLRMINRLIEPTSGRILIDGEDI---RDLD----------PV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 89 LLRTRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQDARDRAVKYLAKVGIDERQQM-KYPVHLSGGQQQRVSIARAL 167
Cdd:COG1125 73 ELRRRIGYVIQQIGLFPHMTVAENIATVP-RLLGWDKERIRARVDELLELVGLDPEEYRdRYPHELSGGQQQRVGVARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 168 AMEPEVLLFDEPTSALDP----ELVGEVLRIMQKLaeeGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANP 243
Cdd:COG1125 152 AADPPILLMDEPFGALDPitreQLQDELLRLQREL---GKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANP 228
|
....*....
gi 527036387 244 QSPRLQQFL 252
Cdd:COG1125 229 ANDFVADFV 237
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-253 |
1.44e-51 |
|
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: 168.25 E-value: 1.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRYGE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNI---NLVRdkdgqlkvadkn 85
Cdd:cd03295 5 NVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIreqDPVE------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 qlrlLRTRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQDARDRAVKYLAKVGIDERQQM-KYPVHLSGGQQQRVSIA 164
Cdd:cd03295 73 ----LRRKIGYVIQQIGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLDPAEFAdRYPHELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 165 RALAMEPEVLLFDEPTSALDP----ELVGEVLRIMQKLaeeGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVL 240
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPitrdQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
250
....*....|...
gi 527036387 241 ANPQSPRLQQFLK 253
Cdd:cd03295 225 RSPANDFVAEFVG 237
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-210 |
2.02e-51 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 168.34 E-value: 2.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAENKLNVIDLHKRY----GEHEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkd 76
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFvalvgpsgcgKSTLLRLIAGLEKPTSGEVLVDGKPV------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 77 gqlkvadknqlRLLRTRLTMVFQHFNL--WshMTVLENVMeAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLS 154
Cdd:COG1116 76 -----------TGPGPDRGVVFQEPALlpW--LTVLDNVA-LGLELRGVPKAERRERARELLELVGLAGFED-AYPHQLS 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRImqkLAEEGKTMVVVTH 210
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTH 197
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-245 |
2.42e-51 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 170.64 E-value: 2.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAEnkLNVIDLHKRYGEHEVLKGVSLQAN------------AGdvisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQN 68
Cdd:COG3839 1 MAS--LELENVSKSYGGVEALKDIDLDIEdgeflvllgpsgCG------------KSTLLRMIAGLEDPTSGEILIGGRD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 69 INlvrdkdgQLKVADKNqlrllrtrLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQDaRDRAVKYLAK-VGIDERQQm 147
Cdd:COG3839 67 VT-------DLPPKDRN--------IAMVFQSYALYPHMTVYEN-IAFPLKLRKVPKAE-IDRRVREAAElLGLEDLLD- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 148 KYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRIMQKLaeeGKTMVVVTHE----MGFArnvs 219
Cdd:COG3839 129 RKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAklrvEMRAEIKRLHRRL---GTTTIYVTHDqveaMTLA---- 201
|
250 260
....*....|....*....|....*.
gi 527036387 220 NHVIFLHQGKIEEQGHPDEVLANPQS 245
Cdd:COG3839 202 DRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-254 |
2.48e-51 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 167.91 E-value: 2.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 2 AENKLNVIDLHKRYGEHEVLKGVSLQANA------------GdvisiigssgsgKSTFLRCINFL--EKPS---EGSIVV 64
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPEnkvtaligpsgcG------------KSTLLRCLNRMndLIPGarvEGEILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 65 SGQNINlvrDKDgqlkvADKNQLRllrTRLTMVFQHFNLWShMTVLENVmeapiqVLGL------SKQDARDRAVKYLAK 138
Cdd:COG1117 76 DGEDIY---DPD-----VDVVELR---RRVGMVFQKPNPFP-KSIYDNV------AYGLrlhgikSKSELDEIVEESLRK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 139 VGI-DE---RQQmKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPelvGEVLRI---MQKLAEEgKTMVVVTHE 211
Cdd:COG1117 138 AALwDEvkdRLK-KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDP---ISTAKIeelILELKKD-YTIVIVTHN 212
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 527036387 212 MGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQSPRLQQFLKG 254
Cdd:COG1117 213 MQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYITG 255
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-229 |
8.53e-51 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 164.95 E-value: 8.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkvadKNQL 87
Cdd:cd03225 4 NLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT-------------KLSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 88 RLLRTRLTMVFQH-----FNLwshmTVLENVMEAPIQvLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVS 162
Cdd:cd03225 71 KELRRKVGLVFQNpddqfFGP----TVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRD-RSPFTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527036387 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGK 229
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-253 |
9.60e-51 |
|
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: 167.24 E-value: 9.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkVADKNQLRLLRTRLTM 96
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDIT----------AKKKKKLKDLRKKVGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 97 VFQH-----FNLwshmTVLENVMEAPIQvLGLSKQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQRVSIARALAMEP 171
Cdd:TIGR04521 87 VFQFpehqlFEE----TVYKDIAFGPKN-LGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 172 EVLLFDEPTSALDPELVGEVLRIMQKLA-EEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLAN-------- 242
Cdd:TIGR04521 162 EVLILDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDvdelekig 241
|
250
....*....|....
gi 527036387 243 ---PQSPRLQQFLK 253
Cdd:TIGR04521 242 ldvPEITELARKLK 255
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-252 |
2.70e-49 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 162.12 E-value: 2.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 8 VIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdGQLKVADKNql 87
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-------TDVPVQERN-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 88 rllrtrLTMVFQHFNLWSHMTVLENV---MEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIA 164
Cdd:cd03296 76 ------VGFVFQHYALFRHMTVFDNVafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLAD-RYPAQLSGGQRQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANP 243
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
....*....
gi 527036387 244 QSPRLQQFL 252
Cdd:cd03296 229 ASPFVYSFL 237
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6-244 |
4.55e-49 |
|
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: 162.13 E-value: 4.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQAN------------AGdvisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINlvr 73
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVErgeivgligpngAG------------KTTLFNLITGFYRPTSGRILFDGRDIT--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 74 dkdgQLKVADKNQLRLLRTrltmvFQHFNLWSHMTVLENVMEAPIQVLGLS--------------KQDARDRAVKYLAKV 139
Cdd:COG0411 70 ----GLPPHRIARLGIART-----FQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreEREARERAEELLERV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 140 GIDERQQmKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMGFARNV 218
Cdd:COG0411 141 GLADRAD-EPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGL 219
|
250 260
....*....|....*....|....*.
gi 527036387 219 SNHVIFLHQGKIEEQGHPDEVLANPQ 244
Cdd:COG0411 220 ADRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-245 |
8.88e-49 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 167.77 E-value: 8.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRY--GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPS---EGSIVVSGQNINLVRDkdgqlk 80
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 81 vadknqlRLLRTRLTMVFQH----FNLwshMTVLENVMEApIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGG 156
Cdd:COG1123 79 -------ALRGRRIGMVFQDpmtqLNP---VTVGDQIAEA-LENLGLSRAEARARVLELLEAVGLERRLD-RYPHQLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGH 235
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
250
....*....|
gi 527036387 236 PDEVLANPQS 245
Cdd:COG1123 227 PEEILAAPQA 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-240 |
3.56e-48 |
|
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: 159.82 E-value: 3.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDgqlkvadkn 85
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVtallgpngsgKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 qlrlLRTRLTMVFQHFNLWSHMTVLENVMeapiqvLG----------LSKQDaRDRAVKYLAKVGIDERQQMKYPvHLSG 155
Cdd:COG1120 73 ----LARRIAYVPQEPPAPFGLTVRELVA------LGryphlglfgrPSAED-REAVEEALERTGLEHLADRPVD-ELSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLA-EEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQG 234
Cdd:COG1120 141 GERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQG 220
|
....*.
gi 527036387 235 HPDEVL 240
Cdd:COG1120 221 PPEEVL 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-252 |
4.64e-48 |
|
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: 159.25 E-value: 4.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdgqlkvadKN 85
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV--------------RK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLRTRLTMVFQHFNLWSHMTVLENV-MEAPIQvlGLSKQDARDRAVKYLAKVGIDERQQMKYpVHLSGGQQQRVSIA 164
Cdd:COG4555 68 EPREARRQIGVLPDERGLYDRLTVRENIrYFAELY--GLFDEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVALA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQ 244
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIG 224
|
....*...
gi 527036387 245 SPRLQQFL 252
Cdd:COG4555 225 EENLEDAF 232
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-246 |
1.68e-46 |
|
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: 157.52 E-value: 1.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRY----GEHEVLKGVSLQANAGDVisiigssgsgKSTFLRCI-NFLEKP--SEGSIVVSGQNInlvrdkdgq 78
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETlglvgesgsgKSTLARAIlGLLPPPgiTSGEILFDGEDL--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 79 LKvADKNQLRLLRTR-LTMVFQH----FNlwSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQM--KYPV 151
Cdd:COG0444 73 LK-LSEKELRKIRGReIQMIFQDpmtsLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRldRYPH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKI 230
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
250
....*....|....*.
gi 527036387 231 EEQGHPDEVLANPQSP 246
Cdd:COG0444 230 VEEGPVEELFENPRHP 245
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
11-229 |
1.95e-46 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 153.94 E-value: 1.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 11 LHKRY-GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKdgqlkvadknQLRL 89
Cdd:TIGR02673 7 VSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGR----------QLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 90 LRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALAM 169
Cdd:TIGR02673 77 LRRRIGVVFQDFRLLPDRTVYENV-ALPLEVRGKKEREIQRRVGAALRQVGLEHKAD-AFPEQLSGGEQQRVAIARAIVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 170 EPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGK 229
Cdd:TIGR02673 155 SPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
10-233 |
3.47e-46 |
|
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: 153.78 E-value: 3.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRYG----EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDkdgqlkvadkn 85
Cdd:cd03293 5 NVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 qlrllrtRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIAR 165
Cdd:cd03293 74 -------DRGYVFQQDALLPWLTVLDNVA-LGLELQGVPKAEARERAEELLELVGLSGFEN-AYPHQLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036387 166 ALAMEPEVLLFDEPTSALDP----ELVGEVLRImqkLAEEGKTMVVVTHEMGFARNVSNHVIFLHQ--GKIEEQ 233
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDAltreQLQEELLDI---WRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-230 |
7.93e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 149.58 E-value: 7.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgQLKVADkn 85
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLS-------AMPPPE-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 qlrlLRTRLTMVFQHFNLWsHMTVLENvMEAPIQVLGlsKQDARDRAVKYLAKVGIDErQQMKYPVH-LSGGQQQRVSIA 164
Cdd:COG4619 72 ----WRRQVAYVPQEPALW-GGTVRDN-LPFPFQLRE--RKFDRERALELLERLGLPP-DILDKPVErLSGGERQRLALI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527036387 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMGFARNVSNHVIFLHQGKI 230
Cdd:COG4619 143 RALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-238 |
8.13e-45 |
|
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: 150.66 E-value: 8.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAENKLNVIDLHKRY--GEHEV--LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkd 76
Cdd:COG4181 4 SSAPIIELRGLTKTVgtGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 77 GQLkvaDKNQL-RLLRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSkqDARDRAVKYLAKVGIDERQQmKYPVHLSG 155
Cdd:COG4181 77 FAL---DEDARaRLRARHVGFVFQSFQLLPTLTALENVM-LPLELAGRR--DARARARALLERVGLGHRLD-HYPAQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPElVGEvlRIMQKL----AEEGKTMVVVTHEMGFARNvSNHVIFLHQGKIE 231
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAA-TGE--QIIDLLfelnRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLV 225
|
....*..
gi 527036387 232 EQGHPDE 238
Cdd:COG4181 226 EDTAATA 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-245 |
1.56e-44 |
|
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: 149.69 E-value: 1.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkvadknQLRLLRT 92
Cdd:cd03300 8 KFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT---------------NLPPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 93 RLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALAMEPE 172
Cdd:cd03300 73 PVNTVFQNYALFPHLTVFENIA-FGLRLKKLPKAEIKERVAEALDLVQLEGYAN-RKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527036387 173 VLLFDEPTSALDPELVGEV---LRIMQKlaEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQS 245
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMqleLKRLQK--ELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPAN 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-230 |
2.73e-44 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 147.16 E-value: 2.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdgqlkvadKN 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIygllgpngagKTTLIKIILGLLKPDSGEIKVLGKDI--------------KK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVmeapiqvlglskqdardravkylakvgiderqqmkypvHLSGGQQQRVSIAR 165
Cdd:cd03230 67 EPEEVKRRIGYLPEEPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQ 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527036387 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKI 230
Cdd:cd03230 109 ALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-240 |
3.83e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 146.39 E-value: 3.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAENKLNVIDLHKRYGEHEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINLVRDkdgqlk 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFvaivgpngagKSTLLKAILGLLPPTSGTVRLFGKPPRRARR------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 81 vadknqlrllrtRLTMVFQHFNL-WS-HMTVLENVM---EAPIQVLGLSKQDARDRAVKYLAKVGIDE--RQQMKypvHL 153
Cdd:COG1121 76 ------------RIGYVPQRAEVdWDfPITVRDVVLmgrYGRRGLFRRPSRADREAVDEALERVGLEDlaDRPIG---EL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEq 233
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH- 219
|
....*..
gi 527036387 234 GHPDEVL 240
Cdd:COG1121 220 GPPEEVL 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-253 |
1.09e-42 |
|
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: 146.04 E-value: 1.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 8 VIDLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGqninlvrdkdgqLKVADKN 85
Cdd:TIGR04520 3 VENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG------------LDTLDEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLRTRLTMVFQH-FNLWSHMTV-------LENvmeapiqvLGLSKQDARDRAVKYLAKVGIDErQQMKYPVHLSGGQ 157
Cdd:TIGR04520 71 NLWEIRKKVGMVFQNpDNQFVGATVeddvafgLEN--------LGVPREEMRKRVDEALKLVGMED-FRDREPHLLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMGFARNvSNHVIFLHQGKIEEQGHP 236
Cdd:TIGR04520 142 KQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTP 220
|
250 260
....*....|....*....|....*...
gi 527036387 237 DEVLAN-----------PQSPRLQQFLK 253
Cdd:TIGR04520 221 REIFSQvellkeigldvPFITELAKALK 248
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-253 |
1.45e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 146.77 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDGQLKVADKNQLRL------- 89
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKtrfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 90 ----LRTRLTMVFQ--HFNLWSHmTVLENVMEAPIQvLGLSKQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQRVSI 163
Cdd:PRK13651 99 kikeIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVS-MGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLA-- 241
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSdn 256
|
250
....*....|....*...
gi 527036387 242 ------NPQSPRLQQFLK 253
Cdd:PRK13651 257 kflienNMEPPKLLNFVN 274
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-251 |
3.68e-42 |
|
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: 147.11 E-value: 3.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdgqlkvadkn 85
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDI---------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 qlrllrTRLT-------MVFQHFNLWSHMTVLENVmEAPIQVLGLSKQDARDRAVKYLAKVGIDErQQMKYPVHLSGGQQ 158
Cdd:TIGR03265 69 ------TRLPpqkrdygIVFQSYALFPNLTVADNI-AYGLKNRGMGRAEVAERVAELLDLVGLPG-SERKYPGQLSGGQQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 159 QRVSIARALAMEPEVLLFDEPTSALDPE----LVGEVLRIMQKLaeeGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQG 234
Cdd:TIGR03265 141 QRVALARALATSPGLLLLDEPLSALDARvrehLRTEIRQLQRRL---GVTTIMVTHDQEEALSMADRIVVMNHGVIEQVG 217
|
250
....*....|....*..
gi 527036387 235 HPDEVLANPQSPRLQQF 251
Cdd:TIGR03265 218 TPQEIYRHPATPFVADF 234
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-225 |
4.63e-42 |
|
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: 142.75 E-value: 4.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 8 VIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdgqLKVADKNQL 87
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQET---------PPLNSKKAS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 88 RLLRTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARAL 167
Cdd:TIGR03608 72 KFRREKLGYLFQNFALIENETVEEN-LDLGLKYKKLSKKEKREKKKEALEKVGLNLKLK-QKIYELSGGEQQRVALARAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 527036387 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFArNVSNHVIFL 225
Cdd:TIGR03608 150 LKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-230 |
6.17e-42 |
|
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: 142.55 E-value: 6.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 9 IDLHKRYGEHEV-LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRdkdgqlkvadKNQL 87
Cdd:cd03292 4 INVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLR----------GRAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 88 RLLRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARAL 167
Cdd:cd03292 74 PYLRRKIGVVFQDFRLLPDRNVYENVA-FALEVTGVPPREIRKRVPAALELVGLSHKHR-ALPAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527036387 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKI 230
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
13-254 |
8.60e-42 |
|
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: 146.54 E-value: 8.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVrdkdgqlkvaDKNQLRLLRT 92
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQ----------SPVELREVRR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 93 R-LTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALAMEP 171
Cdd:TIGR01186 71 KkIGMVFQQFALFPHMTILQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEH-RYPDELSGGMQQRVGLARALAAEP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 172 EVLLFDEPTSALDP----ELVGEVLRIMQKLaeeGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQSPR 247
Cdd:TIGR01186 149 DILLMDEAFSALDPlirdSMQDELKKLQATL---QKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEY 225
|
....*..
gi 527036387 248 LQQFLKG 254
Cdd:TIGR01186 226 VEEFIGK 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
13-252 |
1.01e-41 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 146.00 E-value: 1.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDgqlkvadknqlrllrT 92
Cdd:PRK10851 10 KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---------------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 93 RLTMVFQHFNLWSHMTVLENVmeapiqVLGLSKQDARDRAVKYLAKVGIDERQQM--------KYPVHLSGGQQQRVSIA 164
Cdd:PRK10851 75 KVGFVFQHYALFRHMTVFDNI------AFGLTVLPRRERPNAAAIKAKVTQLLEMvqlahladRYPAQLSGGQKQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGK-TMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANP 243
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
....*....
gi 527036387 244 QSPRLQQFL 252
Cdd:PRK10851 229 ATRFVLEFM 237
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
44-246 |
1.14e-41 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 145.26 E-value: 1.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkVADKNQLRLLRTRLTMVFQH----FNlwSHMTVLENVMEaPIQ 119
Cdd:COG4608 57 KSTLGRLLLRLEEPTSGEILFDGQDIT----------GLSGRELRPLRRRMQMVFQDpyasLN--PRMTVGDIIAE-PLR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 120 VLGL-SKQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL 198
Cdd:COG4608 124 IHGLaSKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDL 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 527036387 199 AEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQSP 246
Cdd:COG4608 204 QDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHP 252
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
44-257 |
7.31e-41 |
|
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: 147.14 E-value: 7.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEkPSEGSIVVSGQNINLvrdkdgqlkvADKNQLRLLRTRLTMVFQ----HFNlwSHMTVLENVMEaPIQ 119
Cdd:COG4172 325 KSTLGLALLRLI-PSEGEIRFDGQDLDG----------LSRRALRPLRRRMQVVFQdpfgSLS--PRMTVGQIIAE-GLR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 120 VL--GLSKQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQK 197
Cdd:COG4172 391 VHgpGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRD 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036387 198 L-AEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQSPRLQQFLKGSLK 257
Cdd:COG4172 471 LqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPL 531
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
44-253 |
4.78e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 140.76 E-value: 4.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSI----VVSGQNINLVRDKDGQLKVADKNQLRLlRTRLTMVFQ--HFNLWSHmTVLENVMEAP 117
Cdd:PRK13631 65 KSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNPYSKKIKNFKEL-RRRVSMVFQfpEYQLFKD-TIEKDIMFGP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 118 IQvLGLSKQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQK 197
Cdd:PRK13631 143 VA-LGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036387 198 LAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANP--------QSPRLQQFLK 253
Cdd:PRK13631 222 AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQhiinstsiQVPRVIQVIN 285
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-229 |
6.20e-40 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 135.45 E-value: 6.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 8 VIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkvadKNQL 87
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA-------------KLPL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 88 RLLRTRLTMVFQhfnlwshmtvlenvmeapiqvlglskqdardravkylakvgiderqqmkypvhLSGGQQQRVSIARAL 167
Cdd:cd00267 69 EELRRRIGYVPQ-----------------------------------------------------LSGGQRQRVALARAL 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527036387 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGK 229
Cdd:cd00267 96 LLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-253 |
7.62e-40 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 137.58 E-value: 7.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHevLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdGQLKVADkn 85
Cdd:COG3840 2 LRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-------TALPPAE-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 qlrllrtR-LTMVFQHFNLWSHMTVLENVmeapiqVLGLS---KQDARDRA--VKYLAKVGIDERQQmKYPVHLSGGQQQ 159
Cdd:COG3840 71 -------RpVSMLFQENNLFPHLTVAQNI------GLGLRpglKLTAEQRAqvEQALERVGLAGLLD-RLPGQLSGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDE 238
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
250
....*....|....*
gi 527036387 239 VLANPQSPRLQQFLK 253
Cdd:COG3840 217 LLDGEPPPALAAYLG 231
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
10-234 |
2.19e-39 |
|
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: 135.85 E-value: 2.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKdgqlkvaDKNqlrl 89
Cdd:cd03301 5 NVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-------DRD---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 90 lrtrLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKqDARDRAVKYLAKV-GIDERQQmKYPVHLSGGQQQRVSIARALA 168
Cdd:cd03301 74 ----IAMVFQNYALYPHMTVYDN-IAFGLKLRKVPK-DEIDERVREVAELlQIEHLLD-RKPKQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 169 MEPEVLLFDEPTSALDP----ELVGEVLRIMQKLaeeGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQG 234
Cdd:cd03301 147 REPKVFLMDEPLSNLDAklrvQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
44-244 |
7.62e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 136.69 E-value: 7.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdgqlkVADKNQ--LRLLRTRLTMVFQ--HFNLWSHmTVLENVMEAPIQ 119
Cdd:PRK13634 46 KSTLLQHLNGLLQPTSGTVTIGERVI-----------TAGKKNkkLKPLRKKVGIVFQfpEHQLFEE-TVEKDICFGPMN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 120 vLGLSKQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL- 198
Cdd:PRK13634 114 -FGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLh 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 527036387 199 AEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQ 244
Cdd:PRK13634 193 KEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-254 |
1.82e-38 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 141.79 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVrdkdgqlkvaDKNQL-RLLRTRLTMV 97
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATL----------DADALaQLRREHFGFI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 98 FQHFNLWSHMTVLENVmEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQMkYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
Cdd:PRK10535 92 FQRYHLLSHLTAAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEY-QPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 178 EPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFArNVSNHVIFLHQGKI----------EEQGHPDEVLanPQSPR 247
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVA-AQAERVIEIRDGEIvrnppaqekvNVAGGTEPVV--NTASG 246
|
....*..
gi 527036387 248 LQQFLKG 254
Cdd:PRK10535 247 WRQFVSG 253
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-247 |
4.82e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 134.43 E-value: 4.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLvrDKDGQLKVadk 84
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY--DKKSLLEV--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 85 nqlrllRTRLTMVFQHFN--LWSHmTVLENVMEAPIQvLGLSKQDARDRAVKYLAKVGIdERQQMKYPVHLSGGQQQRVS 162
Cdd:PRK13639 77 ------RKTVGIVFQNPDdqLFAP-TVEEDVAFGPLN-LGLSKEEVEKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLAN 242
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
....*
gi 527036387 243 PQSPR 247
Cdd:PRK13639 228 IETIR 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-256 |
7.74e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 133.11 E-value: 7.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 4 NKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFL-----EKPSEGSIVVSGQNINlvrdkdgq 78
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIF-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 79 lkvadKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAP-IQVLGLSKQDARDRAVKYLAKVGI-DE-RQQMKYPV-HLS 154
Cdd:PRK14247 74 -----KMDVIELRRRVQMVFQIPNPIPNLSIFENVALGLkLNRLVKSKKELQERVRWALEKAQLwDEvKDRLDAPAgKLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQG 234
Cdd:PRK14247 149 GGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
250 260
....*....|....*....|..
gi 527036387 235 HPDEVLANPQSPRLQQFLKGSL 256
Cdd:PRK14247 228 PTREVFTNPRHELTEKYVTGRL 249
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-242 |
2.64e-37 |
|
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: 130.63 E-value: 2.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdgqlkvADKN 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI------------TGLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLRTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQDAR-DRAVKYLAKVGiDERQQMKYpvHLSGGQQQRVSIA 164
Cdd:cd03224 69 PHERARAGIGYVPEGRRIFPELTVEEN-LLLGAYARRRAKRKARlERVYELFPRLK-ERRKQLAG--TLSGGEQQMLAIA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527036387 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLAN 242
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
44-244 |
3.79e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 132.26 E-value: 3.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVSGQNINLvrdkdgqlKVADKNqLRLLRTRLTMVFQ--HFNLWSHmTVLENVMEAPIQvL 121
Cdd:PRK13641 46 KSTLMQHFNALLKPSSGTITIAGYHITP--------ETGNKN-LKKLRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKN-F 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 122 GLSKQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE 201
Cdd:PRK13641 115 GFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA 194
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 527036387 202 GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQ 244
Cdd:PRK13641 195 GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-252 |
5.01e-37 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 132.78 E-value: 5.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRY--------GEHEV--LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNinlvrdk 75
Cdd:PRK11308 6 LQAIDLKKHYpvkrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQD------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 76 dgqLKVADKNQLRLLRTRLTMVFQ--HFNLWSHMTVlENVMEAPIQV-LGLSKQDARDRAVKYLAKVGIDERQQMKYPVH 152
Cdd:PRK11308 79 ---LLKADPEAQKLLRQKIQIVFQnpYGSLNPRKKV-GQILEEPLLInTSLSAAERREKALAMMAKVGLRPEHYDRYPHM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIE 231
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
250 260
....*....|....*....|.
gi 527036387 232 EQGHPDEVLANPQSPRLQQFL 252
Cdd:PRK11308 235 EKGTKEQIFNNPRHPYTQALL 255
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-230 |
6.92e-37 |
|
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: 129.58 E-value: 6.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDG---QLKVADKNq 86
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGyvpQRRSIDRD- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 87 lrllrtrltmvfqhFNLwshmTVLENVMEAPIQVLGLSK---QDARDRAVKYLAKVGIDE--RQQMKypvHLSGGQQQRV 161
Cdd:cd03235 83 --------------FPI----SVRDVVLMGLYGHKGLFRrlsKADKAKVDEALERVGLSElaDRQIG---ELSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKI 230
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-256 |
1.15e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 129.96 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFL-----EKPSEGSIVVSGQNInlvrdkdg 77
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNI-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 78 qlKVADKNQLRLlRTRLTMVFQHFNLWSHMTVLENVMEApIQVLGLSK-QDARDRAVKY-LAKVGI-DE-RQQMK-YPVH 152
Cdd:PRK14267 74 --YSPDVDPIEV-RREVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLVKsKKELDERVEWaLKKAALwDEvKDRLNdYPSN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMGFARNVSNHVIFLHQGKIEE 232
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
250 260
....*....|....*....|....
gi 527036387 233 QGHPDEVLANPQSPRLQQFLKGSL 256
Cdd:PRK14267 229 VGPTRKVFENPEHELTEKYVTGAL 252
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-252 |
1.50e-36 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 129.38 E-value: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEvLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNI-NLVRDKDGqlkvadk 84
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDItNLPPEKRD------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 85 nqlrllrtrLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQDaRDRAVKYLAKV-GIDERQQmKYPVHLSGGQQQRVSI 163
Cdd:cd03299 73 ---------ISYVPQNYALFPHMTVYKNI-AYGLKKRKVDKKE-IERKVLEIAEMlGIDHLLN-RKPETLSGGEQQRVAI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVV-VTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLAN 242
Cdd:cd03299 141 ARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
250
....*....|
gi 527036387 243 PQSPRLQQFL 252
Cdd:cd03299 221 PKNEFVAEFL 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-253 |
2.58e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 130.17 E-value: 2.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdgqlkvADKN-QLRLLRTRLT 95
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI------------TDKKvKLSDIRKKVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 96 MVFQH--FNLWSHmTVLENVMEAPIQvLGLSKQDARDRAVKYLAKVGID-ERQQMKYPVHLSGGQQQRVSIARALAMEPE 172
Cdd:PRK13637 87 LVFQYpeYQLFEE-TIEKDIAFGPIN-LGLSEEEIENRVKRAMNIVGLDyEDYKDKSPFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 173 VLLFDEPTSALDPELVGEVLRIMQKLAEEGK-TMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEV-----------L 240
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVfkevetlesigL 244
|
250
....*....|...
gi 527036387 241 ANPQSPRLQQFLK 253
Cdd:PRK13637 245 AVPQVTYLVRKLR 257
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-246 |
3.06e-36 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 134.43 E-value: 3.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAENKLNVIDLHKRYG----EHEVLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLEKPS---EGSIVVSGQNInlv 72
Cdd:COG4172 2 MSMPLLSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 73 rdkdgqLKvADKNQLRLLR-TRLTMVFQH----FNlwSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDE-RQQ 146
Cdd:COG4172 79 ------LG-LSERELRRIRgNRIAMIFQEpmtsLN--PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDpERR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 147 MK-YPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMGFARNVSNHVIF 224
Cdd:COG4172 150 LDaYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAV 229
|
250 260
....*....|....*....|..
gi 527036387 225 LHQGKIEEQGHPDEVLANPQSP 246
Cdd:COG4172 230 MRQGEIVEQGPTAELFAAPQHP 251
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-241 |
4.14e-36 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 135.35 E-value: 4.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRYGEHE--VLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgQLKVADknql 87
Cdd:COG2274 478 NVSFRYPGDSppVLDNISLTIKPGERvaivgrsgsgKSTLLKLLLGLYEPTSGRILIDGIDLR-------QIDPAS---- 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 88 rlLRTRLTMVFQHFNLWShMTVLENVMeapiqvlgLSKQDARDRAVKYLAK-VGIDE---RQQMKY--PVH-----LSGG 156
Cdd:COG2274 547 --LRRQIGVVLQDVFLFS-GTIRENIT--------LGDPDATDEEIIEAARlAGLHDfieALPMGYdtVVGeggsnLSGG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMGFARNVsNHVIFLHQGKIEEQGHP 236
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDGTH 693
|
....*
gi 527036387 237 DEVLA 241
Cdd:COG2274 694 EELLA 698
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
10-243 |
4.94e-36 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 131.22 E-value: 4.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRdkdgqlkvADKnqlRL 89
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP--------AEN---RH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 90 LRTrltmVFQHFNLWSHMTVLENVmeapiqVLGL-----SKQDARDRAVKYLAKVGIDERQQMKyPVHLSGGQQQRVSIA 164
Cdd:PRK09452 88 VNT----VFQSYALFPHMTVFENV------AFGLrmqktPAAEITPRVMEALRMVQLEEFAQRK-PHQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 165 RALAMEPEVLLFDEPTSALDPELVGEV---LRIMQKlaEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLA 241
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMqneLKALQR--KLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYE 234
|
..
gi 527036387 242 NP 243
Cdd:PRK09452 235 EP 236
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-234 |
5.15e-36 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 126.01 E-value: 5.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgQLKVADKNQlrl 89
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA-------SLSPKELAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 90 lrtrltmvfqhfnlwsHMTVLENVMEApiqvLGLSkqdardravkYLAKVGIDErqqmkypvhLSGGQQQRVSIARALAM 169
Cdd:cd03214 74 ----------------KIAYVPQALEL----LGLA----------HLADRPFNE---------LSGGERQRVLLARALAQ 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527036387 170 EPEVLLFDEPTSALDPELVGEVLRIMQKLA-EEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQG 234
Cdd:cd03214 115 EPPILLLDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-254 |
9.65e-36 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 127.58 E-value: 9.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFL-----EKPSEGSIVVSGQNINLVRdk 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 76 dgqlkvADKNQLRllrTRLTMVFQHFNLWShMTVLENVmeapiqVLGLSKQDARDRAV------KYLAKVGI-DErqqMK 148
Cdd:PRK14239 79 ------TDTVDLR---KEIGMVFQQPNPFP-MSIYENV------VYGLRLKGIKDKQVldeaveKSLKGASIwDE---VK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 149 YPVH-----LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMGFARNVSNHVI 223
Cdd:PRK14239 140 DRLHdsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTG 218
|
250 260 270
....*....|....*....|....*....|.
gi 527036387 224 FLHQGKIEEQGHPDEVLANPQSPRLQQFLKG 254
Cdd:PRK14239 219 FFLDGDLIEYNDTKQMFMNPKHKETEDYISG 249
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
44-250 |
1.01e-35 |
|
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: 130.22 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVsgqninlvrdkDGQLKVADKNQLRLL--RTRLTMVFQHFNLWSHMTVLENVmeapiqvl 121
Cdd:COG4148 38 KTTLLRAIAGLERPDSGRIRL-----------GGEVLQDSARGIFLPphRRRIGYVFQEARLFPHLSVRGNL-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 122 glskQDARDRAVKYLAKVGIDERQQM--------KYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR 193
Cdd:COG4148 99 ----LYGRKRAPRAERRISFDEVVELlgighlldRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 527036387 194 IMQKLAEEGKT-MVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQSPRLQQ 250
Cdd:COG4148 175 YLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-252 |
1.29e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 129.84 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNI--NLVRDKDgqlkvadknqlrll 90
Cdd:PRK11432 14 KRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRD-------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 91 rtrLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQDARDRAVKYLAKV---GIDERqqmkYPVHLSGGQQQRVSIARAL 167
Cdd:PRK11432 80 ---ICMVFQSYALFPHMSLGENV-GYGLKMLGVPKEERKQRVKEALELVdlaGFEDR----YVDQISGGQQQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 168 AMEPEVLLFDEPTSALDPEL---VGEVLRIMQKlaEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQ 244
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLrrsMREKIRELQQ--QFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
....*...
gi 527036387 245 SPRLQQFL 252
Cdd:PRK11432 230 SRFMASFM 237
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
44-239 |
1.34e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 127.94 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkVADKNQ-LRLLRTRLTMVFQ--HFNLWSHmTVLENVMEAPiQV 120
Cdd:PRK13649 46 KSTIMQLLNGLHVPTQGSVRVDDTLIT----------STSKNKdIKQIRKKVGLVFQfpESQLFEE-TVLKDVAFGP-QN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 121 LGLSKQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAE 200
Cdd:PRK13649 114 FGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQ 193
|
170 180 190
....*....|....*....|....*....|....*....
gi 527036387 201 EGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEV 239
Cdd:PRK13649 194 SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
20-230 |
3.41e-35 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 125.22 E-value: 3.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgQLKVADKNQLRllRTRLTMVFQ 99
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVT-------NLSYSQKIILR--RELIGYIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 100 HFNLWSHMTVLENVmEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQMKyPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
Cdd:NF038007 91 SFNLIPHLSIFDNV-ALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHK-PMQLSGGQQQRVAIARAMVSNPALLLADEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 527036387 180 TSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGfARNVSNHVIFLHQGKI 230
Cdd:NF038007 169 TGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-254 |
1.48e-34 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 127.84 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdgqLKVADKNQLRLLRTRLTMVFQH 100
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI---------AKISDAELREVRRKKIAMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 101 FNLWSHMTVLENVMEApIQVLGLSKQDARDRAVKYLAKVGIdERQQMKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
Cdd:PRK10070 115 FALMPHMTVLDNTAFG-MELAGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527036387 181 SALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQSPRLQQFLKG 254
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-244 |
1.49e-34 |
|
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: 123.94 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdGQLKVAdkn 85
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIvallgrngagKTTLLKAISGLLPPRSGSIRFDGEDI-------TGLPPH--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 qlRLLRTRLTMVFQHFNLWSHMTVLENVMeapiqvLGLSKQDARDRAVKYLAKVgiderqqmkY---PV----------H 152
Cdd:COG0410 74 --RIARLGIGYVPEGRRIFPSLTVEENLL------LGAYARRDRAEVRADLERV---------YelfPRlkerrrqragT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEE 232
Cdd:COG0410 137 LSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVL 216
|
250
....*....|..
gi 527036387 233 QGHPDEVLANPQ 244
Cdd:COG0410 217 EGTAAELLADPE 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
16-230 |
2.64e-34 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 123.06 E-value: 2.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKdgqlkvadknQLRLLRTRLT 95
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNR----------EVPFLRRQIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 96 MVFQHFNLWSHMTVLENVmEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALAMEPEVLL 175
Cdd:PRK10908 83 MIFQDHHLLMDRTVYDNV-AIPLIIAGASGDDIRRRVSAALDKVGLLDKAK-NFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 527036387 176 FDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKI 230
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-215 |
8.43e-34 |
|
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: 120.61 E-value: 8.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLvrdkdgqlkvaDKNQLRLLRTRLT 95
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDY-----------SRKGLLERRQRVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 96 MVFQHFN--LWShMTVLENVMEAPIQvLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALAMEPEV 173
Cdd:TIGR01166 72 LVFQDPDdqLFA-ADVDQDVAFGPLN-LGLSEAEVERRVREALTAVGASGLRE-RPTHCLSGGEKKRVAIAGAVAMRPDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 527036387 174 LLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFA 215
Cdd:TIGR01166 149 LLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-242 |
1.04e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 127.97 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 14 RY-GEHEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgQLKVADknqlrlLRT 92
Cdd:COG1132 348 SYpGDRPVLKDISLTIPPGETvalvgpsgsgKSTLVNLLLRFYDPTSGRILIDGVDIR-------DLTLES------LRR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 93 RLTMVFQHFNLWsHMTVLENvmeapiqvLGLSKQDA-RDRAVKYLAKVGIDERQqMKYP-----------VHLSGGQQQR 160
Cdd:COG1132 415 QIGVVPQDTFLF-SGTIREN--------IRYGRPDAtDEEVEEAAKAAQAHEFI-EALPdgydtvvgergVNLSGGQRQR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMGFARNVsNHVIFLHQGKIEEQGHPDEVL 240
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRNA-DRILVLDDGRIVEQGTHEELL 562
|
..
gi 527036387 241 AN 242
Cdd:COG1132 563 AR 564
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
44-181 |
1.30e-33 |
|
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: 118.90 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkvadKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEaPIQVLGL 123
Cdd:pfam00005 24 KSTLLKLIAGLLSPTEGTILLDGQDLT-------------DDERKSLRKEIGYVFQDPQLFPRLTVRENLRL-GLLLKGL 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036387 124 SKQDARDRAVKYLAKVGIDE---RQQMKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTS 181
Cdd:pfam00005 90 SKREKDARAEEALEKLGLGDladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
10-229 |
4.00e-33 |
|
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: 118.25 E-value: 4.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRYG--EHEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkvadKNQL 87
Cdd:cd03228 5 NVSFSYPgrPKPVLKDVSLTIKPGEKvaivgpsgsgKSTLLKLLLRLYDPTSGEILIDGVDLR-------------DLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 88 RLLRTRLTMVFQHFNLWShMTVLENVmeapiqvlglskqdardravkylakvgiderqqmkypvhLSGGQQQRVSIARAL 167
Cdd:cd03228 72 ESLRKNIAYVPQDPFLFS-GTIRENI---------------------------------------LSGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527036387 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMGFARNVsNHVIFLHQGK 229
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-234 |
1.04e-32 |
|
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: 118.75 E-value: 1.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 5 KLNVIdlhkRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdGQLKVADK 84
Cdd:cd03298 2 RLDKI----RFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-------TAAPPADR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 85 NqlrllrtrLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQDaRDRAVKYLAKVGIDERQQMKyPVHLSGGQQQRVSIA 164
Cdd:cd03298 71 P--------VSMLFQENNLFAHLTVEQNVGLGLSPGLKLTAED-RQAIEVALARVGLAGLEKRL-PGELSGGERQRVALA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036387 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQG 234
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-246 |
1.15e-32 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 121.35 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 22 KGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdgqLKVADKnQLRLLRTRLTMVFQH- 100
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL---------LGMKDD-EWRAVRSDIQMIFQDp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 101 -FNLWSHMTVLENVMEaPIQVL--GLSKQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
Cdd:PRK15079 108 lASLNPRMTIGEIIAE-PLRTYhpKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 178 EPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQSP 246
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHP 256
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
44-245 |
1.27e-32 |
|
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: 121.45 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVSGQNINLVRDKdgqlkvadknqlrllRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGL 123
Cdd:TIGR01187 9 KTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH---------------LRHINMVFQSYALFPHMTVEENV-AFGLKMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 124 SKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVG----EVLRIMQKLa 199
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQLEEFAD-RKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDqmqlELKTIQEQL- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 527036387 200 eeGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQS 245
Cdd:TIGR01187 151 --GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPAN 194
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-242 |
1.70e-32 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 124.49 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRY-GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEkPSEGSIVVSGQNINlvrdkdgQLKVADknql 87
Cdd:COG4988 341 DVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLlGFLP-PYSGSILINGVDLS-------DLDPAS---- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 88 rlLRTRLTMVFQH---FnlwsHMTVLENvmeapiqvLGLSKQDARDRAVKY-LAKVGIDE-----RQQMKYPVH-----L 153
Cdd:COG4988 409 --WRRQIAWVPQNpylF----AGTIREN--------LRLGRPDASDEELEAaLEAAGLDEfvaalPDGLDTPLGeggrgL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMGFARNvSNHVIFLHQGKIEEQ 233
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDGRIVEQ 552
|
....*....
gi 527036387 234 GHPDEVLAN 242
Cdd:COG4988 553 GTHEELLAK 561
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-244 |
1.78e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.84 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 3 ENKLNVIDLHKRYGE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkv 81
Cdd:PRK13647 2 DNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 82 aDKNQlRLLRTRLTMVFQHFN--LWShMTVLENVMEAPIQvLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQ 159
Cdd:PRK13647 71 -AENE-KWVRSKVGLVFQDPDdqVFS-STVWDDVAFGPVN-MGLDKDEVERRVEEALKAVRMWDFRD-KPPYHLSYGQKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPdEV 239
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SL 224
|
....*
gi 527036387 240 LANPQ 244
Cdd:PRK13647 225 LTDED 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-212 |
1.84e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 123.59 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRYGEHEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDGQlkvadknqlrl 89
Cdd:COG1129 9 GISKSFGGVKALDGVSLELRPGEVhallgengagKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQ----------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 90 lRTRLTMVFQHFNLWSHMTVLENVMeapiqvLG--------LSKQDARDRAVKYLAKVG--IDERQQMKypvHLSGGQQQ 159
Cdd:COG1129 78 -AAGIAIIHQELNLVPNLSVAENIF------LGreprrgglIDWRAMRRRARELLARLGldIDPDTPVG---DLSVAQQQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 527036387 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEM 212
Cdd:COG1129 148 LVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRL 200
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
13-238 |
2.48e-32 |
|
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: 119.80 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlVRDKDGqlkvadknqlrlLRT 92
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV--VREPRK------------VRR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 93 RLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALAMEPE 172
Cdd:TIGR01188 67 SIGIVPQYASVDEDLTGREN-LEMMGRLYGLPKDEAEERAEELLELFELGEAAD-RPVGTYSGGMRRRLDIAASLIHQPD 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527036387 173 VLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDE 238
Cdd:TIGR01188 145 VLFLDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
9-256 |
9.08e-32 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 119.45 E-value: 9.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 9 IDLHKRYGEHEVlkGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkDGQLKVadknQLR 88
Cdd:TIGR02142 3 ARFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF-----DSRKGI----FLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 89 LLRTRLTMVFQHFNLWSHMTVLENVmeapiqVLGLSKQDARDRAV---KYLAKVGIDERQQmKYPVHLSGGQQQRVSIAR 165
Cdd:TIGR02142 72 PEKRRIGYVFQEARLFPHLSVRGNL------RYGMKRARPSERRIsfeRVIELLGIGHLLG-RLPGRLSGGEKQRVAIGR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQ 244
Cdd:TIGR02142 145 ALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
250
....*....|..
gi 527036387 245 SPRLQQFLKGSL 256
Cdd:TIGR02142 225 LPWLAREDQGSL 236
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-250 |
1.29e-31 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 116.75 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdgqlkvADKN 85
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPL------------AAWS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLRTRLTMVfQHfnlwSHM----TVLENVMeapiqvLGL-----SKQDARDRAVKYLAKVGIDERQQMKYPvHLSGG 156
Cdd:COG4559 70 PWELARRRAVLP-QH----SSLafpfTVEEVVA------LGRaphgsSAAQDRQIVREALALVGLAHLAGRSYQ-TLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 157 QQQRVSIARALA-------MEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGK 229
Cdd:COG4559 138 EQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGR 217
|
250 260
....*....|....*....|.
gi 527036387 230 IEEQGHPDEVLanpQSPRLQQ 250
Cdd:COG4559 218 LVAQGTPEEVL---TDELLER 235
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-225 |
3.99e-31 |
|
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: 114.84 E-value: 3.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHE-------VLKGVSLQANAGDVISIIGSSGSGKSTFLRCI--NFLekPSEGSIVV--SGQNINLVRD 74
Cdd:COG4778 5 LEVENLSKTFTLHLqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYL--PDSGSILVrhDGGWVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 75 KDGQLkvadknqLRLLRTRLTMVFQHFNLWSHMTVLENVMEaPIQVLGLSKQDARDRAVKYLAKVGIDERQQMKYPVHLS 154
Cdd:COG4778 83 SPREI-------LALRRRTIGYVSQFLRVIPRVSALDVVAE-PLLERGVDREEARARARELLARLNLPERLWDLPPATFS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036387 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFL 225
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-230 |
4.74e-31 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 115.55 E-value: 4.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKdgqlkvadkn 85
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 qlrllrTRltMVFQHFNLWSHMTVLENVMeapiqvLGLsKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIAR 165
Cdd:PRK11247 83 ------TR--LMFQDARLLPWKKVIDNVG------LGL-KGQWRDAALQALAAVGLADRAN-EWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036387 166 ALAMEPEVLLFDEPTSALDPelvgeVLRI-MQKLAE-----EGKTMVVVTHEMGFARNVSNHVIFLHQGKI 230
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDA-----LTRIeMQDLIEslwqqHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-239 |
1.04e-30 |
|
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: 113.77 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvRDKDGQlkvadkn 85
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDIT--KLPPHE------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 qlrllRTRLTM--VFQHFNLWSHMTVLENVMeapiqvLGLSKQDARDRAvkylakvgIDERQQMKYPV----------HL 153
Cdd:TIGR03410 72 -----RARAGIayVPQGREIFPRLTVEENLL------TGLAALPRRSRK--------IPDEIYELFPVlkemlgrrggDL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGK-TMVVVTHEMGFARNVSNHVIFLHQGKIEE 232
Cdd:TIGR03410 133 SGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVA 212
|
....*..
gi 527036387 233 QGHPDEV 239
Cdd:TIGR03410 213 SGAGDEL 219
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
6-246 |
2.69e-30 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 113.78 E-value: 2.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEH---------EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQninlvrdkd 76
Cdd:COG4167 5 LEVRNLSKTFKYRtglfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 77 gQLKVAD-KNQLRLLRtrltMVFQHFN--LWSHMTVLEnVMEAPIQVL-GLSKQDARDRAVKYLAKVGIDERQQMKYPVH 152
Cdd:COG4167 76 -KLEYGDyKYRCKHIR----MIFQDPNtsLNPRLNIGQ-ILEEPLRLNtDLTAEEREERIFATLRLVGLLPEHANFYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIE 231
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
250
....*....|....*
gi 527036387 232 EQGHPDEVLANPQSP 246
Cdd:COG4167 230 EYGKTAEVFANPQHE 244
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
44-234 |
2.72e-30 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 112.39 E-value: 2.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVSGQNINlvrdkDGQLKVADKNQLRllrtRLTMVFQHFNLWSHMTVLENVmeapiqVLGL 123
Cdd:cd03297 36 KSTLLRCIAGLEKPDGGTIVLNGTVLF-----DSRKKINLPPQQR----KIGLVFQQYALFPHLNVRENL------AFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 124 SKQDA---RDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAE 200
Cdd:cd03297 101 KRKRNredRISVDELLDLLGLDHLLN-RYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....*
gi 527036387 201 E-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQG 234
Cdd:cd03297 180 NlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
10-238 |
2.93e-30 |
|
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: 112.46 E-value: 2.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlVRDKDGqlkvadknqlrl 89
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV--VREPRE------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 90 LRTRLTMVFQHFNLWSHMTVLENV-MEAPIQvlGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALA 168
Cdd:cd03265 71 VRRRIGIVFQDLSVDDELTGWENLyIHARLY--GVPGAERRERIDELLDFVGLLEAAD-RLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036387 169 MEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDE 238
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-230 |
2.94e-30 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 111.97 E-value: 2.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 8 VIDLHKRYGEH-EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLvrdkdgqlkvadknq 86
Cdd:cd03226 2 IENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA--------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 87 lRLLRTRLTMVFQH--FNLWSHmTVLENvmeapiqvLGLSKQDARD---RAVKYLAKVGIDERQQmKYPVHLSGGQQQRV 161
Cdd:cd03226 67 -KERRKSIGYVMQDvdYQLFTD-SVREE--------LLLGLKELDAgneQAETVLKDLDLYALKE-RHPLSLSGGQKQRL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKI 230
Cdd:cd03226 136 AIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-230 |
3.93e-30 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 110.21 E-value: 3.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQninlvrdkdgqlkvadkn 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 qlrllrtrltmvfqhfnlwshmtvlenvmeapiQVLGLSKQDARDRavkylakvGIderqqmkYPVH-LSGGQQQRVSIA 164
Cdd:cd03216 63 ---------------------------------EVSFASPRDARRA--------GI-------AMVYqLSVGERQMVEIA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527036387 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKI 230
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-211 |
4.35e-30 |
|
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: 111.42 E-value: 4.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKdgqlkvadkn 85
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEAlaltgpngsgKTTLLRILAGLLPPSAGEVLWNGEPIRDARED---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 qlrlLRTRLTMVFQHFNLWSHMTVLENV-MEApiQVLGLSKQDARDRAVkyLAKVGIDERQQmKYPVHLSGGQQQRVSIA 164
Cdd:COG4133 73 ----YRRRLAYLGHADGLKPELTVRENLrFWA--ALYGLRADREAIDEA--LEAVGLAGLAD-LPVRQLSAGQKRRVALA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 527036387 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHE 211
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-239 |
4.46e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 114.05 E-value: 4.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQ-----------AN-AGdvisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINL-V 72
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTvpkgeifgllgPNgAG------------KTTTIRIILGILAPDSGEVLWDGEPLDPeD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 73 RDKDG----------QLKVADknQLRLLrTRLTmvfqhfnlwshmtvlenvmeapiqvlGLSKQDARDRAVKYLAKVGID 142
Cdd:COG4152 70 RRRIGylpeerglypKMKVGE--QLVYL-ARLK--------------------------GLSKAEAKRRADEWLERLGLG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 143 ERQQMKypVH-LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNH 221
Cdd:COG4152 121 DRANKK--VEeLSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDR 198
|
250
....*....|....*...
gi 527036387 222 VIFLHQGKIEEQGHPDEV 239
Cdd:COG4152 199 IVIINKGRKVLSGSVDEI 216
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-247 |
6.96e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 113.02 E-value: 6.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAENKLNVIDLHKRYGE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDkdGQL 79
Cdd:PRK13636 1 MEDYILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRK--GLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 80 KvadknqlrlLRTRLTMVFQH--FNLWShMTVLENVMEAPIQvLGLSKQDARDRAVKYLAKVGIDERQQMkyPVH-LSGG 156
Cdd:PRK13636 79 K---------LRESVGMVFQDpdNQLFS-ASVYQDVSFGAVN-LKLPEDEVRKRVDNALKRTGIEHLKDK--PTHcLSFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGH 235
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN 225
|
250
....*....|..
gi 527036387 236 PDEVLANPQSPR 247
Cdd:PRK13636 226 PKEVFAEKEMLR 237
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-240 |
7.94e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 112.17 E-value: 7.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdGQLKVADkn 85
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPL-------ADWSPAE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 qlrlLRTRLTMVFQHFNLWSHMTVLEnVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQMKYPvHLSGGQQQRVSIAR 165
Cdd:PRK13548 74 ----LARRRAVLPQHSSLSFPFTVEE-VVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYP-QLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 166 ALA------MEPEVLLFDEPTSALDPELVGEVLRIMQKLA-EEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDE 238
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
..
gi 527036387 239 VL 240
Cdd:PRK13548 228 VL 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
8-244 |
1.07e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 112.39 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 8 VIDLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkvadKN 85
Cdd:PRK13632 10 VENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS-------------KE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLRTRLTMVFQH-FNLWSHMTV-------LENVMEAPiqvlglskQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQ 157
Cdd:PRK13632 77 NLKEIRKKIGIIFQNpDNQFIGATVeddiafgLENKKVPP--------KKMKDIIDDLAKKVGMEDYLD-KEPQNLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEG-KTMVVVTHEMGFARNvSNHVIFLHQGKIEEQGHP 236
Cdd:PRK13632 148 KQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKP 226
|
....*...
gi 527036387 237 DEVLANPQ 244
Cdd:PRK13632 227 KEILNNKE 234
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-244 |
1.10e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 111.27 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 5 KLNVIDLHKRYGEHEVLKGVSLQANAGDVisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdgqlkvadk 84
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIvgllgpngagKTTTFYMIVGLVKPDSGRIFLDGEDI--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 85 nqlrllrTRLTM----------------VFQHfnlwshMTVLENVMeAPIQVLGLSKQDARDRAVKYLAKVGIDE-RQQM 147
Cdd:COG1137 68 -------THLPMhkrarlgigylpqeasIFRK------LTVEDNIL-AVLELRKLSKKEREERLEELLEEFGITHlRKSK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 148 KYpvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGktM-VVVT-HemgfarNVS------ 219
Cdd:COG1137 134 AY--SLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERG--IgVLITdH------NVRetlgic 203
|
250 260
....*....|....*....|....*
gi 527036387 220 NHVIFLHQGKIEEQGHPDEVLANPQ 244
Cdd:COG1137 204 DRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-237 |
1.20e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.88 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYG----EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrDKDGqlkv 81
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV----TGPG---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 82 ADKNqlrllrtrltMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRV 161
Cdd:COG4525 76 ADRG----------VVFQKDALLPWLNVLDNV-AFGLRLRGVPKAERRARAEELLALVGLADFAR-RRIWQLSGGMRQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 162 SIARALAMEPEVLLFDEPTSALDpELVGEVlriMQKL-----AEEGKTMVVVTHEMGFARNVSNHVIFL--HQGKIEEQG 234
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALD-ALTREQ---MQELlldvwQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVERL 219
|
...
gi 527036387 235 HPD 237
Cdd:COG4525 220 ELD 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-239 |
1.25e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 115.89 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAENKLNVIDLHKRYGEHEVLKGVSLQAN------------AGdvisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQn 68
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRpgeihallgengAG------------KSTLMKILYGLYQPDSGEILIDGK- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 69 inlvrdkdgqlKVADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVM--EAPIQVLGLSKQDARDRAVKYLAKVGID---E 143
Cdd:COG3845 68 -----------PVRIRSPRDAIALGIGMVHQHFMLVPNLTVAENIVlgLEPTKGGRLDRKAARARIRELSERYGLDvdpD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 144 RqqmkyPVH-LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHV 222
Cdd:COG3845 137 A-----KVEdLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRV 211
|
250
....*....|....*..
gi 527036387 223 IFLHQGKIEEQGHPDEV 239
Cdd:COG3845 212 TVLRRGKVVGTVDTAET 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-234 |
1.43e-29 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 110.45 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQninlvrdkdgQLKVADKN 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK----------PLDIAARN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLRtrltmvfQHFNLWSHMTVLENVMEAPiQVLGLSKQDARDRAVKYLAKVGIDERQQMKYPvHLSGGQQQRVSIAR 165
Cdd:cd03269 71 RIGYLP-------EERGLYPKMKVIDQLVYLA-QLKGLKKEEARRRIDEWLERLELSEYANKRVE-ELSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQG 234
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-240 |
1.48e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 112.52 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlKVADKNQLRLLRTRLTMVFQ--HF 101
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVS---------STSKQKEIKPVRKKVGVVFQfpES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 102 NLWSHmTVLENVMEAPiQVLGLSKQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTS 181
Cdd:PRK13643 96 QLFEE-TVLKDVAFGP-QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 182 ALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVL 240
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-245 |
2.09e-29 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 113.40 E-value: 2.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAenKLNVIDLHKRY-GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgQL 79
Cdd:PRK11650 1 MA--GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN-------EL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 80 KVADKNqlrllrtrLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQDaRDRAVKYLAKV-GIDERQQMKyPVHLSGGQQ 158
Cdd:PRK11650 72 EPADRD--------IAMVFQNYALYPHMSVREN-MAYGLKIRGMPKAE-IEERVAEAARIlELEPLLDRK-PRELSGGQR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 159 QRVSIARALAMEPEVLLFDEPTSALDPEL-VGEVLRImQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHP 236
Cdd:PRK11650 141 QRVAMGRAIVREPAVFLFDEPLSNLDAKLrVQMRLEI-QRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTP 219
|
....*....
gi 527036387 237 DEVLANPQS 245
Cdd:PRK11650 220 VEVYEKPAS 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
10-250 |
2.88e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 110.56 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRYGEHEVLKGVSLQ-----------AN-AGdvisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDg 77
Cdd:COG4604 6 NVSKRYGGKVVLDDVSLTipkggitaligPNgAG------------KSTLLSMISRLLPPDSGEVLVDGLDVATTPSRE- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 78 qlkvadknqlrlLRTRLTMVFQ--HFNlwSHMTVLENVMeapiqvLG--------LSKQDAR--DRAVKYLAKVGIDERq 145
Cdd:COG4604 73 ------------LAKRLAILRQenHIN--SRLTVRELVA------FGrfpyskgrLTAEDREiiDEAIAYLDLEDLADR- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 146 qmkYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIF 224
Cdd:COG4604 132 ---YLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVA 208
|
250 260
....*....|....*....|....*.
gi 527036387 225 LHQGKIEEQGHPDEVLanpQSPRLQQ 250
Cdd:COG4604 209 MKDGRVVAQGTPEEII---TPEVLSD 231
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
6-249 |
3.20e-29 |
|
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: 110.69 E-value: 3.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVsgqninlvRDKDGQ----LKV 81
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATY--------IMRSGAelelYQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 82 ADKNQLRLLRTRLTMVFQHFNLWSHMTVLE--NVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQ 159
Cdd:TIGR02323 76 SEAERRRLMRTEWGFVHQNPRDGLRMRVSAgaNIGERLMAIGARHYGNIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDE 238
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQ 235
|
250
....*....|.
gi 527036387 239 VLANPQSPRLQ 249
Cdd:TIGR02323 236 VLDDPQHPYTQ 246
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-245 |
3.51e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 113.01 E-value: 3.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDkdgqlkvadkn 85
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP----------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 qlrlLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVlGLSKQDARDRAVKYLAKVGIDERQQMKyPVHLSGGQQQRVSIAR 165
Cdd:PRK11607 89 ----YQRPINMMFQSYALFPHMTVEQNIAFGLKQD-KLPKAEIASRVNEMLGLVHMQEFAKRK-PHQLSGGQRQRVALAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 166 ALAMEPEVLLFDEPTSALDPELVG----EVLRIMQKLaeeGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLA 241
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKKLRDrmqlEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
....
gi 527036387 242 NPQS 245
Cdd:PRK11607 240 HPTT 243
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-222 |
3.62e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 109.91 E-value: 3.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGE----HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgQLKV 81
Cdd:PRK11629 6 LQCDNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMS-------KLSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 82 ADKNQLRllRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQMKyPVHLSGGQQQRV 161
Cdd:PRK11629 79 AAKAELR--NQKLGFIYQFHHLLPDFTALENV-AMPLLIGKKKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527036387 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMGFARNVSNHV 222
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-252 |
4.84e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 114.42 E-value: 4.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKST----FLRCINflekpSEGSIVVSGQninlvrdkdgQLKVADKNQ 86
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQ----------PLHNLNRRQ 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 87 LRLLRTRLTMVFQHFN--LWSHMTVLENVMEApIQV--LGLSKQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQRVS 162
Cdd:PRK15134 357 LLPVRHRIQVVFQDPNssLNPRLNVLQIIEEG-LRVhqPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGK-TMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLA 241
Cdd:PRK15134 436 IARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFA 515
|
250
....*....|.
gi 527036387 242 NPQSPRLQQFL 252
Cdd:PRK15134 516 APQQEYTRQLL 526
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-233 |
7.76e-29 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 109.89 E-value: 7.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEH---------EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkd 76
Cdd:TIGR02769 3 LEVRDVTHTYRTGglfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLY------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 77 gQLkvaDKNQLRLLRTRLTMVFQH----FNlwSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQMKYPVH 152
Cdd:TIGR02769 77 -QL---DRKQRRAFRRDVQLVFQDspsaVN--PRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIE 231
Cdd:TIGR02769 151 LSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
..
gi 527036387 232 EQ 233
Cdd:TIGR02769 231 EE 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-253 |
1.59e-28 |
|
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: 113.32 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRY--GEHEVLKGVSLQANAGDvisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDgqlkvad 83
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGErvaivgpsgsgKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 84 knqlrlLRTRLTMVFQHFNLWsHMTVLENvmeapiqvLGLSKQDARD---RAVkyLAKVGIDE-----RQQMKYPVH--- 152
Cdd:COG4987 407 ------LRRRIAVVPQRPHLF-DTTLREN--------LRLARPDATDeelWAA--LERVGLGDwlaalPDGLDTWLGegg 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 --LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMGFARNVsNHVIFLHQGKI 230
Cdd:COG4987 470 rrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGLERM-DRILVLEDGRI 547
|
250 260
....*....|....*....|...
gi 527036387 231 EEQGHPDEVLAnpQSPRLQQFLK 253
Cdd:COG4987 548 VEQGTHEELLA--QNGRYRQLYQ 568
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-243 |
1.84e-28 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 108.01 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNI-NLVRDKdgqlkvadk 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMHK--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 85 nqlrllRTRLTMVF--QHFNLWSHMTVLENVMeAPIQVLGLSKQDARDRAVKYLAKVGIDE-RQQMKYpvHLSGGQQQRV 161
Cdd:cd03218 72 ------RARLGIGYlpQEASIFRKLTVEENIL-AVLEIRGLSKKEREEKLEELLEEFHITHlRKSKAS--SLSGGERRRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHemgfarNVS------NHVIFLHQGKIEEQGH 235
Cdd:cd03218 143 EIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDH------NVRetlsitDRAYIIYEGKVLAEGT 216
|
....*...
gi 527036387 236 PDEVLANP 243
Cdd:cd03218 217 PEEIAANE 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-243 |
3.43e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 108.35 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 12 HKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkvadKNQLRLLR 91
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT-------------KENIREVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 92 TRLTMVFQHFN--LWShMTVLENVMEAPIQvLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALAM 169
Cdd:PRK13652 78 KFVGLVFQNPDdqIFS-PTVEQDIAFGPIN-LGLDEETVAHRVSSALHMLGLEELRD-RVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527036387 170 EPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANP 243
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-242 |
3.63e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 108.64 E-value: 3.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGqninlvrdkdgqLKVADKNQLRLLRTRLTM 96
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG------------LDTSDEENLWDIRNKAGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 97 VFQH-FNLWSHMTVLENVMEAPiQVLGLSKQDARDRAVKYLAKVGIDERQqmKYPVH-LSGGQQQRVSIARALAMEPEVL 174
Cdd:PRK13633 90 VFQNpDNQIVATIVEEDVAFGP-ENLGIPPEEIRERVDESLKKVGMYEYR--RHAPHlLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 175 LFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMGFARNvSNHVIFLHQGKIEEQGHPDEVLAN 242
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-241 |
4.40e-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: 111.82 E-value: 4.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLE--KPSEGSIVVS----------------GQ 67
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHvalcekcgyverpskvGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 68 NINLVRDKDGQLKV----ADKNQLRLLRTRLTMVFQH-FNLWSHMTVLENVMEApIQVLGLSKQDARDRAVKYLAKVGID 142
Cdd:TIGR03269 81 PCPVCGGTLEPEEVdfwnLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEA-LEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 143 ERQqMKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRIMQKlaEEGKTMVVVTHEMGFARNVS 219
Cdd:TIGR03269 160 HRI-THIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtakLVHNALEEAVK--ASGISMVLTSHWPEVIEDLS 236
|
250 260
....*....|....*....|..
gi 527036387 220 NHVIFLHQGKIEEQGHPDEVLA 241
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
10-241 |
6.36e-28 |
|
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: 106.55 E-value: 6.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRYGEH-EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVrdkdgqlkvadknQLR 88
Cdd:cd03253 5 NVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV-------------TLD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 89 LLRTRLTMVFQHFNLWsHMTVLENVmeapiqvlGLSKQDARDRAVKYLAKVGIDERQQMKYP-----------VHLSGGQ 157
Cdd:cd03253 72 SLRRAIGVVPQDTVLF-NDTIGYNI--------RYGRPDATDEEVIEAAKAAQIHDKIMRFPdgydtivgergLKLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMGFARNvSNHVIFLHQGKIEEQGHPD 237
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHE 220
|
....
gi 527036387 238 EVLA 241
Cdd:cd03253 221 ELLA 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-243 |
7.97e-28 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 107.00 E-value: 7.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvRDKDGQlK 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI---EGLPGH-Q 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 81 VADKNqlrLLRTrltmvFQHFNLWSHMTVLENVMEAPIQVL------GL--------SKQDARDRAVKYLAKVGIDE--- 143
Cdd:PRK11300 77 IARMG---VVRT-----FQHVRLFREMTVIENLLVAQHQQLktglfsGLlktpafrrAESEALDRAATWLERVGLLEhan 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 144 RQQMkypvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHV 222
Cdd:PRK11300 149 RQAG----NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRI 224
|
250 260
....*....|....*....|.
gi 527036387 223 IFLHQGKIEEQGHPDEVLANP 243
Cdd:PRK11300 225 YVVNQGTPLANGTPEEIRNNP 245
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
44-243 |
8.98e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 107.38 E-value: 8.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVSGqninlvrdkdgqLKVADKNQLRLLRTRLTMVFQHFNL-WSHMTVLENVMEAPiQVLG 122
Cdd:PRK13644 41 KSTLALHLNGLLRPQKGKVLVSG------------IDTGDFSKLQGIRKLVGIVFQNPETqFVGRTVEEDLAFGP-ENLC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 123 LSKQDARDRAVKYLAKVGIdERQQMKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEG 202
Cdd:PRK13644 108 LPPIEIRKRVDRALAEIGL-EKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKG 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 527036387 203 KTMVVVTHEMGfARNVSNHVIFLHQGKIEEQGHPDEVLANP 243
Cdd:PRK13644 187 KTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-238 |
9.71e-28 |
|
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: 105.66 E-value: 9.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkvad 83
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 84 kNQLRLLRTRLTMVFQHFNLWSHMTVLENVM-EAPIQvlGLSKQDARDRAVKYLAKVGIdeRQQMKYPVH-LSGGQQQRV 161
Cdd:cd03263 68 -TDRKAARQSLGYCPQFDALFDELTVREHLRfYARLK--GLPKSEIKEEVELLLRVLGL--TDKANKRARtLSGGMKRKL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527036387 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDE 238
Cdd:cd03263 143 SLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-250 |
1.31e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 106.69 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEH---------EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkd 76
Cdd:PRK10419 4 LNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPL------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 77 GQLkvaDKNQLRLLRTRLTMVFQH----FNlwSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQMKYPVH 152
Cdd:PRK10419 77 AKL---NRAQRKAFRRDIQMVFQDsisaVN--PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKT-MVVVTHEMGFARNVSNHVIFLHQGKI- 230
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQIv 231
|
250 260
....*....|....*....|..
gi 527036387 231 EEQ--GHPDEvLANPQSPRLQQ 250
Cdd:PRK10419 232 ETQpvGDKLT-FSSPAGRVLQN 252
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-234 |
1.37e-27 |
|
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: 104.97 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGdVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKdgqlkvadkn 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 qlrlLRTRLTMVFQHFNLWSHMTVLENVmeAPIQVL-GLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIA 164
Cdd:cd03264 70 ----LRRRIGYLPQEFGVYPNFTVREFL--DYIAWLkGIPSKEVKARVDEVLELVNLGDRAK-KKIGSLSGGMRRRVGIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQG 234
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-234 |
1.39e-27 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 105.33 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 25 SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvsgqninlvrdkdgqlKVADKNQLRLLRTR--LTMVFQHFN 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSI-----------------KVNDQSHTGLAPYQrpVSMLFQENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 103 LWSHMTVLENV---MEAPIQVLGLSKQDARDRAvkylAKVGIDERQQmKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
Cdd:TIGR01277 81 LFAHLTVRQNIglgLHPGLKLNAEQQEKVVDAA----QQVGIADYLD-RLPEQLSGGQRQRVALARCLVRPNPILLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 527036387 180 TSALDPELVGEVLRIMQKLAEEGK-TMVVVTHEMGFARNVSNHVIFLHQGKIEEQG 234
Cdd:TIGR01277 156 FSALDPLLREEMLALVKQLCSERQrTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-253 |
1.67e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 106.64 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAENKLNVIDLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgQ 78
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS-------E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 79 LKVADknqlrlLRTRLTMVFQH-FNLWSHMTV-------LENVmeapiqvlGLSKQDARDRAVKYLAKVGIDERQQMKyP 150
Cdd:PRK13635 74 ETVWD------VRRQVGMVFQNpDNQFVGATVqddvafgLENI--------GVPREEMVERVDQALRQVGMEDFLNRE-P 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGK-TMVVVTHEMGFARNvSNHVIFLHQGK 229
Cdd:PRK13635 139 HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGE 217
|
250 260 270
....*....|....*....|....*....|....*
gi 527036387 230 IEEQGHPDEVLAN-----------PQSPRLQQFLK 253
Cdd:PRK13635 218 ILEEGTPEEIFKSghmlqeigldvPFSVKLKELLK 252
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
8-240 |
2.40e-27 |
|
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: 105.55 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 8 VIDLHK---RYGEHEVLKGVSLQ-----------AN-AGdvisiigssgsgKSTFLRCINFLEKPSEG-SIVVSGQninl 71
Cdd:COG1119 3 LLELRNvtvRRGGKTILDDISWTvkpgehwailgPNgAG------------KSTLLSLITGDLPPTYGnDVRLFGE---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 72 vrdKDGQLKVADknqlrlLRTRLTMV--FQHFNLWSHMTVLENVMEAPIQVLGLSKQ---DARDRAVKYLAKVGIDERQQ 146
Cdd:COG1119 67 ---RRGGEDVWE------LRKRIGLVspALQLRFPRDETVLDVVLSGFFDSIGLYREptdEQRERARELLELLGLAHLAD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 147 MKYPvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEG-KTMVVVTH---EM--GFarnvsN 220
Cdd:COG1119 138 RPFG-TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhveEIppGI-----T 211
|
250 260
....*....|....*....|
gi 527036387 221 HVIFLHQGKIEEQGHPDEVL 240
Cdd:COG1119 212 HVLLLKDGRVVAAGPKEEVL 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-252 |
3.09e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 105.50 E-value: 3.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFL-----EKPSEGSIVVSGQNINLVRdkdgqlk 80
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERR------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 81 vadkNQLRLLRTRLTMVFQHFNLWShMTVLENVMEApIQVLGLSKQDARDRAVKYLAKVGiDERQQMKYPVH-----LSG 155
Cdd:PRK14258 81 ----VNLNRLRRQVSMVHPKPNLFP-MSVYDNVAYG-VKIVGWRPKLEIDDIVESALKDA-DLWDEIKHKIHksaldLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGK-TMVVVTHEMGFARNVSNHVIFLHQ-----GK 229
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFFKGnenriGQ 233
|
250 260
....*....|....*....|...
gi 527036387 230 IEEQGHPDEVLANPQSPRLQQFL 252
Cdd:PRK14258 234 LVEFGLTKKIFNSPHDSRTREYV 256
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-241 |
6.13e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 105.25 E-value: 6.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLvrdkdgqlKVADKnQLRLLRTRLTM 96
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITH--------KTKDK-YIRPVRKRIGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 97 VFQhfnlWSHMTVLENVMEAPIQV----LGLSKQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQRVSIARALAMEPE 172
Cdd:PRK13646 90 VFQ----FPESQLFEDTVEREIIFgpknFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 173 VLLFDEPTSALDPELVGEVLRIMQKLA-EEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLA 241
Cdd:PRK13646 166 IIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-249 |
7.77e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 104.24 E-value: 7.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvsgqninLVRDKDGQLK----V 81
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV--------HYRMRDGQLRdlyaL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 82 ADKNQLRLLRTRLTMVFQHFNLWSHMTVLE--NVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQ 159
Cdd:PRK11701 79 SEAERRRLLRTEWGFVHQHPRDGLRMQVSAggNIGERLMAVGARHYGDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDE 238
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQ 238
|
250
....*....|.
gi 527036387 239 VLANPQSPRLQ 249
Cdd:PRK11701 239 VLDDPQHPYTQ 249
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-234 |
9.20e-27 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 103.22 E-value: 9.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRY----GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGqnINLVRDKdgqlkv 81
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 82 adknqlRLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQDARDRaVKYLAKVgIDERQQMKYPVH-LSGGQQQR 160
Cdd:cd03266 74 ------AEARRRLGFVSDSTGLYDRLTARENL-EYFAGLYGLKGDELTAR-LEELADR-LGMEELLDRRVGgFSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036387 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQG 234
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-241 |
1.82e-26 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 107.20 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRY-----GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVsgqninlvRDKDGQLK 80
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV--------RVGDEWVD 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 81 VADKNQLrlLRTRLT----MVFQHFNLWSHMTVLENVMEApIQvLGLSKQDARDRAVKYLAKVGIDERQQM----KYPVH 152
Cdd:TIGR03269 352 MTKPGPD--GRGRAKryigILHQEYDLYPHRTVLDNLTEA-IG-LELPDELARMKAVITLKMVGFDEEKAEeildKYPDE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR-IMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIE 231
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
250
....*....|
gi 527036387 232 EQGHPDEVLA 241
Cdd:TIGR03269 508 KIGDPEEIVE 517
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-254 |
2.94e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 103.31 E-value: 2.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 2 AENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdgqlKV 81
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI----------PA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 82 ADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQMKyPVHLSGGQQQRV 161
Cdd:PRK11831 74 MSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLM-PSELSGGMARRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVL 240
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQ 232
|
250
....*....|....
gi 527036387 241 ANPqSPRLQQFLKG 254
Cdd:PRK11831 233 ANP-DPRVRQFLDG 245
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-228 |
3.87e-26 |
|
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: 101.77 E-value: 3.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrDKDGQLKVadknqlrllrtrltMVFQH 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI----TEPGPDRM--------------VVFQN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 101 FNLWSHMTVLENVMEAPIQVL-GLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
Cdd:TIGR01184 63 YSLLPWLTVRENIALAVDRVLpDLSKSERRAIVEEHIALVGLTEAAD-KRPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 527036387 180 TSALDP----ELVGEVLRIMQklaEEGKTMVVVTHEMGFARNVSNHVIFLHQG 228
Cdd:TIGR01184 142 FGALDAltrgNLQEELMQIWE---EHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
13-244 |
4.31e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 104.73 E-value: 4.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDgqlkvadknqlrllrT 92
Cdd:PRK11000 11 KAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE---------------R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 93 RLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQDaRDRAVKYLAKV----GIDERQqmkyPVHLSGGQQQRVSIARALA 168
Cdd:PRK11000 76 GVGMVFQSYALYPHLSVAEN-MSFGLKLAGAKKEE-INQRVNQVAEVlqlaHLLDRK----PKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 169 MEPEVLLFDEPTSALDPEL----VGEVLRIMQKLaeeGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQ 244
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALrvqmRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
15-250 |
4.90e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 102.40 E-value: 4.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDgqlkvadknqlrlLRTRL 94
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-------------LARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 95 TMVFQHFNLWSHMTVLENVM--EAP-IQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALAMEP 171
Cdd:PRK11231 79 ALLPQHHLTPEGITVRELVAygRSPwLSLWGRLSAEDNARVNQAMEQTRINHLAD-RRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 172 EVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLanpqSPRLQQ 250
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM----TPGLLR 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-234 |
5.32e-26 |
|
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: 100.75 E-value: 5.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVsgqninlvrdkDGQLKVADKN 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF-----------DGKSYQKNIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRllrtRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQDArDRAvkyLAKVGIDERQQMKYPvHLSGGQQQRVSIAR 165
Cdd:cd03268 70 ALR----RIGALIEAPGFYPNLTAREN-LRLLARLLGIRKKRI-DEV---LDVVGLKDSAKKKVK-GFSLGMKQRLGIAL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQG 234
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-254 |
6.86e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 102.17 E-value: 6.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 2 AENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEK--PS---EGSIVVSGQNINlvrdkD 76
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLY-----A 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 77 GQLKVADknqlrlLRTRLTMVFQHFNLWSHmTVLENVMEAPiQVLGLsKQDARDRAVKYLAKVGI-DE-RQQMKYP-VHL 153
Cdd:PRK14243 82 PDVDPVE------VRRRIGMVFQKPNPFPK-SIYDNIAYGA-RINGY-KGDMDELVERSLRQAALwDEvKDKLKQSgLSL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMGFARNVSNHVIFLH------- 226
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNveltegg 231
|
250 260 270
....*....|....*....|....*....|
gi 527036387 227 --QGKIEEQGHPDEVLANPQSPRLQQFLKG 254
Cdd:PRK14243 232 grYGYLVEFDRTEKIFNSPQQQATRDYVSG 261
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-230 |
8.26e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 102.01 E-value: 8.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFL---EKPSEGSIVVSGQNINlvrdKDGQLKva 82
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQ----REGRLA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 83 dkNQLRLLRTRLTMVFQHFNLWSHMTVLENVMeapIQVLGLS----------KQDARDRAVKYLAKVGIDERQQMKYPVh 152
Cdd:PRK09984 79 --RDIRKSRANTGYIFQQFNLVNRLSVLENVL---IGALGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVST- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRIMQKlaEEGKTMVVVTHEMGFARNVSNHVIFLHQGK 229
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPEsarIVMDTLRDINQ--NDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
.
gi 527036387 230 I 230
Cdd:PRK09984 231 V 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-242 |
1.38e-25 |
|
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: 100.69 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTflrCINFLEK---PSEGSIVVSGQNINlvrdkdgqlkvadKNQLRLLRTR 93
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERfydPTSGEILLDGVDIR-------------DLNLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 94 LTMVFQHFNLWShMTVLENVmeapiqvlGLSKQDARDRAVKYLAKVGIDERQQMKYP-----------VHLSGGQQQRVS 162
Cdd:cd03249 79 IGLVSQEPVLFD-GTIAENI--------RYGKPDATDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMGFARNvSNHVIFLHQGKIEEQGHPDEVLAN 242
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-256 |
1.66e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.89 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 2 AENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDkdgqlkV 81
Cdd:PRK14246 7 AEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKD------I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 82 ADKNQLRLlRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLS-KQDARDRAVKYLAKVGI--DERQQMKYPV-HLSGGQ 157
Cdd:PRK14246 81 FQIDAIKL-RKEVGMVFQQPNPFPHLSIYDNI-AYPLKSHGIKeKREIKKIVEECLRKVGLwkEVYDRLNSPAsQLSGGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPD 237
Cdd:PRK14246 159 QQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSN 237
|
250
....*....|....*....
gi 527036387 238 EVLANPQSPRLQQFLKGSL 256
Cdd:PRK14246 238 EIFTSPKNELTEKYVIGRI 256
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-241 |
2.71e-25 |
|
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: 99.61 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKdgqlkvadknqlrLLRTRLT 95
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRK-------------SLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 96 MVFQHFNLWSHmTVLENVMeapiqvlgLSKQDARDRAVKYLAK-VGIDErQQMKYP-----------VHLSGGQQQRVSI 163
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIR--------LGRPNATDEEVIEAAKeAGAHD-FIMKLPngydtvlgengGNLSQGERQLLAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527036387 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLaEEGKTMVVVTHEMGFARNvSNHVIFLHQGKIEEQGHPDEVLA 241
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
13-241 |
5.37e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 99.00 E-value: 5.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 13 KRYGEHEVLKGVSLQANAGDVisiigssgSGKSTFLRCINFLEKPSEGSIVVSGqninlvrdkdgqlKVADknqlrLLrt 92
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESvgiigrngAGKSTLLKLIAGILEPTSGRVEVNG-------------RVSA-----LL-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 93 RLTMVFQhfnlwSHMTVLENV-MEApiQVLGLSKQDARDR--AVKYLAKVG--IDErqqmkyPV-HLSGGQQQRVSIARA 166
Cdd:COG1134 94 ELGAGFH-----PELTGRENIyLNG--RLLGLSRKEIDEKfdEIVEFAELGdfIDQ------PVkTYSSGMRARLAFAVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527036387 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLA 241
Cdd:COG1134 161 TAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-254 |
6.22e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 99.79 E-value: 6.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 2 AENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFL-EKPS----EGSIVVSGQNINLVRDkd 76
Cdd:PRK14271 18 AAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSgyrySGDVLLGGRSIFNYRD-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 77 gqlkvadknqLRLLRTRLTMVFQHFNLWShMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQMKY---PVHL 153
Cdd:PRK14271 96 ----------VLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQ 233
Cdd:PRK14271 165 SGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
250 260
....*....|....*....|.
gi 527036387 234 GHPDEVLANPQSPRLQQFLKG 254
Cdd:PRK14271 244 GPTEQLFSSPKHAETARYVAG 264
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-241 |
6.35e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 99.70 E-value: 6.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLvrdkdgqlkvaDKN 85
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY-----------SKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDE-RQQmkyPVH-LSGGQQQRVSI 163
Cdd:PRK13638 71 GLLALRQQVATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHfRHQ---PIQcLSHGQKKRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527036387 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLA 241
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
59-246 |
9.76e-25 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 100.18 E-value: 9.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 59 EGSIVVSGQNI-NLvrdkdgqlkvaDKNQLRLLRT-RLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQDARDRAVK 134
Cdd:PRK09473 73 GGSATFNGREIlNL-----------PEKELNKLRAeQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 135 YLAKVGIDE-RQQMK-YPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKT-MVVVTHE 211
Cdd:PRK09473 142 MLDAVKMPEaRKRMKmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHD 221
|
170 180 190
....*....|....*....|....*....|....*
gi 527036387 212 MGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQSP 246
Cdd:PRK09473 222 LGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHP 256
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-241 |
1.83e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 99.11 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdgqlk 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 81 vadKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQDARDRAVKYLAKVGIDERQQMKYPvHLSGGQQQR 160
Cdd:PRK13537 72 ---PSRARHARQRVGVVPQFDNLDPDFTVRENLLVFG-RYFGLSAAAARALVPPLLEFAKLENKADAKVG-ELSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 161 VSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRimqKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPD 237
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQarhLMWERLR---SLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPH 223
|
....
gi 527036387 238 EVLA 241
Cdd:PRK13537 224 ALIE 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
44-252 |
2.16e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 101.47 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVSGQNINLVRDkdgqlkvadkNQLRLLRTRLTMVFQ--HFNLWSHMTVLENVMEaPIQVL 121
Cdd:PRK10261 363 KSTTGRALLRLVESQGGEIIFNGQRIDTLSP----------GKLQALRRDIQFIFQdpYASLDPRQTVGDSIME-PLRVH 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 122 GLSKQD-ARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAE 200
Cdd:PRK10261 432 GLLPGKaAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQR 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 527036387 201 E-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQSPRLQQFL 252
Cdd:PRK10261 512 DfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-241 |
3.44e-24 |
|
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: 96.79 E-value: 3.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 14 RYG--EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVrdkdgqlkvaDKNQLRllr 91
Cdd:cd03252 9 RYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA----------DPAWLR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 92 TRLTMVFQHfNLWSHMTVLENVmeapiqvlGLSKQDARDRAVKYLAKVGIDERQQMKYP-----------VHLSGGQQQR 160
Cdd:cd03252 76 RQVGVVLQE-NVLFNRSIRDNI--------ALADPGMSMERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMGFARNvSNHVIFLHQGKIEEQGHPDEVL 240
Cdd:cd03252 147 IAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELL 224
|
.
gi 527036387 241 A 241
Cdd:cd03252 225 A 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
44-242 |
5.81e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 97.39 E-value: 5.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLekpsegSIVVSGQNInlVRDKDGQLKVADKNQLRLLRTRLTMVFQ--HFNLWSHmTVLENVMEAPIQvL 121
Cdd:PRK13645 50 KSTMIQLTNGL------IISETGQTI--VGDYAIPANLKKIKEVKRLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVN-L 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 122 GLSKQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AE 200
Cdd:PRK13645 120 GENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKE 199
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 527036387 201 EGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLAN 242
Cdd:PRK13645 200 YKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-243 |
1.00e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 98.38 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDGQLKVADKN 85
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QlrllRTRLTMVFqhfnlwSHMTVLEnvMEAPIQVLGLSKQDARDRAV--KYLAKVGIDerQQMKYPV-HLSGGQQQRVS 162
Cdd:PRK09536 84 Q----DTSLSFEF------DVRQVVE--MGRTPHRSRFDTWTETDRAAveRAMERTGVA--QFADRPVtSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLAN 242
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTA 229
|
.
gi 527036387 243 P 243
Cdd:PRK09536 230 D 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-212 |
1.74e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.54 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQninlvrdkdgqlKVADKN 85
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK------------PVEGPG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRllrtrlTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIAR 165
Cdd:PRK11248 70 AER------GVVFQNEGLLPWRNVQDNV-AFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEK-RYIWQLSGGQRQRVGIAR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 527036387 166 ALAMEPEVLLFDEPTSALDP---ELVGEVLriMQKLAEEGKTMVVVTHEM 212
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALDAftrEQMQTLL--LKLWQETGKQVLLITHDI 189
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-241 |
2.47e-23 |
|
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: 94.60 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 14 RYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvRDKdgqlkvadknQLRLLR 91
Cdd:cd03251 9 RYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV---RDY----------TLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 92 TRLTMVFQHFNLWSHmTVLENVMeapiqvlgLSKQDARDRAVKYLAKVGIDERQQMKYP-----------VHLSGGQQQR 160
Cdd:cd03251 76 RQIGLVSQDVFLFND-TVAENIA--------YGRPGATREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMGFARNvSNHVIFLHQGKIEEQGHPDEVL 240
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELL 224
|
.
gi 527036387 241 A 241
Cdd:cd03251 225 A 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-230 |
2.59e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.21 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 8 VIDLHKRYGEHEVLKGVSLQ-----------AN-AGdvisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQninlvrdk 75
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSinpgdriglvgRNgAG------------KSTLLKILAGELEPDSGEVSIPKG-------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 76 dgqlkvadknqlrllrTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQ----------------------------- 126
Cdd:COG0488 61 ----------------LRIGYLPQEPPLDDDLTVLDTVLDGDAELRALEAEleeleaklaepdedlerlaelqeefealg 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 127 --DARDRAVKYLAKVGIDERQQMKyPV-HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLRimQKLAEEGK 203
Cdd:COG0488 125 gwEAEARAEEILSGLGFPEEDLDR-PVsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESI-EWLE--EFLKNYPG 200
|
250 260
....*....|....*....|....*..
gi 527036387 204 TMVVVTHEMGFARNVSNHVIFLHQGKI 230
Cdd:COG0488 201 TVLVVSHDRYFLDRVATRILELDRGKL 227
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-215 |
3.14e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 94.08 E-value: 3.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 2 AENKLNVIDLHKRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNinlvrdkdg 77
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 78 qLKVADKNQLRLLRTR-LTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGG 156
Cdd:PRK10584 74 -LHQMDEEARAKLRAKhVGFVFQSFMLIPTLNALENV-ELPALLRGESSRQSRNGAKALLEQLGLGKRLD-HLPAQLSGG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFA 215
Cdd:PRK10584 151 EQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLA 210
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
20-241 |
3.40e-23 |
|
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: 98.10 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdgqlkvaDKNQLRLLRTRLTMVFQ 99
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDL-------------AGLDVQAVRRQLGVVLQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 100 HFNLWSHmTVLENVM-EAPIQVlglskqdarDRAVKYLAKVGIDER-QQMKYPVH---------LSGGQQQRVSIARALA 168
Cdd:TIGR03797 535 NGRLMSG-SIFENIAgGAPLTL---------DEAWEAARMAGLAEDiRAMPMGMHtvisegggtLSGGQRQRLLIARALV 604
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527036387 169 MEPEVLLFDEPTSALDPELVGEVlriMQKLAEEGKTMVVVTHEMGFARNvSNHVIFLHQGKIEEQGHPDEVLA 241
Cdd:TIGR03797 605 RKPRILLFDEATSALDNRTQAIV---SESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMA 673
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
7-241 |
4.79e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.80 E-value: 4.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 7 NVIDLHK---RYG---EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgQLK 80
Cdd:PRK13650 3 NIIEVKNltfKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT-------EEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 81 VADKnqlrllRTRLTMVFQH-FNLWSHMTVLENVMEApIQVLGLSKQDARDRAVKYLAKVGIDERQqMKYPVHLSGGQQQ 159
Cdd:PRK13650 76 VWDI------RHKIGMVFQNpDNQFVGATVEDDVAFG-LENKGIPHEEMKERVNEALELVGMQDFK-EREPARLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGfARNVSNHVIFLHQGKIEEQGHPDE 238
Cdd:PRK13650 148 RVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLD-EVALSDRVLVMKNGQVESTSTPRE 226
|
...
gi 527036387 239 VLA 241
Cdd:PRK13650 227 LFS 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-252 |
5.42e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.47 E-value: 5.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 17 EHEVLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLEKPS----EGSIVVSGQNinlvrdkdgqLKVADKNQLRLLR 91
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGES----------LLHASEQTLRGVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 92 -TRLTMVFQHfnLWSHMTVLENVMEAPIQVL----GLSKQDARDRAVKYLAKVGIdeRQQMK----YPVHLSGGQQQRVS 162
Cdd:PRK15134 91 gNKIAMIFQE--PMVSLNPLHTLEKQLYEVLslhrGMRREAARGEILNCLDRVGI--RQAAKrltdYPHQLSGGERQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLA 241
Cdd:PRK15134 167 IAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFS 246
|
250
....*....|.
gi 527036387 242 NPQSPRLQQFL 252
Cdd:PRK15134 247 APTHPYTQKLL 257
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
17-247 |
9.33e-23 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 96.86 E-value: 9.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgQLKVADknqlrlLRTRLTM 96
Cdd:TIGR03375 477 ETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIR-------QIDPAD------LRRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 97 VFQHFNLWsHMTVLENVMeapiqvlgLSKQDARDRAV-KYLAKVGIDE-----RQQMKYPVH-----LSGGQQQRVSIAR 165
Cdd:TIGR03375 544 VPQDPRLF-YGTLRDNIA--------LGAPYADDEEIlRAAELAGVTEfvrrhPDGLDMQIGergrsLSGGQRQAVALAR 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMGFARNVsNHVIFLHQGKIEEQGHPDEVLANPQS 245
Cdd:TIGR03375 615 ALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLLDLV-DRIIVMDNGRIVADGPKDQVLEALRK 692
|
..
gi 527036387 246 PR 247
Cdd:TIGR03375 693 GR 694
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-234 |
1.69e-22 |
|
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: 91.88 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdGQLKVADknqlrlLRTRLTM 96
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI-------RQLDPAD------LRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 97 VFQHFNLWSHmTVLENVMeapiqvlgLSKQDARDRAVKYLAKV-GIDE--RQQ---MKYPV-----HLSGGQQQRVSIAR 165
Cdd:cd03245 83 VPQDVTLFYG-TLRDNIT--------LGAPLADDERILRAAELaGVTDfvNKHpngLDLQIgergrGLSGGQRQAVALAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036387 166 ALAMEPEVLLFDEPTSALDPElvGEVlRIMQKLAE--EGKTMVVVTHEMGFARNVsNHVIFLHQGKIEEQG 234
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMN--SEE-RLKERLRQllGDKTLIIITHRPSLLDLV-DRIIVMDSGRIVADG 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-216 |
1.73e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.14 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGqninlvrdkdgqlkvadknqlrllRTR 93
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG------------------------GAR 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 94 LTMVFQHFNL-WS-HMTVLENVMEAPIQVLGLSKQ-DARDRAV--KYLAKVGIDERQqmKYPVH-LSGGQQQRVSIARAL 167
Cdd:NF040873 57 VAYVPQRSEVpDSlPLTVRDLVAMGRWARRGLWRRlTRDDRAAvdDALERVGLADLA--GRQLGeLSGGQRQRALLAQGL 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 527036387 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFAR 216
Cdd:NF040873 135 AQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVR 183
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
86-252 |
2.27e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 95.69 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLR-TRLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQM--KYPVHLSGGQQQR 160
Cdd:PRK10261 97 QMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTIlsRYPHQLSGGMRQR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVV-VTHEMGFARNVSNHVIFLHQGKIEEQGHPDEV 239
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIfITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
170
....*....|...
gi 527036387 240 LANPQSPRLQQFL 252
Cdd:PRK10261 257 FHAPQHPYTRALL 269
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-230 |
3.34e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.07 E-value: 3.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYG-----EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgQLK 80
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT-------KLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 81 VADknqlrllRTRL-TMVFQHFNL--WSHMTVLENVMEA-------PIQvLGLSKQDaRDRAVKYLAKVGIDERQQMKYP 150
Cdd:COG1101 75 EYK-------RAKYiGRVFQDPMMgtAPSMTIEENLALAyrrgkrrGLR-RGLTKKR-RELFRELLATLGLGLENRLDTK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 151 V-HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGK-TMVVVTHEMGFARNVSNHVIFLHQG 228
Cdd:COG1101 146 VgLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNRLIMMHEG 225
|
..
gi 527036387 229 KI 230
Cdd:COG1101 226 RI 227
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
79-253 |
3.44e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 93.27 E-value: 3.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 79 LKVADKNQLRLLRTRLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGI-DERQQMK-YPVHLS 154
Cdd:PRK11022 76 QRISEKERRNLVGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpDPASRLDvYPHQLS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAE-EGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQ 233
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
170 180
....*....|....*....|
gi 527036387 234 GHPDEVLANPQSPRLQQFLK 253
Cdd:PRK11022 236 GKAHDIFRAPRHPYTQALLR 255
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-225 |
1.76e-21 |
|
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: 93.12 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgQLKVADknqlrlLRTRLT 95
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA-------DADADS------WRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 96 MVFQHFNLWSHmTVLENVmeapiqvlGLSKQDARDRAVK-YLAKVGIDE----RQQM------KYPVHLSGGQQQRVSIA 164
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENI--------RLARPDASDAEIReALERAGLDEfvaaLPQGldtpigEGGAGLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036387 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMGFARNVsNHVIFL 225
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
44-244 |
3.01e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 91.09 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVSG-------QNINLVRDKdgqlkvadknqlrllrTRLTMVFQHFNLWSHMTVLENVMea 116
Cdd:PRK11144 37 KTSLINAISGLTRPQKGRIVLNGrvlfdaeKGICLPPEK----------------RRIGYVFQDARLFPHYKVRGNLR-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 117 piqvLGLSKQDAR--DRAVKYLakvGID---ERqqmkYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEV 191
Cdd:PRK11144 99 ----YGMAKSMVAqfDKIVALL---GIEpllDR----YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 527036387 192 LRIMQKLAEEGKT-MVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQ 244
Cdd:PRK11144 168 LPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-232 |
3.66e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.05 E-value: 3.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQ-----------AN-AGdvisiigssgsgKSTFLRCINFLEKPSEGSIVVsGQNinlvr 73
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRidrgdrigligPNgAG------------KSTLLKLLAGELEPDSGTVKL-GET----- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 74 dkdgqLKVA--DKNQlrllrtrltmvfQHFNLwsHMTVLENVME-APiqvlGLSKQDARDravkYLAKVGIDERQQMKyP 150
Cdd:COG0488 378 -----VKIGyfDQHQ------------EELDP--DKTVLDELRDgAP----GGTEQEVRG----YLGRFLFSGDDAFK-P 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 151 VH-LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLriMQKLAE-EGkTMVVVTHEMGFARNVSNHVIFLHQG 228
Cdd:COG0488 430 VGvLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETL-EAL--EEALDDfPG-TVLLVSHDRYFLDRVATRILEFEDG 505
|
....
gi 527036387 229 KIEE 232
Cdd:COG0488 506 GVRE 509
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
44-244 |
8.91e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 88.70 E-value: 8.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKP---SEGSIVVSGQNINlvrdkdgQLKVADknqlrlLRTRLTMVFQH-FNLWSHMTVLENVmeapiq 119
Cdd:PRK13640 46 KSTISKLINGLLLPddnPNSKITVDGITLT-------AKTVWD------IREKVGIVFQNpDNQFVGATVGDDV------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 120 VLGL-SKQDARDRAVK----YLAKVGIDERQQMKyPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRI 194
Cdd:PRK13640 107 AFGLeNRAVPRPEMIKivrdVLADVGMLDYIDSE-PANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 527036387 195 MQKLAEE-GKTMVVVTHEMGFArNVSNHVIFLHQGKIEEQGHPDEVLANPQ 244
Cdd:PRK13640 186 IRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
44-241 |
1.13e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 87.33 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVSGQninlvrdkdgqlkvaDKNQLRLLRTRLTMVFQHFNLWSHMTVLENVmeapiqVLGL 123
Cdd:PRK10771 38 KSTLLNLIAGFLTPASGSLTLNGQ---------------DHTTTPPSRRPVSMLFQENNLFSHLTVAQNI------GLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 124 S-----KQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL 198
Cdd:PRK10771 97 NpglklNAAQREKLHAIARQMGIEDLLA-RLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 527036387 199 AEEGK-TMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLA 241
Cdd:PRK10771 176 CQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
44-239 |
1.47e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.88 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkvadKNQLRLLRTRLTMVFQH---------------FNLWSHMT 108
Cdd:PRK13648 48 KSTIAKLMIGIEKVKSGEIFYNNQAIT-------------DDNFEKLRKHIGIVFQNpdnqfvgsivkydvaFGLENHAV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 109 VLENVMEAPIQVLglSKQDARDRAvkylakvgiDERqqmkyPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELV 188
Cdd:PRK13648 115 PYDEMHRRVSEAL--KQVDMLERA---------DYE-----PNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 527036387 189 GEVLRIMQKLAEEGK-TMVVVTHEMGFARNvSNHVIFLHQGKIEEQGHPDEV 239
Cdd:PRK13648 179 QNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-251 |
1.62e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 90.27 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRY--GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDgqlkvad 83
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA------- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 84 knqlrlLRTRLTMVFQHFNLWSHmTVLENvmeapiqvLGLSKQDARD-RAVKYLAKVGIDE----------------RQq 146
Cdd:PRK11160 412 ------LRQAISVVSQRVHLFSA-TLRDN--------LLLAAPNASDeALIEVLQQVGLEKlleddkglnawlgeggRQ- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 147 mkypvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMgFARNVSNHVIFLH 226
Cdd:PRK11160 476 ------LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRL-TGLEQFDRICVMD 547
|
250 260
....*....|....*....|....*
gi 527036387 227 QGKIEEQGHPDEVLAnpQSPRLQQF 251
Cdd:PRK11160 548 NGQIIEQGTHQELLA--QQGRYYQL 570
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
14-241 |
2.54e-20 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 89.80 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 14 RYGEH--EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNinlvrdkdgqLKVADKNQLRllr 91
Cdd:TIGR01846 464 RYAPDspEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVD----------LAIADPAWLR--- 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 92 TRLTMVFQHFNLWSHmTVLENVmeapiqvlGLSKQDARDRAVKYLAKVG------IDERQQMKYPV-----HLSGGQQQR 160
Cdd:TIGR01846 531 RQMGVVLQENVLFSR-SIRDNI--------ALCNPGAPFEHVIHAAKLAgahdfiSELPQGYNTEVgekgaNLSGGQRQR 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMGFARNvSNHVIFLHQGKIEEQGHPDEVL 240
Cdd:TIGR01846 602 IAIARALVGNPRILIFDEATSALDYESEALIMRNMREIC-RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELL 679
|
.
gi 527036387 241 A 241
Cdd:TIGR01846 680 A 680
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
107-230 |
2.74e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.31 E-value: 2.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 107 MTVLENVMEAPIQVLG----LSKQDARDRAVKYLAKVGI---DERQQMKypvHLSGGQQQRVSIARALAMEPEVLLFDEP 179
Cdd:COG1129 345 LSIRENITLASLDRLSrgglLDRRRERALAEEYIKRLRIktpSPEQPVG---NLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 527036387 180 TSALDpelVG---EVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKI 230
Cdd:COG1129 422 TRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
150-230 |
4.91e-20 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 84.41 E-value: 4.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 150 PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGK 229
Cdd:cd03215 102 SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
.
gi 527036387 230 I 230
Cdd:cd03215 182 I 182
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-248 |
1.13e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.95 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLvrdkdgqLKVADKn 85
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISL-------LPLHAR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 qlrlLRTRLTMVFQHFNLWSHMTVLENVMeAPIQVL-GLSKQDARDRAVKYLAKVGIDE-RQQMKYPvhLSGGQQQRVSI 163
Cdd:PRK10895 76 ----ARRGIGYLPQEASIFRRLSVYDNLM-AVLQIRdDLSAEQREDRANELMEEFHIEHlRDSMGQS--LSGGERRRVEI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANP 243
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
....*
gi 527036387 244 QSPRL 248
Cdd:PRK10895 229 HVKRV 233
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
44-230 |
1.79e-19 |
|
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: 83.37 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCInflekpsegsivvSGQNINLvRDKdGQLKVADKNQ-LRLLRTRLTMVFQHFNLWSHMTVLENVMeapiqvlg 122
Cdd:cd03213 48 KSTLLNAL-------------AGRRTGL-GVS-GEVLINGRPLdKRSFRKIIGYVPQDDILHPTLTVRETLM-------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 123 lskqdardravkYLAKVgideRQqmkypvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEG 202
Cdd:cd03213 105 ------------FAAKL----RG-------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTG 161
|
170 180 190
....*....|....*....|....*....|..
gi 527036387 203 KTMVVVTH----EMgFarNVSNHVIFLHQGKI 230
Cdd:cd03213 162 RTIICSIHqpssEI-F--ELFDKLLLLSQGRV 190
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-210 |
2.32e-19 |
|
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: 86.65 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRY-GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDgqlkvadk 84
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE-------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 85 nqlrlLRTRLTMVFQHFNLWsHMTVLENVMeapiqvlgLSKQDARDRAV-KYLAKVG----IDERQQ-MKYPVH-----L 153
Cdd:TIGR02868 407 -----VRRRVSVCAQDAHLF-DTTVRENLR--------LARPDATDEELwAALERVGladwLRALPDgLDTVLGeggarL 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 527036387 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKlAEEGKTMVVVTH 210
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-222 |
7.41e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 82.14 E-value: 7.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCIN-FLEKP--SEGSIVVSGQNINlvrdkdgqlkva 82
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRLT------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 83 dknQLRLLRTRLTMVFQHFNLWSHMTVLENVMEApiqvL--GLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQR 160
Cdd:COG4136 70 ---ALPAEQRRIGILFQDDLLFPHLSVGENLAFA----LppTIGRAQRRARVEQALEEAGLAGFAD-RDPATLSGGQRAR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527036387 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLR-IMQKLAEEGKTMVVVTHEMGFARNVSNHV 222
Cdd:COG4136 142 VALLRALLAEPRALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEEDAPAAGRVL 204
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
153-247 |
7.45e-19 |
|
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: 85.18 E-value: 7.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvGE--VLRIMQKLAEEGKTMVVVTHEMGfARNVSNHVIFLHQGKI 230
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDE--GEaaLAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRV 544
|
90
....*....|....*..
gi 527036387 231 EEQGHPDEVLANPQSPR 247
Cdd:COG4618 545 QAFGPRDEVLARLARPA 561
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-240 |
8.04e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.11 E-value: 8.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVsgqninlvrdkdgqLK 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV--------------LG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 81 VADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQDArDRAVKYLAKVGIDERQQMKYPVHLSGGQQQR 160
Cdd:PRK13536 103 VPVPARARLARARIGVVPQFDNLDLEFTVRENLLVFG-RYFGMSTREI-EAVIPSLLEFARLESKADARVSDLSGGMKRR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 161 VSIARALAMEPEVLLFDEPTSALDP---ELVGEVLRimqKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPD 237
Cdd:PRK13536 181 LTLARALINDPQLLILDEPTTGLDPharHLIWERLR---SLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPH 257
|
...
gi 527036387 238 EVL 240
Cdd:PRK13536 258 ALI 260
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-234 |
8.63e-19 |
|
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: 82.20 E-value: 8.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 12 HKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRdkdgqlkvadknqlrllr 91
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG------------------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 92 trLTMVFQhfnlwSHMTVLENV-MEAPIqvLGLSKQDARDR--AVKYLAKVG--IDErqqmkyPV-HLSGGQQQRVSIAR 165
Cdd:cd03220 91 --LGGGFN-----PELTGRENIyLNGRL--LGLSRKEIDEKidEIIEFSELGdfIDL------PVkTYSSGMKARLAFAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQG 234
Cdd:cd03220 156 ATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
44-244 |
1.23e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.53 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVSGQninlvrdkdgQLKVADknqLRLLRTRLTMVFQH-FNLWSHMTVLENVMEAPIQV-L 121
Cdd:PRK15112 52 KSTLAKMLAGMIEPTSGELLIDDH----------PLHFGD---YSYRSQRIRMIFQDpSTSLNPRQRISQILDFPLRLnT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 122 GLSKQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE 201
Cdd:PRK15112 119 DLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEK 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 527036387 202 -GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQ 244
Cdd:PRK15112 199 qGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPL 242
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-230 |
1.99e-18 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 79.95 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 14 RYG--EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRdkdgqlkvadknqLRLLR 91
Cdd:cd03246 9 RYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD-------------PNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 92 TRLTMVFQHFNLWSHmTVLENVmeapiqvlglskqdardravkylakvgiderqqmkypvhLSGGQQQRVSIARALAMEP 171
Cdd:cd03246 76 DHVGYLPQDDELFSG-SIAENI---------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036387 172 EVLLFDEPTSALDPElvGE--VLRIMQKLAEEGKTMVVVTHEMGFARNVsNHVIFLHQGKI 230
Cdd:cd03246 116 RILVLDEPNSHLDVE--GEraLNQAIAALKAAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-241 |
4.54e-18 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 83.23 E-value: 4.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 2 AENKLNVIDLHKRYG--EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRdkdgql 79
Cdd:TIGR02203 327 ARGDVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT------ 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 80 kvadknqLRLLRTRLTMVFQHFNLWSHmTVLENV-MEAPIQVlglSKQDARDRAVKYLAKVGIDerqQMKYPVH------ 152
Cdd:TIGR02203 401 -------LASLRRQVALVSQDVVLFND-TIANNIaYGRTEQA---DRAEIERALAAAYAQDFVD---KLPLGLDtpigen 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 ---LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVL-RIMQklaeeGKTMVVVTHEMGFARNvSNHVIFL 225
Cdd:TIGR02203 467 gvlLSGGQRQRLAIARALLKDAPILILDEATSALDNEserLVQAALeRLMQ-----GRTTLVIAHRLSTIEK-ADRIVVM 540
|
250
....*....|....*.
gi 527036387 226 HQGKIEEQGHPDEVLA 241
Cdd:TIGR02203 541 DDGRIVERGTHNELLA 556
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-240 |
4.92e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.80 E-value: 4.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlKVADKNQLRllrtRL 94
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ---------HYASKEVAR----RI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 95 TMVFQHFNLWSHMTVLENVMEA--PIQVL--GLSKQDArDRAVKYLAKVGIDERQQMKYPVhLSGGQQQRVSIARALAME 170
Cdd:PRK10253 84 GLLAQNATTPGDITVQELVARGryPHQPLftRWRKEDE-EAVTKAMQATGITHLADQSVDT-LSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036387 171 PEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVL 240
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-243 |
5.18e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 83.23 E-value: 5.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 20 VLKGVSLQANAGDVISIIGSSGSGKSTflrCINFLE---KPSEGSIVVSGQNINlvrdkdgqlkvadKNQLRLLRTRLTM 96
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQnlyQPTGGQVLLDGVPLV-------------QYDHHYLHRQVAL 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 97 VFQHFNLWSHmTVLENV--------MEapiQVLGLSKQDARDRAVKYLAKvGIDERQQMKyPVHLSGGQQQRVSIARALA 168
Cdd:TIGR00958 560 VGQEPVLFSG-SVRENIaygltdtpDE---EIMAAAKAANAHDFIMEFPN-GYDTEVGEK-GSQLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527036387 169 MEPEVLLFDEPTSALDpelvGEVLRIMQKLAE-EGKTMVVVTHEMGFARNvSNHVIFLHQGKIEEQGHPDEVLANP 243
Cdd:TIGR00958 634 RKPRVLILDEATSALD----AECEQLLQESRSrASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-234 |
8.74e-18 |
|
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: 78.51 E-value: 8.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDkdgqlkvad 83
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 84 knqlrLLRTRLTMVFQHFNLWShMTVLENVMEapiqvlglskqdardravkylakvgiderqqmkypvHLSGGQQQRVSI 163
Cdd:cd03247 72 -----ALSSLISVLNQRPYLFD-TTLRNNLGR------------------------------------RFSGGERQRLAL 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036387 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEgKTMVVVTHEMGFARNVsNHVIFLHQGKIEEQG 234
Cdd:cd03247 110 ARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-212 |
8.94e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.27 E-value: 8.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDGqlkvadknqlrlLRTRLTMVFQH 100
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAA------------LAAGVAIIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 101 FNLWSHMTVLENVMeapiqvLG--------LSKQDARDRAVKYLAKVG--IDERQQMKYpvhLSGGQQQRVSIARALAME 170
Cdd:PRK11288 88 LHLVPEMTVAENLY------LGqlphkggiVNRRLLNYEAREQLEHLGvdIDPDTPLKY---LSIGQRQMVEIAKALARN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 527036387 171 PEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEM 212
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRM 200
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
121-246 |
2.23e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.97 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 121 LGLSKQDARDRAVKYLAKVGIDERQQM--KYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL 198
Cdd:PRK10418 107 LALGKPADDATLTAALEAVGLENAARVlkLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESI 186
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 527036387 199 AEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQSP 246
Cdd:PRK10418 187 VQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-240 |
2.32e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 77.57 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLE--KPSEGSIVVSGQNINlvrdkdgQLKVAD 83
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDIT-------DLPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 84 KNqlrllRTRLTMVFQHfnlwshmtvlenvmeaPIQVLGLSKQDardravkYLAKVGiderqqmkypVHLSGGQQQRVSI 163
Cdd:cd03217 74 RA-----RLGIFLAFQY----------------PPEIPGVKNAD-------FLRYVN----------EGFSGGEKKRNEI 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527036387 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTH-EMGFARNVSNHVIFLHQGKIEEQGHPDEVL 240
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDKELAL 193
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
151-252 |
2.90e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 80.94 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVsNHVIFLHQGKI 230
Cdd:PLN03130 739 VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMI 817
|
90 100
....*....|....*....|..
gi 527036387 231 EEQGHPDEVLANpqSPRLQQFL 252
Cdd:PLN03130 818 KEEGTYEELSNN--GPLFQKLM 837
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-250 |
4.83e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.29 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDGQLKVAdknqlrllrtrltMVFQ 99
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVA-------------YLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 100 HFNLWSHMTVLENVM--EAPIQ-VLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALAMEPEVLLF 176
Cdd:PRK10575 93 QLPAAEGMTVRELVAigRYPWHgALGRFGAADREKVEEAISLVGLKPLAH-RLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527036387 177 DEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLanpQSPRLQQ 250
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM---RGETLEQ 243
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-241 |
4.84e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.01 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 21 LKGVSLQANAGDVISIIGSSGSGKSTFlrcINFLEK---PSEGSIVVSGQNINLVrdkdgqlkvadknQLRLLRTRLTMV 97
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRvfdPQSGRILIDGTDIRTV-------------TRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 98 FQHFNLWSHmTVLENvmeapiqvLGLSKQDARD----RAVKYLAKVGIDERQQMKYPVH-------LSGGQQQRVSIARA 166
Cdd:PRK13657 415 FQDAGLFNR-SIEDN--------IRVGRPDATDeemrAAAERAQAHDFIERKPDGYDTVvgergrqLSGGERQRLAIARA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527036387 167 LAMEPEVLLFDEPTSALDPELvgEVlRIMQKLAE--EGKTMVVVTHEMGFARNvSNHVIFLHQGKIEEQGHPDEVLA 241
Cdd:PRK13657 486 LLKDPPILILDEATSALDVET--EA-KVKAALDElmKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVA 558
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
7-244 |
9.80e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.44 E-value: 9.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 7 NVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkvadKNQ 86
Cdd:PRK13642 9 NLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT-------------AEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 87 LRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQqMKYPVHLSGGQQQRVSIARA 166
Cdd:PRK13642 76 VWNLRRKIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFK-TREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGK-TMVVVTHEMGFARNvSNHVIFLHQGKIEEQGHPDEVLANPQ 244
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
5-242 |
1.05e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.84 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 5 KLNVIDLHkrYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkvaDK 84
Cdd:PRK11614 7 SFDKVSAH--YGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT------------DW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 85 NQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQDARDRAVKYLAKvgIDERQQMKYPVhLSGGQQQRVSIA 164
Cdd:PRK11614 73 QTAKIMREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGT-MSGGEQQMLAIG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527036387 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLAN 242
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
13-238 |
2.49e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.17 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPS---EGSIVVSGQNINL--VRDKDGQLKVADKNqL 87
Cdd:TIGR00955 33 RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAkeMRAISAYVQQDDLF-I 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 88 RLLRTRLTMVFQ-HFNLWSHMTVLENV--MEAPIQVLGLskQDARDravkylAKVGIDERqqMKypvHLSGGQQQRVSIA 164
Cdd:TIGR00955 112 PTLTVREHLMFQaHLRMPRRVTKKEKRerVDEVLQALGL--RKCAN------TRIGVPGR--VK---GLSGGERKRLAFA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTH-------EMgFarnvsNHVIFLHQGKIEEQGHPD 237
Cdd:TIGR00955 179 SELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHqpsselfEL-F-----DKIILMAEGRVAYLGSPD 252
|
.
gi 527036387 238 E 238
Cdd:TIGR00955 253 Q 253
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-234 |
4.47e-16 |
|
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: 74.61 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKPS--EGSIVVSGQNinlvRDKDgqlkvadknqlrLLRTRLTM 96
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGGttSGQILFNGQP----RKPD------------QFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 97 VFQHFNLWSHMTVLENVMEAPIQVLGLSKQDARDR---AVKYLAKVGiDERQQMKYPVHLSGGQQQRVSIARALAMEPEV 173
Cdd:cd03234 86 VRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKkrvEDVLLRDLA-LTRIGGNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036387 174 LLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMG---FarNVSNHVIFLHQGKIEEQG 234
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIVYSG 226
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
67-246 |
4.92e-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: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 67 QNINLvrdkdgqLKVADKNQLRLLRTRLTMVFQHFNlwSHMTVLENVMEAPIQVLGLS---------KQDARDRAVKYLA 137
Cdd:COG4170 71 NGIDL-------LKLSPRERRKIIGREIAMIFQEPS--SCLDPSAKIGDQLIEAIPSWtfkgkwwqrFKWRKKRAIELLH 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 138 KVGI-DERQQMK-YPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVV-VTHEMGF 214
Cdd:COG4170 142 RVGIkDHKDIMNsYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILlISHDLES 221
|
170 180 190
....*....|....*....|....*....|..
gi 527036387 215 ARNVSNHVIFLHQGKIEEQGHPDEVLANPQSP 246
Cdd:COG4170 222 ISQWADTITVLYCGQTVESGPTEQILKSPHHP 253
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
44-236 |
6.73e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 76.98 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdgqlkvadKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPiQVLGL 123
Cdd:TIGR01257 969 KTTTLSILTGLLPPTSGTVLVGGKDI--------------ETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYA-QLKGR 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 124 SKQDARDRAVKYLAKVGIDERQQMKyPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLaEEGK 203
Cdd:TIGR01257 1034 SWEEAQLEMEAMLEDTGLHHKRNEE-AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGR 1111
|
170 180 190
....*....|....*....|....*....|...
gi 527036387 204 TMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHP 236
Cdd:TIGR01257 1112 TIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
153-229 |
8.66e-16 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 73.66 E-value: 8.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElVGEvlRIMQKL----AEEGKTMVVVTHEMGFARNVsNHVIFLHQG 228
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH-VGR--HIFENCilglLLNNKTRILVTHQLQLLPHA-DQIVVLDNG 203
|
.
gi 527036387 229 K 229
Cdd:cd03250 204 R 204
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-228 |
1.14e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.98 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgQLK 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYN-------KLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 81 VADKNQLRLlrtrlTMVFQHFNLWSHMTVLEN--VMEAPI-QVLGLSKQD---ARDRAVKYLAKVGIdERQQMKYPVHLS 154
Cdd:PRK09700 74 HKLAAQLGI-----GIIYQELSVIDELTVLENlyIGRHLTkKVCGVNIIDwreMRVRAAMMLLRVGL-KVDLDEKVANLS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036387 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQG 228
Cdd:PRK09700 148 ISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-210 |
1.82e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.07 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI--NFLEKPSEGSIVVSGQNInlvrdkdgqlkvadknqlrllr 91
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQF---------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 92 trltmvfqhfnlWSHMTVLENVmeapiqvlgLSKQDARDrAVKYLAKVGIDERQQMKYPV-HLSGGQQQRVSIARALAME 170
Cdd:COG2401 97 ------------GREASLIDAI---------GRKGDFKD-AVELLNAVGLSDAVLWLRRFkELSTGQKFRFRLALLLAER 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 527036387 171 PEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTH 210
Cdd:COG2401 155 PKLLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATH 195
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
131-253 |
1.91e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 74.45 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 131 RAVKYLAKVGI-DERQQMK-YPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAE-EGKTMVV 207
Cdd:PRK15093 135 RAIELLHRVGIkDHKDAMRsFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILL 214
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 527036387 208 VTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANPQSPRLQQFLK 253
Cdd:PRK15093 215 ISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQALIR 260
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
6-241 |
3.34e-15 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 74.78 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYG-EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRC-INFLEkPSEGSIVVSGQNINLVrdkdgqlkvaD 83
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLlVGFFQ-ARSGEILLNGFSLKDI----------D 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 84 KNQLRLLrtrLTMVFQHFNLWSHmTVLENVMeapIQVLGLSKQDARDRAVKyLAKVGID-ERQQMKYPVHL-------SG 155
Cdd:TIGR01193 543 RHTLRQF---INYLPQEPYIFSG-SILENLL---LGAKENVSQDEIWAACE-IAEIKDDiENMPLGYQTELseegssiSG 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEegKTMVVVTHEMGFARNVSNhVIFLHQGKIEEQGH 235
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLSVAKQSDK-IIVLDHGKIIEQGS 691
|
....*.
gi 527036387 236 PDEVLA 241
Cdd:TIGR01193 692 HDELLD 697
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-240 |
5.32e-15 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 71.66 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkvadKN 85
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT-------------RK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRllrtRLTMVFQHFNLWSHMTVLENVMeapIQVLGLSKQDARDRAVKYLAKVGIDERQQMKypvHLSGGQQQRVSIAR 165
Cdd:TIGR03740 68 DLH----KIGSLIESPPLYENLTARENLK---VHTTLLGLPDSRIDEVLNIVDLTNTGKKKAK---QFSLGMKQRLGIAI 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527036387 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQG--HPDEVL 240
Cdd:TIGR03740 138 ALLNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGkiNKSENL 214
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
152-229 |
5.56e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 69.78 E-value: 5.56e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527036387 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLRIMqkLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGK 229
Cdd:cd03221 70 QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI-EALEEA--LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-210 |
1.02e-14 |
|
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: 70.47 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDGQlKVADKN 85
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE-NILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLRTRLtmvfqhfnlwshmTVLENvmeapIQVLGLSKQDARDRAVKYLAKVGIDERQQMkyPVH-LSGGQQQRVSIA 164
Cdd:TIGR01189 80 HLPGLKPEL-------------SALEN-----LHFWAAIHGGAQRTIEDALAAVGLTGFEDL--PAAqLSAGQQRRLALA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 527036387 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTH 210
Cdd:TIGR01189 140 RLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-236 |
1.61e-14 |
|
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: 70.13 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 5 KLNVIDLHKRYGEH--EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEkPSEGSIVVSGQNINLVrdkdgqlkv 81
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALfRFLE-AEEGKIEIDGIDISTI--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 82 adknQLRLLRTRLTMVFQHFNLWSHmTVLENVmeapiqvlglskqdarDRAVKYlakvgiDERQQMKY------PVHLSG 155
Cdd:cd03369 76 ----PLEDLRSSLTIIPQDPTLFSG-TIRSNL----------------DPFDEY------SDEEIYGAlrvsegGLNLSQ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMGFARNVSNhVIFLHQGKIEEQGH 235
Cdd:cd03369 129 GQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEF-TNSTILTIAHRLRTIIDYDK-ILVMDAGEVKEYDH 206
|
.
gi 527036387 236 P 236
Cdd:cd03369 207 P 207
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-230 |
1.90e-14 |
|
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: 70.19 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTflrCINFLEK---PSEGSIVVSGQNINLVRDKdgqlkvadknqlrLLRTR 93
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKST---VVALLENfyqPQGGQVLLDGKPISQYEHK-------------YLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 94 LTMVFQHFNLWSHmTVLENVMEAPIQVlglSKQDARDRAVKYLAKVGIDERQQMKYP------VHLSGGQQQRVSIARAL 167
Cdd:cd03248 90 VSLVGQEPVLFAR-SLQDNIAYGLQSC---SFECVKEAAQKAHAHSFISELASGYDTevgekgSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527036387 168 AMEPEVLLFDEPTSALDPElvgEVLRIMQKLAE--EGKTMVVVTHEMGFARNvSNHVIFLHQGKI 230
Cdd:cd03248 166 IRNPQVLILDEATSALDAE---SEQQVQQALYDwpERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-232 |
3.00e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.74 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 22 KGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDgqlkvADKNQLRLL--RTRLTMVFQ 99
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLD-----AVKKGMAYIteSRRDNGFFP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 100 HFNLWSHMTVLENVMEAPIQ-VLGLSkqDARDRAvkylaKVGIDERQQMKYPVH--------LSGGQQQRVSIARALAME 170
Cdd:PRK09700 355 NFSIAQNMAISRSLKDGGYKgAMGLF--HEVDEQ-----RTAENQRELLALKCHsvnqniteLSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527036387 171 PEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEE 232
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-235 |
4.49e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 69.36 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAENK--LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDgq 78
Cdd:PRK10247 1 MQENSplLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 79 lkvadknqlrlLRTRLTMVFQHFNLWSHmTVLENVMeAPIQVLGlsKQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQQ 158
Cdd:PRK10247 79 -----------YRQQVSYCAQTPTLFGD-TVYDNLI-FPWQIRN--QQPDPAIFLDDLERFALPDTILTKNIAELSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVV-VTHEmgfaRNVSNH---VIFL--HQGKIEE 232
Cdd:PRK10247 144 QRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwVTHD----KDEINHadkVITLqpHAGEMQE 219
|
...
gi 527036387 233 QGH 235
Cdd:PRK10247 220 ARY 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-234 |
5.43e-14 |
|
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: 69.28 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 12 HKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQninlvrdkdgqlkVADKNQLRLLR 91
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-------------VPWKRRKKFLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 92 tRLTMVF-QHFNLWSHMTVLE--NVMEApiqVLGLSKQDARDRaVKYLAKVgIDERQQMKYPV-HLSGGQQQRVSIARAL 167
Cdd:cd03267 95 -RIGVVFgQKTQLWWDLPVIDsfYLLAA---IYDLPPARFKKR-LDELSEL-LDLEELLDTPVrQLSLGQRMRAEIAAAL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 168 AMEPEVLLFDEPTSALD---PELVGEVLRIMQKlaEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQG 234
Cdd:cd03267 169 LHEPEILFLDEPTIGLDvvaQENIRNFLKEYNR--ERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-230 |
5.51e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.85 E-value: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgQLKVADKN 85
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA-------RLTPAKAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLrtrltMVFQHFNLWSHMTVLENVMeapiqvLGLSK-QDARDRAVKYLAKVGIDERQQMKYPVhLSGGQQQRVSIA 164
Cdd:PRK15439 85 QLGIY-----LVPQEPLLFPNLSVKENIL------FGLPKrQASMQKMKQLLAALGCQLDLDSSAGS-LEVADRQIVEIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527036387 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKI 230
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-213 |
5.95e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.53 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 18 HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDGQLKVADKNQLRllrtrltmv 97
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVD--------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 98 fqhfnlWSHMTVLENV-MEAPIQVLG-LSKQDARDRAV--KYLAKVGIDERQQMKYPvHLSGGQQQRVSIARALAMEPEV 173
Cdd:PRK15056 91 ------WSFPVLVEDVvMMGRYGHMGwLRRAKKRDRQIvtAALARVDMVEFRHRQIG-ELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 527036387 174 LLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMG 213
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLG 203
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
123-257 |
7.37e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 70.58 E-value: 7.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 123 LSKQDARDRAVKYLAKVGIDErqQMKYPV-HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGE---VLRIMQKL 198
Cdd:COG1245 184 LEKVDERGKLDELAEKLGLEN--ILDRDIsELSGGELQRVAIAAALLRDADFYFFDEPSSYLD---IYQrlnVARLIREL 258
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527036387 199 AEEGKTMVVVTHEMG----FARNVsnHVIFlhqgkieeqGHPDE--VLANPQSPR--LQQFLKGSLK 257
Cdd:COG1245 259 AEEGKYVLVVEHDLAildyLADYV--HILY---------GEPGVygVVSKPKSVRvgINQYLDGYLP 314
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
153-241 |
9.58e-14 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 70.45 E-value: 9.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvGE--VLRIMQKLAEEGKTMVVVTHEMGfARNVSNHVIFLHQGKI 230
Cdd:TIGR01842 455 LSGGQRQRIALARALYGDPKLVVLDEPNSNLDEE--GEqaLANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
90
....*....|.
gi 527036387 231 EEQGHPDEVLA 241
Cdd:TIGR01842 532 ARFGERDEVLA 542
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
153-241 |
1.10e-13 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 70.23 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAeEGKTMVVVTHEMGFARNvSNHVIFLHQGKIEE 232
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAHRLSTIVD-ADEILVLEAGRIVE 572
|
....*....
gi 527036387 233 QGHPDEVLA 241
Cdd:COG5265 573 RGTHAELLA 581
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-236 |
1.33e-13 |
|
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: 67.90 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 14 RYGEHE--VLKGVSLQAN------------AGdvisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINLVRdkdgql 79
Cdd:cd03244 11 RYRPNLppVLKNISFSIKpgekvgivgrtgSG------------KSSLLLALFRLVELSSGSILIDGVDISKIG------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 80 kvadknqLRLLRTRLTMVFQHFNLWSHmTVLENVmeAPiqvLGLSKQDARDRAvkyLAKVGIDER-QQMKY--------- 149
Cdd:cd03244 73 -------LHDLRSRISIIPQDPVLFSG-TIRSNL--DP---FGEYSDEELWQA---LERVGLKEFvESLPGgldtvveeg 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 150 PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgevlRIMQKLAEE---GKTMVVVTHE----MGFARnvsnhV 222
Cdd:cd03244 137 GENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETD----ALIQKTIREafkDCTVLTIAHRldtiIDSDR-----I 207
|
250
....*....|....
gi 527036387 223 IFLHQGKIEEQGHP 236
Cdd:cd03244 208 LVLDKGRVVEFDSP 221
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
119-239 |
1.76e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.99 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 119 QVLGLSKQDARDRAVKYLAKVGIDE---RQQMKYpvhlSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIM 195
Cdd:NF000106 112 R*LDLSRKDARARADELLERFSLTEaagRAAAKY----SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV 187
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 527036387 196 QKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEV 239
Cdd:NF000106 188 RSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
151-242 |
2.09e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.62 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVsNHVIFLHQGKI 230
Cdd:PLN03232 739 VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMI 817
|
90
....*....|..
gi 527036387 231 EEQGHPDEVLAN 242
Cdd:PLN03232 818 KEEGTFAELSKS 829
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
144-210 |
3.33e-13 |
|
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: 65.64 E-value: 3.33e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 144 RQQMKYPVH--LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGevlRIMQKLAEEGKTMVVVTH 210
Cdd:cd03223 81 REQLIYPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED---RLYQLLKELGITVISVGH 146
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
44-241 |
5.20e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.52 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSivvSGQNINLVRDK-----DGqLKVADKNqLRLLRTRLTMVFQHFNLWShMTVLENVMeapi 118
Cdd:PTZ00265 1248 QNVGMKNVNEFSLTKEGG---SGEDSTVFKNSgkillDG-VDICDYN-LKDLRNLFSIVSQEPMLFN-MSIYENIK---- 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 119 qvlgLSKQDARDRAVKYLAK-VGIDERQQM----------KYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP-- 185
Cdd:PTZ00265 1318 ----FGKEDATREDVKRACKfAAIDEFIESlpnkydtnvgPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSns 1393
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036387 186 -ELVGEVLRIMQKLAEegKTMVVVTHEMGFARNVSNHVIFLHQGK----IEEQGHPDEVLA 241
Cdd:PTZ00265 1394 eKLIEKTIVDIKDKAD--KTIITIAHRIASIKRSDKIVVFNNPDRtgsfVQAHGTHEELLS 1452
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-243 |
5.60e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.20 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkvadknQLRL--LRTRL 94
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT---------------KLQLdsWRSRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 95 TMVFQHFNLWSHmTVLENVmeapiqvlGLSKQDARDRAVKYLAKVGIDERQQMKYP-----------VHLSGGQQQRVSI 163
Cdd:PRK10789 392 AVVSQTPFLFSD-TVANNI--------ALGRPDATQQEIEHVARLASVHDDILRLPqgydtevgergVMLSGGQKQRISI 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 164 ARALAMEPEVLLFDEPTSALDPELVGEvlrIMQKLAE--EGKTMVVVTHEMGfARNVSNHVIFLHQGKIEEQGHPDEVLA 241
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGRTEHQ---ILHNLRQwgEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
..
gi 527036387 242 NP 243
Cdd:PRK10789 539 QS 540
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
106-243 |
5.61e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.95 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 106 HMTVLENVMeapiqvlgLSKQDARDRAVKY-LAKVGIDE-----RQQMKYPVH-----LSGGQQQRVSIARALAMEPEVL 174
Cdd:PRK11174 436 HGTLRDNVL--------LGNPDASDEQLQQaLENAWVSEflpllPQGLDTPIGdqaagLSVGQAQRLALARALLQPCQLL 507
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036387 175 LFDEPTSALDpelVGEVLRIMQKL--AEEGKTMVVVTHEMGFARNVsNHVIFLHQGKIEEQGHPDEVLANP 243
Cdd:PRK11174 508 LLDEPTASLD---AHSEQLVMQALnaASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
153-210 |
5.79e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.91 E-value: 5.79e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGevlRIMQKLAEE--GKTMVVVTH 210
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEA---ALYQLLREElpGTTVISVGH 542
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
151-241 |
1.23e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 67.28 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQKLAEEGKTMVVVTHEMGFARNVsNHVIFLHQG 228
Cdd:TIGR00957 759 VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhvIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGG 837
|
90
....*....|...
gi 527036387 229 KIEEQGHPDEVLA 241
Cdd:TIGR00957 838 KISEMGSYQELLQ 850
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
44-229 |
1.32e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDGqlkvadknqlrlLRTRLTMVFQHFNLWSHMTVLENVM--EAPIQVL 121
Cdd:PRK10982 37 KSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA------------LENGISMVHQELNLVLQRSVMDNMWlgRYPTKGM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 122 GLSKQDARDRAVKYLAKVGIDERQQMKYpVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE 201
Cdd:PRK10982 105 FVDQDKMYRDTKAIFDELDIDIDPRAKV-ATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER 183
|
170 180
....*....|....*....|....*...
gi 527036387 202 GKTMVVVTHEMGFARNVSNHVIFLHQGK 229
Cdd:PRK10982 184 GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
120-230 |
1.65e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 120 VLGLS-KQDARDRAVKYLAKVGI-----DERQ---------QMKYPVH------LSGGQQQRVSIARALAMEPEVLLFDE 178
Cdd:PRK10762 342 VLGMSvKENMSLTALRYFSRAGGslkhaDEQQavsdfirlfNIKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDE 421
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 527036387 179 PTSALDpelVG---EVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKI 230
Cdd:PRK10762 422 PTRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
152-230 |
2.32e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.11 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVG---EVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQG 228
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
..
gi 527036387 229 KI 230
Cdd:PRK13549 482 KL 483
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
153-231 |
3.15e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 65.62 E-value: 3.15e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIE 231
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-234 |
4.69e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 63.93 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVisiigssgsgKSTFLRCI--NFLEKPSEGSIVVSGQNINlvrdkdgQLKVAD 83
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVhaimgpngsgKSTLAKVLmgHPKYEVTSGSILLDGEDIL-------ELSPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 84 knqlrllRTR--LTMVFQH---------FNLWshMTVLENVMEAPIqvlglSKQDARDRAVKYLAKVGIDE----Rqqmk 148
Cdd:COG0396 74 -------RARagIFLAFQYpveipgvsvSNFL--RTALNARRGEEL-----SAREFLKLLKEKMKELGLDEdfldR---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 149 yPVH--LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHemgFAR----NVSNHV 222
Cdd:COG0396 136 -YVNegFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH---YQRildyIKPDFV 211
|
250
....*....|..
gi 527036387 223 IFLHQGKIEEQG 234
Cdd:COG0396 212 HVLVDGRIVKSG 223
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
151-241 |
5.95e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.04 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvGEvlRIMQKLAEE---GKTMVVVTHEMGFARNvSNHVIFLHQ 227
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALDTE--SE--RAIQAALDElqkNRTSLVIAHRLSTIEK-ADEILVVED 553
|
90
....*....|....
gi 527036387 228 GKIEEQGHPDEVLA 241
Cdd:PRK11176 554 GEIVERGTHAELLA 567
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-210 |
1.42e-11 |
|
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: 61.74 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDGQ--LKVADKNQlrlLRTR 93
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARglLYLGHAPG---IKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 94 LTmVFQHFNLWSHMTVLENVMEApiqvlglskqdardravkyLAKVGIDERQQMkyPVH-LSGGQQQRVSIARALAMEPE 172
Cdd:cd03231 88 LS-VLENLRFWHADHSDEQVEEA-------------------LARVGLNGFEDR--PVAqLSAGQQRRVALARLLLSGRP 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 527036387 173 VLLFDEPTSALDpelVGEVLRIMQKLA---EEGKTMVVVTH 210
Cdd:cd03231 146 LWILDEPTTALD---KAGVARFAEAMAghcARGGMVVLTTH 183
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-210 |
1.56e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.81 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 4 NKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRdkdgqlkvad 83
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 84 knqlrlLRTRLTMVfQHFN-LWSHMTVLENV-------------MEAPIQVLGLskQDARDRAVKYLakvgiderqqmky 149
Cdd:PRK13539 71 ------VAEACHYL-GHRNaMKPALTVAENLefwaaflggeeldIAAALEAVGL--APLAHLPFGYL------------- 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036387 150 pvhlSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTH 210
Cdd:PRK13539 129 ----SAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-229 |
1.57e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLR--CINFLEKPSEGSIVVSGQNINLVRDKDGQ 78
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKvlSGVYPHGTYEGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 79 lkvadknqlrllRTRLTMVFQHFNLWSHMTVLENV-MEAPIQVLGLSKQDA-RDRAVKYLAKVGIDerQQMKYPV-HLSG 155
Cdd:PRK13549 81 ------------RAGIAIIHQELALVKELSVLENIfLGNEITPGGIMDYDAmYLRAQKLLAQLKLD--INPATPVgNLGL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036387 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGK 229
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
128-230 |
1.61e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 63.73 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 128 ARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQKLAEEGKTMVV 207
Cdd:PLN03073 320 AEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIV 396
|
90 100
....*....|....*....|...
gi 527036387 208 VTHEMGFARNVSNHVIFLHQGKI 230
Cdd:PLN03073 397 VSHAREFLNTVVTDILHLHGQKL 419
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
152-240 |
1.64e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.55 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 152 HLSGGQQQRVSIARAL-----AMEPE--VLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIF 224
Cdd:COG4138 126 QLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWL 205
|
90
....*....|....*.
gi 527036387 225 LHQGKIEEQGHPDEVL 240
Cdd:COG4138 206 LKQGKLVASGETAEVM 221
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
10-211 |
1.77e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.75 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsEGSIvvSGQNINlvrdkdGQLKVADKNQLRL 89
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRI--QGNNFT------GTILANNRKPTKQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 90 LRTRLTMVFQHFNLWSHMTVLENVMEAPIQVL--GLSKQDARDRAVKYLAKVGIDERQQM----KYPVHLSGGQQQRVSI 163
Cdd:PLN03211 138 ILKRTGFVTQDDILYPHLTVRETLVFCSLLRLpkSLTKQEKILVAESVISELGLTKCENTiignSFIRGISGGERKRVSI 217
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 527036387 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHE 211
Cdd:PLN03211 218 AHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
44-253 |
2.67e-11 |
|
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: 61.66 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVSGQNINLvrdKDGQLKVADKNQLRLLRTRLTMVFQHFNLWShmtvlENVMEaPIQVLGL 123
Cdd:cd03237 38 KTTFIKMLAGVLKPDEGDIEIELDTVSY---KPQYIKADYEGTVRDLLSSITKDFYTHPYFK-----TEIAK-PLQIEQI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 124 SKQDARDravkylakvgiderqqmkypvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEG- 202
Cdd:cd03237 109 LDREVPE----------------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNe 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 527036387 203 KTMVVVTHEMGFARNVSNHVIfLHQGKIEEQGHpdevlAN-PQSPR--LQQFLK 253
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRLI-VFEGEPSVNGV-----ANpPQSLRsgMNRFLK 214
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
151-234 |
3.29e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.26 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElVGEvlRIMQKL---AEEGKTMVVVTHEMGFARNvSNHVIFLHQ 227
Cdd:PTZ00243 781 VNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH-VGE--RVVEECflgALAGKTRVLATHQVHVVPR-ADYVVALGD 856
|
....*..
gi 527036387 228 GKIEEQG 234
Cdd:PTZ00243 857 GRVEFSG 863
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
6-215 |
3.35e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.97 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKdgqlkvadkn 85
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 qlrllrtrltmvFQHFNLW--------SHMTVLENVMEApiqvLGLSKQDARDRAVKYLAKVGIDERQQMkyPVH-LSGG 156
Cdd:PRK13538 72 ------------YHQDLLYlghqpgikTELTALENLRFY----QRLHGPGDDEALWEALAQVGLAGFEDV--PVRqLSAG 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036387 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKtMVVVT--HEMGFA 215
Cdd:PRK13538 134 QQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGG-MVILTthQDLPVA 193
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
152-212 |
3.90e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 3.90e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036387 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGE---VLRIMQKLAeEGKTMVVVTHEM 212
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD---IRQrlnVARLIRELA-EGKYVLVVEHDL 271
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-229 |
5.07e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 62.15 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLR--CINFLEKPSEGSIVVSGQNINL--VRDKDgqlkvadknqlr 88
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKilSGVYPHGTWDGEIYWSGSPLKAsnIRDTE------------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 89 llRTRLTMVFQHFNLWSHMTVLENV-MEAPIQVLGLSKQDAR--DRAVKYLAKVGIDERQQMKYPVHLSGGQQQRVSIAR 165
Cdd:TIGR02633 77 --RAGIVIIHQELTLVPELSVAENIfLGNEITLPGGRMAYNAmyLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036387 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGK 229
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
111-257 |
7.92e-11 |
|
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: 60.46 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 111 ENVMEAPIQVLG-----LSKQDAR---DRAVKYLAKVGIDERQQMkypvHLSGGQQQRVSIARALAMEPEVLLFDEPTSA 182
Cdd:cd03236 94 QYVDLIPKAVKGkvgelLKKKDERgklDELVDQLELRHVLDRNID----QLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 183 LDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHqgkieeqGHPDE--VLANPQSPR--LQQFLKGSLK 257
Cdd:cd03236 170 LDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLY-------GEPGAygVVTLPKSVRegINEFLDGYLP 241
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
153-212 |
7.94e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.73 E-value: 7.94e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVG---EVLRIMQKLAEEGKTMVVVTHEM 212
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSEL 464
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
129-246 |
8.01e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.47 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 129 RDRAVKYLAKVGI---DERQQMkypVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVG---EVLRIMQKLAEEG 202
Cdd:PRK11288 373 AENADRFIRSLNIktpSREQLI---MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID---VGakhEIYNVIYELAAQG 446
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 527036387 203 KTMVVVTHEMGFARNVSNHVIFLHQGKI-----EEQGHPDEV--LANPQSP 246
Cdd:PRK11288 447 VAVLFVSSDLPEVLGVADRIVVMREGRIagelaREQATERQAlsLALPRTS 497
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
142-214 |
8.81e-11 |
|
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: 60.04 E-value: 8.81e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527036387 142 DERQQMKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQKLAEEGKTMVVVTHEMGF 214
Cdd:cd03290 130 DQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY 204
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
54-230 |
1.29e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.83 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 54 LEKPSEGSIVVSGQNINlvrdkdgQLKVADknqlrllRTRLTMVF-----QHFNLWSHMTVLENVMEAPIQVLGLSKQDA 128
Cdd:PRK15439 312 LRPARGGRIMLNGKEIN-------ALSTAQ-------RLARGLVYlpedrQSSGLYLDAPLAWNVCALTHNRRGFWIKPA 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 129 RDRAV--KYLAKVGI---DERQQMKypvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGK 203
Cdd:PRK15439 378 RENAVleRYRRALNIkfnHAEQAAR---TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNV 454
|
170 180
....*....|....*....|....*..
gi 527036387 204 TMVVVTHEMGFARNVSNHVIFLHQGKI 230
Cdd:PRK15439 455 AVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-230 |
1.76e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.10 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 11 LHKRYGEHEVLKGVSLQ-----------AN-AGdvisiigssgsgKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgq 78
Cdd:COG4586 28 FRREYREVEAVDDISFTiepgeivgfigPNgAG------------KSTTIKMLTGILVPTSGEVRVLGYVPF-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 79 lkvadKNQLRLLRtRLTMVF-QHFNLWSHMTVLE--NVMEApiqVLGLSKQDARDRaVKYLAKV-GIDErqQMKYPV-HL 153
Cdd:COG4586 88 -----KRRKEFAR-RIGVVFgQRSQLWWDLPAIDsfRLLKA---IYRIPDAEYKKR-LDELVELlDLGE--LLDTPVrQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDP---ELVGEVLRIMQKlaEEGKTMVVVTHEMGFARNVSNHVIFLHQGKI 230
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVvskEAIREFLKEYNR--ERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
153-253 |
4.49e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE-GKTMVVVTHEMGFARNVSNHVI-FlhQGKI 230
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLMvF--EGEP 531
|
90 100
....*....|....*....|....*
gi 527036387 231 EEQGHPDEvlanPQSPR--LQQFLK 253
Cdd:PRK13409 532 GKHGHASG----PMDMRegMNRFLK 552
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
82-236 |
5.29e-10 |
|
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: 59.18 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 82 ADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEApiqvLGLSKQDArdravkylakvgiderqqmkyPV-HLSGGQQQR 160
Cdd:TIGR03719 115 ADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDA----LRCPPWDA---------------------DVtKLSGGERRR 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527036387 161 VSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGkieeQGHP 236
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRG----RGIP 238
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
132-257 |
8.73e-10 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 56.43 E-value: 8.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 132 AVKYLAKVGIDERQQMKYP----------VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE 201
Cdd:cd03222 41 AVKILAGQLIPNGDNDEWDgitpvykpqyIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036387 202 G-KTMVVVTHEMGFARNVSNHVIFLhqgkieeQGHPDE--VLANPQSPR--LQQFLKGSLK 257
Cdd:cd03222 121 GkKTALVVEHDLAVLDYLSDRIHVF-------EGEPGVygIASQPKGTRegINRFLRGYLI 174
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
126-231 |
9.84e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.26 E-value: 9.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 126 QDARDRAVKYLAKVGIDERQQMKYpVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTM 205
Cdd:NF040905 114 NETNRRARELLAKVGLDESPDTLV-TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITS 192
|
90 100
....*....|....*....|....*..
gi 527036387 206 VVVTHEMGFARNVSNHVIFLHQGK-IE 231
Cdd:NF040905 193 IIISHKLNEIRRVADSITVLRDGRtIE 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
148-230 |
1.02e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.20 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 148 KYPVH------LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNH 221
Cdd:PRK10982 381 KTPGHrtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDR 460
|
....*....
gi 527036387 222 VIFLHQGKI 230
Cdd:PRK10982 461 ILVMSNGLV 469
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
44-212 |
1.19e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.26 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIvvsgqninlvrdkDGQLKVADKNQLrlLRTRltmvfqhfnlwSHMTVLENVMEAPIQVLGL 123
Cdd:COG1245 379 KTTFAKILAGVLKPDEGEV-------------DEDLKISYKPQY--ISPD-----------YDGTVEEFLRSANTDDFGS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 124 SKqdARDRAVKYLakvGIDE--RQQMKypvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEE 201
Cdd:COG1245 433 SY--YKTEIIKPL---GLEKllDKNVK---DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEN 504
|
170
....*....|..
gi 527036387 202 -GKTMVVVTHEM 212
Cdd:COG1245 505 rGKTAMVVDHDI 516
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
153-211 |
1.77e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 55.71 E-value: 1.77e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHE 211
Cdd:cd03232 109 LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQ 167
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-212 |
4.43e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLVRDKDGQlkvadknqlrllRTRLTMVFQH 100
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQ------------EAGIGIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 101 FNLWSHMTVLENVM--EAPIQVLGLSK-QDARDRAVKYLAKVGIDERQQMKYPvHLSGGQQQRVSIARALAMEPEVLLFD 177
Cdd:PRK10762 88 LNLIPQLTIAENIFlgREFVNRFGRIDwKKMYAEADKLLARLNLRFSSDKLVG-ELSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190
....*....|....*....|....*....|....*
gi 527036387 178 EPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEM 212
Cdd:PRK10762 167 EPTDALTDTETESLFRVIRELKSQGRGIVYISHRL 201
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
153-239 |
4.80e-09 |
|
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: 56.56 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARAL---AMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARnVSNHVIFL---- 225
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIK-TADYIIDLgpeg 908
|
90
....*....|....*.
gi 527036387 226 --HQGKIEEQGHPDEV 239
Cdd:TIGR00630 909 gdGGGTVVASGTPEEV 924
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
99-250 |
6.34e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.29 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 99 QHFNLWSHMTVLEN-VMEApiQVLGLSKQDARDRAVKYLAKVGIDERQQmKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
Cdd:NF033858 346 QAFSLYGELTVRQNlELHA--RLFHLPAAEIAARVAEMLERFDLADVAD-ALPDSLPLGIRQRLSLAVAVIHKPELLILD 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527036387 178 EPTSALDPELVGEVLRIMQKLA-EEGKTMVVVTHEMGFA----RnVSnhviFLHQGKIEEQGHPDEVLANPQSPRLQQ 250
Cdd:NF033858 423 EPTSGVDPVARDMFWRLLIELSrEDGVTIFISTHFMNEAercdR-IS----LMHAGRVLASDTPAALVAARGAATLEE 495
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-230 |
1.07e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.03 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 3 ENKLNVIDLH-KRYGEHEVLKGVSLQANAGDVisiigssgsgkSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdGQLKV 81
Cdd:COG3845 255 EVVLEVENLSvRDDRGVPALKDVSLEVRAGEIlgiagvagngqSELAEALAGLRPPASGSIRLDGEDI-------TGLSP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 82 ADKNQLRLLRT---RLTM-VFQHFNLWSHMtVLENVMEAPIQVLG-LSKQDARDRAVKYLAKVGI---DERQQMKypvHL 153
Cdd:COG3845 328 RERRRLGVAYIpedRLGRgLVPDMSVAENL-ILGRYRRPPFSRGGfLDRKAIRAFAEELIEEFDVrtpGPDTPAR---SL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQKL---AEEGKTMVVVTHEMGFARNVSNHVIFLHQGKI 230
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGLD---VGAIEFIHQRLlelRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
83-230 |
1.46e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 83 DKNQLRLlrTRLTMVFQHFNLWShmtvLENVMEAPIQVLGLSkqdardrAVKYLAKvgiderqqmkypvhLSGGQQQRVS 162
Cdd:PRK11147 114 EKNLNEL--AKLQEQLDHHNLWQ----LENRINEVLAQLGLD-------PDAALSS--------------LSGGWLRKAA 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527036387 163 IARALAMEPEVLLFDEPTSALDPELVgEVLRimQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKI 230
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDIETI-EWLE--GFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
153-236 |
1.47e-08 |
|
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: 54.16 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAME---PEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNvSNHVIFL---- 225
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKC-ADWIIDLgpeg 248
|
90
....*....|...
gi 527036387 226 --HQGKIEEQGHP 236
Cdd:cd03271 249 gdGGGQVVASGTP 261
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
152-244 |
2.45e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.40 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 152 HLSGGQQQRVSIA-------RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMgfarnvsNH--- 221
Cdd:PRK03695 126 QLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDL-------NHtlr 198
|
90 100
....*....|....*....|....*..
gi 527036387 222 ----VIFLHQGKIEEQGHPDEVLANPQ 244
Cdd:PRK03695 199 hadrVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
153-246 |
3.89e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKL-AEEGKTMVVVTHEMGFARnVSNHVIFLHQgkiE 231
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLSTIR-YANTIFVLSN---R 655
|
90
....*....|....*
gi 527036387 232 EQGHPDEVLANPQSP 246
Cdd:PTZ00265 656 ERGSTVDVDIIGEDP 670
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
153-257 |
4.86e-08 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 53.49 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPE---VLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNvSNHVIFL---- 225
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKT-ADWIIDLgpeg 905
|
90 100 110
....*....|....*....|....*....|....
gi 527036387 226 --HQGKIEEQGHPDEVLANPQSPrLQQFLKGSLK 257
Cdd:COG0178 906 gdGGGEIVAEGTPEEVAKVKASY-TGRYLKEYLE 938
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
152-218 |
7.50e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 7.50e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527036387 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQKLAEEGKTMVVVTHEMGFARNV 218
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLEQFLHDYPGTVVAVTHDRYFLDNV 226
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
153-234 |
7.93e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.78 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPE--VLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNvSNHVIFL----- 225
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFgpgsg 166
|
90
....*....|
gi 527036387 226 -HQGKIEEQG 234
Cdd:cd03238 167 kSGGKVVFSG 176
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-254 |
9.46e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.59 E-value: 9.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 18 HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQN--INLVRDKDGQLkvadknqlrllrtrlt 95
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAalIAISSGLNGQL---------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 96 mvfqhfnlwshmTVLENVmEAPIQVLGLSKQDARDRAVKYL--AKVGiderQQMKYPVH-LSGGQQQRVSIARALAMEPE 172
Cdd:PRK13545 101 ------------TGIENI-ELKGLMMGLTKEKIKEIIPEIIefADIG----KFIYQPVKtYSSGMKSRLGFAISVHINPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 173 VLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLANpqsprLQQFL 252
Cdd:PRK13545 164 ILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH-----YDEFL 238
|
..
gi 527036387 253 KG 254
Cdd:PRK13545 239 KK 240
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
129-210 |
1.03e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 129 RDRAVKYLAKVGIDERQQmKYPVH-LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKT-MV 206
Cdd:PRK10938 378 QKLAQQWLDILGIDKRTA-DAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLL 456
|
....
gi 527036387 207 VVTH 210
Cdd:PRK10938 457 FVSH 460
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
153-209 |
1.58e-07 |
|
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: 50.34 E-value: 1.58e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVT 209
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS 175
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-253 |
2.67e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.20 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvsgqninlvrDKDGQLKVADKNQlrllrtrltmvfqh 100
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------DRNGEVSVIAISA-------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 101 fNLWSHMTVLENVmEAPIQVLGLSKQDARDRAVKYlakVGIDERQQMKY-PV-HLSGGQQQRVSIARALAMEPEVLLFDE 178
Cdd:PRK13546 95 -GLSGQLTGIENI-EFKMLCMGFKRKEIKAMTPKI---IEFSELGEFIYqPVkKYSSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527036387 179 PTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIEEQGHPDEVLanpqsPRLQQFLK 253
Cdd:PRK13546 170 ALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL-----PKYEAFLN 239
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
153-211 |
3.71e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 3.71e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLF-DEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHE 211
Cdd:TIGR00956 902 LNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-210 |
5.03e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 49.26 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 1 MAENK--LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInfLEKPS----EGSIVVSGQNINlvrd 74
Cdd:CHL00131 1 MNKNKpiLEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--AGHPAykilEGDILFKGESIL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 75 kdgQLKVADKNQLRLLrtrltMVFQHfnlwshmtvlenvmeaPIQVLGLSKQD----ARDRAVKYLAKVGIDERQQMKY- 149
Cdd:CHL00131 75 ---DLEPEERAHLGIF-----LAFQY----------------PIEIPGVSNADflrlAYNSKRKFQGLPELDPLEFLEIi 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 150 ----------PVHL--------SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTH 210
Cdd:CHL00131 131 neklklvgmdPSFLsrnvnegfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
153-250 |
5.56e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 50.10 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPelvGEVLRIMQKLAE--EGKTMVVVTHEMGFARNvSNHVIFLHQGKI 230
Cdd:PRK10790 477 LSVGQKQLLALARVLVQTPQILILDEATANIDS---GTEQAIQQALAAvrEHTTLVVIAHRLSTIVE-ADTILVLHRGQA 552
|
90 100
....*....|....*....|....
gi 527036387 231 EEQGHPDEVLANP----QSPRLQQ 250
Cdd:PRK10790 553 VEQGTHQQLLAAQgrywQMYQLQL 576
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
154-245 |
6.27e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 6.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQKLAEEGK--TMVVVTHEMgfarNV---SNHVIFLHQG 228
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVD---VRTDALIQKTIREEFKscTMLIIAHRL----NTiidCDRILVLDAG 1448
|
90
....*....|....*..
gi 527036387 229 KIEEQGHPDEVLANPQS 245
Cdd:PLN03130 1449 RVVEFDTPENLLSNEGS 1465
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
153-240 |
7.54e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.05 E-value: 7.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAM---------EPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVV-VTHEMGFARNVSNHV 222
Cdd:PRK13547 146 LSGGELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLaIVHDPNLAARHADRI 225
|
90
....*....|....*...
gi 527036387 223 IFLHQGKIEEQGHPDEVL 240
Cdd:PRK13547 226 AMLADGAIVAHGAPADVL 243
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
6-211 |
1.09e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.02 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrDKDgqlkvadkn 85
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKD--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 qLRLLRTRLTMVFQHFNLWSHMTVLENVMEApiqvLGLSKQDARDRAVKYLAKVGiderQQMKYPVH-LSGGQQQRVSIA 164
Cdd:PRK13540 69 -LCTYQKQLCFVGHRSGINPYLTLRENCLYD----IHFSPGAVGITELCRLFSLE----HLIDYPCGlLSSGQKRQVALL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 527036387 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHE 211
Cdd:PRK13540 140 RLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
153-256 |
1.53e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.06 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARAL---AMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARnVSNHVIFLHQ-- 227
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYVLELGPeg 888
|
90 100 110
....*....|....*....|....*....|....*
gi 527036387 228 ----GKIEEQGHPDEV--LANPQSPRLQQFLKGSL 256
Cdd:PRK00635 889 gnlgGYLLASCSPEELihLHTPTAKALRPYLSSPQ 923
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
43-211 |
2.66e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.04 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 43 GKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdgqlkvaDKNQLRLLRTRLTMVFQHFNLWSHMtvlenvmeapiqvLG 122
Cdd:PRK10522 361 GKSTLAMLLTGLYQPQSGEILLDGKPV-------------TAEQPEDYRKLFSAVFTDFHLFDQL-------------LG 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 123 LSKQDARDRAV-KYLakvgidERQQMKYPVH----------LSGGQQQRVSIARALAMEPEVLLFDEPTSALDP----EL 187
Cdd:PRK10522 415 PEGKPANPALVeKWL------ERLKMAHKLEledgrisnlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPhfrrEF 488
|
170 180
....*....|....*....|....
gi 527036387 188 VGEVLRIMQklaEEGKTMVVVTHE 211
Cdd:PRK10522 489 YQVLLPLLQ---EMGKTIFAISHD 509
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-241 |
3.18e-06 |
|
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: 48.02 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINLV--RDKDGQLKVADKNQLrLLRTRLTMV 97
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIglHDLRFKITIIPQDPV-LFSGSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 98 FQHFNLWSHMTVLENVMEAPIQVLGLSKQDARDRAVkylAKVGiderqqmkypVHLSGGQQQRVSIARALAMEPEVLLFD 177
Cdd:TIGR00957 1380 LDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHEC---AEGG----------ENLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036387 178 EPTSALDPE---LVGEVLRIMQklaeEGKTMVVVTHE----MGFARnvsnhVIFLHQGKIEEQGHPDEVLA 241
Cdd:TIGR00957 1447 EATAAVDLEtdnLIQSTIRTQF----EDCTVLTIAHRlntiMDYTR-----VIVLDKGEVAEFGAPSNLLQ 1508
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
44-223 |
4.19e-06 |
|
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: 47.24 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 44 KSTFLRCINFLEKPSEGSIVVsGQNInlvrdkdgqlKVADKNQLRLlrtrltmvfqhfNLWSHMTVLENVMEApIQVLGL 123
Cdd:TIGR03719 361 KSTLFRMITGQEQPDSGTIEI-GETV----------KLAYVDQSRD------------ALDPNKTVWEEISGG-LDIIKL 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 124 SKQDARDRAvkYLAKVGIDERQQMKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPelvgEVLRIMQK-LAEEG 202
Cdd:TIGR03719 417 GKREIPSRA--YVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV----ETLRALEEaLLNFA 490
|
170 180
....*....|....*....|.
gi 527036387 203 KTMVVVTHEMGFARNVSNHVI 223
Cdd:TIGR03719 491 GCAVVISHDRWFLDRIATHIL 511
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
154-212 |
5.60e-06 |
|
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: 47.32 E-value: 5.60e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEM 212
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSM 2130
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
153-211 |
5.79e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 5.79e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHE 211
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
71-210 |
6.06e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.00 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 71 LVRDKDGQLKVADKNQLRLLRTRLTMVFQHF-NLWSHMTVLENVMeapiQVLGLSKQDARDRAVKYLAKVGIDERQQMKY 149
Cdd:PRK13543 60 LLHVESGQIQIDGKTATRGDRSRFMAYLGHLpGLKADLSTLENLH----FLCGLHGRRAKQMPGSALAIVGLAGYEDTLV 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527036387 150 PvHLSGGQQQRVSIARaLAMEPEVL-LFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTH 210
Cdd:PRK13543 136 R-QLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
150-210 |
6.40e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 46.61 E-value: 6.40e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036387 150 PVHLSGGQQQ---RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTH 210
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
115-231 |
7.09e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 7.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 115 EAPIQVLG-LSKQDARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelvgevLR 193
Cdd:PRK10636 392 ESPLQHLArLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD-------LD 464
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 527036387 194 IMQKLAE-----EGkTMVVVTHEMGFARNVSNHVIFLHQGKIE 231
Cdd:PRK10636 465 MRQALTEalidfEG-ALVVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
153-245 |
7.36e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPE--VLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHE---MGFARNVSN----HVI 223
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLADRIIDigpgAGI 556
|
90 100
....*....|....*....|..
gi 527036387 224 FlhQGKIEEQGHPDEVLANPQS 245
Cdd:PRK00635 557 F--GGEVLFNGSPREFLAKSDS 576
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
153-245 |
7.82e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.89 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQklaEEGK--TMVVVTHEMGFARNVsNHVIFLHQGKI 230
Cdd:PLN03232 1372 FSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR---EEFKscTMLVIAHRLNTIIDC-DKILVLSSGQV 1447
|
90
....*....|....*
gi 527036387 231 EEQGHPDEVLANPQS 245
Cdd:PLN03232 1448 LEYDSPQELLSRDTS 1462
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
15-244 |
9.25e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 45.49 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvsgqninlvrDKDGQLKVADKNQLRLLRTRL 94
Cdd:PRK09544 14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQKLYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 95 TMVFQHFnlwshMTVLENVMEAPIqvlglskqdardraVKYLAKVgiDERQQMKYPVH-LSGGQQQRVSIARALAMEPEV 173
Cdd:PRK09544 83 PLTVNRF-----LRLRPGTKKEDI--------------LPALKRV--QAGHLIDAPMQkLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036387 174 LLFDEPTSALDpeLVGEVL---RIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQgKIEEQGHPDEVLANPQ 244
Cdd:PRK09544 142 LVLDEPTQGVD--VNGQVAlydLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHPE 212
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
137-234 |
1.10e-05 |
|
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: 45.33 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 137 AKVGIDERQQMKYPV------------HLSGGQQQRVSIARALAMEPEVLL--FDEPTSALDPELVGEVLRIMQKLAEEG 202
Cdd:cd03270 110 ARVGIRERLGFLVDVglgyltlsrsapTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLG 189
|
90 100 110
....*....|....*....|....*....|....*...
gi 527036387 203 KTMVVVTHEMGFARNvSNHVIFL------HQGKIEEQG 234
Cdd:cd03270 190 NTVLVVEHDEDTIRA-ADHVIDIgpgagvHGGEIVAQG 226
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
153-257 |
1.13e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.22 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEP---EVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNvSNHVIFL---- 225
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKT-ADWIIDLgpeg 909
|
90 100 110
....*....|....*....|....*....|....
gi 527036387 226 --HQGKIEEQGHPDEVLANPQSpRLQQFLKGSLK 257
Cdd:PRK00349 910 gdGGGEIVATGTPEEVAKVEAS-YTGRYLKPVLE 942
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
100-241 |
1.72e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 100 HFnlwSHMTVLENV-----MEAP-IQVLGLSKQD-ARDRAVKYLAKVGIDERQQMK----YPVHLSGGQQQRVSIARALA 168
Cdd:TIGR00956 149 HF---PHLTVGETLdfaarCKTPqNRPDGVSREEyAKHIADVYMATYGLSHTRNTKvgndFVRGVSGGERKRVSIAEASL 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527036387 169 MEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVT--HEMGFARNVSNHVIFLHQGKIEEQGHPDEVLA 241
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQ 300
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
153-216 |
1.79e-05 |
|
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: 43.52 E-value: 1.79e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRI------MQKLAEEGKTMVVVTHEMGFAR 216
Cdd:smart00382 61 GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrllLLLKSEKNLTVILTTNDEKDLG 130
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
153-228 |
2.34e-05 |
|
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: 43.50 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALA---MEPEVL-LFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARN--VSNHVIFLH 226
Cdd:cd03227 78 LSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELadKLIHIKKVI 157
|
..
gi 527036387 227 QG 228
Cdd:cd03227 158 TG 159
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
152-241 |
2.74e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVSNHVIFLHQGKIE 231
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLA 214
|
90
....*....|
gi 527036387 232 EQGHPDEVLA 241
Cdd:PRK10938 215 ETGEREEILQ 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
151-228 |
4.17e-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: 44.52 E-value: 4.17e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVL-RIMQKLAEEgKTMVVVTHEMGFARNvSNHVIFLHQG 228
Cdd:TIGR01271 547 ITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFeSCLCKLMSN-KTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
153-245 |
4.20e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.62 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLF--DEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARnVSNHVIFL----- 225
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIR-AADYVIDIgpgag 567
|
90 100
....*....|....*....|.
gi 527036387 226 -HQGKIEEQGHPDEVLANPQS 245
Cdd:TIGR00630 568 eHGGEVVASGTPEEILANPDS 588
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
129-232 |
5.56e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 129 RDRAVKYLAKVGIDErQQMKYPVH-LSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQKLAEEGKTMVV 207
Cdd:PRK10636 126 RSRAASLLHGLGFSN-EQLERPVSdFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLIL 201
|
90 100
....*....|....*....|....*
gi 527036387 208 VTHEMGFARNVSNHVIFLHQGKIEE 232
Cdd:PRK10636 202 ISHDRDFLDPIVDKIIHIEQQSLFE 226
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
128-230 |
5.88e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 128 ARDRAVKYLAKVGIDERQQMKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQKLAEEGKTMVV 207
Cdd:PRK15064 131 AEARAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD---INTIRWLEDVLNERNSTMII 207
|
90 100
....*....|....*....|...
gi 527036387 208 VTHEMGFARNVSNHVIFLHQGKI 230
Cdd:PRK15064 208 ISHDRHFLNSVCTHMADLDYGEL 230
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
151-234 |
6.31e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.24 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVS-NHVIFLHQGK 229
Cdd:PRK09580 144 VGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGR 223
|
....*
gi 527036387 230 IEEQG 234
Cdd:PRK09580 224 IVKSG 228
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
42-232 |
7.01e-05 |
|
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: 43.63 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 42 SGKSTFLRCINFLEKPSEGSIVVsgqninlvrdkDGQLkVADKNQLRlLRTRLTMVFQHFNLWSHmtvlenvmeapiqVL 121
Cdd:COG4615 369 SGKSTLAKLLTGLYRPESGEILL-----------DGQP-VTADNREA-YRQLFSAVFSDFHLFDR-------------LL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 122 GLSKQDARDRAVKYLAKVGIDERQQMK----YPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP--------ELVG 189
Cdd:COG4615 423 GLDGEADPARARELLERLELDHKVSVEdgrfSTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPefrrvfytELLP 502
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 527036387 190 EvlrimqkLAEEGKTMVVVTH-EMGFarNVSNHVIFLHQGKIEE 232
Cdd:COG4615 503 E-------LKARGKTVIAISHdDRYF--DLADRVLKMDYGKLVE 537
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
153-210 |
8.17e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 43.58 E-value: 8.17e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGevlRIMQKLAEEGKTMVVVTH 210
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG---YMYRLCREFGITLFSVSH 637
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
151-228 |
1.84e-04 |
|
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: 41.77 E-value: 1.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVL-RIMQKLAEEgKTMVVVTHEMGFARNvSNHVIFLHQG 228
Cdd:cd03291 158 ITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFeSCVCKLMAN-KTRILVTSKMEHLKK-ADKILILHEG 234
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
121-245 |
2.44e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 121 LGLSKQDA----------RDRaVKYLAKVGID----ERQQMKypvhLSGGQQQRVSIARALAMEpevL---LF--DEPTS 181
Cdd:COG0178 445 LELTEREAeiaerilkeiRSR-LGFLVDVGLDyltlDRSAGT----LSGGEAQRIRLATQIGSG---LvgvLYvlDEPSI 516
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527036387 182 ALDPELVGEVLRIMQKLAEEGKTMVVVTH--EMGFArnvSNHVIFL------HQGKIEEQGHPDEVLANPQS 245
Cdd:COG0178 517 GLHQRDNDRLIETLKRLRDLGNTVIVVEHdeDTIRA---ADYIIDIgpgageHGGEVVAQGTPEEILKNPDS 585
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
153-242 |
2.87e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLRIMQKLAEegKTMVVVTHEMGFARNVSNHVIFLHQGKIEE 232
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESI-ESLNMALEKYE--GTLIFVSHDREFVSSLATRIIEITPDGVVD 515
|
90
....*....|.
gi 527036387 233 -QGHPDEVLAN 242
Cdd:PRK15064 516 fSGTYEEYLRS 526
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
9-245 |
4.38e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 9 IDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVSGQNINlvrdkdgqlkvadKNQLR 88
Cdd:PTZ00243 1314 VQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG-------------AYGLR 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 89 LLRTRLTMVFQHFNLWSHmTVLENV---MEA-------PIQVLGLSKQDARDRAvkylakvGIDERQQ---MKYPVhlsg 155
Cdd:PTZ00243 1381 ELRRQFSMIPQDPVLFDG-TVRQNVdpfLEAssaevwaALELVGLRERVASESE-------GIDSRVLeggSNYSV---- 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 156 GQQQRVSIARALAMEPE-VLLFDEPTSALDPELVGEV-LRIMQklAEEGKTMVVVTHEMgfaRNVSNH--VIFLHQGKIE 231
Cdd:PTZ00243 1449 GQRQLMCMARALLKKGSgFILMDEATANIDPALDRQIqATVMS--AFSAYTVITIAHRL---HTVAQYdkIIVMDHGAVA 1523
|
250
....*....|....
gi 527036387 232 EQGHPDEVLANPQS 245
Cdd:PTZ00243 1524 EMGSPRELVMNRQS 1537
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
108-232 |
6.75e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.70 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 108 TVLENVMEApiqvlglsKQD----ARDRAV-KYLAKVGIDERQQMKyPVH-LSGGQQQRVSIARALAMEPEVLLFDEPTS 181
Cdd:PRK11147 399 TVMDNLAEG--------KQEvmvnGRPRHVlGYLQDFLFHPKRAMT-PVKaLSGGERNRLLLARLFLKPSNLLILDEPTN 469
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 527036387 182 ALDPELVgEVLRIMqkLAEEGKTMVVVTHEMGFARN-VSNHVIFLHQGKIEE 232
Cdd:PRK11147 470 DLDVETL-ELLEEL--LDSYQGTVLLVSHDRQFVDNtVTECWIFEGNGKIGR 518
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-250 |
7.14e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.49 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 14 RYGEHEVLKGVSLQANAG--------DvisiigssGSGKSTFLRCINFLEKPSEGSIVVSGQNInlvrdkdgqlkvADKN 85
Cdd:NF033858 10 RYGKTVALDDVSLDIPAGcmvgligpD--------GVGKSSLLSLIAGARKIQQGRVEVLGGDM------------ADAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 86 QLRLLRTRLTMVFQHF--NLWSHMTVLENvmeapIQ----VLGLSKQDARDRAVKYLAKVGID---ERQQMKypvhLSGG 156
Cdd:NF033858 70 HRRAVCPRIAYMPQGLgkNLYPTLSVFEN-----LDffgrLFGQDAAERRRRIDELLRATGLApfaDRPAGK----LSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 157 QQQRVSIARALAMEPEVLLFDEPTSALDP-------ELVGEvLRimqklAE-EGKTMVVVTHEMGFARNVsNHVIFLHQG 228
Cdd:NF033858 141 MKQKLGLCCALIHDPDLLILDEPTTGVDPlsrrqfwELIDR-IR-----AErPGMSVLVATAYMEEAERF-DWLVAMDAG 213
|
250 260
....*....|....*....|..
gi 527036387 229 KIEEQGHPDEVLANPQSPRLQQ 250
Cdd:NF033858 214 RVLATGTPAELLARTGADTLEA 235
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
145-186 |
9.56e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.10 E-value: 9.56e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 527036387 145 QQMKYPVhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE 186
Cdd:PRK11819 439 QQKKVGV-LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
153-210 |
1.79e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.40 E-value: 1.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527036387 153 LSGGQQQRVSIARALAMEPEV---------LLF-DEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTH 210
Cdd:cd03279 124 LSGGETFLASLSLALALSEVLqnrggarleALFiDEGFGTLDPEALEAVATALELIRTENRMVGVISH 191
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
153-211 |
3.06e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.69 E-value: 3.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLriMQKLAEEGKTMVVVTHE 211
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAV-EAL--IQGLVLFQGGVLMVSHD 683
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
153-234 |
3.29e-03 |
|
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: 37.59 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEP------EVLLFDEPTSALDPELVGEVL-RIMQK-LAEEGKTMVVVTHEMGFaRNVSNHVIF 224
Cdd:cd03240 116 CSGGEKVLASLIIRLALAEtfgsncGILALDEPTTNLDEENIEESLaEIIEErKSQKNFQLIVITHDEEL-VDAADHIYR 194
|
90
....*....|
gi 527036387 225 LhqGKIEEQG 234
Cdd:cd03240 195 V--EKDGRQK 202
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
84-252 |
5.22e-03 |
|
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: 37.67 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 84 KNQLRLLRTRLTMVFQHFNlwshmTVLENVMEAPIQVLGLSKQDARDRAVKYLAKVGIDERQQMKYPVHLSG-GQQQRVS 162
Cdd:COG3593 98 EEALEELNEELKEALKALN-----ELLSEYLKELLDGLDLELELSLDELEDLLKSLSLRIEDGKELPLDRLGsGFQRLIL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 163 IARALAM-------EPEVLLFDEPTSALDPELVGEVLRIMQKLAEEGKTMVVVTHEMGFARNVS-NHVIFLHQGKIEEQG 234
Cdd:COG3593 173 LALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVPlENIRRLRRDSGGTTS 252
|
170
....*....|....*...
gi 527036387 235 HPDEVLANPQSPRLQQFL 252
Cdd:COG3593 253 TKLIDLDDEDLRKLLRYL 270
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
153-212 |
6.98e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 37.58 E-value: 6.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPeLVGEVLRIMQKLAEEGKTMVVVTHEM 212
Cdd:TIGR01271 1354 LSNGHKQLMCLARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
153-212 |
8.47e-03 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 36.76 E-value: 8.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036387 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPeLVGEVLRIMQKLAEEGKTMVVVTHEM 212
Cdd:cd03289 139 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQVIRKTLKQAFADCTVILSEHRI 197
|
|
| |
