|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-241 |
3.01e-179 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 491.05 E-value: 3.01e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNINKVRQEVG 82
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHFNLFPHKTVLENITIAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLF 162
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 163 DEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHERTKSFLSKV 241
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-216 |
3.71e-143 |
|
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: 398.83 E-value: 3.71e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNINKVRQEVGM 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VFQHFNLFPHKTVLENITIAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFD 163
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 637158246 164 EPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYI 216
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-242 |
1.47e-131 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 371.44 E-value: 1.47e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTI------------TDP 70
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgelvpADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 71 KvNINKVRQEVGMVFQHFNLFPHKTVLENITIAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIA 150
Cdd:COG4598 88 R-QLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 151 RALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPK 246
|
250
....*....|..
gi 637158246 231 HERTKSFLSKVL 242
Cdd:COG4598 247 SERLRQFLSSSL 258
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-241 |
6.55e-126 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 356.33 E-value: 6.55e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNINKVRQEVG 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHFNLFPHKTVLENITIAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLF 162
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 163 DEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHERTKSFLSKV 241
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-242 |
7.92e-113 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 323.63 E-value: 7.92e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTI------TDPKVNI 74
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 75 NKVRQEVGMVFQHFNLFPHKTVLENITIAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALA 154
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 155 MDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHERT 234
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRT 240
|
....*...
gi 637158246 235 KSFLSKVL 242
Cdd:PRK11264 241 RQFLEKFL 248
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-242 |
1.40e-104 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 305.85 E-value: 1.40e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSF----GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-PKVNINKV 77
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 78 RQEVGMVFQHFNLFPHKTVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDP 157
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVAL-PLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 158 KVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHERTKS 236
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRR 239
|
....*.
gi 637158246 237 FLSKVL 242
Cdd:COG1135 240 FLPTVL 245
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-242 |
8.99e-100 |
|
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: 290.58 E-value: 8.99e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKV----------- 72
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGrngplvpadek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 73 NINKVRQEVGMVFQHFNLFPHKTVLENITIAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARA 152
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 153 LAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQH 231
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|.
gi 637158246 232 ERTKSFLSKVL 242
Cdd:TIGR03005 241 ERTREFLSKVI 251
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-239 |
2.12e-95 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 279.21 E-value: 2.12e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSmITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDP-KVNINKV-- 77
Cdd:COG4161 1 MS-IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSqKPSEKAIrl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 78 -RQEVGMVFQHFNLFPHKTVLENITIAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMD 156
Cdd:COG4161 80 lRQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 157 PKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEaLFGNPQHERTKS 236
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQPQTEAFAH 238
|
...
gi 637158246 237 FLS 239
Cdd:COG4161 239 YLS 241
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-239 |
2.33e-95 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 279.21 E-value: 2.33e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSmITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGH-----TITDPKvNIN 75
Cdd:PRK11124 1 MS-IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfsKTPSDK-AIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 76 KVRQEVGMVFQHFNLFPHKTVLENITIAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAM 155
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 156 DPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAlFGNPQHERTK 235
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAFK 237
|
....
gi 637158246 236 SFLS 239
Cdd:PRK11124 238 NYLS 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-230 |
1.53e-92 |
|
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: 271.76 E-value: 1.53e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDH----EVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-PKVNINKV 77
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 78 RQEVGMVFQHFNLFPHKTVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDP 157
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAL-PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 637158246 158 KVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-242 |
3.83e-90 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 266.45 E-value: 3.83e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTIT-----------DPKV 72
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 73 NINKVRQEVGMVFQHFNLFPHKTVLENITIAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQ-SFPNQLSGGQKQRVAIAR 151
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 152 ALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQH 231
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
250
....*....|.
gi 637158246 232 ERTKSFLSKVL 242
Cdd:PRK10619 246 PRLQQFLKGSL 256
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-239 |
1.23e-86 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 257.66 E-value: 1.23e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDI-----TAGEVVVHGHTITDPKVNINKVR 78
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDGEDIYDPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 79 QEVGMVFQHFNLFPhKTVLENITIAPiKVKGIEKKA----AVEKAldlLEKVGL----KDKAQSFPNQLSGGQKQRVAIA 150
Cdd:COG1117 92 RRVGMVFQKPNPFP-KSIYDNVAYGL-RLHGIKSKSeldeIVEES---LRKAALwdevKDRLKKSALGLSGGQQQRLCIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 151 RALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAvEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDPISTAKIEELILELK-KDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPK 245
|
....*....
gi 637158246 231 HERTKSFLS 239
Cdd:COG1117 246 DKRTEDYIT 254
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-219 |
4.16e-86 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 254.97 E-value: 4.16e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 2 SMITVKNLKKSFGD----HEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-PKVNINK 76
Cdd:COG1136 3 PLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 77 VR-QEVGMVFQHFNLFPHKTVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAM 155
Cdd:COG1136 83 LRrRHIGFVFQFFNLLPELTALENVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 156 DPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFArEVGDRVIFMDGGYIVEE 219
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELA-ARADRVIRLRDGRIVSD 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-238 |
1.77e-84 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 255.41 E-value: 1.77e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKvRQe 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG--LPPEK-RN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFNLFPHKTVLENITiAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVL 160
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVA-FGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 161 LFDEPTSALDP----EVVGDVLAVMKQLaveGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHERTKS 236
Cdd:COG3842 158 LLDEPLSALDAklreEMREELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVAD 234
|
..
gi 637158246 237 FL 238
Cdd:COG3842 235 FI 236
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-242 |
1.53e-83 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 252.80 E-value: 1.53e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSF----GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVN-INKV 77
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKeLRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 78 RQEVGMVFQHFNLFPHKTVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDP 157
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 158 KVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHERTKS 236
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTRE 239
|
....*.
gi 637158246 237 FLSKVL 242
Cdd:PRK11153 240 FIQSTL 245
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-239 |
1.33e-82 |
|
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: 255.60 E-value: 1.33e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSF-----GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-PKVNINK 76
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 77 VRQEVGMVFQH-FN-LFPHKTVLENITiAPIKVKGIEKKAAV-EKALDLLEKVGL-KDKAQSFPNQLSGGQKQRVAIARA 152
Cdd:COG1123 340 LRRRVQMVFQDpYSsLNPRMTVGDIIA-EPLRLHGLLSRAERrERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 153 LAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQH 231
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQH 498
|
....*...
gi 637158246 232 ERTKSFLS 239
Cdd:COG1123 499 PYTRALLA 506
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-219 |
4.98e-82 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 245.77 E-value: 4.98e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSF----GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPkvnink 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 77 vRQEVGMVFQHFNLFPHKTVLENITIAPiKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMD 156
Cdd:COG1116 79 -GPDRGVVFQEPALLPWLTVLDNVALGL-ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637158246 157 PKVLLFDEPTSALDP---EVVGDVLavMKQLAVEGMTMIVVTHEMgfaRE---VGDRVIFMDG--GYIVEE 219
Cdd:COG1116 157 PEVLLMDEPFGALDAltrERLQDEL--LRLWQETGKTVLFVTHDV---DEavfLADRVVVLSArpGRIVEE 222
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-225 |
1.13e-81 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 244.58 E-value: 1.13e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 2 SMITVKNLKKSF-GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTIT-DPKVNINKVRQ 79
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTaLRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQHFNLFPHKTVLENI------TIAPIK-VKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARA 152
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVlagrlgRTSTWRsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 637158246 153 LAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-225 |
1.51e-81 |
|
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: 243.63 E-value: 1.51e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDI-----TAGEVVVHGHTITDPKVNINKVR 78
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 79 QEVGMVFQHFNLFPhKTVLENITIAPiKVKGIEKKAAVEK-ALDLLEKVGLKD--KAQSFPNQLSGGQKQRVAIARALAM 155
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGL-RLHGIKLKEELDErVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 156 DPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEgMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-238 |
2.04e-81 |
|
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: 243.73 E-value: 2.04e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-PKVNINKVRQEV 81
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFNLFPHKTVLENITIAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLL 161
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 637158246 162 FDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFgNPQHERTKSFL 238
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL-ASDDPWVRQFL 241
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-216 |
3.44e-81 |
|
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: 242.40 E-value: 3.44e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGD----HEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVN--INKV 77
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 78 RQEVGMVFQHFNLFPHKTVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDP 157
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVEL-PLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 158 KVLLFDEPTSALDPEVVGDVLAVMKQLA-VEGMTMIVVTHEMGFAREvGDRVIFMDGGYI 216
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-214 |
6.61e-78 |
|
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: 232.46 E-value: 6.61e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNINKVRQEVGM 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VFQHFNLFPHKTVLENITIApikvkgiekkaavekaldllekvglkdkaqsfpnqLSGGQKQRVAIARALAMDPKVLLFD 163
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 637158246 164 EPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGG 214
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-225 |
7.86e-77 |
|
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: 232.07 E-value: 7.86e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGD-HEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTIT-DPKVNINKVRQEV 81
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINkLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFNLFPHKTVLENI------TIAPIKV-KGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALA 154
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlgRRSTWRSlFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637158246 155 MDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-230 |
1.26e-76 |
|
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: 231.07 E-value: 1.26e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSF-GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQEVG 82
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT--KKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQhfN----LFpHKTVLENITIAPiKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPK 158
Cdd:COG1122 79 LVFQ--NpddqLF-APTVEEDVAFGP-ENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637158246 159 VLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-221 |
1.94e-76 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 230.32 E-value: 1.94e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSF-GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-PKVNINKVRQE 80
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFNLFPHKTVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVL 160
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVAL-PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637158246 161 LFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDK 221
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-225 |
3.64e-75 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 227.64 E-value: 3.64e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHtitDPKVNINKVRQEVGM 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGE---DVARDPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VFQHFNLFPHKTVLENITIApIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFD 163
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFF-ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637158246 164 EPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-218 |
3.72e-75 |
|
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: 226.63 E-value: 3.72e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNinkvRQEVGM 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE----RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VFQHFNLFPHKTVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFD 163
Cdd:cd03259 77 VFQDYALFPHLTVAENIAF-GLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 164 EPTSALDP----EVVGDVLAVMKQLaveGMTMIVVTHEMGFAREVGDRVIFMDGGYIVE 218
Cdd:cd03259 156 EPLSALDAklreELREELKELQREL---GITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-219 |
6.56e-75 |
|
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: 226.20 E-value: 6.56e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGD----HEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPkvninkvRQ 79
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-------GP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQHFNLFPHKTVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKV 159
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVAL-GLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 160 LLFDEPTSALDP---EVVGDVLavMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDG--GYIVEE 219
Cdd:cd03293 153 LLLDEPFSALDAltrEQLQEEL--LDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-225 |
1.60e-74 |
|
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: 226.41 E-value: 1.60e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFG-DHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPK-VNINKVRQE 80
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFNLFPHKTVLENITIAPIKVK-------GIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARAL 153
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGYKptwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637158246 154 AMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-238 |
1.44e-73 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 227.26 E-value: 1.44e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD--PKvninkvR 78
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDlpPK------D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 79 QEVGMVFQHFNLFPHKTVLENITIaPIKVKGI---EKKAAVEKALDLLekvGLKDKAQSFPNQLSGGQKQRVAIARALAM 155
Cdd:COG3839 75 RNIAMVFQSYALYPHMTVYENIAF-PLKLRKVpkaEIDRRVREAAELL---GLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 156 DPKVLLFDEPTSALDP----EVVGDVLAVMKQLaveGMTMIVVTHE----MGFArevgDRVIFMDGGYIVEEDKPEALFG 227
Cdd:COG3839 151 EPKVFLLDEPLSNLDAklrvEMRAEIKRLHRRL---GTTTIYVTHDqveaMTLA----DRIAVMNDGRIQQVGTPEELYD 223
|
250
....*....|.
gi 637158246 228 NPQHERTKSFL 238
Cdd:COG3839 224 RPANLFVAGFI 234
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-219 |
2.46e-73 |
|
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: 222.77 E-value: 2.46e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSF----GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNINKVR 78
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 79 -QEVGMVFQH----FNlfPHKTVLENITiAPIKVKGIEKK--AAVEKALDLLEKVGL-KDKAQSFPNQLSGGQKQRVAIA 150
Cdd:cd03257 81 rKEIQMVFQDpmssLN--PRMTIGEQIA-EPLRIHGKLSKkeARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 151 RALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEE 219
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-242 |
4.22e-73 |
|
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: 222.76 E-value: 4.22e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFG----DHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKvnINKVR 78
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRR--RKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 79 QEVGMVFQH----FNlfPHKTVLEniTIA-PIKVKGIekKAAVEKALDLLEKVGL-KDKAQSFPNQLSGGQKQRVAIARA 152
Cdd:COG1124 79 RRVQMVFQDpyasLH--PRHTVDR--ILAePLRIHGL--PDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 153 LAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQH 231
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
250
....*....|.
gi 637158246 232 ERTKSFLSKVL 242
Cdd:COG1124 233 PYTRELLAASL 243
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-238 |
1.77e-72 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 224.64 E-value: 1.77e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSmITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTitdpkVNINKVRQE 80
Cdd:COG1118 1 MS-IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD-----LFTNLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 --VGMVFQHFNLFPHKTVLENITIAPiKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPK 158
Cdd:COG1118 75 rrVGFVFQHYALFPHMTVAENIAFGL-RVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 159 VLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHERTKSF 237
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARF 233
|
.
gi 637158246 238 L 238
Cdd:COG1118 234 L 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-237 |
2.75e-71 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 217.75 E-value: 2.75e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-PKVNINKVRQEVG 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHFNLFPHKTVLENITIaPIKVKGIEKKAAV-EKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLL 161
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAF-PLREHTRLSEEEIrEIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 637158246 162 FDEPTSALDPEVVGDVLAVMKQL-AVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFgNPQHERTKSF 237
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR-ASDDPLVRQF 235
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-229 |
7.56e-71 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 221.52 E-value: 7.56e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDH---------------EVLK---------DINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDIT 56
Cdd:COG4175 1 MPKIEVRNLYKIFGKRperalklldqgkskdEILEktgqtvgvnDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 57 AGEVVVHGHTITD-PKVNINKVRQE-VGMVFQHFNLFPHKTVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQS 134
Cdd:COG4175 81 AGEVLIDGEDITKlSKKELRELRRKkMSMVFQHFALLPHRTVLENVAF-GLEIQGVPKAERRERAREALELVGLAGWEDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 135 FPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDP----EVVGDVLAVMKQLaveGMTMIVVTHEMGFAREVGDRVIF 210
Cdd:COG4175 160 YPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrEMQDELLELQAKL---KKTIVFITHDLDEALRLGDRIAI 236
|
250
....*....|....*....
gi 637158246 211 MDGGYIVEEDKPEALFGNP 229
Cdd:COG4175 237 MKDGRIVQIGTPEEILTNP 255
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-241 |
1.20e-69 |
|
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: 214.81 E-value: 1.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDH---------------EVLK---------DINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGE 59
Cdd:cd03294 1 IKIKGLYKIFGKNpqkafkllakgkskeEILKktgqtvgvnDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 60 VVVHGHTIT--DPKVNINKVRQEVGMVFQHFNLFPHKTVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPN 137
Cdd:cd03294 81 VLIDGQDIAamSRKELRELRRKKISMVFQSFALLPHRTVLENVAF-GLEVQGVPRAEREERAAEALELVGLEGWEHKYPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 138 QLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYI 216
Cdd:cd03294 160 ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
250 260
....*....|....*....|....*
gi 637158246 217 VEEDKPEALFGNPQHERTKSFLSKV 241
Cdd:cd03294 240 VQVGTPEEILTNPANDYVREFFRGV 264
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-214 |
2.10e-69 |
|
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: 211.94 E-value: 2.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 6 VKNLKKSFGDHE--VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQEVGM 83
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT--KLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VFQHFNL-FPHKTVLENITIAPiKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLF 162
Cdd:cd03225 80 VFQNPDDqFFGPTVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 637158246 163 DEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGG 214
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-231 |
1.69e-68 |
|
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: 213.38 E-value: 1.69e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSF----GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLED---ITAGEVVVHGHTITD-PKVNI 74
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKlSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 75 NKVR-QEVGMVFQH----FNlfPHKTVLENITIAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQ---SFPNQLSGGQKQR 146
Cdd:COG0444 81 RKIRgREIQMIFQDpmtsLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERrldRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 147 VAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
....*.
gi 637158246 226 FGNPQH 231
Cdd:COG0444 239 FENPRH 244
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-230 |
7.94e-67 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 214.77 E-value: 7.94e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MS-MITVKNLKKSF--GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITA---GEVVVHGHTITDPKVNI 74
Cdd:COG1123 1 MTpLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 75 NkvRQEVGMVFQHF--NLFPHkTVLENITIApIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARA 152
Cdd:COG1123 81 R--GRRIGMVFQDPmtQLNPV-TVGDQIAEA-LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 153 LAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-240 |
1.29e-64 |
|
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: 200.99 E-value: 1.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGD-HEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQEVG 82
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE--QDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHFNLFPHKTVLENITIAPiKVKGIEKKAAVEKALDLLEKVGLKDK--AQSFPNQLSGGQKQRVAIARALAMDPKVL 160
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 161 LFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHERTKSFLS 239
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
|
.
gi 637158246 240 K 240
Cdd:cd03295 238 A 238
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-238 |
5.91e-63 |
|
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: 196.79 E-value: 5.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSmITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNinkvRQE 80
Cdd:cd03296 1 MS-IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ----ERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFNLFPHKTVLENITIApIKVKGIEK---KAAV-EKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMD 156
Cdd:cd03296 76 VGFVFQHYALFRHMTVFDNVAFG-LRVKPRSErppEAEIrAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 157 PKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHERTK 235
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVY 234
|
...
gi 637158246 236 SFL 238
Cdd:cd03296 235 SFL 237
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-228 |
8.63e-63 |
|
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: 197.27 E-value: 8.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHE--VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKvNINKVRQEV 81
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEE-NLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQH-FNLFPHKTV-------LENITIAPIKVKGIekkaaVEKALdllEKVGLKDKAQSFPNQLSGGQKQRVAIARAL 153
Cdd:TIGR04520 80 GMVFQNpDNQFVGATVeddvafgLENLGVPREEMRKR-----VDEAL---KLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 154 AMDPKVLLFDEPTSALDPEVVGDVLAVMKQL-AVEGMTMIVVTHEMGFAREvGDRVIFMDGGYIVEEDKPEALFGN 228
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-230 |
1.57e-62 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 195.15 E-value: 1.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKvRQeVGM 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPHK-RP-VNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VFQHFNLFPHKTVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFD 163
Cdd:cd03300 77 VFQNYALFPHLTVFENIAF-GLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 637158246 164 EPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-230 |
4.22e-62 |
|
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: 194.19 E-value: 4.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 6 VKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNInKVRQEVGMVF 85
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 86 QHFNLFPHKTVLENITIAPIKVKG---------IEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMD 156
Cdd:cd03219 82 QIPRLFPELTVLENVMVAAQARTGsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 637158246 157 PKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-230 |
3.20e-61 |
|
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: 193.44 E-value: 3.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNL-----KKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTIT-DPKVNINKV 77
Cdd:TIGR04521 1 IKLKNVsyiyqPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITaKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 78 RQEVGMVFQhfnlFPHK-----TVLENITIAPIKVkGIEKKAAVEKALDLLEKVGLKD--KAQSfPNQLSGGQKQRVAIA 150
Cdd:TIGR04521 81 RKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNL-GLSEEEAEERVKEALELVGLDEeyLERS-PFELSGGQMRRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 151 RALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNP 229
Cdd:TIGR04521 155 GVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
.
gi 637158246 230 Q 230
Cdd:TIGR04521 235 D 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-239 |
4.56e-61 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 192.30 E-value: 4.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDI-----TAGEVVVHGHTITDPKVNINKV 77
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 78 RQEVGMVFQHFNLFPHkTVLENItIAPIKVKGIEKKA----AVEKAL---DLLEKVglKDKAQSFPNQLSGGQKQRVAIA 150
Cdd:PRK14239 85 RKEIGMVFQQPNPFPM-SIYENV-VYGLRLKGIKDKQvldeAVEKSLkgaSIWDEV--KDRLHDSALGLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 151 RALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAvEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLK-DDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
....*....
gi 637158246 231 HERTKSFLS 239
Cdd:PRK14239 240 HKETEDYIS 248
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-214 |
1.07e-60 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 189.64 E-value: 1.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQEVGM 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA--MPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VFQHFNLFPhKTVLENITiAPIKVKgiEKKAAVEKALDLLEKVGLKDKA--QSFpNQLSGGQKQRVAIARALAMDPKVLL 161
Cdd:COG4619 79 VPQEPALWG-GTVRDNLP-FPFQLR--ERKFDRERALELLERLGLPPDIldKPV-ERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 637158246 162 FDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGG 214
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-224 |
4.25e-60 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 189.18 E-value: 4.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 2 SMITVKNLKKSFGDHE----VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTIT----DPKVn 73
Cdd:COG4181 7 PIIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaldeDARA- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 74 inKVR-QEVGMVFQHFNLFPHKTVLENITIaPIKVKGieKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARA 152
Cdd:COG4181 86 --RLRaRHVGFVFQSFQLLPTLTALENVML-PLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637158246 153 LAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVgDRVIFMDGGYIVEEDKPEA 224
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAARC-DRVLRLRAGRLVEDTAATA 232
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-234 |
5.01e-60 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 189.14 E-value: 5.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHtitdpkvNINKVRQE 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK-------PPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFNL---FPhKTVLENIT---IAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALA 154
Cdd:COG1121 77 IGYVPQRAEVdwdFP-ITVRDVVLmgrYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 155 MDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGyIVEEDKPEALFGNPQHERT 234
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLSRA 234
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-214 |
9.86e-60 |
|
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: 187.46 E-value: 9.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSF-GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-PKVNINKVRQE 80
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFNLFPHKTVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVL 160
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 637158246 161 LFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGG 214
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-225 |
2.94e-59 |
|
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: 186.49 E-value: 2.94e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-PKVNInkVRQEVG 82
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlPPHER--ARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHFNLFPHKTVLENITIAPIKVKGIEKKAAVEKALDLLEKvgLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLF 162
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637158246 163 DEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-230 |
4.70e-59 |
|
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: 187.17 E-value: 4.70e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVN-InkVRQ 79
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHrI--ARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQHFNLFPHKTVLENITIA--------------PIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQ 145
Cdd:COG0411 80 GIARTFQNPRLFPELTVLENVLVAaharlgrgllaallRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 146 RVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQL-AVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEA 224
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
....*.
gi 637158246 225 LFGNPQ 230
Cdd:COG0411 240 VRADPR 245
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-241 |
5.31e-59 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 190.29 E-value: 5.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSmITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpkvNINKVRQE 80
Cdd:PRK10851 1 MS-IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS----RLHARDRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFNLFPHKTVLENI----TIAPiKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMD 156
Cdd:PRK10851 76 VGFVFQHYALFRHMTVFDNIafglTVLP-RRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 157 PKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHERTK 235
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVL 234
|
....*.
gi 637158246 236 SFLSKV 241
Cdd:PRK10851 235 EFMGEV 240
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-226 |
1.44e-58 |
|
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: 186.02 E-value: 1.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQEVG 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAS--LSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHFNLFPHKTVLENITI--AP-IKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKV 159
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALgrYPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 637158246 160 LLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALF 226
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-214 |
3.08e-58 |
|
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: 182.21 E-value: 3.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHtitDPKVNINKVRQEVGM 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK---DIKKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VFQHFNLFPHKTVLENItiapikvkgiekkaavekaldllekvglkdkaqsfpnQLSGGQKQRVAIARALAMDPKVLLFD 163
Cdd:cd03230 78 LPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 637158246 164 EPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGG 214
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-225 |
4.17e-58 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 184.29 E-value: 4.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHtitDPKVNINKVRQEVG 82
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE---DVRKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHFNLFPHKTVLENITIApIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLF 162
Cdd:COG4555 78 VLPDERGLYDRLTVRENIRYF-AELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637158246 163 DEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
4-217 |
9.36e-58 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 182.91 E-value: 9.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHE----VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDP-KVNINKVR 78
Cdd:TIGR02982 2 ISIRNLNHYYGHGSlrkqVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGAsKKQLVQLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 79 QEVGMVFQHFNLFPHKTVLENITIAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPK 158
Cdd:TIGR02982 82 RRIGYIFQAHNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637158246 159 VLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEmgfAR--EVGDRVIFMDGGYIV 217
Cdd:TIGR02982 162 LVLADEPTAALDSKSGRDVVELMQKLAKEqGCTILMVTHD---NRilDVADRILQMEDGKLL 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-238 |
4.25e-57 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 181.49 E-value: 4.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHevLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHG--HTITDPKvninkvRQE 80
Cdd:COG3840 1 MLRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdLTALPPA------ERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFNLFPHKTVLENITIapikvkGI--------EKKAAVEKALdllEKVGLKDKAQSFPNQLSGGQKQRVAIARA 152
Cdd:COG3840 73 VSMLFQENNLFPHLTVAQNIGL------GLrpglkltaEQRAQVEQAL---ERVGLAGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 153 LAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQH 231
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPP 223
|
....*..
gi 637158246 232 ERTKSFL 238
Cdd:COG3840 224 PALAAYL 230
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-225 |
1.04e-56 |
|
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: 191.97 E-value: 1.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHE--VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQEV 81
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQ--IDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFNLFpHKTVLENITIApikvkgiEKKAAVEKALDLLEKVGLKDKAQSFPN-----------QLSGGQKQRVAIA 150
Cdd:COG2274 552 GVVLQDVFLF-SGTIRENITLG-------DPDATDEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 151 RALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAvEGMTMIVVTHEMGFAREVgDRVIFMDGGYIVEEDKPEAL 225
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDGTHEEL 696
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-241 |
3.61e-56 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 182.24 E-value: 3.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSF--------GDHEVLKDINAV---IEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-PK 71
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgRTVGVVKAVDGVsfdIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGlSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 72 VNINKVRQEVGMVFQ--HFNLFPHKTVLENITiAPIKVKGIEKKAAV-EKALDLLEKVGLK-DKAQSFPNQLSGGQKQRV 147
Cdd:COG4608 88 RELRPLRRRMQMVFQdpYASLNPRMTVGDIIA-EPLRIHGLASKAERrERVAELLELVGLRpEHADRYPHEFSGGQRQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 148 AIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALF 226
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELY 246
|
250
....*....|....*
gi 637158246 227 GNPQHERTKSFLSKV 241
Cdd:COG4608 247 ARPLHPYTQALLSAV 261
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-239 |
4.81e-56 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 179.34 E-value: 4.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKL-----EDITAGEVVVHGHTITdpKVNIN 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIF--KMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 76 KVRQEVGMVFQHFNLFPHKTVLENITIAPIKVKGIEKKAAV-EKALDLLEKVGL----KDKAQSFPNQLSGGQKQRVAIA 150
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELqERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 151 RALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEgMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
....*....
gi 637158246 231 HERTKSFLS 239
Cdd:PRK14247 238 HELTEKYVT 246
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-239 |
5.66e-56 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 179.59 E-value: 5.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 7 KNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDI-----TAGEVVVHGHTITDPKVNINKVRQEV 81
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPDVDPVEVRRRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFNLFPhKTVLENITIAPiKVKGIEKK--AAVEKALD---LLEKVglKDKAQSFPNQLSGGQKQRVAIARALAMD 156
Cdd:PRK14243 94 GMVFQKPNPFP-KSIYDNIAYGA-RINGYKGDmdELVERSLRqaaLWDEV--KDKLKQSGLSLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 157 PKVLLFDEPTSALDPEVVGDVLAVMKQLaVEGMTMIVVTHEMGFAREVGDRVIFMDG---------GYIVEEDKPEALFG 227
Cdd:PRK14243 170 PEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSDMTAFFNVeltegggryGYLVEFDRTEKIFN 248
|
250
....*....|..
gi 637158246 228 NPQHERTKSFLS 239
Cdd:PRK14243 249 SPQQQATRDYVS 260
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-218 |
1.13e-55 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 177.06 E-value: 1.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD--PKvninkvRQEV 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlpPK------DRDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFNLFPHKTVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLL 161
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAF-GLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 637158246 162 FDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVE 218
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-242 |
2.89e-55 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 177.34 E-value: 2.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITA-----GEVVVHGHTITDPKVNINKVR 78
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 79 QEVGMVFQHFNLFPHKTVLENITIApIKVKGI--EKKAAVEKALDLLEKVGL----KDKAQSFPNQLSGGQKQRVAIARA 152
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 153 LAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEgMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHE 232
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHE 242
|
250
....*....|
gi 637158246 233 RTKSFLSKVL 242
Cdd:PRK14267 243 LTEKYVTGAL 252
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-235 |
9.35e-55 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 183.35 E-value: 9.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGD----HEVLKDINAVIEEKEVVCVIGPSGSGKS-TFLRCLNKLED---ITAGEVVVHGHTITD-PK 71
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDpaaHPSGSILFDGQDLLGlSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 72 VNINKVR-QEVGMVFQH----FNlfPHKTVLENItIAPIKV-KGIEKKAAVEKALDLLEKVGLKDKAQ---SFPNQLSGG 142
Cdd:COG4172 84 RELRRIRgNRIAMIFQEpmtsLN--PLHTIGKQI-AEVLRLhRGLSGAAARARALELLERVGIPDPERrldAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 143 QKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQL-AVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDK 221
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
250
....*....|....
gi 637158246 222 PEALFGNPQHERTK 235
Cdd:COG4172 241 TAELFAAPQHPYTR 254
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-225 |
2.33e-54 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 183.44 E-value: 2.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLkkSF---GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQE 80
Cdd:COG1132 340 IEFENV--SFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD--LTLESLRRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFNLFpHKTVLENITIAPIKVKgiekKAAVEKALdllEKVGLKDKAQSFPNQ-----------LSGGQKQRVAI 149
Cdd:COG1132 416 IGVVPQDTFLF-SGTIRENIRYGRPDAT----DEEVEEAA---KAAQAHEFIEALPDGydtvvgergvnLSGGQRQRIAI 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 150 ARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAvEGMTMIVVTHEMGFAREVgDRVIFMDGGYIVEEDKPEAL 225
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRNA-DRILVLDDGRIVEQGTHEEL 561
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-230 |
4.49e-54 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 173.63 E-value: 4.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNiNKVRQE 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPH-RIARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFNLFPHKTVLENITIAPIKVKGIEK-KAAVEKALDLLEKvgLKDKAQSFPNQLSGGQKQRVAIARALAMDPKV 159
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLLLGAYARRDRAEvRADLERVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637158246 160 LLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-214 |
1.74e-53 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 169.73 E-value: 1.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 5 TVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQEVGMV 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA--KLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 85 FQhfnlfphktvlenitiapikvkgiekkaavekaldllekvglkdkaqsfpnqLSGGQKQRVAIARALAMDPKVLLFDE 164
Cdd:cd00267 79 PQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 637158246 165 PTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGG 214
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-211 |
2.63e-53 |
|
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: 170.87 E-value: 2.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 6 VKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHG---HTITDPKVNINKvRQEVG 82
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGqetPPLNSKKASKFR-REKLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHFNLFPHKTVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLF 162
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDL-GLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 637158246 163 DEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFArEVGDRVIFM 211
Cdd:TIGR03608 159 DEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-214 |
4.71e-53 |
|
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: 170.41 E-value: 4.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 6 VKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGhtitdpkVNINKVRQEVGMVF 85
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-------KPLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 86 QHFNL---FPhKTVLENITIAPIKVKG---IEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKV 159
Cdd:cd03235 75 QRRSIdrdFP-ISVRDVVLMGLYGHKGlfrRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 160 LLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGG 214
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-238 |
1.03e-52 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 174.45 E-value: 1.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVvhghtITDPKVN-INKVRQ 79
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLF-----IGEKRMNdVPPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQHFNLFPHKTVLENITIApIKVKGIEK---KAAVEKALDLLEKVGLKDKAqsfPNQLSGGQKQRVAIARALAMD 156
Cdd:PRK11000 76 GVGMVFQSYALYPHLSVAENMSFG-LKLAGAKKeeiNQRVNQVAEVLQLAHLLDRK---PKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 157 PKVLLFDEPTSALDPevvgdvlAVMKQLAVE--------GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGN 228
Cdd:PRK11000 152 PSVFLLDEPLSNLDA-------ALRVQMRIEisrlhkrlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHY 224
|
250
....*....|
gi 637158246 229 PQHERTKSFL 238
Cdd:PRK11000 225 PANRFVAGFI 234
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-216 |
5.41e-52 |
|
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: 167.97 E-value: 5.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSF-GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-PKVNINKVRQEV 81
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFNLFPHKTVLENITIApIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLL 161
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFA-LEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 162 FDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYI 216
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-214 |
1.23e-51 |
|
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: 165.25 E-value: 1.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGD--HEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQEV 81
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRD--LDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFNLFpHKTVLENItiapikvkgiekkaavekaldllekvglkdkaqsfpnqLSGGQKQRVAIARALAMDPKVLL 161
Cdd:cd03228 79 AYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 637158246 162 FDEPTSALDPEVVGDVLAVMKQLAvEGMTMIVVTHEMGFAREVgDRVIFMDGG 214
Cdd:cd03228 120 LDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRDA-DRIIVLDDG 170
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-238 |
7.66e-51 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 169.13 E-value: 7.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 7 KNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNinkvRQEVGMVFQ 86
Cdd:PRK11432 10 KNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ----QRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 87 HFNLFPHKTVLENITIApIKVKGI---EKKAAVEKALDLLEKVGLKDKaqsFPNQLSGGQKQRVAIARALAMDPKVLLFD 163
Cdd:PRK11432 86 SYALFPHMSLGENVGYG-LKMLGVpkeERKQRVKEALELVDLAGFEDR---YVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 164 EPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHERTKSFL 238
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFM 237
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-229 |
1.22e-50 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 168.97 E-value: 1.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpkvNINKVRQE 80
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT----HVPAENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFNLFPHKTVLENITIApIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVL 160
Cdd:PRK09452 88 VNTVFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 161 LFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNP 229
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-167 |
5.52e-50 |
|
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: 160.51 E-value: 5.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 19 LKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPkvNINKVRQEVGMVFQHFNLFPHKTVLE 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD--ERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637158246 99 NITIAPIkVKGIEKKAAVEKALDLLEKVGLKDKA----QSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTS 167
Cdd:pfam00005 79 NLRLGLL-LKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-225 |
7.88e-50 |
|
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: 171.09 E-value: 7.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 2 SMITVKNLkkSF---GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVR 78
Cdd:COG4988 335 PSIELEDV--SFsypGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD--LDPASWR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 79 QEVGMVFQHFNLFpHKTVLENITIApikvkgieKKAAVEKAL-DLLEKVGLKDKAQSFPN-----------QLSGGQKQR 146
Cdd:COG4988 411 RQIAWVPQNPYLF-AGTIRENLRLG--------RPDASDEELeAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 147 VAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAvEGMTMIVVTHEMGFAREVgDRVIFMDGGYIVEEDKPEAL 225
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHEEL 558
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-170 |
8.16e-50 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 163.88 E-value: 8.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFG----DHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVnink 76
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 77 vrqEVGMVFQHFNLFPHKTVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMD 156
Cdd:COG4525 77 ---DRGVVFQKDALLPWLNVLDNVAF-GLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170
....*....|....
gi 637158246 157 PKVLLFDEPTSALD 170
Cdd:COG4525 153 PRFLLMDEPFGALD 166
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
2-229 |
8.32e-50 |
|
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: 166.43 E-value: 8.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 2 SMITVkNLKKSFGDHEVlkDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNIN-KVRQ- 79
Cdd:COG4148 1 MMLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFlPPHRr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQHFNLFPHKTVLENITIAPIKVKGIEKKAAVEKALDLLekvGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKV 159
Cdd:COG4148 78 RIGYVFQEARLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637158246 160 LLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNP 229
Cdd:COG4148 155 LLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-217 |
2.61e-49 |
|
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: 159.91 E-value: 2.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 5 TVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKvnINKVRQEVGMV 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS--PKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 85 FQhfnlfphktvlenitiapikvkgiekkaavekaldLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDE 164
Cdd:cd03214 79 PQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 637158246 165 PTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIV 217
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-239 |
3.10e-49 |
|
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: 161.35 E-value: 3.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEvLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpkvNINKVRQEVGM 83
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT----NLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VFQHFNLFPHKTVLENITIApIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFD 163
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 637158246 164 EPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHERTKSFLS 239
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
3-216 |
5.40e-49 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 160.27 E-value: 5.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDH----EVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVN--INK 76
Cdd:NF038007 1 MLNMQNAEKCYITKtiktKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSqkIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 77 VRQEVGMVFQHFNLFPHKTVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMD 156
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVAL-PLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 157 PKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGfAREVGDRVIFMDGGYI 216
Cdd:NF038007 160 PALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-230 |
2.45e-48 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 160.16 E-value: 2.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 2 SMITVKNLKKSFGDHE--VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQ 79
Cdd:PRK13632 6 VMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS--KENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQH-FNLFPHKTV-------LENITIAPIKVKGIekkaavekALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIAR 151
Cdd:PRK13632 84 KIGIIFQNpDNQFIGATVeddiafgLENKKVPPKKMKDI--------IDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 152 ALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGM-TMIVVTHEMgfaREV--GDRVIFMDGGYIVEEDKPEALFGN 228
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDM---DEAilADKVIVFSEGKLIAQGKPKEILNN 232
|
..
gi 637158246 229 PQ 230
Cdd:PRK13632 233 KE 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-230 |
4.45e-48 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 160.19 E-value: 4.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 19 LKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNIN--KVRQEVGMVFQhfnlFPH--- 93
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKlkPLRKKVGIVFQ----FPEhql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 94 --KTVLENITIAPIKVkGIEKKAAVEKALDLLEKVGLKDK--AQSfPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSAL 169
Cdd:PRK13634 99 feETVEKDICFGPMNF-GVSEEDAKQKAREMIELVGLPEEllARS-PFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637158246 170 DPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-239 |
1.12e-47 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 164.86 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSF-----------GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDiTAGEVVVHGHTITD-PK 71
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGlSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 72 VNINKVRQEVGMVFQ----HFNlfPHKTVLEniTIA-PIKVKGIEKKAA--VEKALDLLEKVGLK-DKAQSFPNQLSGGQ 143
Cdd:COG4172 355 RALRPLRRRMQVVFQdpfgSLS--PRMTVGQ--IIAeGLRVHGPGLSAAerRARVAEALEEVGLDpAARHRYPHEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 144 KQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKP 222
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPT 510
|
250
....*....|....*..
gi 637158246 223 EALFGNPQHERTKSFLS 239
Cdd:COG4172 511 EQVFDAPQHPYTRALLA 527
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-204 |
1.64e-47 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 156.10 E-value: 1.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNinkVRQEVG 82
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED---YRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHFNLFPHKTVLENITIApIKVKGIEkkAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLF 162
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFW-AALYGLR--ADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 637158246 163 DEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTH---EMGFAREV 204
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqplELAAARVL 200
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-241 |
2.88e-47 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 159.20 E-value: 2.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 34 VIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpkvNINKVRQEVGMVFQHFNLFPHKTVLENITIaPIKVKGIEKK 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT----NVPPHLRHINMVFQSYALFPHMTVEENVAF-GLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 114 AAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALD----PEVVGDVLAVMKQLaveGM 189
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQEQL---GI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 637158246 190 TMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHERTKSFLSKV 241
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-228 |
3.57e-47 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 157.90 E-value: 3.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSmITVKNL-----KKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNIN 75
Cdd:PRK13637 1 MS-IKIENLthiymEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 76 KVRQEVGMVFQH--FNLFpHKTVLENITIAPIKVkGIEK---KAAVEKALDL--LEKVGLKDKAqsfPNQLSGGQKQRVA 148
Cdd:PRK13637 80 DIRKKVGLVFQYpeYQLF-EETIEKDIAFGPINL-GLSEeeiENRVKRAMNIvgLDYEDYKDKS---PFELSGGQKRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 149 IARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFG 227
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
.
gi 637158246 228 N 228
Cdd:PRK13637 235 E 235
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-225 |
5.29e-47 |
|
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: 163.40 E-value: 5.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLkkSFG----DHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQ 79
Cdd:COG4987 334 LELEDV--SFRypgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD--LDEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQHFNLFpHKTVLENITIA-PikvkgiekKAAVEKALDLLEKVGLKDKAQSFPN-----------QLSGGQKQRV 147
Cdd:COG4987 410 RIAVVPQRPHLF-DTTLRENLRLArP--------DATDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 148 AIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAvEGMTMIVVTHemgfaREVG----DRVIFMDGGYIVEEDKPE 223
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITH-----RLAGlermDRILVLEDGRIVEQGTHE 554
|
..
gi 637158246 224 AL 225
Cdd:COG4987 555 EL 556
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-214 |
7.73e-47 |
|
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: 154.59 E-value: 7.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHE--VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkvNINKVRQEV 81
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT---DRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFNLFPHKTVLENITI-APIKvkGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVL 160
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFyARLK--GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 637158246 161 LFDEPTSALDPEVVGDVLAVMKQLaVEGMTMIVVTHEMGFAREVGDRVIFMDGG 214
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-213 |
8.36e-47 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 154.18 E-value: 8.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCL--NKLEDITA-GEVVVHGHTITDPKVNinkvRQ 79
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagTLSPAFSAsGEVLLNGRRLTALPAE----QR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQHFNLFPHKTVLENITIA-PIKVKGIEKKAAVEKALdllEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPK 158
Cdd:COG4136 77 RIGILFQDDLLFPHLSVGENLAFAlPPTIGRAQRRARVEQAL---EEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 159 VLLFDEPTSALDPEVVGDVLA-VMKQLAVEGMTMIVVTHEMGFAREVGdRVIFMDG 213
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEEDAPAAG-RVLDLGN 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
11-214 |
1.32e-46 |
|
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: 153.99 E-value: 1.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 11 KSFGDHEVlkDINAVIEEkEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNINKVRQE--VGMVFQHF 88
Cdd:cd03297 8 KRLPDFTL--KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQrkIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 89 NLFPHKTVLENITIAPIKVKGIEKKAAVEKALDLLekvGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSA 168
Cdd:cd03297 85 ALFPHLNVRENLAFGLKRKRNREDRISVDELLDLL---GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 637158246 169 LDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGG 214
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-220 |
1.42e-46 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 161.34 E-value: 1.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHG--HTITDPKVNInkvRQE 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDAQ---AAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFNLFPHKTVLENITIA--PIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPK 158
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637158246 159 VLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRV-IFMDGGYIVEED 220
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVtVLRDGRLVGTGP 223
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-238 |
1.55e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 155.58 E-value: 1.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITA-----GEVVVHGHTITDPKVNINKVR 78
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 79 QEVGMVFQHFNLFPhKTVLENITIApIKVKG----IEKKAAVEKAL---DLLEKVglKDKAQSFPNQLSGGQKQRVAIAR 151
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYG-VKIVGwrpkLEIDDIVESALkdaDLWDEI--KHKIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 152 ALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEG-MTMIVVTHEMGFAREVGDRVIFMDG-----GYIVEEDKPEAL 225
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKI 243
|
250
....*....|...
gi 637158246 226 FGNPQHERTKSFL 238
Cdd:PRK14258 244 FNSPHDSRTREYV 256
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
10-217 |
2.27e-46 |
|
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: 153.42 E-value: 2.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 10 KKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHG--HTITDPKvninkvRQEVGMVFQH 87
Cdd:cd03298 5 KIRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdVTAAPPA------DRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 88 FNLFPHKTVLENITIApiKVKGIEKKAAVEKALD-LLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPT 166
Cdd:cd03298 79 NNLFAHLTVEQNVGLG--LSPGLKLTAEDRQAIEvALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 637158246 167 SALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIV 217
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-222 |
5.37e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 155.24 E-value: 5.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFG-----DHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAG------------------EV 60
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 61 VVHGHTITDPKV----NINKVRQEVGMVFQ--HFNLFpHKTVLENITIAPIKVkGIEKKAAVEKALDLLEKVGL-KDKAQ 133
Cdd:PRK13651 83 VLEKLVIQKTRFkkikKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLdESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 134 SFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDG 213
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
....*....
gi 637158246 214 GYIVEEDKP 222
Cdd:PRK13651 241 GKIIKDGDT 249
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
8.36e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 153.81 E-value: 8.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSF-GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQ 79
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT--KENIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQHFN--LFPhKTVLENITIAPIKVkGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDP 157
Cdd:PRK13652 79 FVGLVFQNPDdqIFS-PTVEQDIAFGPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637158246 158 KVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNP 229
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-241 |
8.81e-46 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 157.12 E-value: 8.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEV------------------------LKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGE 59
Cdd:PRK10070 5 LEIKNLYKIFGEHPQrafkyieqglskeqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 60 VVVHG---HTITDPKVNINKvRQEVGMVFQHFNLFPHKTVLENITIApIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFP 136
Cdd:PRK10070 85 VLIDGvdiAKISDAELREVR-RKKIAMVFQSFALMPHMTVLDNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 137 NQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVL-AVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGY 215
Cdd:PRK10070 163 DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGE 242
|
250 260
....*....|....*....|....*.
gi 637158246 216 IVEEDKPEALFGNPQHERTKSFLSKV 241
Cdd:PRK10070 243 VVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-226 |
1.08e-45 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 155.77 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSF-GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD--PKvninkv 77
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElePA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 78 RQEVGMVFQHFNLFPHKTVLENITIApIKVKGIEK---KAAVEKALDLLEKVGLKDKAqsfPNQLSGGQKQRVAIARALA 154
Cdd:PRK11650 75 DRDIAMVFQNYALYPHMSVRENMAYG-LKIRGMPKaeiEERVAEAARILELEPLLDRK---PRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 155 MDPKVLLFDEPTSALDPEvvgdvLAVmkQLAVE--------GMTMIVVTHEMGFAREVGDRVIFMDGGYIvEE------- 219
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAK-----LRV--QMRLEiqrlhrrlKTTSLYVTHDQVEAMTLADRVVVMNGGVA-EQigtpvev 222
|
....*...
gi 637158246 220 -DKPEALF 226
Cdd:PRK11650 223 yEKPASTF 230
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
7-239 |
1.66e-45 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 154.35 E-value: 1.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 7 KNLKKS-------FGDHEVLKDINAV---IEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDP-KVNIN 75
Cdd:PRK11308 9 IDLKKHypvkrglFKPERLVKALDGVsftLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdPEAQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 76 KVRQEVGMVFQ--HFNLFPHKTVlENITIAPIKVK-GIEKKAAVEKALDLLEKVGLK-DKAQSFPNQLSGGQKQRVAIAR 151
Cdd:PRK11308 89 LLRQKIQIVFQnpYGSLNPRKKV-GQILEEPLLINtSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 152 ALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
....*....
gi 637158246 231 HERTKSFLS 239
Cdd:PRK11308 248 HPYTQALLS 256
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-230 |
2.85e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 152.54 E-value: 2.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGD-HEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNINKVRQEV 81
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFN--LFPhKTVLENITIAPIKVkGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKV 159
Cdd:PRK13639 81 GIVFQNPDdqLFA-PTVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637158246 160 LLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-217 |
4.16e-45 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 149.71 E-value: 4.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 5 TVKNLKKSFGDH-EVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGhtitdpKVNINKVRQE-VG 82
Cdd:cd03226 1 RIENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG------KPIKAKERRKsIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQH--FNLFpHKTVLENITI-APIKVKGIEKKAAVEKALDLLEkvgLKDKaqsFPNQLSGGQKQRVAIARALAMDPKV 159
Cdd:cd03226 75 YVMQDvdYQLF-TDSVREELLLgLKELDAGNEQAETVLKDLDLYA---LKER---HPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 637158246 160 LLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIV 217
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-239 |
5.32e-45 |
|
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: 150.37 E-value: 5.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 5 TVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNiNKVRQEVGMV 84
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPH-ERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 85 FQHFNLFPHKTVLENITIapikvkGIEKKAAVEKAL--DLLE--KVgLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVL 160
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLT------GLAALPRRSRKIpdEIYElfPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 161 LFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALfgnpQHERTKSFLS 239
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DEDKVRRYLA 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-216 |
6.41e-45 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 150.98 E-value: 6.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVhGHTitdPkvnINKVRQEVGM 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-GTA---P---LAEAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VFQHFNLFPHKTVLENITIApikVKGIEKkaavEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFD 163
Cdd:PRK11247 86 MFQDARLLPWKKVIDNVGLG---LKGQWR----DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637158246 164 EPTSALDpevvgdvlAV----MKQLAV-----EGMTMIVVTHEMGFAREVGDRVIFMDGGYI 216
Cdd:PRK11247 159 EPLGALD--------ALtrieMQDLIEslwqqHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-223 |
1.26e-44 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 158.35 E-value: 1.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 2 SMITVKNLKKSF----GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVN-INK 76
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADaLAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 77 VRQE-VGMVFQHFNLFPHKTVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAM 155
Cdd:PRK10535 83 LRREhFGFIFQRYHLLSHLTAAQNVEV-PAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 637158246 156 DPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREvGDRVIFMDGGYIVEEDKPE 223
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQ 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-226 |
2.12e-44 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 150.17 E-value: 2.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 2 SMITVKNLKKSFGDHE--VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPkvNINKVRQ 79
Cdd:PRK13635 4 EIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEE--TVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQH-FNLFPHKTV-------LENItiapikvkGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIAR 151
Cdd:PRK13635 82 QVGMVFQNpDNQFVGATVqddvafgLENI--------GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 152 ALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGM-TMIVVTHEMGFAREvGDRVIFMDGGYIVEEDKPEALF 226
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-238 |
2.46e-44 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 149.43 E-value: 2.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 15 DHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPK----VNINKVRQEVGMVFQHFNL 90
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKdifqIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 91 FPHKTVLENITIaPIKVKGIEKKAAVEKALD-LLEKVGL----KDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEP 165
Cdd:PRK14246 102 FPHLSIYDNIAY-PLKSHGIKEKREIKKIVEeCLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637158246 166 TSALDPEVVGDVLAVMKQLAVEgMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHERTKSFL 238
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-238 |
3.64e-44 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 149.22 E-value: 3.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDH---------EVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTIT--D 69
Cdd:COG4167 2 SALLEVRNLSKTFKYRtglfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEygD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 70 PKVNINKVRqevgMVFQHFN--LFPHKTV---LEnitiAPIK----VKGIEKKAAVEkalDLLEKVGL-KDKAQSFPNQL 139
Cdd:COG4167 82 YKYRCKHIR----MIFQDPNtsLNPRLNIgqiLE----EPLRlntdLTAEEREERIF---ATLRLVGLlPEHANFYPHML 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 140 SGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVE 218
Cdd:COG4167 151 SSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEVVE 230
|
250 260
....*....|....*....|
gi 637158246 219 EDKPEALFGNPQHERTKSFL 238
Cdd:COG4167 231 YGKTAEVFANPQHEVTKRLI 250
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-225 |
7.41e-44 |
|
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: 149.46 E-value: 7.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 11 KSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTIT-DPKvninKVRQEVGMVFQHFN 89
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVrEPR----KVRRSIGIVPQYAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 90 LFPHKTVLENITIAPiKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSAL 169
Cdd:TIGR01188 77 VDEDLTGRENLEMMG-RLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 170 DP---EVVGDVLAVMKQlavEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:TIGR01188 156 DPrtrRAIWDYIRALKE---EGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-241 |
9.26e-44 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 151.14 E-value: 9.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkvnINKVRQEVG 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH----VPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHFNLFPHKTVLENITIApIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLF 162
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 163 DEPTSALDPEVVGDV-LAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHERTKSFLSKV 241
Cdd:PRK11607 174 DEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSV 253
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-225 |
1.58e-43 |
|
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: 146.92 E-value: 1.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 15 DHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQEVGMVFQHFNLFPhK 94
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRD--LNLRWLRSQIGLVSQEPVLFD-G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 95 TVLENIT--IAPIKVKGIEKKAAVEKALDLLEkvglkdkaqSFPN-----------QLSGGQKQRVAIARALAMDPKVLL 161
Cdd:cd03249 92 TIAENIRygKPDATDEEVEEAAKKANIHDFIM---------SLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 637158246 162 FDEPTSALDPEVVGDVLAVMKQlAVEGMTMIVVTHEMGFAREVgDRVIFMDGGYIVEEDKPEAL 225
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDR-AMKGRTTIVIAHRLSTIRNA-DLIAVLQNGQVVEQGTHDEL 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-225 |
3.73e-43 |
|
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: 145.21 E-value: 3.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTIT-DPKvninKVRQEVG 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVrEPR----EVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHFNLFPHKTVLENITIAPiKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLF 162
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYIHA-RLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 637158246 163 DEPTSALDPEVVGDVLAVMKQL-AVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-223 |
4.24e-43 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 152.10 E-value: 4.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGH--TITDPKVNInkvRQE 80
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAI---ALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFNLFPHKTVLENITIA--PIKVKGIEKKAAVEKALDLLEKVGLK-DkaqsfPN----QLSGGQKQRVAIARAL 153
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDvD-----PDakveDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 154 AMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPE 223
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-201 |
4.57e-43 |
|
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: 144.10 E-value: 4.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 14 GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNINKVRQEVGMVFQHFN--LF 91
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQRVGLVFQDPDdqLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 92 pHKTVLENITIAPIKV--KGIEKKAAVEKALDLLEKVGLKDKAqsfPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSAL 169
Cdd:TIGR01166 83 -AADVDQDVAFGPLNLglSEAEVERRVREALTAVGASGLRERP---THCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180 190
....*....|....*....|....*....|..
gi 637158246 170 DPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFA 201
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-227 |
6.94e-43 |
|
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: 144.92 E-value: 6.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 19 LKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKvninkvrQEVGMVFQHFNLFPHKTVLE 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG-------PDRMVVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 99 NITIAPIKV----KGIEKKAAVEKALDLlekVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVV 174
Cdd:TIGR01184 74 NIALAVDRVlpdlSKSERRAIVEEHIAL---VGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 637158246 175 GDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGyiveedkPEALFG 227
Cdd:TIGR01184 151 GNLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG-------PAANIG 197
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-219 |
9.80e-43 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 144.57 E-value: 9.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 17 EVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-PKVNINKVR-QEVGMVFQHFNLFPHK 94
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlSSAAKAELRnQKLGFIYQFHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 95 TVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVV 174
Cdd:PRK11629 103 TALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 637158246 175 GDVLAVMKQLAV-EGMTMIVVTHEMGFAREVgDRVIFMDGGYIVEE 219
Cdd:PRK11629 182 DSIFQLLGELNRlQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-225 |
1.25e-42 |
|
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: 144.30 E-value: 1.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDH-EVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQEVG 82
Cdd:cd03253 1 IEFENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRE--VTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHFNLFpHKTVLENITIAPIKVKGIEKKAAVEKAldllekvGLKDKAQSFPNQ-----------LSGGQKQRVAIAR 151
Cdd:cd03253 79 VVPQDTVLF-NDTIGYNIRYGRPDATDEEVIEAAKAA-------QIHDKIMRFPDGydtivgerglkLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 152 ALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAvEGMTMIVVTHEMgfaREV--GDRVIFMDGGYIVEEDKPEAL 225
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRL---STIvnADKIIVLKDGRIVERGTHEEL 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-230 |
2.81e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 144.97 E-value: 2.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 19 LKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNIN--KVRQEVGMVFQhfnlFPH--- 93
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlkKLRKKVSLVFQ----FPEaql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 94 --KTVLENITIAPIKVkGIEKKAAVEKALDLLEKVGLKDK-AQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALD 170
Cdd:PRK13641 99 feNTVLKDVEFGPKNF-GFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 171 PEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-239 |
3.51e-42 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 144.47 E-value: 3.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 8 NLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAG-----EVVVHGHTITDPKvNINKVRQEVG 82
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYR-DVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHFNLFPhKTVLENITIAPIKVKGIEKKAAVEKALDLLEKVGL----KDKAQSFPNQLSGGQKQRVAIARALAMDPK 158
Cdd:PRK14271 105 MLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 159 VLLFDEPTSALDPEVVGDVLAVMKQLAvEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHERTKSFL 238
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
|
.
gi 637158246 239 S 239
Cdd:PRK14271 263 A 263
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-214 |
7.85e-42 |
|
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: 142.19 E-value: 7.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHE-------VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVV-HGHTITD----- 69
Cdd:COG4778 4 LLEVENLSKTFTLHLqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrHDGGWVDlaqas 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 70 PKVNINKVRQEVGMVFQHFNLFPHKTVLEnITIAPIKVKGIEKKAAVEKALDLLEKVGLKDK-AQSFPNQLSGGQKQRVA 148
Cdd:COG4778 84 PREILALRRRTIGYVSQFLRVIPRVSALD-VVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 149 IARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGG 214
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-219 |
3.39e-41 |
|
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: 140.04 E-value: 3.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKvninKVRQEVGM 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI----EALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VFQHFNLFPHKTVLENITIAPiKVKGIEKKAAVEkaldLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFD 163
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLLA-RLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 164 EPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEE 219
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-236 |
3.57e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 142.15 E-value: 3.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHE------VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKvNINK 76
Cdd:PRK13633 4 MIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEE-NLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 77 VRQEVGMVFQH-FNLFPHKTVLENITIAPIKVkGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAM 155
Cdd:PRK13633 83 IRNKAGMVFQNpDNQIVATIVEEDVAFGPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 156 DPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREvGDRVIFMDGGYIVEEDKPEALFgnPQHERT 234
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF--KEVEMM 238
|
..
gi 637158246 235 KS 236
Cdd:PRK13633 239 KK 240
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-229 |
3.58e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 143.07 E-value: 3.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHE-----VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKL-----EDITAGEVVVHGHTITDPKV 72
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskyGTIQVGDIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 73 ---------NINKVRQEVGMVFQ--HFNLFpHKTVLENITIAPIKVkGIEKKAAVEKALDLLEKVGLKDkaqSF----PN 137
Cdd:PRK13631 101 tnpyskkikNFKELRRRVSMVFQfpEYQLF-KDTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDD---SYlersPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 138 QLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIV 217
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
250
....*....|..
gi 637158246 218 EEDKPEALFGNP 229
Cdd:PRK13631 256 KTGTPYEIFTDQ 267
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
15-216 |
4.45e-41 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 140.00 E-value: 4.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 15 DHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHG--HTITDPKvninkvRQEVGMVFQHFNLFP 92
Cdd:TIGR01277 10 YEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDqsHTGLAPY------QRPVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 93 HKTVLENIT--IAP-IKVKGIEKkaavEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSAL 169
Cdd:TIGR01277 84 HLTVRQNIGlgLHPgLKLNAEQQ----EKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 637158246 170 DPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYI 216
Cdd:TIGR01277 160 DPLLREEMLALVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
8-229 |
5.06e-41 |
|
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: 143.71 E-value: 5.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 8 NLKKSFGDHEVlkDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDP--KVNINKVRQEVGMVF 85
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSrkGIFLPPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 86 QHFNLFPHKTVLENITIAPIKVKGIEKKAAVEKALDLLekvGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEP 165
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 166 TSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNP 229
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-226 |
1.15e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 140.65 E-value: 1.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 19 LKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVN--INKVRQEVGMVFQhfnlFPH--- 93
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdIKQIRKKVGLVFQ----FPEsql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 94 --KTVLENITIAPIKVkGIEKKAAVEKALDLLEKVGLKDKA-QSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALD 170
Cdd:PRK13649 99 feETVLKDVAFGPQNF-GVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 171 PEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALF 226
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-227 |
1.64e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 140.25 E-value: 1.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLK---KSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPkvNINKV 77
Cdd:PRK13650 2 SNIIEVKNLTfkyKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEE--NVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 78 RQEVGMVFQH-FNLFPHKTVLENITIApIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMD 156
Cdd:PRK13650 80 RHKIGMVFQNpDNQFVGATVEDDVAFG-LENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 637158246 157 PKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGfarEVG--DRVIFMDGGYIVEEDKPEALFG 227
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLD---EVAlsDRVLVMKNGQVESTSTPRELFS 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-227 |
3.51e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 139.53 E-value: 3.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 15 DHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVN--INKVRQEVGMVFQhfnlFP 92
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyIRPVRKRIGMVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 93 HKTVLEN-----ITIAPiKVKGIEKKAAVEKALDLLEKVGL-KDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPT 166
Cdd:PRK13646 95 ESQLFEDtvereIIFGP-KNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637158246 167 SALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFG 227
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-219 |
4.60e-40 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 138.67 E-value: 4.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDH---------EVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-P 70
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 71 KVNINKVRQEVGMVFQH----FNlfPHKTVLEnITIAPIK-VKGIEKKAAVEKALDLLEKVGLKDK-AQSFPNQLSGGQK 144
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQDsisaVN--PRKTVRE-IIREPLRhLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 145 QRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEE 219
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-217 |
5.22e-40 |
|
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: 135.25 E-value: 5.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHtitdpKVNINKVRQE--- 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK-----EVSFASPRDArra 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 -VGMVFQhfnlfphktvlenitiapikvkgiekkaavekaldllekvglkdkaqsfpnqLSGGQKQRVAIARALAMDPKV 159
Cdd:cd03216 76 gIAMVYQ----------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 637158246 160 LLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIV 217
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-223 |
8.82e-40 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 137.60 E-value: 8.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-PKVNINKVRqev 81
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFNL-FPHkTVLENITI--APIKVKGIEKKAAVEKALDLLEKVGLKDKaqSFPnQLSGGQKQRVAIARALA---- 154
Cdd:PRK13548 79 AVLPQHSSLsFPF-TVEEVVAMgrAPHGLSRAEDDALVAAALAQVDLAHLAGR--DYP-QLSGGEQQRVQLARVLAqlwe 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637158246 155 --MDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPE 223
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-223 |
9.02e-40 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 143.40 E-value: 9.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDI--TAGEVVVH------------------ 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 64 -----GHTITDPKVNI--------NKVRQEVGMVFQH-FNLFPHKTVLENItIAPIKVKGIEKKAAVEKALDLLEKVGLK 129
Cdd:TIGR03269 81 pcpvcGGTLEPEEVDFwnlsdklrRRIRKRIAIMLQRtFALYGDDTVLDNV-LEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 130 DKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRV 208
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*
gi 637158246 209 IFMDGGYIVEEDKPE 223
Cdd:TIGR03269 240 IWLENGEIKEEGTPD 254
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-217 |
1.14e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 138.70 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkvninKVRQEVG 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP------EDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHFNLFPHKTVLENIT-IApiKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLL 161
Cdd:COG4152 75 YLPEERGLYPKMKVGEQLVyLA--RLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 162 FDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIV 217
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-216 |
1.55e-39 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 137.45 E-value: 1.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 2 SMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKL---EDITAGEVVVHGHTITDP---KVNIN 75
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREgrlARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 76 KVRQEVGMVFQHFNLFPHKTVLENITIAPIKVKGIEK-------KAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVA 148
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637158246 149 IARALAMDPKVLLFDEPTSALDPE---VVGDVLAVMKQlaVEGMTMIVVTHEMGFAREVGDRVIFMDGGYI 216
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPEsarIVMDTLRDINQ--NDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-223 |
1.78e-39 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 136.78 E-value: 1.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-PKVNINKVRqev 81
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwSPWELARRR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFNL-FPHkTVLENITI--APIKVKGIEKKAAVEKALDLlekVGLKDKAQSFPNQLSGGQKQRVAIARALA---- 154
Cdd:COG4559 78 AVLPQHSSLaFPF-TVEEVVALgrAPHGSSAAQDRQIVREALAL---VGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwe 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637158246 155 ---MDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPE 223
Cdd:COG4559 154 pvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPE 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-223 |
3.20e-39 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 135.98 E-value: 3.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-PKVNINKV---- 77
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELAKRlail 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 78 RQEvgmvfQHFNL------------FPHKtvlenitiapikvKG---IEKKAAVEKALDLLEkvgLKDKAQSFPNQLSGG 142
Cdd:COG4604 81 RQE-----NHINSrltvrelvafgrFPYS-------------KGrltAEDREIIDEAIAYLD---LEDLADRYLDELSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 143 QKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDK 221
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
..
gi 637158246 222 PE 223
Cdd:COG4604 220 PE 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-219 |
3.37e-39 |
|
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: 135.01 E-value: 3.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKeVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHtitDPKVNINKVRQEVGM 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ---DVLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VFQHFNLFPHKTVLENI-TIAPIKvkGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLF 162
Cdd:cd03264 77 LPQEFGVYPNFTVREFLdYIAWLK--GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 637158246 163 DEPTSALDPEVVGDVLAVMKQLAvEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEE 219
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-213 |
4.37e-39 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 135.29 E-value: 4.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 2 SMITVKNLKKSFGDHE----VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTIT--DPKVNIN 75
Cdd:PRK10584 5 NIVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 76 KVRQEVGMVFQHFNLFPHKTVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAM 155
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIPTLNALENVEL-PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637158246 156 DPKVLLFDEPTSALDPEV---VGDVLAVMKQlaVEGMTMIVVTHEMGFAREVGDRVIFMDG 213
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTgdkIADLLFSLNR--EHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-238 |
5.31e-39 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 137.57 E-value: 5.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDHEV----LKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLED----ITAGEVVVHGHTITD--P 70
Cdd:PRK11022 1 MALLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRisE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 71 KVNINKVRQEVGMVFQH--FNLFPHKTVLENITIApIKV-KGIEKKAAVEKALDLLEKVGLKDKAQS---FPNQLSGGQK 144
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDpmTSLNPCYTVGFQIMEA-IKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 145 QRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLA-VEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPE 223
Cdd:PRK11022 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAH 239
|
250
....*....|....*
gi 637158246 224 ALFGNPQHERTKSFL 238
Cdd:PRK11022 240 DIFRAPRHPYTQALL 254
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-229 |
5.89e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 136.27 E-value: 5.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGD-HEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKvNINKVRQEV 81
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS-KLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFNL-FPHKTVLENITIAP--IKVKGIEKKAAVEKALdllEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPK 158
Cdd:PRK13644 80 GIVFQNPETqFVGRTVEEDLAFGPenLCLPPIEIRKRVDRAL---AEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637158246 159 VLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGfAREVGDRVIFMDGGYIVEEDKPEALFGNP 229
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-225 |
7.08e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 136.02 E-value: 7.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGD-HEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQEVG 82
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN--AENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHFN--LFPhKTVLENITIAPIKVkGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVL 160
Cdd:PRK13647 83 LVFQDPDdqVFS-STVWDDVAFGPVNM-GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 161 LFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
6-241 |
7.42e-39 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 137.14 E-value: 7.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 6 VKNLKKSFG----------DHEVLKDINAV---IEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-PK 71
Cdd:PRK15079 11 VADLKVHFDikdgkqwfwqPPKTLKAVDGVtlrLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 72 VNINKVRQEVGMVFQH--FNLFPHKTVLEnITIAPIKV--KGIEKKAAVEKALDLLEKVGL-KDKAQSFPNQLSGGQKQR 146
Cdd:PRK15079 91 DEWRAVRSDIQMIFQDplASLNPRMTIGE-IIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 147 VAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:PRK15079 170 IGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
250
....*....|....*.
gi 637158246 226 FGNPQHERTKSFLSKV 241
Cdd:PRK15079 250 YHNPLHPYTKALMSAV 265
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-217 |
8.85e-39 |
|
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: 133.56 E-value: 8.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkvninKVRQEVGM 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI------AARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VFQHFNLFPHKTVLEN-ITIApiKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLF 162
Cdd:cd03269 75 LPEERGLYPKMKVIDQlVYLA--QLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 163 DEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIV 217
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-219 |
1.13e-38 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 133.85 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSF-GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVN-INKVRQE 80
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNReVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFNLFPHKTVLENITIaPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVL 160
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 161 LFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEE 219
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGG 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-217 |
2.03e-38 |
|
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: 133.10 E-value: 2.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHE--VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTIT--DPKVninkVRQ 79
Cdd:cd03245 3 IEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqlDPAD----LRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQHFNLFpHKTVLENITIApikvKGIEKKAAVEKALDLLekvGLKDKAQSFPN-----------QLSGGQKQRVA 148
Cdd:cd03245 79 NIGYVPQDVTLF-YGTLRDNITLG----APLADDERILRAAELA---GVTDFVNKHPNgldlqigergrGLSGGQRQAVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 149 IARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAvEGMTMIVVTHEMGFAREVgDRVIFMDGGYIV 217
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLLDLV-DRIIVMDSGRIV 217
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-170 |
3.20e-38 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 133.67 E-value: 3.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLrclnkleDITAGEVVVHGHTITDPKVNINKVRQEVG 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLL-------NLIAGFVPYQHGSITLDGKPVEGPGAERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHFNLFPHKTVLENITIApIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLF 162
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
....*...
gi 637158246 163 DEPTSALD 170
Cdd:PRK11248 153 DEPFGALD 160
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-225 |
7.29e-38 |
|
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: 131.97 E-value: 7.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHE--VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQEV 81
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRD--YTLASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFNLFpHKTVLENITIApikvKGIEKKAAVEKALdllEKVGLKDKAQSFPN-----------QLSGGQKQRVAIA 150
Cdd:cd03251 79 GLVSQDVFLF-NDTVAENIAYG----RPGATREEVEEAA---RAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 151 RALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAvEGMTMIVVTHEMGFAREvGDRVIFMDGGYIVEEDKPEAL 225
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
18-225 |
1.65e-37 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 138.55 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 18 VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQEVGMVFQHFNLFPhKTVL 97
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAG--LDVQAVRRQLGVVLQNGRLMS-GSIF 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 98 ENITI-APIkvkgiekkaAVEKALDLLEKVGLKDKAQSFP-----------NQLSGGQKQRVAIARALAMDPKVLLFDEP 165
Cdd:TIGR03797 545 ENIAGgAPL---------TLDEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRKPRILLFDEA 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 166 TSALDPEVVGDVLAVMKQLAVegmTMIVVTHEMGFAREvGDRVIFMDGGYIVEEDKPEAL 225
Cdd:TIGR03797 616 TSALDNRTQAIVSESLERLKV---TRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDEL 671
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
15-217 |
2.43e-37 |
|
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: 138.46 E-value: 2.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 15 DHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTIT--DPKVninkVRQEVGMVFQHFNLFp 92
Cdd:TIGR03375 477 ETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRqiDPAD----LRRNIGYVPQDPRLF- 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 93 HKTVLENITIApikvkgiekKAAVEKA--LDLLEKVGLKDKAQSFPN-----------QLSGGQKQRVAIARALAMDPKV 159
Cdd:TIGR03375 552 YGTLRDNIALG---------APYADDEeiLRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPI 622
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 637158246 160 LLFDEPTSALDPEVVGDVLAVMKQLaVEGMTMIVVTHEMGFAREVgDRVIFMDGGYIV 217
Cdd:TIGR03375 623 LLLDEPTSAMDNRSEERFKDRLKRW-LAGKTLVLVTHRTSLLDLV-DRIIVMDNGRIV 678
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-211 |
2.89e-37 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 136.65 E-value: 2.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDH-EVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQEVG 82
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD--ADADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHFNLFPhKTVLENITIAPIKVKGIEKKAAVEKA-LDLLEKV---GLKDKAQSFPNQLSGGQKQRVAIARALAMDPK 158
Cdd:TIGR02857 400 WVPQHPFLFA-GTIAENIRLARPDASDAEIREALERAgLDEFVAAlpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 637158246 159 VLLFDEPTSALDPEVVGDVLAVMKQLAvEGMTMIVVTHEMGFAREVgDRVIFM 211
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
30-241 |
3.70e-37 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 137.29 E-value: 3.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 30 EVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTI-TDPKVNINKVRQEVGMVFQ--HFNLFPHKTVLENItIAPIK 106
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdTLSPGKLQALRRDIQFIFQdpYASLDPRQTVGDSI-MEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 107 VKGI-EKKAAVEKALDLLEKVGLK-DKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQL 184
Cdd:PRK10261 430 VHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 637158246 185 AVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHERTKSFLSKV 241
Cdd:PRK10261 510 QRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-214 |
4.23e-37 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 128.10 E-value: 4.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLkkSF----GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQ 79
Cdd:cd03246 1 LEVENV--SFrypgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS--QWDPNELGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQHFNLFPhKTVLENItiapikvkgiekkaavekaldllekvglkdkaqsfpnqLSGGQKQRVAIARALAMDPKV 159
Cdd:cd03246 77 HVGYLPQDDELFS-GSIAENI--------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 160 LLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVgDRVIFMDGG 214
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASA-DRILVLEDG 171
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
10-228 |
5.45e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 131.28 E-value: 5.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 10 KKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNINKV---RQEVGMVFQ 86
Cdd:PRK13645 18 KKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVkrlRKEIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 87 --HFNLFpHKTVLENITIAPIKVkGIEKKAAVEKALDLLEKVGL-KDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFD 163
Cdd:PRK13645 98 fpEYQLF-QETIEKDIAFGPVNL-GENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 164 EPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGN 228
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-225 |
7.71e-37 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 129.32 E-value: 7.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 26 IEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHG--HTITDPKvninkvRQEVGMVFQHFNLFPHKTVLENIT-- 101
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdHTTTPPS------RRPVSMLFQENNLFSHLTVAQNIGlg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 102 IAPikvkGIEKKAAVEKAL-DLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAV 180
Cdd:PRK10771 96 LNP----GLKLNAAQREKLhAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 637158246 181 MKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:PRK10771 172 VSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-230 |
1.42e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 130.31 E-value: 1.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 2 SMITVKNLKKSFGDHE--VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKL---EDITAGEVVVHGHTITDPkvNINK 76
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAK--TVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 77 VRQEVGMVFQH-FNLFPHKTVLENITIApIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAM 155
Cdd:PRK13640 82 IREKVGIVFQNpDNQFVGATVGDDVAFG-LENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 156 DPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFArEVGDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-225 |
2.62e-36 |
|
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: 128.37 E-value: 2.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 17 EVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQEVGMVFQHFNLFpHKTV 96
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA--LADPAWLRRQVGVVLQENVLF-NRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 97 LENITIA--PIKVKGIEKKAAVEKALDLLEKV--GLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPE 172
Cdd:cd03252 93 RDNIALAdpGMSMERVIEAAKLAGAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 637158246 173 VVGDVLAVMKQLAvEGMTMIVVTHEMGFAREvGDRVIFMDGGYIVEEDKPEAL 225
Cdd:cd03252 173 SEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-238 |
4.98e-36 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 133.29 E-value: 4.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSF----GDHEVLKDINAVIEEKEVVCVIGPSGSGKS-TFLRCLNKLED----ITAGEVVVHGHTITD-P 70
Cdd:PRK15134 3 QPLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvvYPSGDIRFHGESLLHaS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 71 KVNINKVR-QEVGMVFQH--FNLFPhktvLENITIAPIKV----KGIEKKAAVEKALDLLEKVGLKDKAQ---SFPNQLS 140
Cdd:PRK15134 83 EQTLRGVRgNKIAMIFQEpmVSLNP----LHTLEKQLYEVlslhRGMRREAARGEILNCLDRVGIRQAAKrltDYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 141 GGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEE 219
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQ 238
|
250
....*....|....*....
gi 637158246 220 DKPEALFGNPQHERTKSFL 238
Cdd:PRK15134 239 NRAATLFSAPTHPYTQKLL 257
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-226 |
1.07e-35 |
|
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: 126.19 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSF-GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQEVG 82
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRD--ISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHFNLFPhKTVLENITIAP--IKVKGIEKKAAVEKALDLLEKV--GLKDKAQSFPNQLSGGQKQRVAIARALAMDPK 158
Cdd:cd03254 81 VVLQDTFLFS-GTIMENIRLGRpnATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 637158246 159 VLLFDEPTSALDPEVVGDVLAVMKQLaVEGMTMIVVTHEMGFAREVgDRVIFMDGGYIVEEDKPEALF 226
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKNA-DKILVLDDGKIIEEGTHDELL 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-227 |
2.18e-35 |
|
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: 131.46 E-value: 2.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFG--DHEVLKDINAV---IEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVH-GHT---ITDPKV- 72
Cdd:TIGR03269 279 IIKVRNVSKRYIsvDRGVVKAVDNVsleVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEwvdMTKPGPd 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 73 NINKVRQEVGMVFQHFNLFPHKTVLENITiapiKVKGIE--KKAAVEKALDLLEKVGL-KDKAQS----FPNQLSGGQKQ 145
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLT----EAIGLElpDELARMKAVITLKMVGFdEEKAEEildkYPDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 146 RVAIARALAMDPKVLLFDEPTSALDPEVVGDVL-AVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEA 224
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVThSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
...
gi 637158246 225 LFG 227
Cdd:TIGR03269 515 IVE 517
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-219 |
2.44e-35 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 125.17 E-value: 2.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHE----VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHG-HTITDPKvninKV 77
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPA----EA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 78 RQEVGMVFQHFNLFPHKTVLENITI--APIKVKGIEKKAAVEKALDLLEKVGLKDKAQSfpnQLSGGQKQRVAIARALAM 155
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYfaGLYGLKGDELTARLEELADRLGMEELLDRRVG---GFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 637158246 156 DPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEE 219
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-210 |
2.83e-35 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 124.27 E-value: 2.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 12 SFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHT--------ITDPKVNINKVRQEVGM 83
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArvayvpqrSEVPDSLPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 vfqhfNLFPHKTVLENITIapikvkgiEKKAAVEKALdllEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFD 163
Cdd:NF040873 81 -----GRWARRGLWRRLTR--------DDRAAVDDAL---ERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 637158246 164 EPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIF 210
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-217 |
8.89e-35 |
|
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: 123.92 E-value: 8.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 18 VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCL-NKLED--ITAGEVVVHGHtitdpKVNINKVRQEVGMVFQHFNLFPHK 94
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGggTTSGQILFNGQ-----PRKPDQFQKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 95 TVLENITIAPIKVKGIEKKAAVEKALD---LLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDP 171
Cdd:cd03234 97 TVRETLTYTAILRLPRKSSDAIRKKRVedvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 637158246 172 EVVGDVLAVMKQLAVEGMTMIVVTHEMG---FarEVGDRVIFMDGGYIV 217
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIV 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-217 |
9.33e-35 |
|
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: 122.66 E-value: 9.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 17 EVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLN--KLEDITAGEVVVHGHTITDpkvniNKVRQEVGMVFQHFNLFPHK 94
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDK-----RSFRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 95 TVLENITIApIKVKGIekkaavekaldllekvglkdkaqsfpnqlSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVV 174
Cdd:cd03213 98 TVRETLMFA-AKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 637158246 175 GDVLAVMKQLAVEGMTMIVVTH----EMgFarEVGDRVIFMDGGYIV 217
Cdd:cd03213 148 LQVMSLLRRLADTGRTIICSIHqpssEI-F--ELFDKLLLLSQGRVI 191
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-214 |
1.93e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 129.03 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 6 VKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTitdpkvninkvrqEVGMVF 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-------------RIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 86 QHFNLFPHKTVLENITIAPIKVKGIEK-KAAVEKALD------------------------------LLEKVGLKDKAQS 134
Cdd:COG0488 68 QEPPLDDDLTVLDTVLDGDAELRALEAeLEELEAKLAepdedlerlaelqeefealggweaearaeeILSGLGFPEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 135 FP-NQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEvvgdvlAVM---KQLAVEGMTMIVVTHEMGFAREVGDRVIF 210
Cdd:COG0488 148 RPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE------SIEwleEFLKNYPGTVLVVSHDRYFLDRVATRILE 221
|
....
gi 637158246 211 MDGG 214
Cdd:COG0488 222 LDRG 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-226 |
2.18e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 124.57 E-value: 2.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGD-HEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNINKVRQEV 81
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQH--FNLFPhKTVLENITIAPIKVkGIEKKAAVEKALDLLEKVG---LKDKAQsfpNQLSGGQKQRVAIARALAMD 156
Cdd:PRK13636 85 GMVFQDpdNQLFS-ASVYQDVSFGAVNL-KLPEDEVRKRVDNALKRTGiehLKDKPT---HCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637158246 157 PKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALF 226
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-225 |
3.75e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 124.53 E-value: 3.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkvNINKVRQEVGM 83
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS---RARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VFQHFNLFPHKTVLENITIAPiKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFD 163
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVFG-RYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637158246 164 EPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-230 |
3.75e-34 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 122.45 E-value: 3.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-PkvnINK-VR 78
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlP---MHKrAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 79 QEVGMVFQHFNLFPHKTVLENItIAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPK 158
Cdd:COG1137 78 LGIGYLPQEASIFRKLTVEDNI-LAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 159 VLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTmIVVT-HEmgfARE---VGDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKERGIG-VLITdHN---VREtlgICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-226 |
9.21e-34 |
|
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: 121.73 E-value: 9.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAG-EVVVHGHTITdpKVNINKVRQ 79
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRG--GEDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMV--FQHFNLFPHKTVLENI------TIapikvkGIEKK---AAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVA 148
Cdd:COG1119 79 RIGLVspALQLRFPRDETVLDVVlsgffdSI------GLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 149 IARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEG-MTMIVVTH---EM--GFarevgDRVIFMDGGYIVEEDKP 222
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhveEIppGI-----THVLLLKDGRVVAAGPK 227
|
....
gi 637158246 223 EALF 226
Cdd:COG1119 228 EEVL 231
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-196 |
9.53e-34 |
|
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: 127.09 E-value: 9.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 14 GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQEVGMVFQHFNLFpH 93
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSS--LDQDEVRRRVSVCAQDAHLF-D 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 94 KTVLENITIApikvkgiEKKAAVEKALDLLEKVGLKDKAQSFPN-----------QLSGGQKQRVAIARALAMDPKVLLF 162
Cdd:TIGR02868 423 TTVRENLRLA-------RPDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....
gi 637158246 163 DEPTSALDPEVVGDVLAVMKQlAVEGMTMIVVTH 196
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-218 |
9.58e-34 |
|
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: 127.53 E-value: 9.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFG--DHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKvnINKVRQEV 81
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT--LASLRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFNLFpHKTVLENITIAPIKVKG---IEKKAAVEKALDLLEKV--GLKDKAQSFPNQLSGGQKQRVAIARALAMD 156
Cdd:TIGR02203 409 ALVSQDVVLF-NDTIANNIAYGRTEQADraeIERALAAAYAQDFVDKLplGLDTPIGENGVLLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637158246 157 PKVLLFDEPTSALDPEVVGDVLAVMKQLaVEGMTMIVVTHEMGfAREVGDRVIFMDGGYIVE 218
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVE 547
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-221 |
1.86e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 121.35 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFG-----DHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKV 77
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT--KLPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 78 RQEVGMVFQHFNL--FPHKTVLENITIAPIKVK------GIEKKaavEKAL--DLLEKVG------LKDKAQSfpnqLSG 141
Cdd:COG1101 79 AKYIGRVFQDPMMgtAPSMTIEENLALAYRRGKrrglrrGLTKK---RRELfrELLATLGlglenrLDTKVGL----LSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 142 GQKQrvaiARALAM----DPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYI 216
Cdd:COG1101 152 GQRQ----ALSLLMatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEEnNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
....*....
gi 637158246 217 V----EEDK 221
Cdd:COG1101 228 IldvsGEEK 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-214 |
2.20e-33 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 125.95 E-value: 2.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEvVVHGHTItdpkvninkvrqEVG 82
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-VKLGETV------------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHF-NLFPHKTVLENitIAPIKVKGIEKKAAvekalDLLEKVGLK-DKAQSFPNQLSGGQKQRVAIARALAMDPKVL 160
Cdd:COG0488 382 YFDQHQeELDPDKTVLDE--LRDGAPGGTEQEVR-----GYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 637158246 161 LFDEPTSALDP---EVVGDVLAvmkqlAVEGmTMIVVTHEMGFAREVGDRVI-FMDGG 214
Cdd:COG0488 455 LLDEPTNHLDIetlEALEEALD-----DFPG-TVLLVSHDRYFLDRVATRILeFEDGG 506
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-226 |
8.96e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 119.86 E-value: 8.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 19 LKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPkvNINKVRQEVGMVFQH-FNLFPHKTV- 96
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDD--NFEKLRKHIGIVFQNpDNQFVGSIVk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 97 ------LENITIAPIKVKGIEKKAavekaldlLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALD 170
Cdd:PRK13648 103 ydvafgLENHAVPYDEMHRRVSEA--------LKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 637158246 171 PEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREvGDRVIFMDGGYIVEEDKPEALF 226
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-241 |
1.20e-32 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 120.98 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSF----GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKL---EDITAGEVVVHGHTITD-PKV 72
Cdd:PRK09473 10 DALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNlPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 73 NINKVR-QEVGMVFQH--FNLFPHKTVLENITIAPIKVKGIEKKAAVEKALDLLEKVGL---KDKAQSFPNQLSGGQKQR 146
Cdd:PRK09473 90 ELNKLRaEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMpeaRKRMKMYPHEFSGGMRQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 147 VAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
250
....*....|....*.
gi 637158246 226 FGNPQHERTKSFLSKV 241
Cdd:PRK09473 250 FYQPSHPYSIGLLNAV 265
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
17-225 |
1.23e-32 |
|
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: 124.85 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 17 EVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGH--TITDPkvniNKVRQEVGMVFQHFNLFpHK 94
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVdlAIADP----AWLRRQMGVVLQENVLF-SR 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 95 TVLENITIA--PIKVKGIEKKAAVEKALDLLEKV--GLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALD 170
Cdd:TIGR01846 546 SIRDNIALCnpGAPFEHVIHAAKLAGAHDFISELpqGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALD 625
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 171 PEVVGDVLAVMKQLAvEGMTMIVVTHEMGFAREVgDRVIFMDGGYIVEEDKPEAL 225
Cdd:TIGR01846 626 YESEALIMRNMREIC-RGRTVIIIAHRLSTVRAC-DRIIVLEKGQIAESGRHEEL 678
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-229 |
1.89e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 118.55 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-PKVNInkVRQEV 81
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlPGHQI--ARMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFNLFPHKTVLENITIAP------------IKVKGIEK--KAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRV 147
Cdd:PRK11300 83 VRTFQHVRLFREMTVIENLLVAQhqqlktglfsglLKTPAFRRaeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 148 AIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALF 226
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
...
gi 637158246 227 GNP 229
Cdd:PRK11300 243 NNP 245
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-226 |
2.10e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 119.45 E-value: 2.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 19 LKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD--PKVNINKVRQEVGMVFQhfnlFPH--- 93
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStsKQKEIKPVRKKVGVVFQ----FPEsql 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 94 --KTVLENITIAPIKVkGIEKKAAVEKALDLLEKVGL-KDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALD 170
Cdd:PRK13643 98 feETVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 171 PEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALF 226
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-229 |
2.17e-32 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 117.64 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKvRQEVGM 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT--KLPMHK-RARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VF--QHFNLFPHKTVLENItIAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLL 161
Cdd:cd03218 78 GYlpQEASIFRKLTVEENI-LAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637158246 162 FDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEmgfARE---VGDRVIFMDGGYIVEEDKPEALFGNP 229
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHN---VREtlsITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-225 |
2.89e-32 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 121.49 E-value: 2.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTI-----TDPKVNIN 75
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsaRAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 76 KVRQEVGMVFQhFNL--------FPHKTVLENITIApikvkgieKKAAVEKALDLLEKVGLKDKAQSfpnQLSGGQKQRV 147
Cdd:PRK09536 81 SVPQDTSLSFE-FDVrqvvemgrTPHRSRFDTWTET--------DRAAVERAMERTGVAQFADRPVT---SLSGGERQRV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 637158246 148 AIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-229 |
5.43e-32 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 123.29 E-value: 5.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 15 DHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTItdPKVNINKVRQEVGMVFQHFNLFpHK 94
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL--VQYDHHYLHRQVALVGQEPVLF-SG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 95 TVLENITIAPIKVKGIEKKAAVEKAldllekvGLKDKAQSFPN-----------QLSGGQKQRVAIARALAMDPKVLLFD 163
Cdd:TIGR00958 570 SVRENIAYGLTDTPDEEIMAAAKAA-------NAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 164 EPTSALDPEVVGDVLAVMKQlavEGMTMIVVTHEMGFAREVgDRVIFMDGGYIVEEDKPEALFGNP 229
Cdd:TIGR00958 643 EATSALDAECEQLLQESRSR---ASRTVLLIAHRLSTVERA-DQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
12-219 |
7.33e-32 |
|
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: 122.24 E-value: 7.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 12 SFG---DHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQEVGMVfqhf 88
Cdd:COG5265 364 SFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRD--VTQASLRAAIGIV---- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 89 nlfPHKTVLENITIA-------PikvkGIEKkAAVEKALDL---------LEK-----VG---LKdkaqsfpnqLSGGQK 144
Cdd:COG5265 438 ---PQDTVLFNDTIAyniaygrP----DASE-EEVEAAARAaqihdfiesLPDgydtrVGergLK---------LSGGEK 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 145 QRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAvEGMTMIVVTHEMGFAREVgDRVIFMDGGYIVEE 219
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAHRLSTIVDA-DEILVLEAGRIVER 573
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-239 |
7.95e-32 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 117.20 E-value: 7.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 2 SMITVKNLKKSF--------GDH-EVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTIT--DP 70
Cdd:PRK15112 3 TLLEVRNLSKTFryrtgwfrRQTvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 71 KVNINKVRqevgMVFQ--HFNLFPHKTVlENITIAPIKVKGIEKKAAVEKALDL-LEKVGLK-DKAQSFPNQLSGGQKQR 146
Cdd:PRK15112 83 SYRSQRIR----MIFQdpSTSLNPRQRI-SQILDFPLRLNTDLEPEQREKQIIEtLRQVGLLpDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 147 VAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQL-AVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
250
....*....|....
gi 637158246 226 FGNPQHERTKSFLS 239
Cdd:PRK15112 238 LASPLHELTKRLIA 251
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-242 |
8.23e-32 |
|
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: 116.85 E-value: 8.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEV--------VVHGHTITDPKVNI 74
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyimrsgaELELYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 75 nKVRQEVGMVFQHFNLFPHKTVLE--NITIAPIKVKGIEKKAAVEKALDLLEKVGL-KDKAQSFPNQLSGGQKQRVAIAR 151
Cdd:TIGR02323 83 -LMRTEWGFVHQNPRDGLRMRVSAgaNIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 152 ALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQ 241
|
250
....*....|..
gi 637158246 231 HERTKSFLSKVL 242
Cdd:TIGR02323 242 HPYTQLLVSSIL 253
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-208 |
1.90e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 115.98 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 2 SMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLrclnkleDI-------TAGEVVVHGHTITD-PKVN 73
Cdd:COG4674 9 PILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLM-------DVitgktrpDSGSVLFGGTDLTGlDEHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 74 InkVRQEVGMVFQHFNLFPHKTVLENITIAPIKVKGI-------EKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQR 146
Cdd:COG4674 82 I--ARLGIGRKFQKPTVFEELTVFENLELALKGDRGVfaslfarLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQW 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 147 VAIARALAMDPKVLLFDEPTSALDP---EVVGDVLavmKQLAvEGMTMIVVTHEMGFAREVGDRV 208
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPVAGMTDaetERTAELL---KSLA-GKHSVVVVEHDMEFVRQIARKV 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-225 |
2.26e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 118.01 E-value: 2.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkvNINKVRQEVGM 83
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA---RARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VFQHFNLFPHKTVLENITIAP--IKVKGIEKKAAVEKaldLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLL 161
Cdd:PRK13536 119 VPQFDNLDLEFTVRENLLVFGryFGMSTREIEAVIPS---LLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 637158246 162 FDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-214 |
4.37e-31 |
|
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: 119.85 E-value: 4.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 18 VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpkvNINKVR--QEVGMVFQHFNLFPhKT 95
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS----QWDREElgRHIGYLPQDVELFD-GT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 96 VLENI----TIAPIKVkgIEkkAAvekaldllEKVGLKDKAQSFPN-----------QLSGGQKQRVAIARALAMDPKVL 160
Cdd:COG4618 422 IAENIarfgDADPEKV--VA--AA--------KLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLARALYGDPRLV 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 161 LFDEPTSALDPEvvGD--VLAVMKQLAVEGMTMIVVTHEMGFAREVgDRVIFMDGG 214
Cdd:COG4618 490 VLDEPNSNLDDE--GEaaLAAAIRALKARGATVVVITHRPSLLAAV-DKLLVLRDG 542
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-238 |
5.10e-31 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 115.25 E-value: 5.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTI-TDPKVNINKVRQ 79
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpAMSRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQHFNLFPHKTVLENITIaPIKvkgiEKKAAVEKALDL-----LEKVGLKDKAQSFPNQLSGGQKQRVAIARALA 154
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNVAY-PLR----EHTQLPAPLLHStvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 155 MDPKVLLFDEPTSALDPEVVGDVLAVMKQL-AVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHeR 233
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDP-R 238
|
....*
gi 637158246 234 TKSFL 238
Cdd:PRK11831 239 VRQFL 243
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-216 |
1.75e-30 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 117.96 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTIT--DPKVNinkVRQE 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLA---AQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFNLFPHKTVLENITIA--PIK----VKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALA 154
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGrhLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637158246 155 MDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFM-DGGYI 216
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMkDGSSV 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-228 |
1.81e-30 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 113.05 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD-PKVNInkVRQ 79
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKI--MRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQHFNLFPHKTVLENITIAPIKVKGIEKKAAVEKALDLLEKvgLKDKAQSFPNQLSGGQKQRVAIARALAMDPKV 159
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 160 LLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGN 228
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-242 |
2.07e-30 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 113.48 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHG--------HTITDPKVNI 74
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlrdlYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 75 nKVRQEVGMVFQHF--NLFPHKTVLENITiapikvkgiEKKAAV---------EKALDLLEKVGL-KDKAQSFPNQLSGG 142
Cdd:PRK11701 86 -LLRTEWGFVHQHPrdGLRMQVSAGGNIG---------ERLMAVgarhygdirATAGDWLERVEIdAARIDDLPTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 143 QKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDK 221
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGL 235
|
250 260
....*....|....*....|.
gi 637158246 222 PEALFGNPQHERTKSFLSKVL 242
Cdd:PRK11701 236 TDQVLDDPQHPYTQLLVSSVL 256
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-239 |
2.44e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 117.50 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 9 LKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKST----FLRCLNklediTAGEVVVHGHtitdPKVNINK-----VRQ 79
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQ----PLHNLNRrqllpVRH 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQHFN--LFPHKTVLEnITIAPIKV--KGIEKKAAVEKALDLLEKVGLK-DKAQSFPNQLSGGQKQRVAIARALA 154
Cdd:PRK15134 363 RIQVVFQDPNssLNPRLNVLQ-IIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 155 MDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHER 233
Cdd:PRK15134 442 LKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
....*.
gi 637158246 234 TKSFLS 239
Cdd:PRK15134 522 TRQLLA 527
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-223 |
3.26e-30 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 112.80 E-value: 3.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 2 SMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITD--PKVninkvrq 79
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlsSRQ------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 evgmVFQHFNLFP-HKTVLENITIAPIKVKG------------IEKKAAVEKALDLLEKVGLKDKAQSfpnQLSGGQKQR 146
Cdd:PRK11231 74 ----LARRLALLPqHHLTPEGITVRELVAYGrspwlslwgrlsAEDNARVNQAMEQTRINHLADRRLT---DLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 637158246 147 VAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPE 223
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-241 |
3.32e-30 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 117.65 E-value: 3.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHE----VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEV-------------VVHGH 65
Cdd:PRK10261 12 VLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 66 TITDPKvnINKVR-QEVGMVFQH--FNLFPHKTVLENITIAPIKVKGIEKKAAVEKALDLLEKVGLKDkAQS----FPNQ 138
Cdd:PRK10261 92 EQSAAQ--MRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPE-AQTilsrYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 139 LSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIV 217
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260
....*....|....*....|....
gi 637158246 218 EEDKPEALFGNPQHERTKSFLSKV 241
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLAAV 272
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-222 |
3.90e-30 |
|
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: 111.82 E-value: 3.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHE--VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQEV 81
Cdd:cd03244 3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS--KIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFNLFPhKTVLENItiapikvkGIEKKAAVEKALDLLEKVGLKDKAQSFP-----------NQLSGGQKQRVAIA 150
Cdd:cd03244 81 SIIPQDPVLFS-GTIRSNL--------DPFGEYSDEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 151 RALAMDPKVLLFDEPTSALDPEvvGDvlAVMKQLAVEGM---TMIVVTHE----MGFarevgDRVIFMDGGYIVEEDKP 222
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPE--TD--ALIQKTIREAFkdcTVLTIAHRldtiIDS-----DRILVLDKGRVVEFDSP 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-218 |
5.80e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 116.85 E-value: 5.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLkkSFG----DHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQ 79
Cdd:PRK11160 339 LTLNNV--SFTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD--YSEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQHFNLFPHkTVLENITIApikvkgiEKKAAVEKALDLLEKVGLKDKAQSFP----------NQLSGGQKQRVAI 149
Cdd:PRK11160 415 AISVVSQRVHLFSA-TLRDNLLLA-------APNASDEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGI 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 150 ARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAvEGMTMIVVTHEMgFAREVGDRVIFMDGGYIVE 218
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRL-TGLEQFDRICVMDNGQIIE 553
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-223 |
7.16e-30 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 116.69 E-value: 7.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 17 EVLKDINAVIEEKEVVCVIGPSGSGKSTFL-----RCLNKLEdiTAGEVVVHGHtitdpKVNINKVRQEVGMVFQHFNLF 91
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVK--GSGSVLLNGM-----PIDAKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 92 PHKTVLENITIA-----PIKVKGIEKKAAVEkalDLLEKVGLKDKAQSF---PNQ---LSGGQKQRVAIARALAMDPKVL 160
Cdd:TIGR00955 112 PTLTVREHLMFQahlrmPRRVTKKEKRERVD---EVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 161 LFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMG---FarEVGDRVIFMDGGYIVEEDKPE 223
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSselF--ELFDKIILMAEGRVAYLGSPD 252
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-218 |
2.29e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 115.44 E-value: 2.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 19 LKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQEVGMVFQHFNLFpHKTVLE 98
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRT--VTRASLRRNIAVVFQDAGLF-NRSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 99 NITIAPIKVKGIEKKAAVEK--ALDLLEK--VGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPE-- 172
Cdd:PRK13657 428 NIRVGRPDATDEEMRAAAERaqAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVEte 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 637158246 173 --VVGDVLAVMKqlaveGMTMIVVTHEMGFAREVgDRVIFMDGGYIVE 218
Cdd:PRK13657 508 akVKAALDELMK-----GRTTFIIAHRLSTVRNA-DRILVFDNGRVVE 549
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-223 |
3.15e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 109.79 E-value: 3.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MS-MITVKNLKKSF----------------------GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITA 57
Cdd:COG1134 1 MSsMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 58 GEVVVHGhtitdpkvninKVRQ--EVGMVFQhfnlfPHKTVLENI---------TIAPI--KVKGIEKKAAVEKALDLle 124
Cdd:COG1134 81 GRVEVNG-----------RVSAllELGAGFH-----PELTGRENIylngrllglSRKEIdeKFDEIVEFAELGDFIDQ-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 125 KVGlkdkaqsfpnQLSGGQKQRVAIARALAMDPKVLLFDEPTSaldpevVGDV------LAVMKQLAVEGMTMIVVTHEM 198
Cdd:COG1134 143 PVK----------TYSSGMRARLAFAVATAVDPDILLVDEVLA------VGDAafqkkcLARIRELRESGRTVIFVSHSM 206
|
250 260
....*....|....*....|....*
gi 637158246 199 GFAREVGDRVIFMDGGYIVEEDKPE 223
Cdd:COG1134 207 GAVRRLCDRAIWLEKGRLVMDGDPE 231
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-216 |
3.35e-29 |
|
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: 109.48 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 15 DHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKvniNK-VRQEVGMVFQHFNLFPh 93
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE---HKyLHSKVSLVGQEPVLFA- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 94 KTVLENITIAPIKVKGIEKKAAVEKA-----LDLLEKvGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSA 168
Cdd:cd03248 102 RSLQDNIAYGLQSCSFECVKEAAQKAhahsfISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 637158246 169 LDPEVvgdvlAVMKQLAV----EGMTMIVVTHEMGFArEVGDRVIFMDGGYI 216
Cdd:cd03248 181 LDAES-----EQQVQQALydwpERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-219 |
3.49e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.96 E-value: 3.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 5 TVKNLkksfGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHtitdpKVNINKVRQEV--G 82
Cdd:COG1129 258 EVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK-----PVRIRSPRDAIraG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVF-----QHFNLFPHKTVLENITIAPIKVKG----IEKKAAVEKALDLLEKVGLKdkAQSfPNQ----LSGGQKQRVAI 149
Cdd:COG1129 329 IAYvpedrKGEGLVLDLSIRENITLASLDRLSrgglLDRRRERALAEEYIKRLRIK--TPS-PEQpvgnLSGGNQQKVVL 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637158246 150 ARALAMDPKVLLFDEPTSALDpevVG---DVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEE 219
Cdd:COG1129 406 AKWLATDPKVLILDEPTRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGE 475
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-218 |
3.54e-29 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 114.73 E-value: 3.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 15 DHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKvnINKVRQEVGMVFQHFNLFpHK 94
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT--LASLRNQVALVSQNVHLF-ND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 95 TVLENITIAPIKV---KGIEKKAAVEKALDLLEKV--GLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSAL 169
Cdd:PRK11176 432 TIANNIAYARTEQysrEQIEEAARMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 637158246 170 DPEVVGDVLAVMKQLAvEGMTMIVVTHEMGfAREVGDRVIFMDGGYIVE 218
Cdd:PRK11176 512 DTESERAIQAALDELQ-KNRTSLVIAHRLS-TIEKADEILVVEDGEIVE 558
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
15-239 |
5.97e-29 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 109.40 E-value: 5.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 15 DHEVLKDINAVIEEKEVVCVIGPSGSGKStfLRCLNKLEDITAGEVVVHGHTITDPK-VNINKVR-QEVGMVFQH----F 88
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKpVAPCALRgRKIATIMQNprsaF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 89 NlfPHKTVLENiTIAPIKVKGIEKKAAVekALDLLEKVGLKDKA---QSFPNQLSGGQKQRVAIARALAMDPKVLLFDEP 165
Cdd:PRK10418 93 N--PLHTMHTH-ARETCLALGKPADDAT--LTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 166 TSALDPEVVGDVLAVMKQL-AVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHERTKSFLS 239
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVS 242
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-223 |
9.45e-29 |
|
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: 107.61 E-value: 9.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLED--ITAGEVVVHGHTITDPKVNiNKVRQEV 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPE-ERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHfnlfphktvlenitiaPIKVKGIekkaaveKALDLLEKVGLKdkaqsfpnqLSGGQKQRVAIARALAMDPKVLL 161
Cdd:cd03217 80 FLAFQY----------------PPEIPGV-------KNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637158246 162 FDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTH-EMGFAREVGDRVIFMDGGYIVEEDKPE 223
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
13-219 |
1.10e-28 |
|
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: 113.68 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 13 FGDhEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQEVGMVFQHFNLFP 92
Cdd:TIGR01193 485 YGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKD--IDRHTLRQFINYLPQEPYIFS 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 93 hKTVLENITIapikvkGIEKKAAVEKALDLLEKVGLKDKAQSFP-----------NQLSGGQKQRVAIARALAMDPKVLL 161
Cdd:TIGR01193 562 -GSILENLLL------GAKENVSQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLI 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 637158246 162 FDEPTSALDpeVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVgDRVIFMDGGYIVEE 219
Cdd:TIGR01193 635 LDESTSNLD--TITEKKIVNNLLNLQDKTIIFVAHRLSVAKQS-DKIIVLDHGKIIEQ 689
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-221 |
1.42e-27 |
|
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: 105.17 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 6 VKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpkvniNKVRQEVGMVF 85
Cdd:TIGR03740 3 TKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT------RKDLHKIGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 86 QHFNLFPHKTVLENItiapiKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEP 165
Cdd:TIGR03740 77 ESPPLYENLTARENL-----KVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 166 TSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDK 221
Cdd:TIGR03740 152 TNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGK 207
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
3-230 |
2.92e-27 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 106.88 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVkNLKKSFGDHEVlkDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDP--KVNINKVRQE 80
Cdd:PRK11144 1 MLEL-NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAekGICLPPEKRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFNLFPHKTVLENITIapikvkGIeKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVL 160
Cdd:PRK11144 78 IGYVFQDARLFPHYKVRGNLRY------GM-AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637158246 161 LFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIV-VTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:PRK11144 151 LMDEPLASLDLPRKRELLPYLERLAREINIPILyVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-230 |
3.68e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.17 E-value: 3.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAV---IEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPkvNINKVRQ 79
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVsfsITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAE--NVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQH-FNLFPHKTVLENITIApIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPK 158
Cdd:PRK13642 82 KIGMVFQNpDNQFVGATVEDDVAFG-MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637158246 159 VLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREvGDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-214 |
4.05e-27 |
|
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: 103.32 E-value: 4.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHE-----VLKDINAVIEEKEVVCVIGPSGSGKSTFLRC-LNKLEdITAGEVVVHGHtitdpkvninkv 77
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSAlLGELE-KLSGSVSVPGS------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 78 rqeVGMVFQ---HFNLfphkTVLENITI-API---KVKGIEKKAAVEKALDLLEK-----VGlkDKAQSfpnqLSGGQKQ 145
Cdd:cd03250 68 ---IAYVSQepwIQNG----TIRENILFgKPFdeeRYEKVIKACALEPDLEILPDgdlteIG--EKGIN----LSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637158246 146 RVAIARALAMDPKVLLFDEPTSALDPEVVGDVL--AVMKQLAvEGMTMIVVTHEMGFAREVgDRVIFMDGG 214
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFenCILGLLL-NNKTRILVTHQLQLLPHA-DQIVVLDNG 203
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-233 |
7.86e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 103.43 E-value: 7.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNiNKVRQE 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH-ARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFNLFPHKTVLENITIAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVL 160
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637158246 161 LFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALFGNPQHER 233
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-219 |
2.26e-26 |
|
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: 100.47 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHE--VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKvniNKVRQEV 81
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE---KALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFNLFpHKTVLENITIapikvkgiekkaavekaldllekvglkdkaqsfpnQLSGGQKQRVAIARALAMDPKVLL 161
Cdd:cd03247 78 SVLNQRPYLF-DTTLRNNLGR-----------------------------------RFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 637158246 162 FDEPTSALDPEVVGDVLAVMKQLAvEGMTMIVVTHEMGfAREVGDRVIFMDGGYIVEE 219
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVL-KDKTLIWITHHLT-GIEHMDKILFLENGKIIMQ 177
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-214 |
2.88e-26 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 107.02 E-value: 2.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSF--GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTItdpKVNINKVRQEV 81
Cdd:TIGR01257 929 VCVKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI---ETNLDAVRQSL 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFNLFPHKTVLENITIAPiKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLL 161
Cdd:TIGR01257 1006 GMCPQHNILFHHLTVAEHILFYA-QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 162 FDEPTSALDP---EVVGDVLAVMKQlaveGMTMIVVTHEMGFAREVGDRVIFMDGG 214
Cdd:TIGR01257 1085 LDEPTSGVDPysrRSIWDLLLKYRS----GRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-226 |
2.96e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 102.78 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNINKVRQEVG 82
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHfnlfPHKTVLEN-------ITIAPIKVKGIEKKAAVEKALDLLEkvglkdkAQSFPNQ----LSGGQKQRVAIAR 151
Cdd:PRK13638 81 TVFQD----PEQQIFYTdidsdiaFSLRNLGVPEAEITRRVDEALTLVD-------AQHFRHQpiqcLSHGQKKRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 152 ALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEALF 226
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
32-225 |
3.16e-26 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 102.56 E-value: 3.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 32 VC-VIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQEVGMVFQHFNLFPHKTVLENITIA------P 104
Cdd:PRK10575 39 VTgLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLES--WSSKAFARKVAYLPQQLPAAEGMTVRELVAIGrypwhgA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 105 IKVKGIEKKAAVEKALDLlekVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQL 184
Cdd:PRK10575 117 LGRFGAADREKVEEAISL---VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 637158246 185 AVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:PRK10575 194 SQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-223 |
9.24e-26 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.91 E-value: 9.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 6 VKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCL--NKLEDITAGEVVVHGHTITDPKVNiNKVRQEVGM 83
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPD-ERARAGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VFQHFNLFPHKTVLENITIAPIKVKGIEKKAA--VEKALDLLEKVGLKDK-AQSFPNQ-LSGGQKQRVAIARALAMDPKV 159
Cdd:COG0396 82 AFQYPVEIPGVSVSNFLRTALNARRGEELSARefLKLLKEKMKELGLDEDfLDRYVNEgFSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 160 LLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVG-DRVIFMDGGYIVEEDKPE 223
Cdd:COG0396 162 AILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIKpDFVHVLVDGRIVKSGGKE 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-216 |
2.67e-25 |
|
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: 97.89 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 5 TVKNLkkSFGDHevLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVninKVRQEVGMV 84
Cdd:cd03215 6 EVRGL--SVKGA--VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSP---RDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 85 F-----QHFNLFPHKTVLENITIapikvkgiekkaavekaldllekvglkdkaqsfPNQLSGGQKQRVAIARALAMDPKV 159
Cdd:cd03215 79 YvpedrKREGLVLDLSVAENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 637158246 160 LLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYI 216
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-216 |
5.03e-25 |
|
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: 102.81 E-value: 5.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 14 GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQEVGMVFQHFNLFPh 93
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK--QWDRETFGKHIGYLPQDVELFP- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 94 KTVLENITiapikvkGIEKKAAVEKALDLLEKVGLKDKAQSFPN-----------QLSGGQKQRVAIARALAMDPKVLLF 162
Cdd:TIGR01842 406 GTVAENIA-------RFGENADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 637158246 163 DEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGfAREVGDRVIFMDGGYI 216
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-214 |
2.63e-24 |
|
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: 94.05 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVvvhghtITDPKVNInkvrqevgm 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------TWGSTVKI--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 vfQHFNlfphktvlenitiapikvkgiekkaavekaldllekvglkdkaqsfpnQLSGGQKQRVAIARALAMDPKVLLFD 163
Cdd:cd03221 66 --GYFE------------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 637158246 164 EPTSALDPEVVgdvlavmkqLAVEGM------TMIVVTHEMGFAREVGDRVIFMDGG 214
Cdd:cd03221 96 EPTNHLDLESI---------EALEEAlkeypgTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-238 |
4.10e-24 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 98.05 E-value: 4.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNL----KKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRC-LNKLED---ITAGEVVVHGHTITD--P 70
Cdd:COG4170 1 MPLLDIRNLtieiDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAiCGITKDnwhVTADRFRWNGIDLLKlsP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 71 KVNINKVRQEVGMVFQHFN--LFPHKTVLENI--TIAPIKVKGI---EKKAAVEKALDLLEKVGLKD-KA--QSFPNQLS 140
Cdd:COG4170 81 RERRKIIGREIAMIFQEPSscLDPSAKIGDQLieAIPSWTFKGKwwqRFKWRKKRAIELLHRVGIKDhKDimNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 141 GGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDV---LAVMKQLavEGMTMIVVTHEMGFAREVGDRVIFMDGGYIV 217
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIfrlLARLNQL--QGTSILLISHDLESISQWADTITVLYCGQTV 238
|
250 260
....*....|....*....|.
gi 637158246 218 EEDKPEALFGNPQHERTKSFL 238
Cdd:COG4170 239 ESGPTEQILKSPHHPYTKALL 259
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-220 |
6.26e-24 |
|
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: 95.29 E-value: 6.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSF----------------------GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVV 61
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 62 VHGhtitdpkvninKVRQ--EVGMVFQhfnlfPHKTVLENITIAPIkVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQL 139
Cdd:cd03220 81 VRG-----------RVSSllGLGGGFN-----PELTGRENIYLNGR-LLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 140 SGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEE 219
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
.
gi 637158246 220 D 220
Cdd:cd03220 224 G 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-216 |
1.03e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 98.83 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 8 NLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHG--HTITDPKVNINkvrQEVGMVF 85
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqeMRFASTTAALA---AGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 86 QHFNLFPHKTVLENITIAPIKVKG--IEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFD 163
Cdd:PRK11288 86 QELHLVPEMTVAENLYLGQLPHKGgiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 637158246 164 EPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRV-IFMDGGYI 216
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAItVFKDGRYV 219
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-197 |
1.76e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.40 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 14 GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQEVGMVFQHFNLFpH 93
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIS--TLKPEIYRQQVSYCAQTPTLF-G 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 94 KTVLENItIAPIKvkgIEKKAAVEKAL-DLLEKVGLKDKAQSFP-NQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDP 171
Cdd:PRK10247 95 DTVYDNL-IFPWQ---IRNQQPDPAIFlDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180
....*....|....*....|....*..
gi 637158246 172 EVVGDVLAVMKQLAVE-GMTMIVVTHE 197
Cdd:PRK10247 171 SNKHNVNEIIHRYVREqNIAVLWVTHD 197
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-225 |
6.28e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.90 E-value: 6.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 7 KNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQEVGMVFQ 86
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ--HYASKEVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 87 HfnlfphKTVLENITIAPIKVKG------------IEKKAAVEKALdllEKVGLKDKAQSFPNQLSGGQKQRVAIARALA 154
Cdd:PRK10253 89 N------ATTPGDITVQELVARGryphqplftrwrKEDEEAVTKAM---QATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637158246 155 MDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-221 |
1.28e-22 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 91.94 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 16 HEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVhghtitdpKVNINKVRQEVgmvfqhfnlfphkT 95
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV--------DVPDNQFGREA-------------S 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 96 VLENITIAPikvkgiEKKAAVEkaldLLEKVGLKDkAQSF---PNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPE 172
Cdd:COG2401 102 LIDAIGRKG------DFKDAVE----LLNAVGLSD-AVLWlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 637158246 173 VVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVG-DRVIFMDGGYIVEEDK 221
Cdd:COG2401 171 TAKRVARNLQKLARRaGITLVVATHHYDVIDDLQpDLLIFVGYGGVPEEKR 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-217 |
1.54e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 95.50 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQeVG 82
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA--RLTPAKAHQ-LG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 --MVFQHFNLFPHKTVLENITIapikvkGIEKKAAVEKAL-DLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKV 159
Cdd:PRK15439 88 iyLVPQEPLLFPNLSVKENILF------GLPKRQASMQKMkQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 637158246 160 LLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIV 217
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIA 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3-196 |
5.64e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.93 E-value: 5.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVniNKVRQEVG 82
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV--AEACHYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 mvfqHFN-LFPHKTVLENITI-ApiKVKGiEKKAAVEKAldlLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVL 160
Cdd:PRK13539 80 ----HRNaMKPALTVAENLEFwA--AFLG-GEELDIAAA---LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIW 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 637158246 161 LFDEPTSALDPEVVGDVLAVMK-QLAVEGMtMIVVTH 196
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIRaHLAQGGI-VIAATH 185
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-196 |
1.47e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.95 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 2 SMITVKNLKKSFGDHEVL-KDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTIT-----DPKVNIN 75
Cdd:COG4178 361 GALALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVlflpqRPYLPLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 76 KVRQEVgmvfqhfnLFPHKTvlENITiapikvkgiekKAAVEKALdllEKVGLK------DKAQSFPNQLSGGQKQRVAI 149
Cdd:COG4178 441 TLREAL--------LYPATA--EAFS-----------DAELREAL---EAVGLGhlaerlDEEADWDQVLSLGEQQRLAF 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 637158246 150 ARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQlAVEGMTMIVVTH 196
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-217 |
4.29e-21 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 87.32 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 10 KKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITA---GEVVVHGHtitDPKVNINKVRQEVGMVFQ 86
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGI---PYKEFAEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 87 HFNLFPHKTVLENITIApikvkgiekkaavekaldllekvgLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPT 166
Cdd:cd03233 91 EDVHFPTLTVRETLDFA------------------------LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 637158246 167 SALDPEVVGDVLAVMKQLA-VEGMTMIV-VTHEMGFAREVGDRVIFMDGGYIV 217
Cdd:cd03233 147 RGLDSSTALEILKCIRTMAdVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-218 |
1.09e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 90.29 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLK-KSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLrclNKLEDITA--GEVVVHGHTITDpkVNINKVRQE 80
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLL---NALLGFLPyqGSLKINGIELRE--LDPESWRKH 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFNLFpHKTVLENITIAPIKVKGIEKKAAVEKA-----LDLLEKvGL----KDKAQSfpnqLSGGQKQRVAIAR 151
Cdd:PRK11174 425 LSWVGQNPQLP-HGTLRDNVLLGNPDASDEQLQQALENAwvsefLPLLPQ-GLdtpiGDQAAG----LSVGQAQRLALAR 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637158246 152 ALAMDPKVLLFDEPTSALD--PEVvgdvlAVMKQL--AVEGMTMIVVTHEMGFAREVgDRVIFMDGGYIVE 218
Cdd:PRK11174 499 ALLQPCQLLLLDEPTASLDahSEQ-----LVMQALnaASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQ 563
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-219 |
3.34e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.69 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 6 VKNLKKSfgDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdPKVNINKVRQEVGMVF 85
Cdd:PRK09700 268 VRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS-PRSPLDAVKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 86 QH---FNLFPHKTVLENITIAP-IKVKGI-----------EKKAAvEKALDLLEKvglkdKAQSFP---NQLSGGQKQRV 147
Cdd:PRK09700 345 ESrrdNGFFPNFSIAQNMAISRsLKDGGYkgamglfhevdEQRTA-ENQRELLAL-----KCHSVNqniTELSGGNQQKV 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637158246 148 AIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEE 219
Cdd:PRK09700 419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-225 |
5.98e-20 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 88.08 E-value: 5.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNK---LEDitaGEVVVHGHTIT-----DPKv 72
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDD---GRIIYEQDLIVarlqqDPP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 73 ninkvRQEVGMVF-----------QHFNLFPHktVLENITIAPIKvKGIEKKAAVEKALD-------------LLEKVGL 128
Cdd:PRK11147 77 -----RNVEGTVYdfvaegieeqaEYLKRYHD--ISHLVETDPSE-KNLNELAKLQEQLDhhnlwqlenrineVLAQLGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 129 KdkAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLavEGmTMIVVTHEMGFAREVGDRV 208
Cdd:PRK11147 149 D--PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QG-SIIFISHDRSFIRNMATRI 223
|
250 260
....*....|....*....|....*.
gi 637158246 209 IFMDGGYIVE---------EDKPEAL 225
Cdd:PRK11147 224 VDLDRGKLVSypgnydqylLEKEEAL 249
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-226 |
6.55e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 88.24 E-value: 6.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSF-GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQEVG 82
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS--SLSHSVLRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVfQHFNLFPHKTVLENITIApikvkgieKKAAVEKALDLLEKVGLKDKAQSFP-----------NQLSGGQKQRVAIAR 151
Cdd:PRK10790 419 MV-QQDPVVLADTFLANVTLG--------RDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 637158246 152 ALAMDPKVLLFDEPTSALDPevvGDVLAVMKQLAV--EGMTMIVVTHEMGFAREvGDRVIFMDGGYIVEEDKPEALF 226
Cdd:PRK10790 490 VLVQTPQILILDEATANIDS---GTEQAIQQALAAvrEHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-217 |
1.28e-19 |
|
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: 84.31 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDH---------------------EVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVV 62
Cdd:cd03267 1 IEVSNLSKSYRVYskepgligslkslfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 63 HGHtitDPKVNINKVRQEVGMVF-QHFNLFPHKTVLENIT-IAPI-KVKGIEKKAAVEKALDLLEKVGLKDKaqsfP-NQ 138
Cdd:cd03267 81 AGL---VPWKRRKKFLRRIGVVFgQKTQLWWDLPVIDSFYlLAAIyDLPPARFKKRLDELSELLDLEELLDT----PvRQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 139 LSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDGGYIV 217
Cdd:cd03267 154 LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-229 |
1.50e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 87.08 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 15 DHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQEVGMVFQHFNLFPhK 94
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTK--LQLDSWRSRLAVVSQTPFLFS-D 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 95 TVLENITIA-----PIKVKGIEKKAAV-EKALDLLE----KVGLKDKaqsfpnQLSGGQKQRVAIARALAMDPKVLLFDE 164
Cdd:PRK10789 404 TVANNIALGrpdatQQEIEHVARLASVhDDILRLPQgydtEVGERGV------MLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 165 PTSALDPEVVGDVLAVMKQLAvEGMTMIVVTHEMGFAREvGDRVIFMDGGYIVEEDKPEALFGNP 229
Cdd:PRK10789 478 ALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
5-197 |
1.72e-19 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 86.86 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 5 TVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLnkleditAGEVvvHGHTITDpKVNIN------KVR 78
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRI--QGNNFTG-TILANnrkptkQIL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 79 QEVGMVFQHFNLFPHKTVLENITIAPIK--VKGIEKKAAVEKALDLLEKVGLKD-----KAQSFPNQLSGGQKQRVAIAR 151
Cdd:PLN03211 140 KRTGFVTQDDILYPHLTVRETLVFCSLLrlPKSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAH 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 637158246 152 ALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHE 197
Cdd:PLN03211 220 EMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-196 |
3.25e-19 |
|
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: 82.41 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGhtitDPKVNINKVRQEVGM 83
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG----TPLAEQRDEPHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VFQHFN-LFPHKTVLENITI-APIKvkgiekKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLL 161
Cdd:TIGR01189 77 YLGHLPgLKPELSALENLHFwAAIH------GGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190
....*....|....*....|....*....|....*
gi 637158246 162 FDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTH 196
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
31-218 |
4.23e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.44 E-value: 4.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 31 VVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHtitdpKVNIN--KVRQE--VGMVFQHFNLFPHKTVLENITIAPIK 106
Cdd:PRK10762 32 VMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGK-----EVTFNgpKSSQEagIGIIHQELNLIPQLTIAENIFLGREF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 107 VK---GIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQ 183
Cdd:PRK10762 107 VNrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRE 186
|
170 180 190
....*....|....*....|....*....|....*.
gi 637158246 184 LAVEGMTMIVVTHEMGFAREVGDRV-IFMDGGYIVE 218
Cdd:PRK10762 187 LKSQGRGIVYISHRLKEIFEICDDVtVFRDGQFIAE 222
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-234 |
5.00e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 83.98 E-value: 5.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSF-------GDHEVLKD--------INAV------IEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVV 61
Cdd:COG4586 1 IIEVENLSKTYrvyekepGLKGALKGlfrreyreVEAVddisftIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 62 VHGHtitDPKVNINKVRQEVGMVF-QHFNLFPHKTVLENITIapIK-VKGIEKKAAvEKALDLLEKV-GLKDKAQSFPNQ 138
Cdd:COG4586 81 VLGY---VPFKRRKEFARRIGVVFgQRSQLWWDLPAIDSFRL--LKaIYRIPDAEY-KKRLDELVELlDLGELLDTPVRQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 139 LSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQL-AVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIV 217
Cdd:COG4586 155 LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
250
....*....|....*..
gi 637158246 218 EEDKPEALFGNPQHERT 234
Cdd:COG4586 235 YDGSLEELKERFGPYKT 251
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-220 |
7.50e-19 |
|
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: 84.88 E-value: 7.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKL--EDITAGEVVVHGHTITDPKVNiNKVRQE 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIR-DTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFNLFPHKTVLENITIA-PIKVKG--IEKKAAVEKALDLLEKVGLKDKAQSFP-NQLSGGQKQRVAIARALAMD 156
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGnEITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 157 PKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRV-IFMDGGYIVEED 220
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTIcVIRDGQHVATKD 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-225 |
9.68e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 84.79 E-value: 9.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTItDPKvNINkVRQEVGM 83
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DAG-DIA-TRRRVGY 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VFQHFNLFPHKTVLENITI-ApiKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLF 162
Cdd:NF033858 344 MSQAFSLYGELTVRQNLELhA--RLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLIL 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 163 DEPTSALDPeVVGDVL-AVMKQLAVE-GMTMIVVTHEMGFArEVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:NF033858 422 DEPTSGVDP-VARDMFwRLLIELSREdGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAAL 484
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-221 |
3.61e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.05 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKL--------EDITAGEVVvHGHTITDPKvni 74
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyegEIIFEGEEL-QASNIRDTE--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 75 nkvRQEVGMVFQHFNLFPHKTVLENITIAPIKVKG--IEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARA 152
Cdd:PRK13549 81 ---RAGIAIIHQELALVKELSVLENIFLGNEITPGgiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 153 LAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRV-IFMDGGYIVEEDK 221
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTIcVIRDGRHIGTRPA 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
7-216 |
3.93e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.92 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 7 KNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKL--------EDITAGEvVVHGHTITDpkvninkvR 78
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyegEILFDGE-VCRFKDIRD--------S 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 79 QEVGMVF--QHFNLFPHKTVLENITIA-PIKVKG-IEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALA 154
Cdd:NF040905 76 EALGIVIihQELALIPYLSIAENIFLGnERAKRGvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637158246 155 MDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRV-IFMDGGYI 216
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSItVLRDGRTI 218
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-222 |
4.85e-18 |
|
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: 79.38 E-value: 4.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDH--EVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQEV 81
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS--TIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFNLFpHKTVLENITIapikvKGIEKKAAVEKALDLLEKvglkdkaqsfPNQLSGGQKQRVAIARALAMDPKVLL 161
Cdd:cd03369 85 TIIPQDPTLF-SGTIRSNLDP-----FDEYSDEEIYGALRVSEG----------GLNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637158246 162 FDEPTSALDPEVVGDVLAVMKQLaVEGMTMIVVTHEMGFAREVgDRVIFMDGGYIVEEDKP 222
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREE-FTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-228 |
1.12e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 81.71 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKN---LKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRC-LNKLEDITAGEVVVHGHTITDPKVN-Inkvr 78
Cdd:PLN03130 615 ISIKNgyfSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAmLGELPPRSDASVVIRGTVAYVPQVSwI---- 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 79 qevgmvfqhFNlfphKTVLENITI-APIKVKGIEKK---AAVEKALDLLEKVGLKDKAQSFPNqLSGGQKQRVAIARALA 154
Cdd:PLN03130 691 ---------FN----ATVRDNILFgSPFDPERYERAidvTALQHDLDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVY 756
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 637158246 155 MDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVgDRVIFMDGGYIVEEDKPEALFGN 228
Cdd:PLN03130 757 SNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-238 |
1.36e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 80.23 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSF----GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLED----ITAGEVVVHGHTIT--DP 70
Cdd:PRK15093 1 MPLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLrlSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 71 KVNINKVRQEVGMVFQHFN--LFPHKTV----LENITIAPIKVK-----GIEKKAAVEkaldLLEKVGLKDKA---QSFP 136
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQscLDPSERVgrqlMQNIPGWTYKGRwwqrfGWRKRRAIE----LLHRVGIKDHKdamRSFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 137 NQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQL-AVEGMTMIVVTHEMGFAREVGDRVIFMDGGY 215
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
250 260
....*....|....*....|...
gi 637158246 216 IVEEDKPEALFGNPQHERTKSFL 238
Cdd:PRK15093 237 TVETAPSKELVTTPHHPYTQALI 259
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-196 |
1.81e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.92 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGhtitdpkVNINKVRQEVg 82
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG-------EPIRRQRDEY- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 mvfqHFNLF---------PHKTVLENITIApikvKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARAL 153
Cdd:PRK13538 73 ----HQDLLylghqpgikTELTALENLRFY----QRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLW 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 637158246 154 AMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTH 196
Cdd:PRK13538 145 LTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-202 |
2.23e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.84 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFG---DHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVH-GHTITDpkVNINKVRQ 79
Cdd:PTZ00265 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKD--INLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQHFNLFPHkTVLENITIAPIKVKGIE------------------------KKAAVE------------------ 117
Cdd:PTZ00265 461 KIGVVSQDPLLFSN-SIKNNIKYSLYSLKDLEalsnyynedgndsqenknkrnscrAKCAGDlndmsnttdsneliemrk 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 118 --------KALDLLEKVGLKDKAQSFPNQ-----------LSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVL 178
Cdd:PTZ00265 540 nyqtikdsEVVDVSKKVLIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250 260
....*....|....*....|....*
gi 637158246 179 AVMKQL-AVEGMTMIVVTHEMGFAR 202
Cdd:PTZ00265 620 KTINNLkGNENRITIIIAHRLSTIR 644
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-196 |
3.39e-17 |
|
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: 76.04 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVL-KDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTitdpkvninkvrqevG 82
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE---------------D 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFqhfnlFPHKTVLENITiapikvkgiekkaavekaldllekvgLKDkAQSFP--NQLSGGQKQRVAIARALAMDPKVL 160
Cdd:cd03223 66 LLF-----LPQRPYLPLGT--------------------------LRE-QLIYPwdDVLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190
....*....|....*....|....*....|....*.
gi 637158246 161 LFDEPTSALDPEVVGDVLAVMKQlavEGMTMIVVTH 196
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKE---LGITVISVGH 146
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
19-218 |
3.53e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 80.02 E-value: 3.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 19 LKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPkvNINKVRQEVGMVFQHFNLFPHktvle 98
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE--QPEDYRKLFSAVFTDFHLFDQ----- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 99 nitiapikVKGIEKKAAVEKALDL-LEKVGLKDKAQSFPN-----QLSGGQKQRVAIARALAMDPKVLLFDEPTSALDP- 171
Cdd:PRK10522 412 --------LLGPEGKPANPALVEKwLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPh 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 637158246 172 ---EVVGDVLAVMKQLaveGMTMIVVTHEMGFArEVGDRVIFMDGGYIVE 218
Cdd:PRK10522 484 frrEFYQVLLPLLQEM---GKTIFAISHDDHYF-IHADRLLEMRNGQLSE 529
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-225 |
3.73e-17 |
|
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: 79.84 E-value: 3.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 22 INAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDpkVNINKVRQEVGMVFQHFNLFPHktvlenit 101
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA--DNREAYRQLFSAVFSDFHLFDR-------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 102 iapikVKGIEKKAAVEKALDLLEKVGLKDKAQ----SFPN-QLSGGQKQRVAIARALAMDPKVLLFDEPTSALDP----- 171
Cdd:COG4615 421 -----LLGLDGEADPARARELLERLELDHKVSvedgRFSTtDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPefrrv 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 637158246 172 ---EVVGDvlavMKQlavEGMTMIVVTH-EMGFarEVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:COG4615 496 fytELLPE----LKA---RGKTVIAISHdDRYF--DLADRVLKMDYGKLVELTGPAAL 544
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-196 |
5.77e-17 |
|
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: 76.38 E-value: 5.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 6 VKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNINKVRQEVGmvf 85
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 86 qHFN-LFPHKTVLENITIapikVKGIEKKAAVEKALDLLEKVGLKDKAQsfpNQLSGGQKQRVAIARALAMDPKVLLFDE 164
Cdd:cd03231 80 -HAPgIKTTLSVLENLRF----WHADHSDEQVEEALARVGLNGFEDRPV---AQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|..
gi 637158246 165 PTSALDPEVVGDVLAVMKQLAVEGMTMIVVTH 196
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-216 |
6.95e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 79.00 E-value: 6.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 7 KNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTItDPKVNINKVRQEVGMVFQ 86
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 87 HFNLFPHKTVLENITIAPIKVKGI---EKK-----AAVEKALDLleKVGLKDKAQSfpnqLSGGQKQRVAIARALAMDPK 158
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKGMfvdQDKmyrdtKAIFDELDI--DIDPRAKVAT----LSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 159 VLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRV-IFMDGGYI 216
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEItILRDGQWI 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-225 |
7.83e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.92 E-value: 7.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 6 VKNLK-KSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVninKVRQEVGMV 84
Cdd:COG3845 260 VENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSP---RERRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 85 F-----QHFNLFPHKTVLENITI-----APIKVKG-IEKKAAVEKALDLLEK-----VGLKDKAQSfpnqLSGGQKQRVA 148
Cdd:COG3845 337 YipedrLGRGLVPDMSVAENLILgryrrPPFSRGGfLDRKAIRAFAEELIEEfdvrtPGPDTPARS----LSGGNQQKVI 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 149 IARALAMDPKVLLFDEPTSALDpevVGDVLAVMKQL---AVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLD---VGAIEFIHQRLlelRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-221 |
1.03e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 78.82 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVhGHTitdpkVNINKVRQevgm 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GET-----VKLAYVDQ---- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 vfQHFNLFPHKTVLENIT--IAPIKVKGIE--KKAAVE----KALDLLEKVGlkdkaqsfpnQLSGGQKQRVAIARALAM 155
Cdd:TIGR03719 393 --SRDALDPNKTVWEEISggLDIIKLGKREipSRAYVGrfnfKGSDQQKKVG----------QLSGGERNRVHLAKTLKS 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 156 DPKVLLFDEPTSALDPEVVG---DVLavmkqLAVEGMTMI----------VVTHEMGFArevGD-RVIFMDGGYI-VEED 220
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDVETLRaleEAL-----LNFAGCAVVishdrwfldrIATHILAFE---GDsHVEWFEGNFSeYEED 532
|
.
gi 637158246 221 K 221
Cdd:TIGR03719 533 K 533
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-213 |
1.09e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.85 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 2 SMITVKNLKKSFGD-HEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpkvniNKVRQE 80
Cdd:PRK15056 5 AGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR------QALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 -VGMVFQHFNL---FPhkTVLENITIAP-------IKVKGIEKKAAVEKALdllEKVGLKDKAQSFPNQLSGGQKQRVAI 149
Cdd:PRK15056 79 lVAYVPQSEEVdwsFP--VLVEDVVMMGryghmgwLRRAKKRDRQIVTAAL---ARVDMVEFRHRQIGELSGGQKKRVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 637158246 150 ARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDG 213
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKG 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-228 |
1.62e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 78.48 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 19 LKDINAVIEEKEVVCVIGPSGSGKSTFLRC-LNKLEDITAGEVVVHGHTITDPKVNinkvrqevgMVFqhfnlfpHKTVL 97
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVIRGSVAYVPQVS---------WIF-------NATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 98 ENITIA----PIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNqLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEV 173
Cdd:PLN03232 697 ENILFGsdfeSERYWRAIDVTALQHDLDLLPGRDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 174 VGDVLAVMKQLAVEGMTMIVVTHEMGFAREVgDRVIFMDGGYIVEEDKPEALFGN 228
Cdd:PLN03232 776 AHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-214 |
2.08e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 77.94 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 21 DINAVIEEKEVVCVIGPSGSGKSTFLRCL-NKLEDITAGEVVVHGHTItDPKVNINKVRQEVGMV---FQHFNLFPHKTV 96
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPV-DIRNPAQAIRAGIAMVpedRKRHGIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 97 LENITIAPIK---VKGIEKKAAVEKALDL-LEKVGLKDKAQSFP-NQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDP 171
Cdd:TIGR02633 357 GKNITLSVLKsfcFKMRIDAAAELQIIGSaIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 637158246 172 EVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGG 214
Cdd:TIGR02633 437 GAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-196 |
2.92e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 75.45 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 2 SMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCL--NKLEDITAGEVVVHGHTITDPKVNInKVRQ 79
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPEE-RAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQHfnlfphktvlenitiaPIKVKGI------------EKKAAVEKALDLLE-------KVGLKDKAQSFPNQ-- 138
Cdd:CHL00131 85 GIFLAFQY----------------PIEIPGVsnadflrlaynsKRKFQGLPELDPLEfleiineKLKLVGMDPSFLSRnv 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637158246 139 ---LSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTH 196
Cdd:CHL00131 149 negFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-213 |
3.34e-16 |
|
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: 75.14 E-value: 3.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 26 IEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTIT-DPKvninKVRQEVGMVFQHFnLFphkTVLENITIAP 104
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSyKPQ----YIKADYEGTVRDL-LS---SITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 105 IKVKGIEKKAAVEKALDllekvglkdkaQSFPNqLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQL 184
Cdd:cd03237 94 YFKTEIAKPLQIEQILD-----------REVPE-LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRF 161
|
170 180 190
....*....|....*....|....*....|
gi 637158246 185 AVEG-MTMIVVTHEMGFAREVGDRVIFMDG 213
Cdd:cd03237 162 AENNeKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-218 |
6.17e-16 |
|
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: 76.91 E-value: 6.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSF--GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPK---VNINKVR 78
Cdd:TIGR00957 637 ITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQqawIQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 79 QEVgmvfqhfnLFPHKtvlenitIAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNqLSGGQKQRVAIARALAMDPK 158
Cdd:TIGR00957 717 ENI--------LFGKA-------LNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNAD 780
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 637158246 159 VLLFDEPTSALDPEV----VGDVLAVMKQLAveGMTMIVVTHEMGFAREVgDRVIFMDGGYIVE 218
Cdd:TIGR00957 781 IYLFDDPLSAVDAHVgkhiFEHVIGPEGVLK--NKTRILVTHGISYLPQV-DVIIVMSGGKISE 841
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-198 |
1.23e-15 |
|
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: 74.12 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSF--GDHEVLKDINAVIEEKEVVCVIGPSGSGKST----FLRCLNklediTAGEVVVHGhtITDPKVNINKV 77
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLN-----TEGDIQIDG--VSWNSVPLQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 78 RQEVGMVFQHFNLFPhKTVLENITiaPikvkgiEKKAAVEKALDLLEKVGLKDKAQSFPNQL-----------SGGQKQR 146
Cdd:cd03289 76 RKAFGVIPQKVFIFS-GTFRKNLD--P------YGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 637158246 147 VAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQlAVEGMTMIVVTHEM 198
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRI 197
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-225 |
2.22e-15 |
|
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: 74.98 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 18 VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQEVGMVFQHFNLFPHKTvl 97
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA--KIGLHDLRFKITIIPQDPVLFSGSL-- 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 98 eNITIAPIkvkgieKKAAVEKALDLLEKVGLKDKAQSFPNQ-----------LSGGQKQRVAIARALAMDPKVLLFDEPT 166
Cdd:TIGR00957 1377 -RMNLDPF------SQYSDEEVWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 167 SALDPEvVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVgDRVIFMDGGYIVEEDKPEAL 225
Cdd:TIGR00957 1450 AAVDLE-TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNL 1506
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-223 |
2.36e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.95 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 19 LKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDiTAGEVVVHGHTITD-PKVNINKVR-----QEV---GM-VFQHF 88
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDwSAAELARHRaylsqQQSppfAMpVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 89 NLF-PHKTVLEnitiapikvkgiekkaAVEKAL-DLLEKVGLKDKAQSFPNQLSGGQKQRVAIARAL-----AMDP--KV 159
Cdd:COG4138 91 ALHqPAGASSE----------------AVEQLLaQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPegQL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 637158246 160 LLFDEPTSALDpevVGDVLAV---MKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPE 223
Cdd:COG4138 155 LLLDEPMNSLD---VAQQAALdrlLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-172 |
4.48e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 74.00 E-value: 4.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVhGHTitdpkVNINKVRQevgm 83
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GET-----VKLAYVDQ---- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 vfQHFNLFPHKTVLENIT----IapIKVKGIE--KKAAVE----KALDLLEKVGlkdkaqsfpnQLSGGQKQRVAIARAL 153
Cdd:PRK11819 395 --SRDALDPNKTVWEEISggldI--IKVGNREipSRAYVGrfnfKGGDQQKKVG----------VLSGGERNRLHLAKTL 460
|
170
....*....|....*....
gi 637158246 154 AMDPKVLLFDEPTSALDPE 172
Cdd:PRK11819 461 KQGGNVLLLDEPTNDLDVE 479
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-238 |
4.88e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 74.30 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 18 VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVNINKVR----QEVGM---------- 83
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTNEQDYQgdeeQNVGMknvnefsltk 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 ---------VFQH----------------------FNLFPHKTVLENITIAPiKVKGIEKKAAVEKALDLLEKVGLKDKA 132
Cdd:PTZ00265 1263 eggsgedstVFKNsgkilldgvdicdynlkdlrnlFSIVSQEPMLFNMSIYE-NIKFGKEDATREDVKRACKFAAIDEFI 1341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 133 QSFPNQ-----------LSGGQKQRVAIARALAMDPKVLLFDEPTSALDP---EVVGDVLAVMKQLAVEgmTMIVVTHEM 198
Cdd:PTZ00265 1342 ESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKADK--TIITIAHRI 1419
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 637158246 199 GFAREvGDRVIfmdggyiveedkpeaLFGNPqhERTKSFL 238
Cdd:PTZ00265 1420 ASIKR-SDKIV---------------VFNNP--DRTGSFV 1441
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-197 |
5.20e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 73.99 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 14 GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLED---ITAGEVVVHGHTITdpkvniNKVRQEVGMVFQHFNL 90
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLD------SSFQRSIGYVQQQDLH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 91 FPHKTVLENITIA-----PIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQ-LSGGQKQRVAIARALAMDPKVLLF-D 163
Cdd:TIGR00956 848 LPTSTVRESLRFSaylrqPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLFlD 927
|
170 180 190
....*....|....*....|....*....|....
gi 637158246 164 EPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHE 197
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-170 |
7.27e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.68 E-value: 7.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVvhghtiTDPKVNINKVRQE 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKLRIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VgmvfqHFNLFPHKTVLENITIAPikvkGIeKKAAVEKALDLLEKVGLKDkaqsFPNQ-LSGGQKQRVAIARALAMDPKV 159
Cdd:PRK09544 76 L-----YLDTTLPLTVNRFLRLRP----GT-KKEDILPALKRVQAGHLID----APMQkLSGGETQRVLLARALLNRPQL 141
|
170
....*....|.
gi 637158246 160 LLFDEPTSALD 170
Cdd:PRK09544 142 LVLDEPTQGVD 152
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-214 |
1.19e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.73 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 22 INAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDiTAGEVVVHGHTITD-PKVNINKVR----QEV----GM-VFQHFNLF 91
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAwSAAELARHRaylsQQQtppfAMpVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 92 -PHKTVLenitiapikvkgiekkAAVEKALDLL-EKVGLKDKAQSFPNQLSGGQKQRVAIARA-LAMDP------KVLLF 162
Cdd:PRK03695 94 qPDKTRT----------------EAVASALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPdinpagQLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 637158246 163 DEPTSALD--PEVVGDVLavMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGG 214
Cdd:PRK03695 158 DEPMNSLDvaQQAALDRL--LSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQG 209
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-214 |
1.54e-14 |
|
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: 69.58 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 2 SMITVKNLKKSF----GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLED--ITAGEVVVHGHTITDpkvnin 75
Cdd:cd03232 2 SVLTWKNLNYTVpvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDK------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 76 KVRQEVGMVFQHFNLFPHKTVLENITIAPiKVKGiekkaavekaldllekvglkdkaqsfpnqLSGGQKQRVAIARALAM 155
Cdd:cd03232 76 NFQRSTGYVEQQDVHSPNLTVREALRFSA-LLRG-----------------------------LSVEQRKRLTIGVELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637158246 156 DPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMG---FarEVGDRVIFMDGG 214
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSasiF--EKFDRLLLLKRG 185
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-196 |
1.77e-14 |
|
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: 72.64 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNL--KKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDiTAGEVVVHGhtITDPKVNINKVRQEV 81
Cdd:TIGR01271 1218 MDVQGLtaKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG--VSWNSVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHF---------NLFPHKtvlenitiapikvkgiekKAAVEKALDLLEKVGLKDKAQSFPNQL-----------SG 141
Cdd:TIGR01271 1295 GVIPQKVfifsgtfrkNLDPYE------------------QWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSN 1356
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 142 GQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQlAVEGMTMIVVTH 196
Cdd:TIGR01271 1357 GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEH 1410
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-241 |
1.91e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.45 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 9 LKKSFGDHE-----VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLED----ITAGEVVVHGHTITDPKvniNKVRQ 79
Cdd:TIGR00956 62 FRKLKKFRDtktfdILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIK---KHYRG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 80 EVGMVFQHFNLFPHKTVLENITIAP------IKVKGIEKKAAVEKALDLL-----------EKVGlkdkaQSFPNQLSGG 142
Cdd:TIGR00956 139 DVVYNAETDVHFPHLTVGETLDFAArcktpqNRPDGVSREEYAKHIADVYmatyglshtrnTKVG-----NDFVRGVSGG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 143 QKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMG-FAREVGDRVIFMDGGYIV--- 217
Cdd:TIGR00956 214 ERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANIlDTTPLVAIYQCSqDAYELFDKVIVLYEGYQIyfg 293
|
250 260
....*....|....*....|....*....
gi 637158246 218 EEDKPEALFGN-----PQHERTKSFLSKV 241
Cdd:TIGR00956 294 PADKAKQYFEKmgfkcPDRQTTADFLTSL 322
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-221 |
2.18e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.89 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 5 TVKNLKKSF-GDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVvhghtitdPKVNINkvrqeVGM 83
Cdd:TIGR03719 6 TMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR--------PQPGIK-----VGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 VFQHFNLFPHKTVLENITIAPIKVKG----------------------IEKKAAVEKALD------LLEKVGLKDKAQSF 135
Cdd:TIGR03719 73 LPQEPQLDPTKTVRENVEEGVAEIKDaldrfneisakyaepdadfdklAAEQAELQEIIDaadawdLDSQLEIAMDALRC 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 136 P------NQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVgdvlAVMKQ-LAVEGMTMIVVTHemgfarevgDRV 208
Cdd:TIGR03719 153 PpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV----AWLERhLQEYPGTVVAVTH---------DRY 219
|
250
....*....|....*
gi 637158246 209 iFMD--GGYIVEEDK 221
Cdd:TIGR03719 220 -FLDnvAGWILELDR 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
30-224 |
3.32e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.10 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 30 EVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTitdpkVNINKVRQEV--GMVF-----QHFNLFPHKTVLENITI 102
Cdd:PRK11288 280 EIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKP-----IDIRSPRDAIraGIMLcpedrKAEGIIPVHSVADNINI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 103 A--PIKVKG---IEKKAAVEKALDLLEKVGLKDK-AQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDpevVG- 175
Cdd:PRK11288 355 SarRHHLRAgclINNRWEAENADRFIRSLNIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID---VGa 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 176 --DVLAVMKQLAVEGMTMIVVTHE----MGfareVGDRVIFMDGGYIVEE-DKPEA 224
Cdd:PRK11288 432 khEIYNVIYELAAQGVAVLFVSSDlpevLG----VADRIVVMREGRIAGElAREQA 483
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-213 |
9.10e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.22 E-value: 9.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEvLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVvvhghtitDPKVNINKVRQEV- 81
Cdd:PRK13409 340 LVEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--------DPELKISYKPQYIk 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 ----GMVFQhfnlfphktVLENITIA----PIKVkgiekkaavekalDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARAL 153
Cdd:PRK13409 411 pdydGTVED---------LLRSITDDlgssYYKS-------------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637158246 154 AMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDG 213
Cdd:PRK13409 469 SRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-225 |
1.02e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 17 EVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVninKVRQEVGMVF-----QHFNLF 91
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST---AQRLARGLVYlpedrQSSGLY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 92 PHKTVLENITIAPIKVKGIEKKAAVEKALdlLEK----VGLK-DKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPT 166
Cdd:PRK15439 354 LDAPLAWNVCALTHNRRGFWIKPARENAV--LERyrraLNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 167 SALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-226 |
1.37e-13 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 68.01 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 18 VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQEVGMVFQ---------HF 88
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS--KLPLHTLRSRLSIILQdpilfsgsiRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 89 NLFPhktvlenitiapikvkgiEKKAAVEKALDLLEKVGLKDKAQSFPNQL-----------SGGQKQRVAIARALAMDP 157
Cdd:cd03288 114 NLDP------------------ECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 158 KVLLFDEPTSALDpEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREvGDRVIFMDGGYIVEEDKPEALF 226
Cdd:cd03288 176 SILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-228 |
1.89e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.62 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 18 VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQEVGMVFQHFNLFPhKTVL 97
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA--KFGLTDLRRVLSIIPQSPVLFS-GTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 98 ENITiaPIKVkgiEKKAAVEKALdllEKVGLKDKAQSFP-----------NQLSGGQKQRVAIARALAMDPKVLLFDEPT 166
Cdd:PLN03232 1328 FNID--PFSE---HNDADLWEAL---ERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637158246 167 SALDPEVVGDVLAVMKQlAVEGMTMIVVTHEMGFAREVgDRVIFMDGGYIVEEDKPEALFGN 228
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSR 1459
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-219 |
2.64e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 19 LKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTIT--DPK-------VNINKVRQEVGMVFQhfn 89
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrSPQdglangiVYISEDRKRDGLVLG--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 90 lfphKTVLENITI--------APIKVKGIEKKAAVEkalDLLEKVGLKDKAQSFP-NQLSGGQKQRVAIARALAMDPKVL 160
Cdd:PRK10762 345 ----MSVKENMSLtalryfsrAGGSLKHADEQQAVS---DFIRLFNIKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 161 LFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEE 219
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGE 476
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-198 |
3.08e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 68.66 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 25 VIEEKEVVCVIGPSGSGKSTFLRclnkledITAGEVvvhghtitdpKVNINKVRQEVG--MVFQHFN---LFPH--KTVL 97
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALK-------ILSGEL----------KPNLGDYDEEPSwdEVLKRFRgteLQDYfkKLAN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 98 ENITIApIKVKGIEK--KAAVEKALDLLEKVGLKDKAQSFP-------------NQLSGGQKQRVAIARALAMDPKVLLF 162
Cdd:COG1245 158 GEIKVA-HKPQYVDLipKVFKGTVRELLEKVDERGKLDELAeklglenildrdiSELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*....
gi 637158246 163 DEPTSALDpevVGDVLAV---MKQLAVEGMTMIVVTHEM 198
Cdd:COG1245 237 DEPSSYLD---IYQRLNVarlIRELAEEGKYVLVVEHDL 272
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
9-172 |
5.15e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.03 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 9 LKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpkvniNKVRQEVGMVFQHF 88
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT------RGDRSRFMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 89 -NLFPHKTVLENITIapikVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARaLAMDPKVL-LFDEPT 166
Cdd:PRK13543 91 pGLKADLSTLENLHF----LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPY 165
|
....*.
gi 637158246 167 SALDPE 172
Cdd:PRK13543 166 ANLDLE 171
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-228 |
7.82e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.46 E-value: 7.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 18 VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQEVGMVFQHFNLFPhKTVL 97
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS--KFGLMDLRKVLGIIPQAPVLFS-GTVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 98 ENITiaPIKvkgiEKKAAvekalDL---LEKVGLKDKAQSFPNQL-----------SGGQKQRVAIARALAMDPKVLLFD 163
Cdd:PLN03130 1331 FNLD--PFN----EHNDA-----DLwesLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 637158246 164 EPTSALDpeVVGDVLaVMKQLAVE--GMTMIVVTHEMGFAREVgDRVIFMDGGYIVEEDKPEALFGN 228
Cdd:PLN03130 1400 EATAAVD--VRTDAL-IQKTIREEfkSCTMLIIAHRLNTIIDC-DRILVLDAGRVVEFDTPENLLSN 1462
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-216 |
1.03e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 17 EVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCL-----NKLEditaGEVVVHGHtitdpKVNINK----VRQEVGMVFQ- 86
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfgaypGRWE----GEIFIDGK-----PVKIRNpqqaIAQGIAMVPEd 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 87 --HFNLFPHKTVLENITIAPI----KVKGIEKKAAVEKALDLLEKvgLKDKAQSfPNQ----LSGGQKQRVAIARALAMD 156
Cdd:PRK13549 347 rkRDGIVPVMGVGKNITLAALdrftGGSRIDDAAELKTILESIQR--LKVKTAS-PELaiarLSGGNQQKAVLAKCLLLN 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637158246 157 PKVLLFDEPTSALDpevVG---DVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYI 216
Cdd:PRK13549 424 PKILILDEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-198 |
1.50e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 65.08 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 25 VIEEKEVVCVIGPSGSGKSTFLRclnkledITAGEVVVHGHTITDPkvninkvrQEVGMVFQHF------NLFphKTVLE 98
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALK-------ILAGKLKPNLGKFDDP--------PDWDEILDEFrgselqNYF--TKLLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 99 ----------NITIAPIKVKG-----IEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFD 163
Cdd:cd03236 85 gdvkvivkpqYVDLIPKAVKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190
....*....|....*....|....*....|....*
gi 637158246 164 EPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEM 198
Cdd:cd03236 165 EPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-196 |
2.03e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 64.81 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLED--ITAGEVVVHGHTIT--DPKvniNKVR 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLelSPE---DRAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 79 QEVGMVFQHFNLFP---HKTVLENITIAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQ-----LSGGQKQRVAIA 150
Cdd:PRK09580 78 EGIFMAFQYPVEIPgvsNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRsvnvgFSGGEKKRNDIL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 637158246 151 RALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTH 196
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-213 |
2.92e-12 |
|
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: 65.58 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 8 NLKKSFGDHEVlkDINA-VIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVvvhghtitDPKVNINKVRQEVGMVFq 86
Cdd:COG1245 346 DLTKSYGGFSL--EVEGgEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------DEDLKISYKPQYISPDY- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 87 hfnlfpHKTVLENItiapikvkgiekKAAVEKALD-------LLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKV 159
Cdd:COG1245 415 ------DGTVEEFL------------RSANTDDFGssyykteIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADL 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 160 LLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVIFMDG 213
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-230 |
2.96e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.96 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 18 VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQEVGMVFQHFNLFpHKTVL 97
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG--AYGLRELRRQFSMIPQDPVLF-DGTVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 98 ENITiaPIkvkgIEKKAA-VEKALDLL---EKV-----GLKDKAQSFPNQLSGGQKQRVAIARA-LAMDPKVLLFDEPTS 167
Cdd:PTZ00243 1402 QNVD--PF----LEASSAeVWAALELVglrERVaseseGIDSRVLEGGSNYSVGQRQLMCMARAlLKKGSGFILMDEATA 1475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 637158246 168 ALDPEVVGDVLA-VMKqlAVEGMTMIVVTHEMGFAREVgDRVIFMDGGYIVEEDKPEALFGNPQ 230
Cdd:PTZ00243 1476 NIDPALDRQIQAtVMS--AFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-198 |
3.91e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.21 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 25 VIEEKEVVCVIGPSGSGKSTFLRclnkledITAGEVVvhghtitdPkvNINKVRQEVGM--VFQHF------NLFphKTV 96
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVK-------ILSGELI--------P--NLGDYEEEPSWdeVLKRFrgtelqNYF--KKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 97 LEN----------ITIAPIKVKG----IEKKAAVEKALD-LLEKVGLK---DKAQSfpnQLSGGQKQRVAIARALAMDPK 158
Cdd:PRK13409 156 YNGeikvvhkpqyVDLIPKVFKGkvreLLKKVDERGKLDeVVERLGLEnilDRDIS---ELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 637158246 159 VLLFDEPTSALDpevVGDVLAV---MKQLAvEGMTMIVVTHEM 198
Cdd:PRK13409 233 FYFFDEPTSYLD---IRQRLNVarlIRELA-EGKYVLVVEHDL 271
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-237 |
4.35e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 4.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKleDITAGeVVVHGHTIT-------DPKVNIN 75
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGG-GAPRGARVTgdvtlngEPLAAID 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 76 KVR-----------QEVGMVFQHFNL-----FPHktvlenitiapIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQL 139
Cdd:PRK13547 78 APRlarlravlpqaAQPAFAFSAREIvllgrYPH-----------ARRAGALTHRDGEIAWQALALAGATALVGRDVTTL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 140 SGGQKQRVAIARALAM---------DPKVLLFDEPTSALDPEVVGDVLAVMKQLAVE-GMTMIVVTHEMGFAREVGDRVI 209
Cdd:PRK13547 147 SGGELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIA 226
|
250 260
....*....|....*....|....*....
gi 637158246 210 FMDGGYIVEEDKPEALFgNPQH-ERTKSF 237
Cdd:PRK13547 227 MLADGAIVAHGAPADVL-TPAHiARCYGF 254
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-217 |
5.25e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.91 E-value: 5.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLnkLEDITAGEVVV--------------HGH---- 65
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL--VGELEPDSGTVkwsenanigyyaqdHAYdfen 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 66 --TITD-------PKVNINKVRQEVG-MVFQHfnlfphktvlenitiapikvKGIEKKAAVekaldllekvglkdkaqsf 135
Cdd:PRK15064 398 dlTLFDwmsqwrqEGDDEQAVRGTLGrLLFSQ--------------------DDIKKSVKV------------------- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 136 pnqLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVgDVLavmkQLAVEGM--TMIVVTHEMGFAREVGDRVIFMDG 213
Cdd:PRK15064 439 ---LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESI-ESL----NMALEKYegTLIFVSHDREFVSSLATRIIEITP 510
|
....
gi 637158246 214 GYIV 217
Cdd:PRK15064 511 DGVV 514
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
110-225 |
5.29e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 64.37 E-value: 5.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 110 IEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGM 189
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
90 100 110
....*....|....*....|....*....|....*.
gi 637158246 190 TMIVVTHEMGFAREVGDRVIFMDGGYIVEEDKPEAL 225
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-214 |
7.42e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 64.65 E-value: 7.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 30 EVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpkVNINKVRQEVGMVFQHFNLFPHKTVLENITIAPiKVKG 109
Cdd:TIGR01257 1966 ECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---TNISDVHQNMGYCPQFDAIDDLLTGREHLYLYA-RLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 110 IEKKAaVEKALDL-LEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEG 188
Cdd:TIGR01257 2042 VPAEE-IEKVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREG 2120
|
170 180
....*....|....*....|....*.
gi 637158246 189 MTMIVVTHEMGFAREVGDRVIFMDGG 214
Cdd:TIGR01257 2121 RAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-180 |
8.84e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 8.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 5 TVKNLKKSFG-DHEVLKDIN------AVIEekevvcVIGPSGSGKSTFLRCLNKLEDITAGEVVVH-GHTitdpkvnink 76
Cdd:PRK11819 8 TMNRVSKVVPpKKQILKDISlsffpgAKIG------VLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIK---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 77 vrqeVGMVFQHFNLFPHKTVLENITIAPIKVKGI--------EKKAAVEKALD-LLEKVG-LKDKAQSF----------- 135
Cdd:PRK11819 72 ----VGYLPQEPQLDPEKTVRENVEEGVAEVKAAldrfneiyAAYAEPDADFDaLAAEQGeLQEIIDAAdawdldsqlei 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 136 -------P------NQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVV-----------GDVLAV 180
Cdd:PRK11819 148 amdalrcPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVawleqflhdypGTVVAV 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-236 |
1.21e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.99 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITDPKVninkvRQEVG- 82
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARH-----RRAVCp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 ----MVfQHF--NLFPHKTVLENI---------TIApikvkgiEKKAAVEkalDLLEKVGLkdkaQSFPN----QLSGGQ 143
Cdd:NF033858 77 riayMP-QGLgkNLYPTLSVFENLdffgrlfgqDAA-------ERRRRID---ELLRATGL----APFADrpagKLSGGM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 144 KQRVAIARALAMDPKVLLFDEPTSALDP-------EVVGDVLAVMkqlavEGMTMIVVTHEMGFArEVGDRVIFMDGGYI 216
Cdd:NF033858 142 KQKLGLCCALIHDPDLLILDEPTTGVDPlsrrqfwELIDRIRAER-----PGMSVLVATAYMEEA-ERFDWLVAMDAGRV 215
|
250 260
....*....|....*....|
gi 637158246 217 VEEDKPEALfgnpqHERTKS 236
Cdd:NF033858 216 LATGTPAEL-----LARTGA 230
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-214 |
1.24e-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: 61.96 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 19 LKDINAVIEEKEVVCVIGPSGSGKSTFLRC-LNKLEDITaGEVVVHGHTITDPKVNINKVRQE--VGMVFQHFNLFpHKT 95
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAiLGEMQTLE-GKVHWSNKNESEPSFEATRSRNRysVAYAAQKPWLL-NAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 96 VLENITI-API---KVKGIEKKAAVEKALDLLeKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDP 171
Cdd:cd03290 95 VEENITFgSPFnkqRYKAVTDACSLQPDIDLL-PFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 637158246 172 EVVGDVL--AVMKQLAVEGMTMIVVTHEMGFAREvGDRVIFMDGG 214
Cdd:cd03290 174 HLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
18-196 |
1.56e-11 |
|
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: 63.61 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 18 VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVhghtitDPKVNINKVRQEvgmvfqhfnlfPHKTV- 96
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK------PAKGKLFYVPQR-----------PYMTLg 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 97 -LENITIAPIKVKGIEKKAAVEKAL----------DLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEP 165
Cdd:TIGR00954 530 tLRDQIIYPDSSEDMKRRGLSDKDLeqildnvqltHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|..
gi 637158246 166 TSALDPEVVGdvlaVMKQLAVE-GMTMIVVTH 196
Cdd:TIGR00954 610 TSAVSVDVEG----YMYRLCREfGITLFSVSH 637
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
4-213 |
8.48e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 59.12 E-value: 8.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDInAVIEEKEVVCVIGPSGSGKSTFLRCLnkleditAGEVVVHGHTITDPKVNInkvrqevgm 83
Cdd:cd03222 1 QLYPDCVKRYGVFFLLVEL-GVVKEGEVIGIVGPNGTGKTTAVKIL-------AGQLIPNGDNDEWDGITP--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 84 vfqhfnlfphktvleniTIAPIKVKgiekkaavekaldllekvglkdkaqsfpnqLSGGQKQRVAIARALAMDPKVLLFD 163
Cdd:cd03222 64 -----------------VYKPQYID------------------------------LSGGELQRVAIAAALLRNATFYLFD 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 637158246 164 EPTSALDPEVVGDVLAVMKQLAVEGM-TMIVVTHEMGFAREVGDRVIFMDG 213
Cdd:cd03222 97 EPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
28-196 |
1.26e-10 |
|
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: 58.14 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 28 EKEVVCVIGPSGSGKSTFLRCLnkleditagEVVVHGHTITDPKVNINKVRQEVGMVFQHFNLFPHktvlenitiapikv 107
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAI---------GLALGGAQSATRRRSGVKAGCIVAAVSAELIFTRL-------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 108 kgiekkaavekaldllekvglkdkaqsfpnQLSGGQKQRVAIARALA---MDPKVL-LFDEPTSALDPEVVGDVLAVMKQ 183
Cdd:cd03227 77 ------------------------------QLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAEAILE 126
|
170
....*....|...
gi 637158246 184 LAVEGMTMIVVTH 196
Cdd:cd03227 127 HLVKGAQVIVITH 139
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-198 |
1.34e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.95 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 17 EVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVhghtitdpKVNINKVRQEVGMVfqhfnlfpHKTV 96
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA--------ERSIAYVPQQAWIM--------NATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 97 LENITI----APIKVKGIEKKAAVEKALDLLEKvGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPE 172
Cdd:PTZ00243 738 RGNILFfdeeDAARLADAVRVSQLEADLAQLGG-GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180
....*....|....*....|....*.
gi 637158246 173 VVGDVLAVMKQLAVEGMTMIVVTHEM 198
Cdd:PTZ00243 817 VGERVVEECFLGALAGKTRVLATHQV 842
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-219 |
3.15e-10 |
|
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: 57.33 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 19 LKDINAVIEEKEVVCVIGPSGSGKSTFLRclnklediTAGEVVVHGHTITDPKVNinkvrqevgmvfqhfnlFPHKTVle 98
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--------EGLYASGKARLISFLPKF-----------------SRNKLI-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 99 nitiapikvkgiekkaaVEKALDLLEKVGL-----KDKAQSfpnqLSGGQKQRVAIARALAMDPK--VLLFDEPTSALDP 171
Cdd:cd03238 64 -----------------FIDQLQFLIDVGLgyltlGQKLST----LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQ 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 637158246 172 EVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREvGDRVIFM------DGGYIVEE 219
Cdd:cd03238 123 QDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFgpgsgkSGGKVVFS 175
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-197 |
5.99e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.09 E-value: 5.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 17 EVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCL--NKLEDITAGEVVVHGHtitdPKvninkvRQEV-----GMVFQHFN 89
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGF----PK------KQETfarisGYCEQNDI 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 90 LFPHKTVLENITIA-----PIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFP--NQLSGGQKQRVAIARALAMDPKVLLF 162
Cdd:PLN03140 964 HSPQVTVRESLIYSaflrlPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190
....*....|....*....|....*....|....*
gi 637158246 163 DEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHE 197
Cdd:PLN03140 1044 DEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
19-222 |
6.36e-10 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 57.62 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 19 LKDINAVIEEKEVVCVIGPSGSGKSTF--------LRCLNKLEDITAGEV-VVHGHTITDPKVNIN-------------- 75
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLindtlypaLARRLHLKKEQPGNHdRIEGLEHIDKVIVIDqspigrtprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 76 --KVRQEVGMVF------QHFN------LFPHKTVLE--NITIAPiKVKGIEKKAAVEKALDLLEKVGLK--DKAQSFPN 137
Cdd:cd03271 91 ytGVFDEIRELFcevckgKRYNretlevRYKGKSIADvlDMTVEE-ALEFFENIPKIARKLQTLCDVGLGyiKLGQPATT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 138 qLSGGQKQRVAIARALAM---DPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAReVGDRVIFM--- 211
Cdd:cd03271 170 -LSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK-CADWIIDLgpe 247
|
250
....*....|....
gi 637158246 212 ---DGGYIVEEDKP 222
Cdd:cd03271 248 ggdGGGQVVASGTP 261
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-224 |
8.93e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.26 E-value: 8.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 15 DHEVLKDINAVIEEKEVVCVIGPSGSGK-----STFLRCLNKleDITaGEVVVHGHtitdpKVNINKVRQEV--GMVF-- 85
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRtelamSVFGRSYGR--NIS-GTVFKDGK-----EVDVSTVSDAIdaGLAYvt 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 86 ---QHFNLFPHKTVLENITIApiKVKGI----------EKKAAVE-------KALDLLEKVGlkdkaqsfpnQLSGGQKQ 145
Cdd:NF040905 344 edrKGYGLNLIDDIKRNITLA--NLGKVsrrgvideneEIKVAEEyrkkmniKTPSVFQKVG----------NLSGGNQQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 146 RVAIARALAMDPKVLLFDEPTSALDpevVG---DVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVEE-DK 221
Cdd:NF040905 412 KVVLSKWLFTDPDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGElPR 488
|
...
gi 637158246 222 PEA 224
Cdd:NF040905 489 EEA 491
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-212 |
1.47e-09 |
|
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: 55.07 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 29 KEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVhghtitdpkVNINKVRQEVGMVFQHFNLFPHKTvlenitiapikvk 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------IDGEDILEEVLDQLLLIIVGGKKA------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 109 giekkaavekaldllekvglkdkaqsfpnQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLA------VMK 182
Cdd:smart00382 60 -----------------------------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLLL 110
|
170 180 190
....*....|....*....|....*....|....*
gi 637158246 183 QLAVEGMTMIVVTHEMGF-----AREVGDRVIFMD 212
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDlgpalLRRRFDRRIVLL 145
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-194 |
1.25e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 1 MSMITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTITdpKVNINKVRQE 80
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHIT--RLSFEQLQKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQHFN---LFPH-----KTVLENITiapikvKGIEKKAAVEKaldLLEKVGLKDKAQSFPNQLSGGQKQRVAIARA 152
Cdd:PRK10938 79 VSDEWQRNNtdmLSPGeddtgRTTAEIIQ------DEVKDPARCEQ---LAQQFGITALLDRRFKYLSTGETRKTLLCQA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 637158246 153 LAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVV 194
Cdd:PRK10938 150 LMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-204 |
2.77e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVhghtitDPKVNINKVRQE-- 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL------DPNERLGKLRQDqf 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 -------VGMVFQ-HFNLFPHKTVLENITIAP-------IKVKGIEKK-------AAVEKALDLLEKVGLKDKAQSFP-N 137
Cdd:PRK15064 75 afeeftvLDTVIMgHTELWEVKQERDRIYALPemseedgMKVADLEVKfaemdgyTAEARAGELLLGVGIPEEQHYGLmS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 138 QLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVV---GDVLAVMKQlavegmTMIVVTHEMGFAREV 204
Cdd:PRK15064 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIrwlEDVLNERNS------TMIIISHDRHFLNSV 218
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-217 |
6.27e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.94 E-value: 6.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLR--CLNKLEDITAGEVVVH------GHTIT------D 69
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymAMHAIDGIPKNCQILHveqevvGDDTTalqcvlN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 70 PKVNINKVRQEVGMVFQHFNLFPHKTVLENITIAPIKvkGIEKKAAVE------KALDLLEKVGLKDKAQSF-------- 135
Cdd:PLN03073 258 TDIERTQLLEEEAQLVAQQRELEFETETGKGKGANKD--GVDKDAVSQrleeiyKRLELIDAYTAEARAASIlaglsftp 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 136 ------PNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDpevVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVI 209
Cdd:PLN03073 336 emqvkaTKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDIL 412
|
....*...
gi 637158246 210 FMDGGYIV 217
Cdd:PLN03073 413 HLHGQKLV 420
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
111-225 |
6.30e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 52.71 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 111 EKKAAVEKALDLLEKVGLK--DKAQSFPNqLSGGQKQRVAIARAL---AMDPKVLLFDEPTSALDPEVVGDVLAVMKQLA 185
Cdd:TIGR00630 801 EAVPSISRKLQTLCDVGLGyiRLGQPATT-LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLV 879
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 637158246 186 VEGMTMIVVTHEMGFAReVGDRVIFM------DGGYIVEEDKPEAL 225
Cdd:TIGR00630 880 DKGNTVVVIEHNLDVIK-TADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-196 |
9.40e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 50.78 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKkSFGDHEVLkDInavieEKEVVCVIGPSGSGKSTFLRClnkledITA---GEVVVhGHTITDPKVNINKVRQE 80
Cdd:COG0419 5 LRLENFR-SYRDTETI-DF-----DDGLNLIVGPNGAGKSTILEA------IRYalyGKARS-RSKLRSDLINVGSEEAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 81 VGMVFQH-------------FNLFPH------KTVLENI----TIAPIKVKGIEKKAAVEKALDLLEKVgLKDKAQSF-- 135
Cdd:COG0419 71 VELEFEHggkryrierrqgeFAEFLEakpserKEALKRLlgleIYEELKERLKELEEALESALEELAEL-QKLKQEILaq 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 637158246 136 ------PNQLSGGQKQRVAIARALAmdpkvLLFDepTSALDPEVVGDVLAVMKQLAvegmtmiVVTH 196
Cdd:COG0419 150 lsgldpIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
139-214 |
1.11e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 1.11e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 139 LSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGG 214
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-172 |
1.20e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 6 VKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLnkLEDITAGEVVVHGHTitdpkvninkvRQEVGMVF 85
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM--LGQLQADSGRIHCGT-----------KLEVAYFD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 86 QH-FNLFPHKTVLENITIAP--IKVKGIEKkaaveKALDLLEKVGLKDKAQSFP-NQLSGGQKQRVAIARALAMDPKVLL 161
Cdd:PRK11147 389 QHrAELDPEKTVMDNLAEGKqeVMVNGRPR-----HVLGYLQDFLFHPKRAMTPvKALSGGERNRLLLARLFLKPSNLLI 463
|
170
....*....|.
gi 637158246 162 FDEPTSALDPE 172
Cdd:PRK11147 464 LDEPTNDLDVE 474
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
23-197 |
1.46e-07 |
|
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: 50.30 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 23 NAVIE-EKEVVCVIGPSGSGKSTFLRCLNkleditageVVVHGHTIT-------DPKV-NINKVRQEVGMVFQHFNlfph 93
Cdd:cd03240 15 RSEIEfFSPLTLIVGQNGAGKTTIIEALK---------YALTGELPPnskggahDPKLiREGEVRAQVKLAFENAN---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 94 ktvlenitiapikvkgiEKKAAVEKALDLLEKVGLKDKAQSF------PNQLSGGQKQ------RVAIARALAMDPKVLL 161
Cdd:cd03240 82 -----------------GKKYTITRSLAILENVIFCHQGESNwplldmRGRCSGGEKVlasliiRLALAETFGSNCGILA 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 637158246 162 FDEPTSALDPEVVGDVLA--VMKQLAVEGMTMIVVTHE 197
Cdd:cd03240 145 LDEPTTNLDEENIEESLAeiIEERKSQKNFQLIVITHD 182
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-214 |
3.60e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.68 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 18 VLKDINAVIEEKEVVCVIGPSGSGKSTFLRC-LNKLEDiTAGEVVVHGHTITDPKVNInkvrqevgmvfqhfnLFPhKTV 96
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMiMGELEP-SEGKIKHSGRISFSPQTSW---------------IMP-GTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 97 LENITIapikvkGIE----KKAAVEKALDLLEKVGLkdkaqsFPNQ-----------LSGGQKQRVAIARALAMDPKVLL 161
Cdd:TIGR01271 504 KDNIIF------GLSydeyRYTSVIKACQLEEDIAL------FPEKdktvlgeggitLSGGQRARISLARAVYKDADLYL 571
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 637158246 162 FDEPTSALDPEVVGDVL--AVMKQLAVEgmTMIVVTHEMGFAREvGDRVIFMDGG 214
Cdd:TIGR01271 572 LDSPFTHLDVVTEKEIFesCLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-197 |
3.62e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.18 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTItdpKVNINKVRQEVG 82
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI---KKDLCTYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 83 MVFQHFNLFPHKTVLEN------ITIAPIKVKGIEKKAAVEKALDllekvglkdkaqsFP-NQLSGGQKQRVAIARALAM 155
Cdd:PRK13540 78 FVGHRSGINPYLTLRENclydihFSPGAVGITELCRLFSLEHLID-------------YPcGLLSSGQKRQVALLRLWMS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 637158246 156 DPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHE 197
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-196 |
3.71e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCL---------NKLedITAGEVVVHGHTITDPKVNI 74
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysNDL--TLFGRRRGSGETIWDIKKHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 75 NKVRQEVgmvfqHFNLFPHKTVLENITIAPIKVKGIEKkaAV-----EKALDLLEKVGLKDKAQSFPNQ-LSGGQKQRVA 148
Cdd:PRK10938 339 GYVSSSL-----HLDYRVSTSVRNVILSGFFDSIGIYQ--AVsdrqqKLAQQWLDILGIDKRTADAPFHsLSWGQQRLAL 411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 637158246 149 IARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMT-MIVVTH 196
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSH 460
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-214 |
4.59e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 49.47 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 18 VLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLnkleditAGEVVvhghtitdPKVNINKVRQEVGMVFQHFNLFPhKTVL 97
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLI-------LGELE--------PSEGKIKHSGRISFSSQFSWIMP-GTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 98 ENItIAPIKVKGIEKKAAVeKALDLLEKVglkdkaQSFPNQ-----------LSGGQKQRVAIARALAMDPKVLLFDEPT 166
Cdd:cd03291 116 ENI-IFGVSYDEYRYKSVV-KACQLEEDI------TKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 637158246 167 SALDPEVVGDVL--AVMKQLAveGMTMIVVTHEMGFAREvGDRVIFMDGG 214
Cdd:cd03291 188 GYLDVFTEKEIFesCVCKLMA--NKTRILVTSKMEHLKK-ADKILILHEG 234
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-217 |
1.26e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.64 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 19 LKDINAVIEEKEVVCVIGPSGSGKSTF----------LRCLNKLEDITAGEVvvhgHTITDPKV-NINKVRQEVGMVFQH 87
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSAYARQFL----GQMDKPDVdSIEGLSPAIAIDQKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 88 FNLFPHKTVLeniTIAPI--KVKGIEKKAAVEKALDLLEKVGLK----DKAQsfpNQLSGGQKQRVAIARALAMDPKVLL 161
Cdd:cd03270 87 TSRNPRSTVG---TVTEIydYLRLLFARVGIRERLGFLVDVGLGyltlSRSA---PTLSGGEAQRIRLATQIGSGLTGVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 637158246 162 --FDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREvGDRVIFM------DGGYIV 217
Cdd:cd03270 161 yvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVIDIgpgagvHGGEIV 223
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
3-172 |
3.22e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.40 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFgDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHghtitdpKVNINKVRQE-V 81
Cdd:PRK13541 1 MLSLHQLQFNI-EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYK-------NCNINNIAKPyC 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQHFNLFPHKTVLENITI-APIKVKGIEKKAAVE--KALDLLEKvglkdKAQSfpnqLSGGQKQRVAIARALAMDPK 158
Cdd:PRK13541 73 TYIGHNLGLKLEMTVFENLKFwSEIYNSAETLYAAIHyfKLHDLLDE-----KCYS----LSSGMQKIVAIARLIACQSD 143
|
170
....*....|....
gi 637158246 159 VLLFDEPTSALDPE 172
Cdd:PRK13541 144 LWLLDEVETNLSKE 157
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
4-212 |
3.90e-06 |
|
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: 46.92 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKkSFGDHEVlkDINavieeKEVVCVIGPSGSGKSTFLRCLNKL-----------------EDITAGEVVV---- 62
Cdd:COG3593 6 IKIKNFR-SIKDLSI--ELS-----DDLTVLVGENNSGKSSILEALRLLlgpsssrkfdeedfylgDDPDLPEIEIeltf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 63 ------------HGHTITDPKVNINKVRQEVGMVFQHFNlfphkTVLENITIAPIKVKGIEKKAAVEKALDLLEKVGLK- 129
Cdd:COG3593 78 gsllsrllrlllKEEDKEELEEALEELNEELKEALKALN-----ELLSEYLKELLDGLDLELELSLDELEDLLKSLSLRi 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 130 DKAQSFP-NQLSGGQKQRVAIARALAM-------DPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFA 201
Cdd:COG3593 153 EDGKELPlDRLGSGFQRLILLALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLL 232
|
250
....*....|..
gi 637158246 202 REVG-DRVIFMD 212
Cdd:COG3593 233 SEVPlENIRRLR 244
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
33-200 |
4.75e-06 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 46.41 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 33 CVIGPSGSGKSTF--------------LRcLNKLEDItagevvVHGHTITDPKVNinkvRQEVGMVFQHFNLfPHKTVLE 98
Cdd:cd03275 26 CIIGPNGSGKSNLmdaisfvlgeksshLR-SKNLKDL------IYRARVGKPDSN----SAYVTAVYEDDDG-EEKTFRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 99 NITIAPIKVKGIEKKAAVEKALDLLEKVGLKDKAQSF---------------PN-------QLSGGQKqrvAIArALAmd 156
Cdd:cd03275 94 IITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFlvfqgdvesiasknpPGkrfrdmdNLSGGEK---TMA-ALA-- 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 637158246 157 pkvLLF-------------DEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGF 200
Cdd:cd03275 168 ---LLFaihsyqpapffvlDEVDAALDNTNVGKVASYIREQAGPNFQFIVISLKEEF 221
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
115-242 |
9.78e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.17 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 115 AVEKALDLLEKVGLkd--kaQSFPnQLSGGQKQRVAIARALAM---DPKVLLFDEPTSALDPEvvgDV---LAVMKQLAV 186
Cdd:COG0178 802 KIARKLQTLQDVGLgyiklgQPAT-TLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFH---DIrklLEVLHRLVD 877
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 187 EGMTMIVVTHEMgfarEV---GDRVIFM------DGGYIVEEDKPEALFGNPQ-HerTKSFLSKVL 242
Cdd:COG0178 878 KGNTVVVIEHNL----DViktADWIIDLgpeggdGGGEIVAEGTPEEVAKVKAsY--TGRYLKEYL 937
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-218 |
1.02e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.04 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 16 HEVLKDINAVIEEKEVVCVIGPSGSGKSTflrclnkLEDITAGevvvhghtITDPKVNINKVRQEVGMVFQHFNLFPHKT 95
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKST-------LSNLIAG--------VTMPNKGTVDIKGSAALIAISSGLNGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 96 VLENitiapIKVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQ----LSGGQKQRVAIARALAMDPKVLLFDEPTSALDP 171
Cdd:PRK13545 102 GIEN-----IELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQpvktYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 637158246 172 EVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVE 218
Cdd:PRK13545 177 TFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKE 223
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-225 |
1.59e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.59 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 139 LSGGQKQRVAIARAL---AMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAReVGDRVIFMD--- 212
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYVLELGpeg 888
|
90
....*....|....*.
gi 637158246 213 ---GGYIVEEDKPEAL 225
Cdd:PRK00635 889 gnlGGYLLASCSPEEL 904
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-228 |
4.30e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 13 FGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLnkleditAGEVVVHGHTITDPKvNInkvrqEVGMVFQH---Fn 89
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL-------AGELAPVSGEIGLAK-GI-----KLGYFAQHqleF- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 90 LFPHKTVLENIT-IAPikvkgiekKAAVEKALDLLEKVGLK-DKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTS 167
Cdd:PRK10636 388 LRADESPLQHLArLAP--------QELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637158246 168 ALDPEvvgdvlavMKQLAVEGM-----TMIVVTHEMGFAREVGDRVifmdggYIVEEDKPEALFGN 228
Cdd:PRK10636 460 HLDLD--------MRQALTEALidfegALVVVSHDRHLLRSTTDDL------YLVHDGKVEPFDGD 511
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-218 |
5.83e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.27 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 19 LKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNKLEDITAGEVVVHGhtitdpkvninkvrqEVGMVFQHFNLFPHKTVLE 98
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG---------------EVSVIAISAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 99 NITIAPIkVKGIEKKAAVEKALDLLEKVGLKDKAQSFPNQLSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGDVL 178
Cdd:PRK13546 105 NIEFKML-CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 637158246 179 AVMKQLAVEGMTMIVVTHEMGFAREVGDRVIFMDGGYIVE 218
Cdd:PRK13546 184 DKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-230 |
5.97e-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: 43.85 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 137 NQLSGGQKQRVAIARALAMDPKVLLF--DEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHEMGFAREvGDRVIFM--- 211
Cdd:TIGR00630 487 GTLSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRA-ADYVIDIgpg 565
|
90 100
....*....|....*....|..
gi 637158246 212 ---DGGYIVEEDKPEALFGNPQ 230
Cdd:TIGR00630 566 ageHGGEVVASGTPEEILANPD 587
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-238 |
7.61e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 137 NQLSGGQKQRVAIARALAMDPK--VLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTHE---MGFArevgDRVIFM 211
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLA----DRIIDI 550
|
90 100 110
....*....|....*....|....*....|...
gi 637158246 212 D------GGYIVEEDKPEAlFGNPQHERTKSFL 238
Cdd:PRK00635 551 GpgagifGGEVLFNGSPRE-FLAKSDSLTAKYL 582
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
139-197 |
1.06e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 1.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 139 LSGGQKQRVAIARALAMDPKVLLFDEPTSALDPEVVGdvlAVMKQLAVEGMTMIVVTHE 197
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVE---ALIQGLVLFQGGVLMVSHD 683
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-209 |
1.38e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 3 MITVKNLKKSFGDHEVLKDINAVIEEKEVVCVIGPSGSGKSTFLRCLNkleditaGEVVVHGHTITDPKV-NINKVRQEV 81
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLK-------NEISADGGSYTFPGNwQLAWVNQET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 82 GMVFQ-----------HFNLFPHKTVLENI-----TIAPI--KVKGIEKKAAVEKALDLLEKVGLKDKAQSFP-NQLSGG 142
Cdd:PRK10636 74 PALPQpaleyvidgdrEYRQLEAQLHDANErndghAIATIhgKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 637158246 143 QKQRVAIARALAMDPKVLLFDEPTSALDPEVvgdVLAVMKQLAVEGMTMIVVTHEMGFAREVGDRVI 209
Cdd:PRK10636 154 WRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQGTLILISHDRDFLDPIVDKII 217
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
4-60 |
1.75e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.84 E-value: 1.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 637158246 4 ITVKNLKkSFGDHEV-LKDINavieekevvCVIGPSGSGKSTFLRCLNKLEDITAGEV 60
Cdd:COG4637 5 IRIKNFK-SLRDLELpLGPLT---------VLIGANGSGKSNLLDALRFLSDAARGGL 52
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
129-185 |
1.82e-04 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 41.48 E-value: 1.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637158246 129 KDKAQSFPNQLSGGQKQRVAIARALAM---DPK-VLLFDEPTSALDPEVVGDVLAVMKQLA 185
Cdd:cd03272 149 KQDEQQEMQQLSGGQKSLVALALIFAIqkcDPApFYLFDEIDAALDAQYRTAVANMIKELS 209
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
120-220 |
2.19e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 120 LDLLEKVGLK----DKAQsfpNQLSGGQKQRVAIARALA--MDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIv 193
Cdd:PRK00635 1368 LTFIDKVGLSyitlGQEQ---DTLSDGEHYRLHLAKKISsnLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVI- 1443
|
90 100 110
....*....|....*....|....*....|...
gi 637158246 194 VTHEMGFAREVGDRVIFM------DGGYIVEED 220
Cdd:PRK00635 1444 ATDRSGSLAEHADHLIHLgpgsgpQGGYLLSTS 1476
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
120-242 |
3.04e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 120 LDLLEKVGL---KdKAQSFPnQLSGGQKQRVAIARALAMDP--KVL-LFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIV 193
Cdd:PRK00349 811 LQTLVDVGLgyiK-LGQPAT-TLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVV 888
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637158246 194 VTH------------EMGfaREVGDRvifmdGGYIVEEDKPEALFGNPQ-HerTKSFLSKVL 242
Cdd:PRK00349 889 IEHnldviktadwiiDLG--PEGGDG-----GGEIVATGTPEEVAKVEAsY--TGRYLKPVL 941
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
32-71 |
4.23e-04 |
|
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442728 [Multi-domain] Cd Length: 402 Bit Score: 40.74 E-value: 4.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 637158246 32 VCVIGPSGSGKSTFLrCLNKLEDITAGEVVVhghtITDPK 71
Cdd:COG3505 2 VLVIGPTGSGKTVGL-VIPNLTQLARGESVV----VTDPK 36
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
4-196 |
5.61e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.37 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 4 ITVKNLKkSFGDHEVlkDINaviEEKEVVCVIGPSGSGKSTFLRCL--------NKLEDITAGEVVVHGHTITD------ 69
Cdd:COG3950 6 LTIENFR-GFEDLEI--DFD---NPPRLTVLVGENGSGKTTLLEAIalalsgllSRLDDVKFRKLLIRNGEFGDsaklil 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 70 -----------PKVNINKVRQEVGMVFQHF-NLFPHKTVLENI------TIAPIKVKGIEK--------KAAVEKALDLL 123
Cdd:COG3950 80 yygtsrllldgPLKKLERLKEEYFSRLDGYdSLLDEDSNLREFlewlreYLEDLENKLSDEldekleavREALNKLLPDF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158246 124 EKVGLKDKAQSF-----------PNQLSGGQKQRVAIARALAMD--------------PKVLLFDEPTSALDP----EVV 174
Cdd:COG3950 160 KDIRIDRDPGRLvildkngeelpLNQLSDGERSLLALVGDLARRlaelnpalenplegEGIVLIDEIDLHLHPkwqrRIL 239
|
250 260
....*....|....*....|..
gi 637158246 175 GDVLAVMKQlavegMTMIVVTH 196
Cdd:COG3950 240 PDLRKIFPN-----IQFIVTTH 256
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
136-196 |
1.55e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.91 E-value: 1.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 637158246 136 PNQLSGGQKQ---RVAIARALAMDPKVLLFDEPTSALDPEVVGDVLAVMKQLAVEGMTMIVVTH 196
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| CDC_Septin |
cd01850 |
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ... |
34-90 |
1.77e-03 |
|
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.
Pssm-ID: 206649 Cd Length: 275 Bit Score: 38.68 E-value: 1.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 637158246 34 VIGPSGSGKSTFLRCLNKLEDITAGEVVVHGHTIT-DPKVNINKVRQEVGMVFQHFNL 90
Cdd:cd01850 9 VVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITkTVEIKISKAELEENGVKLKLTV 66
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
138-183 |
2.18e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.44 E-value: 2.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 138 QLSGGQKQR---VAIARALAM----------DPKVLLFDEPTSALDPEVVGDVLAVMKQ 183
Cdd:pfam13558 32 GLSGGEKQLlayLPLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
136-197 |
2.98e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.48 E-value: 2.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 136 PNQLSGGQKQ------RVAIARALA--------MDPkvLLFDEPTSALDPEVVG---DVLAVMKQLAVEgmTMIVVTHE 197
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAegiegdapLPP--LILDEPTVFLDSGHVSqlvDLVESMRRLGVE--QIVVVSHD 853
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
16-73 |
3.70e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.84 E-value: 3.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 637158246 16 HEVLKDINAVIEEKE-VVCVIGPSGSGKSTFLRCLnkLEDITAGEVVVHghtITDPKVN 73
Cdd:COG3267 29 REALARLEYALAQGGgFVVLTGEVGTGKTTLLRRL--LERLPDDVKVAY---IPNPQLS 82
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
28-47 |
6.15e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 35.96 E-value: 6.15e-03
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
31-62 |
7.14e-03 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 36.36 E-value: 7.14e-03
10 20 30
....*....|....*....|....*....|..
gi 637158246 31 VVCVIGPSGSGKSTFLRCLnkLEDITAGEVVV 62
Cdd:COG0572 9 IIGIAGPSGSGKTTFARRL--AEQLGADKVVV 38
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
32-71 |
8.25e-03 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 35.66 E-value: 8.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 637158246 32 VCVIGPSGSGKSTFLRCLNKLEDITAGEVVvhghtITDPK 71
Cdd:cd01127 2 TLVLGTTGSGKTTSIVIPLLDQAARGGSVI-----ITDPK 36
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
19-46 |
8.28e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.36 E-value: 8.28e-03
10 20
....*....|....*....|....*...
gi 637158246 19 LKDINAVIEEKEVVCVIGPSGSGKSTFL 46
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
15-60 |
9.87e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.22 E-value: 9.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 637158246 15 DHEVLKDINAVIEEKeVVCVIGPSGSGKSTFLRCLNKLEDITAGEV 60
Cdd:cd01854 72 TGEGLDELRELLKGK-TSVLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| |
