|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
9-258 |
1.27e-177 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 487.58 E-value: 1.27e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGyrersdgslvrDSE 88
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-----------DSK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 RNIARQRRDIGMVFQRFNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIAR 168
Cdd:COG1126 70 KDINKLRRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 169 ALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPSH 248
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
250
....*....|
gi 1525903658 249 PRTRAFLSRV 258
Cdd:COG1126 230 ERTRAFLSKV 239
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
10-259 |
1.64e-148 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 414.97 E-value: 1.64e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSDGSLVRDSER 89
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELVPADRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARA 169
Cdd:COG4598 89 QLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPSHP 249
Cdd:COG4598 169 LAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSE 248
|
250
....*....|
gi 1525903658 250 RTRAFLSRVL 259
Cdd:COG4598 249 RLRQFLSSSL 258
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
10-233 |
1.41e-133 |
|
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: 375.33 E-value: 1.41e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVngramgyrersDGSLVRDSER 89
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII-----------DGLKLTDDKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARA 169
Cdd:cd03262 70 NINELRQKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGEL 233
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
9-258 |
1.44e-123 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 351.32 E-value: 1.44e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVngramgyrersDGSLVRDSE 88
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIV-----------DGLKVNDPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 RNIARQRRDIGMVFQRFNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIAR 168
Cdd:PRK09493 70 VDERLIRQEAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 169 ALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPSH 248
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
250
....*....|
gi 1525903658 249 PRTRAFLSRV 258
Cdd:PRK09493 230 QRLQEFLQHV 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
10-259 |
3.04e-112 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 322.85 E-value: 3.04e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersDGSLVRDSER 89
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITI------DTARSLSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQ-RRDIGMVFQRFNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIAR 168
Cdd:PRK11264 78 GLIRQlRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 169 ALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPSH 248
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
250
....*....|.
gi 1525903658 249 PRTRAFLSRVL 259
Cdd:PRK11264 238 PRTRQFLEKFL 248
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
10-259 |
6.66e-104 |
|
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: 301.75 E-value: 6.66e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSDGSLVRDSER 89
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNGPLVPADEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARA 169
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPSH 248
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|.
gi 1525903658 249 PRTRAFLSRVL 259
Cdd:TIGR03005 241 ERTREFLSKVI 251
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-259 |
1.31e-101 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 299.30 E-value: 1.31e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSF----GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgSLV 84
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGV----------DLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 85 RDSERNIARQRRDIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRV 164
Cdd:COG1135 71 ALSERELRAARRKIGMIFQHFNLLSSRTVAENV-ALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 165 AIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIF 243
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVF 229
|
250
....*....|....*.
gi 1525903658 244 SHPSHPRTRAFLSRVL 259
Cdd:COG1135 230 ANPQSELTRRFLPTVL 245
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
14-259 |
9.05e-99 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 289.18 E-value: 9.05e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 14 DLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSDGSLVRDSERNIAR 93
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 94 QRRDIGMVFQRFNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLLARVGLADKAN-HYPSMLSGGQQQRVAIARALAM 172
Cdd:PRK10619 90 LRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 173 KPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPSHPRTR 252
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQ 249
|
....*..
gi 1525903658 253 AFLSRVL 259
Cdd:PRK10619 250 QFLKGSL 256
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
10-254 |
9.10e-94 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 275.74 E-value: 9.10e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSDgslvrdsER 89
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPS-------DK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARA 169
Cdd:PRK11124 76 AIRELRRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPeqifSHPSHP 249
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA----SCFTQP 231
|
....*
gi 1525903658 250 RTRAF 254
Cdd:PRK11124 232 QTEAF 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
10-256 |
9.96e-93 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 273.04 E-value: 9.96e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSdgslvrdSER 89
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKP-------SEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARA 169
Cdd:COG4161 76 AIRLLRQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEqIFSHPSHP 249
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQPQTE 234
|
....*..
gi 1525903658 250 RTRAFLS 256
Cdd:COG4161 235 AFAHYLS 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
9-247 |
5.89e-89 |
|
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: 263.29 E-value: 5.89e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGD----LQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgSLV 84
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGT----------DLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 85 RDSERNIARQRRDIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRV 164
Cdd:cd03258 71 LLSGKELRKARRRIGMIFQHFNLLSSRTVFENV-ALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 165 AIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIF 243
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
....
gi 1525903658 244 SHPS 247
Cdd:cd03258 230 ANPQ 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
7-236 |
6.74e-88 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 260.36 E-value: 6.74e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 7 ELIIDAQDLHKSFGD----LQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGyrersdgs 82
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIS-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 83 lvRDSERNIARQRRD-IGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQ 161
Cdd:COG1136 74 --SLSERELARLRRRhIGFVFQFFNLLPELTALENV-ALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525903658 162 QRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFArEVADRVVVLDQGELIEQ 236
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELA-ARADRVIRLRDGRIVSD 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
5-255 |
1.38e-87 |
|
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: 259.91 E-value: 1.38e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 5 SDELIIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgSLV 84
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQ----------DIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 85 RDSERNIARQRRDIGMVFQRFNLFPHMTALENIiEAPIHVLGT-PRAEALEQARGLLARVGLADKANHYPSMLSGGQQQR 163
Cdd:COG1127 71 GLSEKELYELRRRIGMLFQGGALFDSLTVFENV-AFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 164 VAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQI 242
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
250
....*....|...
gi 1525903658 243 FSHPsHPRTRAFL 255
Cdd:COG1127 230 LASD-DPWVRQFL 241
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
10-259 |
1.72e-87 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 263.20 E-value: 1.72e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSF----GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgSLVR 85
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQ----------DLTA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 86 DSERNIARQRRDIGMVFQRFNLFPHMTALENIieA-PIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRV 164
Cdd:PRK11153 72 LSEKELRKARRQIGMIFQHFNLLSSRTVFDNV--AlPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 165 AIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIF 243
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVF 229
|
250
....*....|....*.
gi 1525903658 244 SHPSHPRTRAFLSRVL 259
Cdd:PRK11153 230 SHPKHPLTREFIQSTL 245
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-258 |
2.05e-84 |
|
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: 260.99 E-value: 2.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 4 KSDELIIDAQDLHKSF-----GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrer 78
Cdd:COG1123 255 AAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGK------- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 79 sdgSLVRDSERNIARQRRDIGMVFQrfN----LFPHMTALEnIIEAPIHVLGT-PRAEALEQARGLLARVGL-ADKANHY 152
Cdd:COG1123 328 ---DLTKLSRRSLRELRRRVQMVFQ--DpyssLNPRMTVGD-IIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRY 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 153 PSMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQG 231
Cdd:COG1123 402 PHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDG 481
|
250 260
....*....|....*....|....*..
gi 1525903658 232 ELIEQGPPEQIFSHPSHPRTRAFLSRV 258
Cdd:COG1123 482 RIVEDGPTEEVFANPQHPYTRALLAAV 508
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
10-233 |
2.67e-84 |
|
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: 250.87 E-value: 2.67e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGD----LQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgSLVR 85
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGT----------DISK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 86 DSERNIARQRRD-IGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRV 164
Cdd:cd03255 71 LSEKELAAFRRRhIGFVFQSFNLLPDLTALENV-ELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 165 AIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREvADRVVVLDQGEL 233
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
9-256 |
2.93e-84 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 251.83 E-value: 2.93e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGrIRVNGRAMgyrerSDGSLVRDSE 88
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPG-VRIEGKVL-----FDGQDIYDKK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 RNIARQRRDIGMVFQRFNLFPhMTALENIIEAP-IHVLgTPRAEALEQARGLLARVGL----ADKANHYPSMLSGGQQQR 163
Cdd:TIGR00972 75 IDVVELRRRVGMVFQKPNPFP-MSIYDNIAYGPrLHGI-KDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 164 VAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEgMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIF 243
Cdd:TIGR00972 153 LCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIF 231
|
250
....*....|...
gi 1525903658 244 SHPSHPRTRAFLS 256
Cdd:TIGR00972 232 TNPKEKRTEDYIS 244
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-249 |
3.31e-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: 3.31e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGyrersdgslvrdse 88
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 rNIARQRRDIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIAR 168
Cdd:COG3842 71 -GLPPEKRNVGMVFQDYALFPHLTVAENV-AFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 169 ALAMKPQAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPS 247
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPA 228
|
..
gi 1525903658 248 HP 249
Cdd:COG3842 229 TR 230
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
9-242 |
3.89e-82 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 246.51 E-value: 3.89e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSF-GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGyrersdgslvRDS 87
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVT----------ALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 ERNIARQRRDIGMVFQRFNLFPHMTALENIIEAPIHVLGTPRA-------EALEQARGLLARVGLADKANHYPSMLSGGQ 160
Cdd:COG3638 72 GRALRRLRRRIGMIFQQFNLVPRLSVLTNVLAGRLGRTSTWRSllglfppEDRERALEALERVGLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 161 QQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPP 239
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPP 231
|
...
gi 1525903658 240 EQI 242
Cdd:COG3638 232 AEL 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
10-246 |
4.21e-78 |
|
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: 235.30 E-value: 4.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSF-GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdSE 88
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI-------------TK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 RNIARQRRDIGMVFQrfN----LFpHMTALENIIEAPIHvLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRV 164
Cdd:COG1122 68 KNLRELRRKVGLVFQ--NpddqLF-APTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 165 AIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFS 244
Cdd:COG1122 144 AIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
..
gi 1525903658 245 HP 246
Cdd:COG1122 224 DY 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
9-235 |
1.42e-77 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 233.79 E-value: 1.42e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSF-GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgSLVRDS 87
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQ----------DLSRLK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 ERNIARQRRDIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIA 167
Cdd:COG2884 71 RREIPYLRRRIGVVFQDFRLLPDRTVYENV-ALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525903658 168 RALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIE 235
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
10-254 |
4.62e-76 |
|
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: 230.47 E-value: 4.62e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgSLVRDSER 89
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGE----------DISGLSEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPHMTALENIiEAPIHVLGT-PRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIAR 168
Cdd:cd03261 71 ELYRLRRRMGMLFQSGALFDSLTVFENV-AFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 169 ALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPs 247
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD- 228
|
....*..
gi 1525903658 248 HPRTRAF 254
Cdd:cd03261 229 DPLVRQF 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
10-242 |
5.32e-75 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 227.64 E-value: 5.32e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgslvrDSER 89
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGE--------------DVAR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPHMTALENI-IEAPIHvlGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIAR 168
Cdd:COG1131 67 DPAEVRRRIGYVPQEPALYPDLTVRENLrFFARLY--GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 169 ALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQI 242
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
10-255 |
6.63e-75 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 231.57 E-value: 6.63e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgslvrDSER 89
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR--------------DLFT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARA 169
Cdd:COG1118 69 NLPPRERRVGFVFQHYALFPHMTVAENI-AFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 170 LAMKPQAMLFDEPTSALDPetvgevlQVMKEL--------AEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQ 241
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDA-------KVRKELrrwlrrlhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDE 220
|
250
....*....|....
gi 1525903658 242 IFSHPSHPRTRAFL 255
Cdd:COG1118 221 VYDRPATPFVARFL 234
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
10-242 |
3.86e-74 |
|
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: 225.52 E-value: 3.86e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRiRVNGRAmgyreRSDGSLVRDSER 89
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGA-PDEGEV-----LLDGKDIYDLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPhMTALENIIEAPIHVLGTPRAEALEQARGLLARVGLAD--KANHYPSMLSGGQQQRVAIA 167
Cdd:cd03260 75 DVLELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 168 RALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEgMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQI 242
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-256 |
4.51e-74 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 226.07 E-value: 4.51e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 5 SDELIIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCIN-LLEDIQG----GRIRVNGRamgyrers 79
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNrMNDLIPGarveGEILLDGE-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 80 DgslVRDSERNIARQRRDIGMVFQRFNLFPhMTALENIIEAP-IHvlG-TPRAEALEQARGLLARVGL----ADKANHYP 153
Cdd:COG1117 79 D---IYDPDVDVVELRRRVGMVFQKPNPFP-KSIYDNVAYGLrLH--GiKSKSELDEIVEESLRKAALwdevKDRLKKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 154 SMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEgMTMVVVTHEMGFAREVADRVVVLDQGEL 233
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
250 260
....*....|....*....|...
gi 1525903658 234 IEQGPPEQIFSHPSHPRTRAFLS 256
Cdd:COG1117 232 VEFGPTEQIFTNPKDKRTEDYIT 254
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
5-231 |
6.30e-73 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 223.43 E-value: 6.30e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 5 SDELIIDAQDLHKSF----GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAmgyrersd 80
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 81 gslvrdsernIARQRRDIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQ 160
Cdd:COG1116 75 ----------VTGPGPDRGVVFQEPALLPWLTVLDNV-ALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGM 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525903658 161 QQRVAIARALAMKPQAMLFDEPTSALDPETvGEVLQ--VMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQG 231
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALDALT-RERLQdeLLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
10-232 |
3.51e-72 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 218.60 E-value: 3.51e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgsLVRDSER 89
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE-----------DLTDLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPHMTALENIIEApihvlgtpraealeqargllarvgladkanhypsmLSGGQQQRVAIARA 169
Cdd:cd03229 70 ELPPLRRRIGMVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARA 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGE 232
Cdd:cd03229 115 LAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
10-248 |
4.61e-72 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 224.18 E-value: 4.61e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGyrersdgslvrdser 89
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARA 169
Cdd:COG3839 69 DLPPKDRNIAMVFQSYALYPHMTVYENI-AFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 170 LAMKPQAMLFDEPTSALDP----ETVGEVLQVMKELaeeGMTMVVVTHE----MGFarevADRVVVLDQGELIEQGPPEQ 241
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAklrvEMRAEIKRLHRRL---GTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPEE 220
|
....*..
gi 1525903658 242 IFSHPSH 248
Cdd:COG3839 221 LYDRPAN 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-237 |
8.81e-72 |
|
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: 218.93 E-value: 8.81e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 13 QDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGyrersdgslvrdserNIA 92
Cdd:cd03259 4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT---------------GVP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 93 RQRRDIGMVFQRFNLFPHMTALENIieA-PIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALA 171
Cdd:cd03259 69 PERRNIGMVFQDYALFPHLTVAENI--AfGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525903658 172 MKPQAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQG 237
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-256 |
9.95e-72 |
|
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: 222.24 E-value: 9.95e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSF----GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCI-NLLED--IQGGRIRVNGRamgyrersdg 81
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlGLLPPpgITSGEILFDGE---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 82 SLVRDSERNIARQR-RDIGMVFQ----RFNlfPHMTALENIIEAPIHVLGTPRAEALEQARGLLARVGLADKANH---YP 153
Cdd:COG0444 71 DLLKLSEKELRKIRgREIQMIFQdpmtSLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRldrYP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 154 SMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGE 232
Cdd:COG0444 149 HELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGR 228
|
250 260
....*....|....*....|....
gi 1525903658 233 LIEQGPPEQIFSHPSHPRTRAFLS 256
Cdd:COG0444 229 IVEEGPVEELFENPRHPYTRALLS 252
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-255 |
2.74e-71 |
|
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: 218.90 E-value: 2.74e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFG----DLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERsdgslvr 85
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRR------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 86 dserniARQRRDIGMVFQ--RFNLFPHMTaLENIIEAPIHVLGTPRAEalEQARGLLARVGL-ADKANHYPSMLSGGQQQ 162
Cdd:COG1124 75 ------KAFRRRVQMVFQdpYASLHPRHT-VDRILAEPLRIHGLPDRE--ERIAELLEQVGLpPSFLDRYPHQLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 163 RVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQ 241
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
250
....*....|....
gi 1525903658 242 IFSHPSHPRTRAFL 255
Cdd:COG1124 226 LLAGPKHPYTRELL 239
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
15-242 |
8.82e-70 |
|
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: 214.74 E-value: 8.82e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 15 LHKSFGDL-QILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGyrersdgslvRDSERNIAR 93
Cdd:cd03256 6 LSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDIN----------KLKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 94 QRRDIGMVFQRFNLFPHMTALENIIEAPIHVLGTPRA-------EALEQARGLLARVGLADKANHYPSMLSGGQQQRVAI 166
Cdd:cd03256 76 LRRQIGMIFQQFNLIERLSVLENVLSGRLGRRSTWRSlfglfpkEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525903658 167 ARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELA-EEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQI 242
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
9-237 |
2.59e-69 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 213.14 E-value: 2.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSF----GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersDGSLV 84
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGK--------DLLKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 85 RDSERNIarQRRDIGMVFQ--RFNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLLAR-VGLADK-ANHYPSMLSGGQ 160
Cdd:cd03257 73 SRRLRKI--RRKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVgVGLPEEvLNRYPHELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525903658 161 QQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQG 237
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
10-228 |
4.55e-69 |
|
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: 212.33 E-value: 4.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGD----LQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAmgyrersdgslvr 85
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 86 dsernIARQRRDIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVA 165
Cdd:cd03293 68 -----VTGPGPDRGYVFQQDALLPWLTVLDNV-ALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 166 IARALAMKPQAMLFDEPTSALDPETvGEVLQ--VMKELAEEGMTMVVVTHEMGFAREVADRVVVL 228
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALT-REQLQeeLLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
10-246 |
2.90e-67 |
|
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: 208.06 E-value: 2.90e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgSLVRDSER 89
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGE----------DITGLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARqrRDIGMVFQRFNLFPHMTALENIIEAPIHVLGTP---------RAEALEQARGLLARVGLADKANHYPSMLSGGQ 160
Cdd:cd03219 71 EIAR--LGIGRTFQIPRLFPELTVLENVMVAAQARTGSGlllararreEREARERAEELLERVGLADLADRPAGELSYGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 161 QQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPE 240
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPD 228
|
....*.
gi 1525903658 241 QIFSHP 246
Cdd:cd03219 229 EVRNNP 234
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-232 |
8.35e-67 |
|
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: 206.16 E-value: 8.35e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 14 DLHKSFGDL--QILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdSERNI 91
Cdd:cd03225 4 NLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL-------------TKLSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 92 ARQRRDIGMVFQRFNL-FPHMTALENIIEAPIHvLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARAL 170
Cdd:cd03225 71 KELRRKVGLVFQNPDDqFFGPTVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525903658 171 AMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGE 232
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-246 |
2.69e-66 |
|
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: 206.43 E-value: 2.69e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgSLVRDSE 88
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGR----------DITGLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 RNIARQrrdiGMV--FQRFNLFPHMTALENIIEAPIH---------VLGTPR-----AEALEQARGLLARVGLADKANHY 152
Cdd:COG0411 74 HRIARL----GIArtFQNPRLFPELTVLENVLVAAHArlgrgllaaLLRLPRarreeREARERAEELLERVGLADRADEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 153 PSMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADRVVVLDQG 231
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFG 229
|
250
....*....|....*
gi 1525903658 232 ELIEQGPPEQIFSHP 246
Cdd:COG0411 230 RVIAEGTPAEVRADP 244
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
9-245 |
2.92e-66 |
|
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: 206.00 E-value: 2.92e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFG-DLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgSLVRDS 87
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGT----------DITKLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 ERNIARQRRDIGMVFQRFNLFPHMTALENIIEAPIHVLGT--------PRAEAlEQARGLLARVGLADKANHYPSMLSGG 159
Cdd:TIGR02315 71 GKKLRKLRRRIGMIFQHYNLIERLTVLENVLHGRLGYKPTwrsllgrfSEEDK-ERALSALERVGLADKAYQRADQLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 160 QQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGP 238
Cdd:TIGR02315 150 QQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGA 229
|
....*..
gi 1525903658 239 PEQIFSH 245
Cdd:TIGR02315 230 PSELDDE 236
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
11-254 |
1.20e-65 |
|
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: 205.18 E-value: 1.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 11 DAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSDGSLVRdsern 90
Cdd:cd03294 26 SKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELR----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 91 iarqRRDIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARAL 170
Cdd:cd03294 101 ----RKKISMVFQSFALLPHRTVLENV-AFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 171 AMKPQAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPSHP 249
Cdd:cd03294 176 AVDPDILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPAND 255
|
....*
gi 1525903658 250 RTRAF 254
Cdd:cd03294 256 YVREF 260
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
15-259 |
1.47e-65 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 207.43 E-value: 1.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 15 LHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgSLVRDSERNIARQ 94
Cdd:TIGR02314 11 FHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQ----------DLTTLSNSELTKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 95 RRDIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKP 174
Cdd:TIGR02314 81 RRQIGMIFQHFNLLSSRTVFGNV-ALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 175 QAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPSHPRTRA 253
Cdd:TIGR02314 160 KVLLCDEATSALDPATTQSILELLKEINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQK 239
|
....*.
gi 1525903658 254 FLSRVL 259
Cdd:TIGR02314 240 FIRSTL 245
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
13-255 |
2.59e-65 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 205.32 E-value: 2.59e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 13 QDLHKSFGDLQI-LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgslvrD-SERN 90
Cdd:COG1125 5 ENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGE--------------DiRDLD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 91 IARQRRDIGMVFQRFNLFPHMTALENIIEAPiHVLGTPRAEALEQARGLLARVGL--ADKANHYPSMLSGGQQQRVAIAR 168
Cdd:COG1125 71 PVELRRRIGYVIQQIGLFPHMTVAENIATVP-RLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 169 ALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPS 247
Cdd:COG1125 150 ALAADPPILLMDEPFGALDPITREQLQDELLRLQRElGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPA 229
|
....*...
gi 1525903658 248 HPRTRAFL 255
Cdd:COG1125 230 NDFVADFV 237
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
9-240 |
1.27e-64 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 201.12 E-value: 1.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGD----LQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgSLV 84
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ----------DLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 85 RDSERNIARQRRD-IGMVFQRFNLFPHMTALENIIeAPIHVLGtpRAEALEQARGLLARVGLADKANHYPSMLSGGQQQR 163
Cdd:COG4181 78 ALDEDARARLRARhVGFVFQSFQLLPTLTALENVM-LPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525903658 164 VAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREvADRVVVLDQGELIEQGPPE 240
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAAT 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-246 |
1.48e-64 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 209.37 E-value: 1.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSF--GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQG---GRIRVNGRamgyrersdgSL 83
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGR----------DL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 84 VRDSERNIARQrrdIGMVFQRF--NLFPhMTALENIIEAPIhVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQ 161
Cdd:COG1123 74 LELSEALRGRR---IGMVFQDPmtQLNP-VTVGDQIAEALE-NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 162 QRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPE 240
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
....*.
gi 1525903658 241 QIFSHP 246
Cdd:COG1123 229 EILAAP 234
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
13-258 |
2.01e-64 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 204.89 E-value: 2.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 13 QDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersDGSlvrdserNIA 92
Cdd:TIGR03265 8 DNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGR--------DIT-------RLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 93 RQRRDIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAM 172
Cdd:TIGR03265 73 PQKRDYGIVFQSYALFPNLTVADNI-AYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALAT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 173 KPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGElIEQ-GPPEQIFSHPSHPR 250
Cdd:TIGR03265 152 SPGLLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGV-IEQvGTPQEIYRHPATPF 230
|
....*...
gi 1525903658 251 TRAFLSRV 258
Cdd:TIGR03265 231 VADFVGEV 238
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-255 |
3.22e-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: 200.60 E-value: 3.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQ-ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdSE 88
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI-------------RE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 RNIARQRRDIGMVFQRFNLFPHMTALENIIEAPiHVLGTPRAEALEQARGLLARVGLADK--ANHYPSMLSGGQQQRVAI 166
Cdd:cd03295 68 QDPVELRRKIGYVIQQIGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 167 ARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSH 245
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
250
....*....|
gi 1525903658 246 PSHPRTRAFL 255
Cdd:cd03295 227 PANDFVAEFV 236
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
10-247 |
3.05e-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: 198.81 E-value: 3.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSF--GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGramgyrersdgsLVRDS 87
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG------------LDTLD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 ERNIARQRRDIGMVFQR-FNLFPHMT-------ALENiieapihvLGTPRAEALEQARGLLARVGLADKANHYPSMLSGG 159
Cdd:TIGR04520 69 EENLWEIRKKVGMVFQNpDNQFVGATveddvafGLEN--------LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 160 QQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREvADRVVVLDQGELIEQGP 238
Cdd:TIGR04520 141 QKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGT 219
|
....*....
gi 1525903658 239 PEQIFSHPS 247
Cdd:TIGR04520 220 PREIFSQVE 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-255 |
2.14e-61 |
|
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: 201.84 E-value: 2.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 5 SDELIIDAQDLHKSFGD----LQILKGISLQVRRGEVVVLIGASGSGKT-TFIRCINLLED---IQGGRIRVNGRamgyr 76
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDpaaHPSGSILFDGQ----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 77 ersdgSLVRDSERNIARQR-RDIGMVFQRfnlfPhMTAL-------ENIIEAPIHVLGTPRAEALEQARGLLARVGLAD- 147
Cdd:COG4172 77 -----DLLGLSERELRRIRgNRIAMIFQE----P-MTSLnplhtigKQIAEVLRLHRGLSGAAARARALELLERVGIPDp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 148 --KANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADR 224
Cdd:COG4172 147 erRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADR 226
|
250 260 270
....*....|....*....|....*....|.
gi 1525903658 225 VVVLDQGELIEQGPPEQIFSHPSHPRTRAFL 255
Cdd:COG4172 227 VAVMRQGEIVEQGPTAELFAAPQHPYTRKLL 257
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
5-256 |
2.97e-61 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 195.72 E-value: 2.97e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 5 SDELIIDAQDLHKSF-----------GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRam 73
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 74 gyrersdgSLVRDSERNIARQRRDIGMVFQrfN----LFPHMTaLENIIEAPIHVLG-TPRAEALEQARGLLARVGL-AD 147
Cdd:COG4608 81 --------DITGLSGRELRPLRRRMQMVFQ--DpyasLNPRMT-VGDIIAEPLRIHGlASKAERRERVAELLELVGLrPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 148 KANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVV 226
Cdd:COG4608 150 HADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVA 229
|
250 260 270
....*....|....*....|....*....|
gi 1525903658 227 VLDQGELIEQGPPEQIFSHPSHPRTRAFLS 256
Cdd:COG4608 230 VMYLGKIVEIAPRDELYARPLHPYTQALLS 259
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-246 |
1.24e-60 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 191.46 E-value: 1.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 5 SDELIIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgslv 84
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 85 rdserNIARQRRDIGMVFQRFNL---FPhMTALEnIIE----APIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLS 157
Cdd:COG1121 69 -----PPRRARRRIGYVPQRAEVdwdFP-ITVRD-VVLmgryGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 158 GGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGeLIEQG 237
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHG 220
|
....*....
gi 1525903658 238 PPEQIFSHP 246
Cdd:COG1121 221 PPEEVLTPE 229
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
9-244 |
4.09e-60 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 190.64 E-value: 4.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGyrersdgSLvrdSE 88
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA-------SL---SR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 RNIARQrrdIGMVFQRFNLFPHMTALEnIIE---AP-IHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRV 164
Cdd:COG1120 71 RELARR---IAYVPQEPPAPFGLTVRE-LVAlgrYPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 165 AIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELA-EEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIF 243
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
.
gi 1525903658 244 S 244
Cdd:COG1120 227 T 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
10-255 |
7.37e-60 |
|
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: 189.47 E-value: 7.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgslvRDSER 89
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE-------------DATDV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIarQRRDIGMVFQRFNLFPHMTALENI---IEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAI 166
Cdd:cd03296 70 PV--QERNVGFVFQHYALFRHMTVFDNVafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 167 ARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSH 245
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
250
....*....|
gi 1525903658 246 PSHPRTRAFL 255
Cdd:cd03296 228 PASPFVYSFL 237
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
10-242 |
1.72e-59 |
|
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: 188.53 E-value: 1.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgslvrDSER 89
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE--------------DVRK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPHMTALENI-IEAPIHvlGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIAR 168
Cdd:COG4555 68 EPREARRQIGVLPDERGLYDRLTVRENIrYFAELY--GLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 169 ALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQI 242
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
25-259 |
2.24e-59 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 192.63 E-value: 2.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGR---AMGYRERSDgslVRdserniarqRRDIGMV 101
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEditKLSKKELRE---LR---------RKKMSMV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 102 FQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAMLFDE 181
Cdd:COG4175 111 FQHFALLPHRTVLENV-AFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 182 PTSALDP----ETVGEVLQVMKELaeeGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPSHPRTRAF--- 254
Cdd:COG4175 190 AFSALDPlirrEMQDELLELQAKL---KKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFved 266
|
....*..
gi 1525903658 255 --LSRVL 259
Cdd:COG4175 267 vdRSKVL 273
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
10-258 |
2.67e-59 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 191.45 E-value: 2.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgslvrDSER 89
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT--------------DVSR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRdIGMVFQRFNLFPHMTALENIIEApIHVL---GTPRAEALEQ-ARGLLARVGLADKANHYPSMLSGGQQQRVA 165
Cdd:PRK10851 69 LHARDRK-VGFVFQHYALFRHMTVFDNIAFG-LTVLprrERPNAAAIKAkVTQLLEMVQLAHLADRYPAQLSGGQKQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 166 IARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGElIEQ-GPPEQIF 243
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGN-IEQaGTPDQVW 225
|
250
....*....|....*
gi 1525903658 244 SHPSHPRTRAFLSRV 258
Cdd:PRK10851 226 REPATRFVLEFMGEV 240
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
10-247 |
9.51e-59 |
|
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: 186.29 E-value: 9.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdseR 89
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI---------------T 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARA 169
Cdd:cd03300 66 NLPPHKRPVNTVFQNYALFPHLTVFENI-AFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPS 247
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-256 |
1.78e-57 |
|
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: 191.44 E-value: 1.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 5 SDELIIDAQDLHKSF-----------GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCI-NLLEdiQGGRIRVNGRA 72
Cdd:COG4172 271 DAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALlRLIP--SEGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 73 mgyrersdgsLVRDSERNIARQRRDIGMVFQ----RFNlfPHMTALEnIIEAPIHVLGTP--RAEALEQARGLLARVGL- 145
Cdd:COG4172 349 ----------LDGLSRRALRPLRRRMQVVFQdpfgSLS--PRMTVGQ-IIAEGLRVHGPGlsAAERRARVAEALEEVGLd 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 146 ADKANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADR 224
Cdd:COG4172 416 PAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHR 495
|
250 260 270
....*....|....*....|....*....|..
gi 1525903658 225 VVVLDQGELIEQGPPEQIFSHPSHPRTRAFLS 256
Cdd:COG4172 496 VMVMKDGKVVEQGPTEQVFDAPQHPYTRALLA 527
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
10-233 |
2.91e-57 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 180.29 E-value: 2.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGramgyrersdgslvRDSER 89
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG--------------KDIKK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPHMTALENIieapihvlgtpraealeqargllarvgladkanhypsMLSGGQQQRVAIARA 169
Cdd:cd03230 67 EPEEVKRRIGYLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQA 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGEL 233
Cdd:cd03230 110 LLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
9-232 |
3.82e-57 |
|
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: 181.68 E-value: 3.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSF-GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAmgyrersdgsLVRDS 87
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGED----------VNRLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 ERNIARQRRDIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIA 167
Cdd:TIGR02673 71 GRQLPLLRRRIGVVFQDFRLLPDRTVYENV-ALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 168 RALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGE 232
Cdd:TIGR02673 150 RAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
10-242 |
8.37e-57 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 181.09 E-value: 8.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGyRERSDgslvrdser 89
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT-GLPPH--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 niARQRRDIGMVFQRFNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLLARvgLADKANHYPSMLSGGQQQRVAIARA 169
Cdd:cd03224 71 --ERARAGIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQI 242
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
23-246 |
7.70e-56 |
|
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: 180.34 E-value: 7.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 23 QILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgSLVRDSERNIARQRRDIGMVF 102
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGR----------DITAKKKKKLKDLRKKVGLVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 103 QrfnlFPHM-----TALENIIEAPIHvLGTPRAEALEQARGLLARVGLADK-ANHYPSMLSGGQQQRVAIARALAMKPQA 176
Cdd:TIGR04521 89 Q----FPEHqlfeeTVYKDIAFGPKN-LGLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAMEPEV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525903658 177 MLFDEPTSALDPETVGEVLQVMKELA-EEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHP 246
Cdd:TIGR04521 164 LILDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
10-233 |
6.65e-55 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 175.77 E-value: 6.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdSER 89
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-------------SAM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPhMTALENIIEAPihvLGTPRAEALEQARGLLARVGLADKANHYP-SMLSGGQQQRVAIAR 168
Cdd:COG4619 68 PPPEWRRQVAYVPQEPALWG-GTVRDNLPFPF---QLRERKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525903658 169 ALAMKPQAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADRVVVLDQGEL 233
Cdd:COG4619 144 ALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
10-256 |
9.10e-55 |
|
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: 176.37 E-value: 9.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQiLKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdseR 89
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI---------------T 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARA 169
Cdd:cd03299 65 NLPPEKRDISYVPQNYALFPHMTVYKNI-AYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPSH 248
Cdd:cd03299 144 LVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKN 223
|
....*...
gi 1525903658 249 PRTRAFLS 256
Cdd:cd03299 224 EFVAEFLG 231
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
9-235 |
1.84e-54 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 174.85 E-value: 1.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGD----LQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgSLV 84
Cdd:TIGR02211 1 LLKCENLGKRYQEgkldTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQ----------SLS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 85 RDSERNIARQR-RDIGMVFQRFNLFPHMTALENIIeAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQR 163
Cdd:TIGR02211 71 KLSSNERAKLRnKKLGFIYQFHHLLPDFTALENVA-MPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525903658 164 VAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREvADRVVVLDQGELIE 235
Cdd:TIGR02211 150 VAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELnRELNTSFLVVTHDLELAKK-LDRVLEMKDGQLFN 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-257 |
2.42e-54 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 174.94 E-value: 2.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 6 DELIIDAQDLHKSFgdlqilkgiSLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvr 85
Cdd:COG3840 5 DDLTYRYGDFPLRF---------DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 86 dSERNIARqrRDIGMVFQRFNLFPHMTALENIieapihVLG-----TPRAEALEQARGLLARVGLADKANHYPSMLSGGQ 160
Cdd:COG3840 64 -TALPPAE--RPVSMLFQENNLFPHLTVAQNI------GLGlrpglKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 161 QQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPP 239
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPT 214
|
250
....*....|....*...
gi 1525903658 240 EQIFSHPSHPRTRAFLSR 257
Cdd:COG3840 215 AALLDGEPPPALAAYLGI 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-236 |
7.13e-54 |
|
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: 173.21 E-value: 7.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 13 QDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSDgslvrdsernia 92
Cdd:cd03301 4 ENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 93 rqrRDIGMVFQRFNLFPHMTALENiIEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAM 172
Cdd:cd03301 72 ---RDIAMVFQNYALYPHMTVYDN-IAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 173 KPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGElIEQ 236
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQ-IQQ 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
14-246 |
1.44e-52 |
|
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: 174.13 E-value: 1.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 14 DLHKSFGDLQIlkGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgsLVRDSERNIAR 93
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE-----------VLQDSARGIFL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 94 --QRRDIGMVFQRFNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLLarvGLADKANHYPSMLSGGQQQRVAIARALA 171
Cdd:COG4148 73 ppHRRRIGYVFQEARLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525903658 172 MKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHP 246
Cdd:COG4148 150 SSPRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
13-228 |
2.26e-52 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 168.95 E-value: 2.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 13 QDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersDGSLVRDSERNIA 92
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQ--------ETPPLNSKKASKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 93 RqRRDIGMVFQRFNLFPHMTALENIIEAPIHVLGtPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAM 172
Cdd:TIGR03608 74 R-REKLGYLFQNFALIENETVEENLDLGLKYKKL-SKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1525903658 173 KPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFArEVADRVVVL 228
Cdd:TIGR03608 152 PPPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
17-258 |
5.17e-52 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 173.11 E-value: 5.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 17 KSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSDGSLVRdserniarqRR 96
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVR---------RK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 97 DIGMVFQRFNLFPHMTALENIIEAPiHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQA 176
Cdd:TIGR01186 72 KIGMVFQQFALFPHMTILQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 177 MLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPSHPRTRAFL 255
Cdd:TIGR01186 151 LLMDEAFSALDPLIRDSMQDELKKLqATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFI 230
|
...
gi 1525903658 256 SRV 258
Cdd:TIGR01186 231 GKV 233
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
17-247 |
1.40e-51 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 171.44 E-value: 1.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 17 KSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVngramgyrersDGSLVrdSERNIarQRR 96
Cdd:PRK11432 14 KRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI-----------DGEDV--THRSI--QQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 97 DIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQA 176
Cdd:PRK11432 79 DICMVFQSYALFPHMSLGENV-GYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525903658 177 MLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPS 247
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
9-246 |
1.44e-51 |
|
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: 167.85 E-value: 1.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGyRERSDgslvrdse 88
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT-GLPPH-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 rniARQRRDIGMVFQRFNLFPHMTALENIieapihVLGTPRAEALEQARGLLARVG-----LADKANHYPSMLSGGQQQR 163
Cdd:COG0410 74 ---RIARLGIGYVPEGRRIFPSLTVEENL------LLGAYARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 164 VAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIF 243
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
...
gi 1525903658 244 SHP 246
Cdd:COG0410 225 ADP 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
9-246 |
2.42e-51 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 171.67 E-value: 2.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGyrersdgslvrdse 88
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 rNIARQRRDIGMVFQRFNLFPHMTALENIIEApIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIAR 168
Cdd:PRK09452 80 -HVPAENRHVNTVFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 169 ALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGElIEQ-GPPEQIFSHP 246
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR-IEQdGTPREIYEEP 236
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-245 |
2.68e-51 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 168.66 E-value: 2.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 7 ELIIDAQDLHKSFGDLQ--ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslv 84
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 85 rdSERNIARQRRDIGMVFQR-FNLFPHMT-------ALENIieapihvlGTPRAEALEQARGLLARVGLADKANHYPSML 156
Cdd:PRK13635 72 --SEETVWDVRRQVGMVFQNpDNQFVGATvqddvafGLENI--------GVPREEMVERVDQALRQVGMEDFLNREPHRL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 157 SGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGM-TMVVVTHEMGFAREvADRVVVLDQGELIE 235
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
250
....*....|
gi 1525903658 236 QGPPEQIFSH 245
Cdd:PRK13635 221 EGTPEEIFKS 230
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
10-233 |
5.93e-51 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 165.66 E-value: 5.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSF-GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAM-GYRERSdgslvrds 87
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsDLRGRA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 ernIARQRRDIGMVFQRFNLFPHMTALENIIeAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIA 167
Cdd:cd03292 73 ---IPYLRRKIGVVFQDFRLLPDRNVYENVA-FALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525903658 168 RALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGEL 233
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-259 |
1.32e-50 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 166.17 E-value: 1.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQG-----GRIRVNGRAMgYRERSDGSLV 84
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNI-YSPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 85 RdserniarqrRDIGMVFQRFNLFPHMTALENI-IEAPIHVLGTPRAEALEQARGLLARVGL----ADKANHYPSMLSGG 159
Cdd:PRK14267 84 R----------REVGMVFQYPNPFPHLTIYDNVaIGVKLNGLVKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 160 QQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEgMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPP 239
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPT 232
|
250 260
....*....|....*....|
gi 1525903658 240 EQIFSHPSHPRTRAFLSRVL 259
Cdd:PRK14267 233 RKVFENPEHELTEKYVTGAL 252
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
9-240 |
3.29e-50 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 174.14 E-value: 3.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSF----GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGyrersdgSLV 84
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVA-------TLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 85 RDSernIARQRRD-IGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQR 163
Cdd:PRK10535 77 ADA---LAQLRREhFGFIFQRYHLLSHLTAAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525903658 164 VAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREvADRVVVLDQGELIEQGPPE 240
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQ 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
7-237 |
4.74e-50 |
|
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: 163.62 E-value: 4.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 7 ELIIDAQDLHKSFgDLQILKGISlqvrrGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgsLVRD 86
Cdd:cd03297 1 MLCVDIEKRLPDF-TLKIDFDLN-----EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-----------VLFD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 87 SERNI--ARQRRDIGMVFQRFNLFPHMTALENIieapihVLGTPRAEALE---QARGLLARVGLADKANHYPSMLSGGQQ 161
Cdd:cd03297 64 SRKKInlPPQQRKIGLVFQQYALFPHLNVRENL------AFGLKRKRNREdriSVDELLDLLGLDHLLNRYPAQLSGGEK 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525903658 162 QRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQG 237
Cdd:cd03297 138 QRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
9-231 |
1.38e-49 |
|
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: 162.60 E-value: 1.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSF-----GDLQI--LKGISLQVRRGEVVVLIGASGSGKTTFIRCI--NLLEDiqGGRIRVngramgyreRS 79
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYLPD--SGSILV---------RH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 80 DGS---LVRDSERNIARQRRD-IGMVFQRFNLFPHMTALEnIIEAPIHVLGTPRAEALEQARGLLARVGLADKANH-YPS 154
Cdd:COG4778 73 DGGwvdLAQASPREILALRRRtIGYVSQFLRVIPRVSALD-VVAEPLLERGVDREEARARARELLARLNLPERLWDlPPA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525903658 155 MLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQG 231
Cdd:COG4778 152 TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
24-248 |
1.43e-49 |
|
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: 173.10 E-value: 1.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdseRNIARQ--RRDIGMV 101
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL---------------RQIDPAslRRQIGVV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 102 FQRFNLFpHMTALENIieapihVLGTPRA--EALEQArglLARVGLADKANHYP-----------SMLSGGQQQRVAIAR 168
Cdd:COG2274 555 LQDVFLF-SGTIRENI------TLGDPDAtdEEIIEA---ARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 169 ALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAeEGMTMVVVTHEMGFAREvADRVVVLDQGELIEQGPPEQIFSHPSH 248
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGL 702
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
10-242 |
1.62e-49 |
|
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: 162.15 E-value: 1.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgSLVRDSeR 89
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGH----------DVVREP-R 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIarqRRDIGMVFQRFNLFPHMTALENI-IEAPIHvlGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIAR 168
Cdd:cd03265 70 EV---RRRIGIVFQDLSVDDELTGWENLyIHARLY--GVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 169 ALAMKPQAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQI 242
Cdd:cd03265 145 SLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-242 |
4.24e-49 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 168.66 E-value: 4.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 6 DELIIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAmgYRERSdgslVR 85
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEP--VRFRS----PR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 86 DSerniarQRRDIGMVFQRFNLFPHMTALENIieapihVLGTP--------RAEALEQARGLLARVGLADKANHYPSMLS 157
Cdd:COG1129 75 DA------QAAGIAIIHQELNLVPNLSVAENI------FLGREprrgglidWRAMRRRARELLARLGLDIDPDTPVGDLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 158 GGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQG 237
Cdd:COG1129 143 VAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTG 222
|
....*
gi 1525903658 238 PPEQI 242
Cdd:COG1129 223 PVAEL 227
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
10-247 |
5.76e-49 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 164.79 E-value: 5.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQI----LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgsLVR 85
Cdd:NF040933 3 VRVENVTKIFKKGKKevvaLDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDK-----------LVA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 86 DSERNIAR-QRRDIGMVFQRFNLFPHMTALENiIEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRV 164
Cdd:NF040933 72 SPGKIIVPpEDRNIGMVFQNWALYPNMTVFDN-IAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 165 AIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIF 243
Cdd:NF040933 151 ALARALVKNPQVLLLDEPFSNLDARIRDSARALVKKIQRElKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIY 230
|
....
gi 1525903658 244 SHPS 247
Cdd:NF040933 231 DNPA 234
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
12-232 |
1.12e-48 |
|
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: 157.79 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 12 AQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdSERNI 91
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI-------------AKLPL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 92 ARQRRDIGMVFQrfnlfphmtaleniieapihvlgtpraealeqargllarvgladkanhypsmLSGGQQQRVAIARALA 171
Cdd:cd00267 69 EELRRRIGYVPQ----------------------------------------------------LSGGQRQRVALARALL 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525903658 172 MKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGE 232
Cdd:cd00267 97 LNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
7-256 |
1.93e-48 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 160.71 E-value: 1.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 7 ELIIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQ-----GGRIRVNGRAMgYRERSDg 81
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNI-YSPRTD- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 82 slvrdsernIARQRRDIGMVFQRFNLFPhMTALENIIEApIHVLGTPRAEALEQA-----RGLLARVGLADKANHYPSML 156
Cdd:PRK14239 81 ---------TVDLRKEIGMVFQQPNPFP-MSIYENVVYG-LRLKGIKDKQVLDEAvekslKGASIWDEVKDRLHDSALGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 157 SGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEgMTMVVVTHEMGFAREVADRVVVLDQGELIEQ 236
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEY 228
|
250 260
....*....|....*....|
gi 1525903658 237 GPPEQIFSHPSHPRTRAFLS 256
Cdd:PRK14239 229 NDTKQMFMNPKHKETEDYIS 248
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-241 |
2.13e-48 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 168.03 E-value: 2.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 20 GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyRERSDGSLvrdserniarqRRDIG 99
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI--RDLTLESL-----------RRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 100 MVFQRFNLFpHMTALENIIeapihvLGTPRA--EALEQArglLARVGLADKANHYP-----------SMLSGGQQQRVAI 166
Cdd:COG1132 418 VVPQDTFLF-SGTIRENIR------YGRPDAtdEEVEEA---AKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAI 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 167 ARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAeEGMTMVVVTHEMGFAREvADRVVVLDQGELIEQGPPEQ 241
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEE 560
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
9-256 |
2.74e-48 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 162.44 E-value: 2.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSF----------GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAmgyrer 78
Cdd:PRK11308 5 LLQAIDLKKHYpvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQD------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 79 sdgsLVRDSERNIARQRRDIGMVFQR--FNLFPHMTaLENIIEAPIhVLGT--PRAEALEQARGLLARVGL-ADKANHYP 153
Cdd:PRK11308 79 ----LLKADPEAQKLLRQKIQIVFQNpyGSLNPRKK-VGQILEEPL-LINTslSAAERREKALAMMAKVGLrPEHYDRYP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 154 SMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGE 232
Cdd:PRK11308 153 HMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGR 232
|
250 260
....*....|....*....|....
gi 1525903658 233 LIEQGPPEQIFSHPSHPRTRAFLS 256
Cdd:PRK11308 233 CVEKGTKEQIFNNPRHPYTQALLS 256
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
11-237 |
3.72e-48 |
|
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: 157.21 E-value: 3.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 11 DAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgSLVRDSERN 90
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGK----------DLASLSPKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 91 IARQrrdIGMVFQrfnlfphmtaleniieapihvlgtpraealeqargLLARVGLADKANHYPSMLSGGQQQRVAIARAL 170
Cdd:cd03214 71 LARK---IAYVPQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARAL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525903658 171 AMKPQAMLFDEPTSALDPETVGEVLQVMKELA-EEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQG 237
Cdd:cd03214 113 AQEPPILLLDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-231 |
3.93e-48 |
|
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: 158.47 E-value: 3.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 12 AQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCI-NLLEDIQGgRIRVNGRamgyrersdgslvrdserN 90
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIlGLLKPTSG-SIRVFGK------------------P 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 91 IARQRRDIGMVFQRFNL---FPhMTALENI---IEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRV 164
Cdd:cd03235 63 LEKERKRIGYVPQRRSIdrdFP-ISVRDVVlmgLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525903658 165 AIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQG 231
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
23-233 |
4.31e-48 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 158.73 E-value: 4.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 23 QILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRA---MGYRERsdgslvrdsernIARQRRDIG 99
Cdd:NF038007 19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEvtnLSYSQK------------IILRRELIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 100 MVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAMLF 179
Cdd:NF038007 87 YIFQSFNLIPHLSIFDNV-ALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 180 DEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGfAREVADRVVVLDQGEL 233
Cdd:NF038007 166 DEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-242 |
1.82e-47 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 159.50 E-value: 1.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRersdgslvrdse 88
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 rniarQRRDIG-MVFQRfNLFPHMTALENIIE-APIHvlGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAI 166
Cdd:COG4152 69 -----DRRRIGyLPEER-GLYPKMKVGEQLVYlARLK--GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525903658 167 ARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQI 242
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-255 |
2.67e-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: 159.97 E-value: 2.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 40 LIGASGSGKTTFIRCINLLEDIQGGRIRVNGramgyrersdgslvrDSERNIARQRRDIGMVFQRFNLFPHMTALENIiE 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDG---------------EDVTNVPPHLRHINMVFQSYALFPHMTVEENV-A 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 120 APIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMK 199
Cdd:TIGR01187 65 FGLKMRKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1525903658 200 ELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPSHPRTRAFL 255
Cdd:TIGR01187 145 TIQEQlGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-256 |
3.94e-47 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 157.00 E-value: 3.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGgRIRVNGRAMgyrerSDGSLVrdSER 89
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYP-EARVSGEVY-----LDGQDI--FKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPHMTALENIIEAP-IHVLGTPRAEALEQARGLLARVGL----ADKANHYPSMLSGGQQQRV 164
Cdd:PRK14247 76 DVIELRRRVQMVFQIPNPIPNLSIFENVALGLkLNRLVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 165 AIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEgMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFS 244
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
250
....*....|..
gi 1525903658 245 HPSHPRTRAFLS 256
Cdd:PRK14247 235 NPRHELTEKYVT 246
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
9-246 |
3.91e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 155.24 E-value: 3.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGD-LQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSdgslvrds 87
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKS-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 ernIARQRRDIGMVFQRFN--LFPHmTALENIIEAPIHvLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVA 165
Cdd:PRK13639 73 ---LLEVRKTVGIVFQNPDdqLFAP-TVEEDVAFGPLN-LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 166 IARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSH 245
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
.
gi 1525903658 246 P 246
Cdd:PRK13639 228 I 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
10-244 |
4.44e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 156.01 E-value: 4.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFG-----DLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSDGSLV 84
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 85 RDSE-----------RNIARQRRDIGMVFQ--RFNLFpHMTALENIIEAPIHvLGTPRAEALEQARGLLARVGL-ADKAN 150
Cdd:PRK13651 83 VLEKlviqktrfkkiKKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVS-MGVSKEEAKKRAAKYIELVGLdESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 151 HYPSMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQ 230
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250
....*....|....
gi 1525903658 231 GELIEQGPPEQIFS 244
Cdd:PRK13651 241 GKIIKDGDTYDILS 254
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-256 |
4.61e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 155.25 E-value: 4.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 12 AQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINllediqggriRVNGRAMGYRERSD---GSLVRDSE 88
Cdd:PRK14271 24 AVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLN----------RMNDKVSGYRYSGDvllGGRSIFNY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 RNIARQRRDIGMVFQRFNLFPhMTALENIIEAPIHVLGTPRAEALEQARGLLARVGL----ADKANHYPSMLSGGQQQRV 164
Cdd:PRK14271 94 RDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 165 AIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEgMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFS 244
Cdd:PRK14271 173 CLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
250
....*....|..
gi 1525903658 245 HPSHPRTRAFLS 256
Cdd:PRK14271 252 SPKHAETARYVA 263
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-184 |
7.61e-46 |
|
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: 150.49 E-value: 7.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERsdgslvrdserniARQRRDIGMVFQR 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER-------------KSLRKEIGYVFQD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 105 FNLFPHMTALENIIEaPIHVLGTPRAEALEQARGLLARVGLADKANH----YPSMLSGGQQQRVAIARALAMKPQAMLFD 180
Cdd:pfam00005 68 PQLFPRLTVRENLRL-GLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLD 146
|
....
gi 1525903658 181 EPTS 184
Cdd:pfam00005 147 EPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
10-232 |
7.80e-46 |
|
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: 151.00 E-value: 7.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGD--LQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAmgYRERSDGSLvrds 87
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD--LRDLDLESL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 erniarqRRDIGMVFQRFNLFpHMTALENIieapihvlgtpraealeqargllarvgladkanhypsmLSGGQQQRVAIA 167
Cdd:cd03228 75 -------RKNIAYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 168 RALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAeEGMTMVVVTHEMGFAREvADRVVVLDQGE 232
Cdd:cd03228 109 RALLRDPPILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-258 |
8.74e-46 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 153.73 E-value: 8.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAmgyrersdgsLVRDSER 89
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRP----------LAAWSPW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRrdiGMVFQRFNL-FPhMTALEnIIEAPIHVLGTPRAEALEQARGLLARVGLADKAN-HYPSmLSGGQQQRVAIA 167
Cdd:COG4559 72 ELARRR---AVLPQHSSLaFP-FTVEE-VVALGRAPHGSSAAQDRQIVREALALVGLAHLAGrSYQT-LSGGEQQRVQLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 168 RALA-------MKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPE 240
Cdd:COG4559 146 RVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPE 225
|
250
....*....|....*...
gi 1525903658 241 QIFshpshprTRAFLSRV 258
Cdd:COG4559 226 EVL-------TDELLERV 236
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
17-242 |
1.64e-45 |
|
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: 154.47 E-value: 1.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 17 KSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgslvrDSERNIARQRR 96
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGY--------------DVVREPRKVRR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 97 DIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQA 176
Cdd:TIGR01188 67 SIGIVPQYASVDEDLTGRENL-EMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525903658 177 MLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQI 242
Cdd:TIGR01188 146 LFLDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
25-244 |
2.03e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 153.70 E-value: 2.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGramgyrersdgsLVRDSERNIARQRRDIGMVFQR 104
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG------------LDTSDEENLWDIRNKAGMVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 105 fnlfPHMTALENIIEAPIHV----LGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAMLFD 180
Cdd:PRK13633 94 ----PDNQIVATIVEEDVAFgpenLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 181 EPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREvADRVVVLDQGELIEQGPPEQIFS 244
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFK 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-245 |
3.00e-45 |
|
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: 159.54 E-value: 3.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGD-LQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdSE 88
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL-------------SD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 RNIARQRRDIGMVFQRFNLFpHMTALENIieapihVLGTPRA--EALEQArglLARVGLADKANHYP-----------SM 155
Cdd:COG4988 404 LDPASWRRQIAWVPQNPYLF-AGTIRENL------RLGRPDAsdEELEAA---LEAAGLDEFVAALPdgldtplgeggRG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 156 LSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAeEGMTMVVVTHEMGFAREvADRVVVLDQGELIE 235
Cdd:COG4988 474 LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDGRIVE 551
|
250
....*....|
gi 1525903658 236 QGPPEQIFSH 245
Cdd:COG4988 552 QGTHEELLAK 561
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-246 |
4.56e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 153.85 E-value: 4.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 5 SDELIIDAQDLH-----KSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERS 79
Cdd:PRK13631 17 SDDIILRVKNLYcvfdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 80 DGSLVRDSERNIA---RQRRDIGMVFQrfnlFPHMTALENIIEAPIH----VLGTPRAEALEQARGLLARVGLADK-ANH 151
Cdd:PRK13631 97 HELITNPYSKKIKnfkELRRRVSMVFQ----FPEYQLFKDTIEKDIMfgpvALGVKKSEAKKLAKFYLNKMGLDDSyLER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 152 YPSMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQG 231
Cdd:PRK13631 173 SPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKG 252
|
250
....*....|....*
gi 1525903658 232 ELIEQGPPEQIFSHP 246
Cdd:PRK13631 253 KILKTGTPYEIFTDQ 267
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-234 |
1.28e-44 |
|
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: 149.33 E-value: 1.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 11 DAQDLHKSFGDLQ-ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERsdgslvrdser 89
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 niarqRRDIGMVFQ--RFNLFPHMTALENIIEAPihvlgtPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIA 167
Cdd:cd03226 70 -----RKSIGYVMQdvDYQLFTDSVREELLLGLK------ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525903658 168 RALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELI 234
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-258 |
1.95e-44 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 152.55 E-value: 1.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 22 LQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgSLVRDSERNIARQRRDIGMV 101
Cdd:PRK15079 34 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGK----------DLLGMKDDEWRAVRSDIQMI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 102 FQR--FNLFPHMTALEnIIEAPIHVL--GTPRAEALEQARGLLARVGL-ADKANHYPSMLSGGQQQRVAIARALAMKPQA 176
Cdd:PRK15079 104 FQDplASLNPRMTIGE-IIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 177 MLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPSHPRTRAFL 255
Cdd:PRK15079 183 IICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALM 262
|
...
gi 1525903658 256 SRV 258
Cdd:PRK15079 263 SAV 265
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
9-252 |
4.29e-44 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 149.60 E-value: 4.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSF---------GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRers 79
Cdd:COG4167 4 LLEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 80 dgslvrdserNIARQRRDIGMVFQRFN--LFPHMTaLENIIEAPIHvLGT--PRAEALEQARGLLARVGL-ADKANHYPS 154
Cdd:COG4167 81 ----------DYKYRCKHIRMIFQDPNtsLNPRLN-IGQILEEPLR-LNTdlTAEEREERIFATLRLVGLlPEHANFYPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 155 MLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGEL 233
Cdd:COG4167 149 MLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEV 228
|
250
....*....|....*....
gi 1525903658 234 IEQGPPEQIFSHPSHPRTR 252
Cdd:COG4167 229 VEYGKTAEVFANPQHEVTK 247
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-241 |
4.85e-44 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 155.18 E-value: 4.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 5 SDELIIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAmgyrersdgslV 84
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP-----------V 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 85 RDSERNIARQRRdIGMVFQRFNLFPHMTALENII--EAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQ 162
Cdd:COG3845 70 RIRSPRDAIALG-IGMVHQHFMLVPNLTVAENIVlgLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1525903658 163 RVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQ 241
Cdd:COG3845 149 RVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-256 |
5.32e-44 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 149.55 E-value: 5.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 7 ELIIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGrIRVNGRAMGYrersdGSLVRD 86
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKVTFH-----GKNLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 87 SERNIARQRRDIGMVFQRFNLFPHmTALENIIEAP-IHVLGTPRAEALEQArglLARVGL----ADKANHYPSMLSGGQQ 161
Cdd:PRK14243 82 PDVDPVEVRRRIGMVFQKPNPFPK-SIYDNIAYGArINGYKGDMDELVERS---LRQAALwdevKDKLKQSGLSLSGGQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 162 QRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEgMTMVVVTHEMGFAREVADRVVVLD---------QGE 232
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNveltegggrYGY 236
|
250 260
....*....|....*....|....
gi 1525903658 233 LIEQGPPEQIFSHPSHPRTRAFLS 256
Cdd:PRK14243 237 LVEFDRTEKIFNSPQQQATRDYVS 260
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-234 |
1.36e-43 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 145.26 E-value: 1.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSDgslvrdser 89
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 niARQRRdIGMVFQrfnlfphmtaleniieapihvlgtpraealeqargllarvgladkanhypsmLSGGQQQRVAIARA 169
Cdd:cd03216 72 --ARRAG-IAMVYQ----------------------------------------------------LSVGERQMVEIARA 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELI 234
Cdd:cd03216 97 LARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
15-257 |
1.74e-43 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 150.92 E-value: 1.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 15 LHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQG--GRIRVNGRAMGYrersdgslvrdsernIA 92
Cdd:TIGR03258 11 LRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGltGRIAIADRDLTH---------------AP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 93 RQRRDIGMVFQRFNLFPHMTALENIIEApIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAM 172
Cdd:TIGR03258 76 PHKRGLALLFQNYALFPHLKVEDNVAFG-LRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 173 KPQAMLFDEPTSALDPETVGEVLQVMKELAEE--GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPSHPR 250
Cdd:TIGR03258 155 EPDVLLLDEPLSALDANIRANMREEIAALHEElpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGF 234
|
....*..
gi 1525903658 251 TRAFLSR 257
Cdd:TIGR03258 235 AAEFLGA 241
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
13-256 |
4.64e-43 |
|
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: 146.13 E-value: 4.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 13 QDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSdgslvrdserniA 92
Cdd:TIGR03410 4 SNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPH------------E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 93 RQRRDIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQA-------RGLLARVGladkanhypSMLSGGQQQRVA 165
Cdd:TIGR03410 72 RARAGIAYVPQGREIFPRLTVEENL-LTGLAALPRRSRKIPDEIyelfpvlKEMLGRRG---------GDLSGGQQQQLA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 166 IARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIfs 244
Cdd:TIGR03410 142 IARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL-- 219
|
250
....*....|..
gi 1525903658 245 hpSHPRTRAFLS 256
Cdd:TIGR03410 220 --DEDKVRRYLA 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
10-244 |
9.20e-43 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 146.07 E-value: 9.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCinLLEDIQ--GGRIRVNGRAmgyrersdgsLVRDS 87
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRA--LSGELSpdSGEVRLNGRP----------LADWS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 ERNIARQRrdiGMVFQRFNL-FPhMTALEnIIE---APiHVLGTPRAEALEQArgLLARVGLADKAN-HYPSmLSGGQQQ 162
Cdd:PRK13548 71 PAELARRR---AVLPQHSSLsFP-FTVEE-VVAmgrAP-HGLSRAEDDALVAA--ALAQVDLAHLAGrDYPQ-LSGGEQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 163 RVAIARALA------MKPQAMLFDEPTSALDPETVGEVLQVMKELA-EEGMTMVVVTHEMGFAREVADRVVVLDQGELIE 235
Cdd:PRK13548 142 RVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRLVA 221
|
....*....
gi 1525903658 236 QGPPEQIFS 244
Cdd:PRK13548 222 DGTPAEVLT 230
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-246 |
4.42e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 145.16 E-value: 4.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVngramGYRERSDGSlvrdSERNIARQRRDIGMVFQr 104
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-----GERVITAGK----KNKKLKPLRKKVGIVFQ- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 105 fnlFPHM-----TALENIIEAPIHvLGTPRAEALEQARGLLARVGL-ADKANHYPSMLSGGQQQRVAIARALAMKPQAML 178
Cdd:PRK13634 93 ---FPEHqlfeeTVEKDICFGPMN-FGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1525903658 179 FDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHP 246
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-258 |
8.85e-42 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 143.64 E-value: 8.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGgRIRVNGRAMGYrersdGSLVRDSER 89
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELES-EVRVEGRVEFF-----NQNIYERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPhMTALENIIEApIHVLG-TPRAEALEQARGLLARVGLADKANH--YPSML--SGGQQQRV 164
Cdd:PRK14258 82 NLNRLRRQVSMVHPKPNLFP-MSVYDNVAYG-VKIVGwRPKLEIDDIVESALKDADLWDEIKHkiHKSALdlSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 165 AIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELA-EEGMTMVVVTHEMGFAREVADRVVVLDQ-----GELIEQGP 238
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGL 239
|
250 260
....*....|....*....|.
gi 1525903658 239 PEQIFSHPSHPRTRAF-LSRV 258
Cdd:PRK14258 240 TKKIFNSPHDSRTREYvLSRL 260
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
10-230 |
1.47e-41 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 141.46 E-value: 1.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgslvrDSER 89
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGE--------------PIRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPHMTALENIIeapIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARA 169
Cdd:COG4133 69 AREDYRRRLAYLGHADGLKPELTVRENLR---FWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTH-EMGFArevADRVVVLDQ 230
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqPLELA---AARVLDLGD 204
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
7-241 |
1.91e-41 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 142.84 E-value: 1.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 7 ELIIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLL---EDIQGGRIRVNGRAMgyreRSDGSL 83
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTV----QREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 84 VRDsernIARQRRDIGMVFQRFNLFPHMTALENIIeapIHVLG-TP---------RAEALEQARGLLARVGLADKANHYP 153
Cdd:PRK09984 78 ARD----IRKSRANTGYIFQQFNLVNRLSVLENVL---IGALGsTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 154 SMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAE-EGMTMVVVTHEMGFAREVADRVVVLDQGE 232
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
....*....
gi 1525903658 233 LIEQGPPEQ 241
Cdd:PRK09984 231 VFYDGSSQQ 239
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
10-237 |
2.23e-41 |
|
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: 140.88 E-value: 2.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCIN--LLEDiqGGRIRVNGRAMGYRERsdgslvrds 87
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILgiILPD--SGEVLFDGKPLDIAAR--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 erniarqrRDIGMVFQRFNLFPHMTALENIIE-APIHvlGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAI 166
Cdd:cd03269 70 --------NRIGYLPEERGLYPKMKVIDQLVYlAQLK--GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525903658 167 ARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQG 237
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-237 |
2.50e-41 |
|
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: 141.09 E-value: 2.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 29 SLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSDgslvrdserniarqrRDIGMVFQRFNLF 108
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD---------------RPVSMLFQENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 109 PHMTALENIieapihVLG-TPRAEALEQARG----LLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEPT 183
Cdd:cd03298 83 AHLTVEQNV------GLGlSPGLKLTAEDRQaievALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 184 SALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQG 237
Cdd:cd03298 157 AALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-255 |
2.77e-41 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 142.49 E-value: 2.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 2 AHKSDELIIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRersdg 81
Cdd:PRK14246 3 AGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFG----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 82 slvRDSER-NIARQRRDIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQ-ARGLLARVGL----ADKANHYPSM 155
Cdd:PRK14246 78 ---KDIFQiDAIKLRKEVGMVFQQPNPFPHLSIYDNI-AYPLKSHGIKEKREIKKiVEECLRKVGLwkevYDRLNSPASQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 156 LSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEgMTMVVVTHEMGFAREVADRVVVLDQGELIE 235
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
250 260
....*....|....*....|
gi 1525903658 236 QGPPEQIFSHPSHPRTRAFL 255
Cdd:PRK14246 233 WGSSNEIFTSPKNELTEKYV 252
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
7-240 |
2.92e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 142.57 E-value: 2.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 7 ELIIDAQDLHKSFGD-LQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvr 85
Cdd:PRK13647 2 DNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 86 dSERNIARQRRDIGMVFQRFN--LFPhMTALENIIEAPIHvLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQR 163
Cdd:PRK13647 70 -NAENEKWVRSKVGLVFQDPDdqVFS-STVWDDVAFGPVN-MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525903658 164 VAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPE 240
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
24-247 |
3.07e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 143.02 E-value: 3.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCIN---LLEDIQGGRIRVNGRAMGyrersdgslvrdsERNIARQRRDIGM 100
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINgllLPDDNPNSKITVDGITLT-------------AKTVWDIREKVGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 101 VFQR-FNLFPHMT-------ALENiieapihvLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAM 172
Cdd:PRK13640 89 VFQNpDNQFVGATvgddvafGLEN--------RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525903658 173 KPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFArEVADRVVVLDQGELIEQGPPEQIFSHPS 247
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
25-258 |
6.12e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 142.28 E-value: 6.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGyrersdgslVRDSERNIARQRRDIGMVFQr 104
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHIT---------PETGNKNLKKLRKKVSLVFQ- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 105 fnlFPHM-----TALENIIEAPIHvLGTPRAEALEQARGLLARVGLADK-ANHYPSMLSGGQQQRVAIARALAMKPQAML 178
Cdd:PRK13641 93 ---FPEAqlfenTVLKDVEFGPKN-FGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 179 FDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHP--------SHPR 250
Cdd:PRK13641 169 LDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKewlkkhylDEPA 248
|
....*...
gi 1525903658 251 TRAFLSRV 258
Cdd:PRK13641 249 TSRFASKL 256
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
10-257 |
6.47e-41 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 147.61 E-value: 6.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSF--GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAmgyrersdgslVRDS 87
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD-----------LRDL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 ERNIARQRrdIGMVFQRFNLFpHMTALENIIeapihvLGTPRA--EALEQArglLARVGLADKANHYP-----------S 154
Cdd:COG4987 403 DEDDLRRR--IAVVPQRPHLF-DTTLRENLR------LARPDAtdEELWAA---LERVGLGDWLAALPdgldtwlgeggR 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 155 MLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAeEGMTMVVVTHEMGfAREVADRVVVLDQGELI 234
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLA-GLERMDRILVLEDGRIV 548
|
250 260
....*....|....*....|...
gi 1525903658 235 EQGPPEQIFSHpsHPRTRAFLSR 257
Cdd:COG4987 549 EQGTHEELLAQ--NGRYRQLYQR 569
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
7-243 |
7.28e-41 |
|
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: 140.99 E-value: 7.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 7 ELIIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINllEDI---QGGRIRVNGRAMGyRErsdgsl 83
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLIT--GDLpptYGNDVRLFGERRG-GE------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 84 vrdserNIARQRRDIGMV----FQRFNlfPHMTALENIIEAPIHVLGTPR---AEALEQARGLLARVGLADKANHYPSML 156
Cdd:COG1119 72 ------DVWELRKRIGLVspalQLRFP--RDETVLDVVLSGFFDSIGLYReptDEQRERARELLELLGLAHLADRPFGTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 157 SGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEG-MTMVVVTH---EM--GFarevaDRVVVLDQ 230
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhveEIppGI-----THVLLLKD 218
|
250
....*....|...
gi 1525903658 231 GELIEQGPPEQIF 243
Cdd:COG1119 219 GRVVAAGPKEEVL 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
23-228 |
1.21e-40 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 140.77 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 23 QILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersDGSlvrDSERniarqrrdiGMVF 102
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV------TGP---GADR---------GVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 103 QRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEP 182
Cdd:COG4525 83 QKDALLPWLNVLDNV-AFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1525903658 183 TSALDPETVGEvlqvMKEL-----AEEGMTMVVVTHEMGFAREVADRVVVL 228
Cdd:COG4525 162 FGALDALTREQ----MQELlldvwQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
17-247 |
1.22e-40 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 143.63 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 17 KSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSDgslvrdserniarqrR 96
Cdd:PRK11000 11 KAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE---------------R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 97 DIGMVFQRFNLFPHMTALENiIEAPIHVLGTPRAEA---LEQARGLLARVGLADKAnhyPSMLSGGQQQRVAIARALAMK 173
Cdd:PRK11000 76 GVGMVFQSYALYPHLSVAEN-MSFGLKLAGAKKEEInqrVNQVAEVLQLAHLLDRK---PKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525903658 174 PQAMLFDEPTSALDP----ETVGEVLQVMKELaeeGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPS 247
Cdd:PRK11000 152 PSVFLLDEPLSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
10-237 |
1.24e-40 |
|
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: 138.89 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGyrersdgslvrdseR 89
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--------------K 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRdIGMVFQRFNLFPHMTALENIIeapIH--VLGTPRAEALEqargLLARVGLADKANHYPSMLSGGQQQRVAIA 167
Cdd:cd03268 67 NIEALRR-IGALIEAPGFYPNLTARENLR---LLarLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 168 RALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQG 237
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
20-218 |
1.24e-40 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 138.32 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 20 GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYrersdgslvrdSERNIARQRRDIG 99
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDY-----------SRKGLLERRQRVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 100 MVFQRFN--LFpHMTALENIIEAPIHvLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAM 177
Cdd:TIGR01166 72 LVFQDPDdqLF-AADVDQDVAFGPLN-LGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1525903658 178 LFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFA 218
Cdd:TIGR01166 150 LLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
5-258 |
1.46e-40 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 144.02 E-value: 1.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 5 SDELIIDAQDLhkSFGdlqiLKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGramgyrerSDGSLV 84
Cdd:PRK10070 30 SKEQILEKTGL--SLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--------VDIAKI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 85 RDSERNIARqRRDIGMVFQRFNLFPHMTALENIIEApIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRV 164
Cdd:PRK10070 96 SDAELREVR-RKKIAMVFQSFALMPHMTVLDNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 165 AIARALAMKPQAMLFDEPTSALDPETVGEVL-QVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIF 243
Cdd:PRK10070 174 GLARALAINPDILLMDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
250
....*....|....*
gi 1525903658 244 SHPSHPRTRAFLSRV 258
Cdd:PRK10070 254 NNPANDYVRTFFRGV 268
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
20-259 |
1.48e-40 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 140.71 E-value: 1.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 20 GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGyrersdgSLVRDSERniaRQRRDIG 99
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLY-------QLDRKQRR---AFRRDVQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 100 MVFQ----RFNlfPHMTALENIIEAPIHVLGTPRAEALEQARGLLARVGL-ADKANHYPSMLSGGQQQRVAIARALAMKP 174
Cdd:TIGR02769 92 LVFQdspsAVN--PRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 175 QAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHpSHPRTRA 253
Cdd:TIGR02769 170 KLIVLDEAVSNLDMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF-KHPAGRN 248
|
....*.
gi 1525903658 254 FLSRVL 259
Cdd:TIGR02769 249 LQSAVL 254
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
9-258 |
1.93e-40 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 143.05 E-value: 1.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYrersdgslvrdse 88
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 rnIARQRRDIGMVFQRFNLFPHMTALENIieapihVLG-----TPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQR 163
Cdd:PRK11607 86 --VPPYQRPINMMFQSYALFPHMTVEQNI------AFGlkqdkLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 164 VAIARALAMKPQAMLFDEPTSALDPETVGEV-LQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQI 242
Cdd:PRK11607 158 VALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
250
....*....|....*.
gi 1525903658 243 FSHPSHPRTRAFLSRV 258
Cdd:PRK11607 238 YEHPTTRYSAEFIGSV 253
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
9-246 |
2.94e-40 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 139.35 E-value: 2.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAmgyrersdgsLVRDSE 88
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQH----------IEGLPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 RNIARQrrdiGMV--FQRFNLFPHMTALENIIEAP-IHV--------LGTPR-----AEALEQARGLLARVGLADKANHY 152
Cdd:PRK11300 75 HQIARM----GVVrtFQHVRLFREMTVIENLLVAQhQQLktglfsglLKTPAfrraeSEALDRAATWLERVGLLEHANRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 153 PSMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQG 231
Cdd:PRK11300 151 AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
250
....*....|....*
gi 1525903658 232 ELIEQGPPEQIFSHP 246
Cdd:PRK11300 231 TPLANGTPEEIRNNP 245
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
10-239 |
3.21e-40 |
|
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: 138.41 E-value: 3.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQ--ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgslvrDS 87
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY--------------SI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 ERNIARQRRDIGMVFQRFNLFPHMTALENI-IEAPIHvlGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAI 166
Cdd:cd03263 67 RTDRKAARQSLGYCPQFDALFDELTVREHLrFYARLK--GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525903658 167 ARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAeEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPP 239
Cdd:cd03263 145 AIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
22-259 |
1.05e-39 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 138.28 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 22 LQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSDgslvrdsernIARQRRDIGMV 101
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ----------RKAFRRDIQMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 102 FQ----RFNlfPHMTALENIIEAPIHVLGTPRAEALEQARGLLARVGLADK-ANHYPSMLSGGQQQRVAIARALAMKPQA 176
Cdd:PRK10419 95 FQdsisAVN--PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 177 MLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGP--PEQIFSHPShprTRA 253
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPvgDKLTFSSPA---GRV 249
|
....*.
gi 1525903658 254 FLSRVL 259
Cdd:PRK10419 250 LQNAVL 255
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
10-246 |
1.15e-39 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 140.75 E-value: 1.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSF-GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSDgslvrdse 88
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 rniarqrRDIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAE----ALEQAR-----GLLARvgladkanhYPSMLSGG 159
Cdd:PRK11650 76 -------RDIAMVFQNYALYPHMSVRENM-AYGLKIRGMPKAEieerVAEAARilelePLLDR---------KPRELSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 160 QQQRVAIARALAMKPQAMLFDEPTSALDPEtvgevLQV-----MKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGEl 233
Cdd:PRK11650 139 QRQRVAMGRAIVREPAVFLFDEPLSNLDAK-----LRVqmrleIQRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGGV- 212
|
250
....*....|....
gi 1525903658 234 IEQ-GPPEQIFSHP 246
Cdd:PRK11650 213 AEQiGTPVEVYEKP 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
14-249 |
2.63e-39 |
|
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: 139.48 E-value: 2.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 14 DLHKSFGDLQIlkGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgsLVRDSERNI-- 91
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR-----------TLFDSRKGIfl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 92 ARQRRDIGMVFQRFNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLLARVGLADKanhYPSMLSGGQQQRVAIARALA 171
Cdd:TIGR02142 71 PPEKRRIGYVFQEARLFPHLSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1525903658 172 MKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPSHP 249
Cdd:TIGR02142 148 SSPRLLLMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLP 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
10-244 |
4.92e-39 |
|
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: 142.25 E-value: 4.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFI---RCINLLEDIQG------------GRIRVNGRA-- 72
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMhvlRGMDQYEPTSGriiyhvalcekcGYVERPSKVge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 73 -----MGYRERSDGSLVRDSERNIARQRRDIGMVFQR-FNLFPHMTALENIIEApIHVLGTPRAEALEQARGLLARVGLA 146
Cdd:TIGR03269 81 pcpvcGGTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEA-LEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 147 DKANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELA-EEGMTMVVVTHEMGFAREVADRV 225
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*....
gi 1525903658 226 VVLDQGELIEQGPPEQIFS 244
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEVVA 258
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
9-244 |
4.97e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 137.29 E-value: 4.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGD-LQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYrersdgslvrdS 87
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDY-----------S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 ERNIARQRRDIGMVFQR--FNLFPhMTALENIIEAPIHvLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVA 165
Cdd:PRK13636 74 RKGLMKLRESVGMVFQDpdNQLFS-ASVYQDVSFGAVN-LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 166 IARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFS 244
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
25-243 |
5.59e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 137.10 E-value: 5.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAmgyrersdgslVRDSERNIARQRRDIGMVFQr 104
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVD-----------ITDKKVKLSDIRKKVGLVFQ- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 105 fnlFPHMTALENIIEAPIHV----LGTPRAEALEQARGLLARVGL-----ADKAnhyPSMLSGGQQQRVAIARALAMKPQ 175
Cdd:PRK13637 91 ---YPEYQLFEETIEKDIAFgpinLGLSEEEIENRVKRAMNIVGLdyedyKDKS---PFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1525903658 176 AMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIF 243
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-243 |
6.23e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 136.66 E-value: 6.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 4 KSDELIIDAQDLHKSFGD--LQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdg 81
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 82 slvrdSERNIARQRRDIGMVFQR-FNLFPHMTA-------LENIIEapihvlgtPRAEALEQARGLLARVGLADKANHYP 153
Cdd:PRK13632 74 -----SKENLKEIRKKIGIIFQNpDNQFIGATVeddiafgLENKKV--------PPKKMKDIIDDLAKKVGMEDYLDKEP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 154 SMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGM-TMVVVTHEMgfaREV--ADRVVVLDQ 230
Cdd:PRK13632 141 QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDM---DEAilADKVIVFSE 217
|
250
....*....|...
gi 1525903658 231 GELIEQGPPEQIF 243
Cdd:PRK13632 218 GKLIAQGKPKEIL 230
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
9-244 |
7.10e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 136.79 E-value: 7.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQ---ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvr 85
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 86 dSERNIARQRRDIGMVFQR-FNLFPHMTaLENIIEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRV 164
Cdd:PRK13650 72 -TEENVWDIRHKIGMVFQNpDNQFVGAT-VEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 165 AIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGfarEVA--DRVVVLDQGELIEQGPPEQ 241
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLD---EVAlsDRVLVMKNGQVESTSTPRE 226
|
...
gi 1525903658 242 IFS 244
Cdd:PRK13650 227 LFS 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
7-236 |
1.48e-38 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 134.14 E-value: 1.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 7 ELIIDAQDLHKSFGD----LQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgS 82
Cdd:PRK10584 4 ENIVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQ----------P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 83 LVRDSERNIARQR-RDIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQ 161
Cdd:PRK10584 74 LHQMDEEARAKLRaKHVGFVFQSFMLIPTLNALENV-ELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525903658 162 QRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREvADRVVVLDQGELIEQ 236
Cdd:PRK10584 153 QRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-258 |
3.31e-38 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 140.76 E-value: 3.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 16 HKSFGDLQILKGISLQVRRGEVVVLIGASGSGKT-TFIRCINLLEDiQGGRIRVNGRAMGYRERSDGSLVRDSERNIARQ 94
Cdd:PRK10261 23 MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMLLRRRSRQVIELSEQSAAQMRHV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 95 R-RDIGMVFQR--FNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLLARVGLADKA---NHYPSMLSGGQQQRVAIAR 168
Cdd:PRK10261 102 RgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAM 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 169 ALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPS 247
Cdd:PRK10261 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQ 261
|
250
....*....|.
gi 1525903658 248 HPRTRAFLSRV 258
Cdd:PRK10261 262 HPYTRALLAAV 272
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-259 |
4.38e-38 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 133.90 E-value: 4.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 5 SDELIIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRvngramgYRERsDGSLV 84
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH-------YRMR-DGQLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 85 RDSERNIARQRR----DIGMVFQ--RFNLFPHMTALENIIEAPIHV----LGTPRAEALEqargLLARVGL-ADKANHYP 153
Cdd:PRK11701 74 DLYALSEAERRRllrtEWGFVHQhpRDGLRMQVSAGGNIGERLMAVgarhYGDIRATAGD----WLERVEIdAARIDDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 154 SMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADRVVVLDQGE 232
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
250 260
....*....|....*....|....*..
gi 1525903658 233 LIEQGPPEQIFSHPSHPRTRAFLSRVL 259
Cdd:PRK11701 230 VVESGLTDQVLDDPQHPYTQLLVSSVL 256
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
10-246 |
5.31e-38 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 133.05 E-value: 5.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersDGSLVRDSEr 89
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQ--------DITKLPMHK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 niaRQRRDIGMVFQRFNLFPHMTALENIIeAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARA 169
Cdd:cd03218 72 ---RARLGIGYLPQEASIFRKLTVEENIL-AVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEmgfARE---VADRVVVLDQGELIEQGPPEQIFSHP 246
Cdd:cd03218 148 LATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHN---VREtlsITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
20-229 |
5.92e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 132.22 E-value: 5.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 20 GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCI--NLLEDIQG-GRIRVNGRAMgyrersdgslvrdseRNIARQRR 96
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagTLSPAFSAsGEVLLNGRRL---------------TALPAEQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 97 DIGMVFQRFNLFPHMTALENIIEA-PIHVLGTPRAEALEQArglLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQ 175
Cdd:COG4136 77 RIGILFQDDLLFPHLSVGENLAFAlPPTIGRAQRRARVEQA---LEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 176 AMLFDEPTSALDPETVGEVLQ-VMKELAEEGMTMVVVTHEMGfAREVADRVVVLD 229
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEE-DAPAAGRVLDLG 207
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
24-236 |
7.54e-38 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 132.63 E-value: 7.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGyrerSDGSLVRDSERNiarqrRDIGMVFQ 103
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMS----KLSSAAKAELRN-----QKLGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 RFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEPT 183
Cdd:PRK11629 95 FHHLLPDFTALENV-AMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 184 SALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVaDRVVVLDQGELIEQ 236
Cdd:PRK11629 174 GNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
23-241 |
1.03e-37 |
|
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: 132.35 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 23 QILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyRERSDGSLvrdserniarqRRDIGMVF 102
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI--REVTLDSL-----------RRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 103 QRFNLFpHMTALENIieapihVLGTPRA--EALEQArgllARVG-LADKANHYPS-----------MLSGGQQQRVAIAR 168
Cdd:cd03253 82 QDTVLF-NDTIGYNI------RYGRPDAtdEEVIEA----AKAAqIHDKIMRFPDgydtivgerglKLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 169 ALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAeEGMTMVVVTHEMgfaREV--ADRVVVLDQGELIEQGPPEQ 241
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRL---STIvnADKIIVLKDGRIVERGTHEE 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-233 |
4.91e-37 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 131.34 E-value: 4.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 13 QDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVnGRAmgyrersdgslvrdserNIA 92
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-GTA-----------------PLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 93 RQRRDIGMVFQRFNLFPHMTALENIieaPIHVLGTPRAEALEQarglLARVGLADKANHYPSMLSGGQQQRVAIARALAM 172
Cdd:PRK11247 78 EAREDTRLMFQDARLLPWKKVIDNV---GLGLKGQWRDAALQA----LAAVGLADRANEWPAALSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525903658 173 KPQAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADRVVVLDQGEL 233
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
9-246 |
7.05e-37 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 130.15 E-value: 7.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGR-----AMgYRersdgsl 83
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlPM-HK------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 84 vrdserniaRQRRDIGMVFQRFNLFPHMTALENIIeAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQR 163
Cdd:COG1137 75 ---------RARLGIGYLPQEASIFRKLTVEDNIL-AVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 164 VAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTmVVVT-HEmgfARE---VADRVVVLDQGELIEQGPP 239
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIG-VLITdHN---VREtlgICDRAYIISEGKVLAEGTP 220
|
....*..
gi 1525903658 240 EQIFSHP 246
Cdd:COG1137 221 EEILNNP 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-245 |
7.20e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 131.41 E-value: 7.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNgramgyrersDGSLVRDSE-RNIARQRRDIGMVFQ 103
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVD----------DTLITSTSKnKDIKQIRKKVGLVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 rfnlFPHM-----TALENIIEAPIHvLGTPRAEALEQARGLLARVGLADKA-NHYPSMLSGGQQQRVAIARALAMKPQAM 177
Cdd:PRK13649 93 ----FPESqlfeeTVLKDVAFGPQN-FGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525903658 178 LFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSH 245
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-256 |
7.48e-37 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 136.37 E-value: 7.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 15 LHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTfiRCINLLEDIQG-GRIRVNGRAMGYRERsdgslvrdseRNIAR 93
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKST--TGLALLRLINSqGEIWFDGQPLHNLNR----------RQLLP 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 94 QRRDIGMVFQRFN--LFPHMTALENIIEA-PIHVLGTPRAEALEQARGLLARVGLADKANH-YPSMLSGGQQQRVAIARA 169
Cdd:PRK15134 360 VRHRIQVVFQDPNssLNPRLNVLQIIEEGlRVHQPTLSAAQREQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPSH 248
Cdd:PRK15134 440 LILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQ 519
|
....*...
gi 1525903658 249 PRTRAFLS 256
Cdd:PRK15134 520 EYTRQLLA 527
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
9-237 |
1.07e-36 |
|
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: 129.02 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDL----QILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgslv 84
Cdd:cd03266 1 MITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 85 rDSERNIARQRRDIGMVFQRFNLFPHMTALENIIE-APIHvlGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQR 163
Cdd:cd03266 68 -DVVKEPAEARRRLGFVSDSTGLYDRLTARENLEYfAGLY--GLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 164 VAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQG 237
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
25-247 |
1.10e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 130.88 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSDGSlvrdserniarqRRDIGMVFQR 104
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGI------------RKLVGIVFQN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 105 FNL-FPHMTALENIIEAPIHvLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEPT 183
Cdd:PRK13644 86 PETqFVGRTVEEDLAFGPEN-LCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 184 SALDPETVGEVLQVMKELAEEGMTMVVVTHEMGfAREVADRVVVLDQGELIEQGPPEQIFSHPS 247
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-231 |
1.45e-36 |
|
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: 129.12 E-value: 1.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgslvrdserNIARQRRDIGMVFQR 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK------------------QITEPGPDRMVVFQN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 105 FNLFPHMTALENIIEAPIHVLGT-PRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEPT 183
Cdd:TIGR01184 63 YSLLPWLTVRENIALAVDRVLPDlSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1525903658 184 SALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQG 231
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
10-237 |
1.90e-36 |
|
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: 128.46 E-value: 1.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGeVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgslvrDSER 89
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ--------------DVLK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQRFNLFPHMTALENIieAPIHVL-GTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIAR 168
Cdd:cd03264 66 QPQKLRRRIGYLPQEFGVYPNFTVREFL--DYIAWLkGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1525903658 169 ALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEgMTMVVVTHEMGFAREVADRVVVLDQGELIEQG 237
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-244 |
2.33e-36 |
|
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: 128.81 E-value: 2.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 21 DLQILKGISLQVRRGEVVVLIGASGSGKTTfirCINLLE---DIQGGRIRVNGramgyrersdgslVRDSERNIARQRRD 97
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLErfyDPTSGEILLDG-------------VDIRDLNLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 98 IGMVFQRFNLFPhMTALENIieapihVLGTPRAEALEQARGllarvglADKANHYP-----------------SMLSGGQ 160
Cdd:cd03249 79 IGLVSQEPVLFD-GTIAENI------RYGKPDATDEEVEEA-------AKKANIHDfimslpdgydtlvgergSQLSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 161 QQRVAIARALAMKPQAMLFDEPTSALDPETVGEVlQVMKELAEEGMTMVVVTHEMGFAREvADRVVVLDQGELIEQGPPE 240
Cdd:cd03249 145 KQRIAIARALLRNPKILLLDEATSALDAESEKLV-QEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHD 222
|
....
gi 1525903658 241 QIFS 244
Cdd:cd03249 223 ELMA 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
24-244 |
5.38e-36 |
|
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: 127.73 E-value: 5.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyRERSDGSLvrdserniarqRRDIGMVFQ 103
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV--RDYTLASL-----------RRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 RFNLFpHMTALENIIEApihVLGTPRAEALEQARGLLARVGLADKANHYPSM-------LSGGQQQRVAIARALAMKPQA 176
Cdd:cd03251 84 DVFLF-NDTVAENIAYG---RPGATREEVEEAARAANAHEFIMELPEGYDTVigergvkLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525903658 177 MLFDEPTSALDPETVGEVLQVMKELAeEGMTMVVVTHEMGFAREvADRVVVLDQGELIEQGPPEQIFS 244
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
28-255 |
5.59e-36 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 130.25 E-value: 5.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 28 ISLQVRRGEVVVLIGASGSGKTTFIRCINllediqgGRIRVNGRAMGYRERSDGslvRDSERNIARQRR-----DIGMVF 102
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIM-------GLIDYPGRVMAEKLEFNG---QDLQRISEKERRnlvgaEVAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 103 Q--RFNLFPHMTALENIIEA-PIHVLGTpRAEALEQARGLLARVGLADKANH---YPSMLSGGQQQRVAIARALAMKPQA 176
Cdd:PRK11022 96 QdpMTSLNPCYTVGFQIMEAiKVHQGGN-KKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 177 MLFDEPTSALDPETVGEVLQVMKELAE-EGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPSHPRTRAFL 255
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALL 254
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-255 |
2.43e-35 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 132.14 E-value: 2.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 23 QILKGISLQVRRGEVVVLIGASGSGKT-TFIRCINLLED----IQGGRIRVNGRamgyrersdgSLVRDSERNIARQRRD 97
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvvYPSGDIRFHGE----------SLLHASEQTLRGVRGN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 98 -IGMVFQR--FNLFPhmtaLENIIEAPIHVLGTPRAEALEQARG----LLARVGL---ADKANHYPSMLSGGQQQRVAIA 167
Cdd:PRK15134 93 kIAMIFQEpmVSLNP----LHTLEKQLYEVLSLHRGMRREAARGeilnCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 168 RALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHP 246
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAP 248
|
....*....
gi 1525903658 247 SHPRTRAFL 255
Cdd:PRK15134 249 THPYTQKLL 257
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
9-259 |
2.95e-35 |
|
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: 126.48 E-value: 2.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCInllediqGGRIRVNGRAMGYRERSDGS--LVRD 86
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCL-------AGRLAPDHGTATYIMRSGAEleLYQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 87 SERNIAR-QRRDIGMVFQ--RFNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLLARVGL-ADKANHYPSMLSGGQQQ 162
Cdd:TIGR02323 76 SEAERRRlMRTEWGFVHQnpRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 163 RVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQ 241
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQ 235
|
250
....*....|....*...
gi 1525903658 242 IFSHPSHPRTRAFLSRVL 259
Cdd:TIGR02323 236 VLDDPQHPYTQLLVSSIL 253
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-237 |
3.29e-35 |
|
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: 125.36 E-value: 3.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 29 SLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgslvrdSERNIARQRRDIGMVFQRFNLF 108
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ---------------SHTGLAPYQRPVSMLFQENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 109 PHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDP 188
Cdd:TIGR01277 83 AHLTVRQNI-GLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1525903658 189 ETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQG 237
Cdd:TIGR01277 162 LLREEMLALVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
23-243 |
1.15e-34 |
|
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: 124.26 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 23 QILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdSERNIARQRRDIGMVF 102
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI-------------RDISRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 103 QRFNLFPHmTALENIIeapihvLGTPRAEALEQARgLLARVGLADKANHYP-----------SMLSGGQQQRVAIARALA 171
Cdd:cd03254 84 QDTFLFSG-TIMENIR------LGRPNATDEEVIE-AAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525903658 172 MKPQAMLFDEPTSALDPETVGEVLQVMKELaEEGMTMVVVTHEMGFAREvADRVVVLDQGELIEQGPPEQIF 243
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-233 |
1.21e-34 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 123.83 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 19 FGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersDGSLVRDSErnIARQRRDI 98
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGH--------DITRLKNRE--VPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 99 GMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAML 178
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNV-AIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 179 FDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGEL 233
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-244 |
1.60e-34 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 129.92 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSF-----GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCI-NLLEDIQGgriRVNGRaMGyRERSDGS 82
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIaGVLEPTSG---EVNVR-VG-DEWVDMT 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 83 LVRDSERniARQRRDIGMVFQRFNLFPHMTALENIIEAPihVLGTPRAEALEQARGLLARVGLADKA-----NHYPSMLS 157
Cdd:TIGR03269 354 KPGPDGR--GRAKRYIGILHQEYDLYPHRTVLDNLTEAI--GLELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 158 GGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQ-VMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQ 236
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
....*...
gi 1525903658 237 GPPEQIFS 244
Cdd:TIGR03269 510 GDPEEIVE 517
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
25-244 |
1.72e-34 |
|
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: 130.76 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSDgslvrdserniarQRRDIGMVFQR 104
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAD-------------LRRNIGYVPQD 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 105 FNLFpHMTALENIIeapihvLGTPRA--EALEQArglLARVGLADKANHYPS-----------MLSGGQQQRVAIARALA 171
Cdd:TIGR03375 548 PRLF-YGTLRDNIA------LGAPYAddEEILRA---AELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALL 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525903658 172 MKPQAMLFDEPTSALDPETVGEVLQVMKELAeEGMTMVVVTHEMGFArEVADRVVVLDQGELIEQGPPEQIFS 244
Cdd:TIGR03375 618 RDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLL-DLVDRIIVMDNGRIVADGPKDQVLE 688
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
9-246 |
3.32e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 124.53 E-value: 3.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDL-HKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdS 87
Cdd:PRK13652 3 LIETRDLcYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI-------------T 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 ERNIARQRRDIGMVFQRFN--LFPhMTALENIIEAPIHvLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVA 165
Cdd:PRK13652 70 KENIREVRKFVGLVFQNPDdqIFS-PTVEQDIAFGPIN-LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 166 IARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFS 244
Cdd:PRK13652 148 IAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFL 227
|
..
gi 1525903658 245 HP 246
Cdd:PRK13652 228 QP 229
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
14-246 |
6.16e-34 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 125.37 E-value: 6.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 14 DLHKSFGDLQIlkGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgsLVRDSERNI-- 91
Cdd:PRK11144 5 NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR-----------VLFDAEKGIcl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 92 ARQRRDIGMVFQRFNLFPHMTALENIIEAPIHVlgtpRAEALEQARGLLarvGLADKANHYPSMLSGGQQQRVAIARALA 171
Cdd:PRK11144 72 PPEKRRIGYVFQDARLFPHYKVRGNLRYGMAKS----MVAQFDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525903658 172 MKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHP 246
Cdd:PRK11144 145 TAPELLLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-244 |
1.38e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 121.61 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 29 SLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGramgyrersdgslvrDSERNIARQRRDIGMVFQRFNLF 108
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG---------------QDHTTTPPSRRPVSMLFQENNLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 109 PHMTALENIieapihVLG-TP----RAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEPT 183
Cdd:PRK10771 84 SHLTVAQNI------GLGlNPglklNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525903658 184 SALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFS 244
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-244 |
1.63e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 122.97 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 23 QILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERsdgslvrdsERNIARQRRDIGMVF 102
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTK---------DKYIRPVRKRIGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 103 QrfnlFPHMTALENIIEAPIHV----LGTPRAEALEQARGLLARVGLA-DKANHYPSMLSGGQQQRVAIARALAMKPQAM 177
Cdd:PRK13646 92 Q----FPESQLFEDTVEREIIFgpknFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525903658 178 LFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFS 244
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
25-233 |
2.43e-33 |
|
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: 119.46 E-value: 2.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdsERNIARQRRDIGMVF-- 102
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV--------------TRRSPRDAIRAGIAYvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 103 ---QRFNLFPHMTALENIIeapihvlgtpraealeqargllarvgladkanhYPSMLSGGQQQRVAIARALAMKPQAMLF 179
Cdd:cd03215 82 edrKREGLVLDLSVAENIA---------------------------------LSSLLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 180 DEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGEL 233
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-258 |
2.47e-33 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 123.30 E-value: 2.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 1 MAHKSDELIIDAQDLHKSF----GDLQILKGISLQVRRGEVVVLIGASGSGKT-TFIRCINLLED--IQGGRIRVNGRam 73
Cdd:PRK09473 4 LAQQQADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAAngRIGGSATFNGR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 74 gyrersdgSLVRDSERNIARQR-RDIGMVFQ--RFNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLLARVGLAD--- 147
Cdd:PRK09473 82 --------EILNLPEKELNKLRaEQISMIFQdpMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEark 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 148 KANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVV 226
Cdd:PRK09473 154 RMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVL 233
|
250 260 270
....*....|....*....|....*....|..
gi 1525903658 227 VLDQGELIEQGPPEQIFSHPSHPRTRAFLSRV 258
Cdd:PRK09473 234 VMYAGRTMEYGNARDVFYQPSHPYSIGLLNAV 265
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-245 |
5.44e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 121.65 E-value: 5.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 21 DLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersDGSLVRDSErnIARQRRDIGM 100
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI------PANLKKIKE--VKRLRKEIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 101 VFQrfnlFPHMTALENIIE-----APIHvLGTPRAEALEQARGLLARVGLA-DKANHYPSMLSGGQQQRVAIARALAMKP 174
Cdd:PRK13645 95 VFQ----FPEYQLFQETIEkdiafGPVN-LGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525903658 175 QAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSH 245
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
20-255 |
7.83e-33 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 121.94 E-value: 7.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 20 GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCI-NLLED---IQGGRIRVNGR---AMGYRERsdgslvrdseRNIA 92
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcGITKDnwhVTADRFRWNGIdllKLSPRER----------RKII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 93 RqrRDIGMVFQ--RFNLFPHMTALENIIEA-PIHVLGTP----RAEALEQARGLLARVGLAD-KA--NHYPSMLSGGQQQ 162
Cdd:COG4170 88 G--REIAMIFQepSSCLDPSAKIGDQLIEAiPSWTFKGKwwqrFKWRKKRAIELLHRVGIKDhKDimNSYPHELTEGECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 163 RVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAE-EGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQ 241
Cdd:COG4170 166 KVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQ 245
|
250
....*....|....
gi 1525903658 242 IFSHPSHPRTRAFL 255
Cdd:COG4170 246 ILKSPHHPYTKALL 259
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
10-247 |
1.77e-32 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 122.64 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRErsdgslVRDSER 89
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS------ARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARQRRDIGMVFQ-------RFNLFPHMTALENIIEapihvlgTPRAeALEQArglLARVGLADKANHYPSMLSGGQQQ 162
Cdd:PRK09536 78 RVASVPQDTSLSFEfdvrqvvEMGRTPHRSRFDTWTE-------TDRA-AVERA---MERTGVAQFADRPVTSLSGGERQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 163 RVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQI 242
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
....*
gi 1525903658 243 FSHPS 247
Cdd:PRK09536 227 LTADT 231
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
10-242 |
2.01e-32 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 119.03 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGyreRSDGslvRDSER 89
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVA---TTPS---RELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIA--RQRRDIGM---VFQ--RFNLFPH----MTALENiieapihvlgtpraEALEQArglLARVGLADKANHYPSMLSG 158
Cdd:COG4604 76 RLAilRQENHINSrltVRElvAFGRFPYskgrLTAEDR--------------EIIDEA---IAYLDLEDLADRYLDELSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 159 GQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQG 237
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
....*
gi 1525903658 238 PPEQI 242
Cdd:COG4604 219 TPEEI 223
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
23-241 |
2.26e-32 |
|
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: 124.68 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 23 QILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdSERNIARQRRDIGMVF 102
Cdd:TIGR03797 467 LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDL-------------AGLDVQAVRRQLGVVL 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 103 QRFNLFPHmTALENIIeapIHVLGTPRaEALEQARgllaRVGLADKANHYP-----------SMLSGGQQQRVAIARALA 171
Cdd:TIGR03797 534 QNGRLMSG-SIFENIA---GGAPLTLD-EAWEAAR----MAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALV 604
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525903658 172 MKPQAMLFDEPTSALDPETvgevlQ--VMKELAEEGMTMVVVTHEMGFAREvADRVVVLDQGELIEQGPPEQ 241
Cdd:TIGR03797 605 RKPRILLFDEATSALDNRT-----QaiVSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDE 670
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
21-244 |
3.54e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 119.04 E-value: 3.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 21 DLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgslvRDSERNIARQRRDIGM 100
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-------------LLTAENVWNLRRKIGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 101 VFQR-FNLFPHMTaLENIIEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAMLF 179
Cdd:PRK13642 86 VFQNpDNQFVGAT-VEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525903658 180 DEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREvADRVVVLDQGELIEQGPPEQIFS 244
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
25-245 |
4.84e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 118.32 E-value: 4.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdSERNIARQRRDIGMVFQR 104
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI-------------TDDNFEKLRKHIGIVFQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 105 ---------------FNLFPHMTALENIIEAPihvlgtprAEALEQargllarVGLADKANHYPSMLSGGQQQRVAIARA 169
Cdd:PRK13648 92 pdnqfvgsivkydvaFGLENHAVPYDEMHRRV--------SEALKQ-------VDMLERADYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREvADRVVVLDQGELIEQGPPEQIFSH 245
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-244 |
6.19e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 118.19 E-value: 6.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 14 DLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYrersdgslvrdSERNIAR 93
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY-----------SKRGLLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 94 QRRDIGMVFQRFNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLLARVGlADKANHYP-SMLSGGQQQRVAIARALAM 172
Cdd:PRK13638 75 LRQQVATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVD-AQHFRHQPiQCLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525903658 173 KPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFS 244
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-235 |
6.44e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 122.48 E-value: 6.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 8 LIIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVngramgyrersdGSLVRds 87
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL------------GETVK-- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 ernIA--RQRRDigmvfqrfNLFPHMTALENIIEApihvlgtpRAEALEQ-ARGLLARVGLA-DKANHYPSMLSGGQQQR 163
Cdd:COG0488 380 ---IGyfDQHQE--------ELDPDKTVLDELRDG--------APGGTEQeVRGYLGRFLFSgDDAFKPVGVLSGGEKAR 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 164 VAIARALAMKPQAMLFDEPTSALDPETvgevLQVMKE-LAE-EGmTMVVVTHEMGFAREVADRVVVLDQGELIE 235
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPTNHLDIET----LEALEEaLDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-256 |
8.56e-32 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 117.49 E-value: 8.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 21 DLQILKGISLQVRRGEVVVLIGASGSGKTtfIRCINLLEDIQGGRIRVNGRAmgyreRSDGSLVRDSerniARQRRDIGM 100
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRV-----LLDGKPVAPC----ALRGRKIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 101 VFQR----FNlfPHMTALENIIEApIHVLGTPRAEAleQARGLLARVGLADKA---NHYPSMLSGGQQQRVAIARALAMK 173
Cdd:PRK10418 84 IMQNprsaFN--PLHTMHTHARET-CLALGKPADDA--TLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 174 PQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPSHPRTR 252
Cdd:PRK10418 159 APFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTR 238
|
....
gi 1525903658 253 AFLS 256
Cdd:PRK10418 239 SLVS 242
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
9-255 |
1.33e-31 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 117.17 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCInllediqGGRIRVNGRAMGYRERSDGSLVRdse 88
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLI-------GGQIAPDHGEILFDGENIPAMSR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 RNIARQRRDIGMVFQRFNLFPHMTALENI-------IEAPIHVLGTPRAEALEQargllarVGLADKANHYPSMLSGGQQ 161
Cdd:PRK11831 77 SRLYTVRKRMSMLFQSGALFTDMNVFDNVayplrehTQLPAPLLHSTVMMKLEA-------VGLRGAAKLMPSELSGGMA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 162 QRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPE 240
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQ 229
|
250
....*....|....*
gi 1525903658 241 QIFSHPShPRTRAFL 255
Cdd:PRK11831 230 ALQANPD-PRVRQFL 243
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-237 |
1.89e-31 |
|
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: 114.96 E-value: 1.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 20 GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCIN--LLEDIQGGRIRVNGRamgyrersdgslvRDSERNIarqRRD 97
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGR-------------PLDKRSF---RKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 98 IGMVFQRFNLFPHMTAleniieapihvlgtprAEALEQARGLlarvgladkanhypSMLSGGQQQRVAIARALAMKPQAM 177
Cdd:cd03213 84 IGYVPQDDILHPTLTV----------------RETLMFAAKL--------------RGLSGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 178 LFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTH----EMgFarEVADRVVVLDQGELIEQG 237
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHqpssEI-F--ELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
28-243 |
1.94e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 117.53 E-value: 1.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 28 ISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVngramgyrersdGSLVRDS---ERNIARQRRDIGMVFQr 104
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV------------GDIVVSStskQKEIKPVRKKVGVVFQ- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 105 fnlFPHM-----TALENIIEAPIHvLGTPRAEALEQARGLLARVGLADKA-NHYPSMLSGGQQQRVAIARALAMKPQAML 178
Cdd:PRK13643 92 ---FPESqlfeeTVLKDVAFGPQN-FGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 179 FDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIF 243
Cdd:PRK13643 168 LDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
28-258 |
4.64e-31 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 120.73 E-value: 4.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 28 ISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyreRSDGSlvrdSERNIARQRRDIGMVFQR--F 105
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQ------RIDTL----SPGKLQALRRDIQFIFQDpyA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 106 NLFPHMTALENIIEaPIHVLGTPRAE-ALEQARGLLARVGL-ADKANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEPT 183
Cdd:PRK10261 413 SLDPRQTVGDSIME-PLRVHGLLPGKaAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525903658 184 SALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHPSHPRTRAFLSRV 258
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
25-228 |
9.50e-31 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 119.31 E-value: 9.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdSERNIARQRRDIGMVFQR 104
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL-------------ADADADSWRDQIAWVPQH 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 105 FNLFPHmTALENIieapihVLGTPRAEALEQARGLlARVGLADKANHYP-----------SMLSGGQQQRVAIARALAMK 173
Cdd:TIGR02857 405 PFLFAG-TIAENI------RLARPDASDAEIREAL-ERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 174 PQAMLFDEPTSALDPETVGEVLQVMKELAeEGMTMVVVTHEMGFAREvADRVVVL 228
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
11-237 |
1.27e-30 |
|
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: 119.54 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 11 DAQDL----------HKSFG---DLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyRE 77
Cdd:COG5265 347 DAPPLvvgggevrfeNVSFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI--RD 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 78 RSDGSLvrdserniarqRRDIGMVFQRFNLFpHMTALENIIEAPihvLGTPRAEALEQARglLARV-----GLADKanhY 152
Cdd:COG5265 425 VTQASL-----------RAAIGIVPQDTVLF-NDTIAYNIAYGR---PDASEEEVEAAAR--AAQIhdfieSLPDG---Y 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 153 PSM-------LSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAeEGMTMVVVTHEMGFAREvADRV 225
Cdd:COG5265 485 DTRvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAHRLSTIVD-ADEI 562
|
250
....*....|..
gi 1525903658 226 VVLDQGELIEQG 237
Cdd:COG5265 563 LVLEAGRIVERG 574
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-245 |
1.60e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 115.29 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSdgslvrdse 88
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 rniARQRrdIGMVFQRFNLFPHMTALENIIEAPIHvLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIAR 168
Cdd:PRK13537 78 ---ARQR--VGVVPQFDNLDPDFTVRENLLVFGRY-FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525903658 169 ALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSH 245
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
25-237 |
2.50e-30 |
|
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: 112.68 E-value: 2.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSDgslvrdserniarQRRDIGMVFQR 104
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-------------LRRNIGYVPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 105 FNLFpHMTALENIieapihVLGTPRA--EALEQArglLARVGLADKANHYP-----------SMLSGGQQQRVAIARALA 171
Cdd:cd03245 87 VTLF-YGTLRDNI------TLGAPLAddERILRA---AELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525903658 172 MKPQAMLFDEPTSALDPETVGEVLQVMKELAeEGMTMVVVTHEMGFArEVADRVVVLDQGELIEQG 237
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
15-231 |
2.71e-30 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 113.64 E-value: 2.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 15 LHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersDGSlvrDSERniarq 94
Cdd:PRK11248 7 LYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV------EGP---GAER----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 95 rrdiGMVFQRFNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKP 174
Cdd:PRK11248 73 ----GVVFQNEGLLPWRNVQDNV-AFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525903658 175 QAMLFDEPTSALDPETvgevLQVMKEL-----AEEGMTMVVVTHEMGFAREVADRVVVLDQG 231
Cdd:PRK11248 148 QLLLLDEPFGALDAFT----REQMQTLllklwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-234 |
5.71e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.09 E-value: 5.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 12 AQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGramGYRersdgslvrdserni 91
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK---GLR--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 92 arqrrdIGMVFQRFNLFPHMTALENIIEA--PIHVLGTPRAEALE-----------------------------QARGLL 140
Cdd:COG0488 63 ------IGYLPQEPPLDDDLTVLDTVLDGdaELRALEAELEELEAklaepdedlerlaelqeefealggweaeaRAEEIL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 141 ARVGLADKANHYP-SMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVgEVLQvmKELAEEGMTMVVVTHEMGFAR 219
Cdd:COG0488 137 SGLGFPEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESI-EWLE--EFLKNYPGTVLVVSHDRYFLD 213
|
250
....*....|....*
gi 1525903658 220 EVADRVVVLDQGELI 234
Cdd:COG0488 214 RVATRILELDRGKLT 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
9-245 |
7.53e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 112.10 E-value: 7.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSF----------------------GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRI 66
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 67 RVNGRAmgyrersdGSLVrdserniarqrrDIGMVFQrfnlfPHMTALENIIeapI--HVLGTPRAEALEQARGLLARVG 144
Cdd:COG1134 84 EVNGRV--------SALL------------ELGAGFH-----PELTGRENIY---LngRLLGLSRKEIDEKFDEIVEFAE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 145 LADKAN----HYPSmlsgGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFARE 220
Cdd:COG1134 136 LGDFIDqpvkTYSS----GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRR 211
|
250 260
....*....|....*....|....*
gi 1525903658 221 VADRVVVLDQGELIEQGPPEQIFSH 245
Cdd:COG1134 212 LCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-242 |
8.00e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.27 E-value: 8.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 2 AHKSDELIIDAQDLHKSfgdlQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAmgYRERSdg 81
Cdd:COG1129 249 AAAPGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKP--VRIRS-- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 82 slVRDSERNiarqrrdiGMVF-----QRFNLFPHMTALENIIEAPIHVLGT----PRAEALEQARGLLARVGLadKAnhy 152
Cdd:COG1129 321 --PRDAIRA--------GIAYvpedrKGEGLVLDLSIRENITLASLDRLSRggllDRRRERALAEEYIKRLRI--KT--- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 153 PSM------LSGGQQQRVAIARALAMKPQAMLFDEPTSALDpetVG---EVLQVMKELAEEGMTMVVVTHEMGFAREVAD 223
Cdd:COG1129 386 PSPeqpvgnLSGGNQQKVVLAKWLATDPKVLILDEPTRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSD 462
|
250
....*....|....*....
gi 1525903658 224 RVVVLDQGELIEQGPPEQI 242
Cdd:COG1129 463 RILVMREGRIVGELDREEA 481
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
24-233 |
1.03e-29 |
|
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: 109.61 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVngramgyrersDGSLVRDSERNIARQRrdIGMVFQ 103
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL-----------DGADISQWDPNELGDH--VGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 RFNLFPHmTALENIieapihvlgtpraealeqargllarvgladkanhypsmLSGGQQQRVAIARALAMKPQAMLFDEPT 183
Cdd:cd03246 84 DDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1525903658 184 SALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREvADRVVVLDQGEL 233
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-244 |
1.40e-29 |
|
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: 111.04 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERsdgslvrdserniARQRRDIGMVFQ 103
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP-------------AWLRRQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 RFNLFpHMTALENIIEAPIhvlGTPRAEALEQARGLLARVGLADKANHYPSM-------LSGGQQQRVAIARALAMKPQA 176
Cdd:cd03252 84 ENVLF-NRSIRDNIALADP---GMSMERVIEAAKLAGAHDFISELPEGYDTIvgeqgagLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525903658 177 MLFDEPTSALDPETVGEVLQVMKELAeEGMTMVVVTHEMGFAREvADRVVVLDQGELIEQGPPEQIFS 244
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-234 |
2.25e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 111.33 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFG-----DLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCI--NLLEDiqGGRIRVNGRamgyrersdg 81
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIagSLPPD--SGSILIDGK---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 82 slvrdserNIAR----QR-RDIGMVFQ--RFNLFPHMTALENIIEA-------PIHvLGTPRAEaLEQARGLLARV--GL 145
Cdd:COG1101 69 --------DVTKlpeyKRaKYIGRVFQdpMMGTAPSMTIEENLALAyrrgkrrGLR-RGLTKKR-RELFRELLATLglGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 146 ADKANHYPSMLSGGQQQrvaiARALAM----KPQAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFARE 220
Cdd:COG1101 139 ENRLDTKVGLLSGGQRQ----ALSLLMatltKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALD 214
|
250
....*....|....
gi 1525903658 221 VADRVVVLDQGELI 234
Cdd:COG1101 215 YGNRLIMMHEGRII 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
23-237 |
2.43e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 115.83 E-value: 2.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 23 QILKGISLQVRRGEVVVLIGASGSGKTTFIrciNLLE---DIQGGRIRVngramgyrersDGSLVRDSerNIARQRRDIG 99
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLI---NLLQrvfDPQSGRILI-----------DGTDIRTV--TRASLRRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 100 MVFQRFNLFPHMTAlENI-------IEAPIHvLGTPRAEALE----QARGLLARVGladkanHYPSMLSGGQQQRVAIAR 168
Cdd:PRK13657 413 VVFQDAGLFNRSIE-DNIrvgrpdaTDEEMR-AAAERAQAHDfierKPDGYDTVVG------ERGRQLSGGERQRLAIAR 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1525903658 169 ALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAeEGMTMVVVTHEMGFAREvADRVVVLDQGELIEQG 237
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-258 |
2.73e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 115.69 E-value: 2.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 4 KSDELIIDAQDLHKSFGD--LQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyRERSDG 81
Cdd:PRK11160 333 AADQVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI--ADYSEA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 82 SLvrdserniarqRRDIGMVFQRFNLFPHmTALENIieapihVLGTPRA--EALEQArglLARVGLADKANHYPSM---- 155
Cdd:PRK11160 411 AL-----------RQAISVVSQRVHLFSA-TLRDNL------LLAAPNAsdEALIEV---LQQVGLEKLLEDDKGLnawl 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 156 ------LSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAeEGMTMVVVTHEMgFAREVADRVVVLD 229
Cdd:PRK11160 470 geggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRL-TGLEQFDRICVMD 547
|
250 260
....*....|....*....|....*....
gi 1525903658 230 QGELIEQGPPEQIFShpSHPRTRAFLSRV 258
Cdd:PRK11160 548 NGQIIEQGTHQELLA--QQGRYYQLKQRL 574
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-237 |
4.70e-29 |
|
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: 109.67 E-value: 4.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 21 DLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCI-NLLED--IQGGRIRVNGRamgyrersdgslvrdsERNIARQRRD 97
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGggTTSGQILFNGQ----------------PRKPDQFQKC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 98 IGMVFQRFNLFPHMTALENIIEAPIHVLGTPRAEALEQAR---GLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKP 174
Cdd:cd03234 83 VAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRvedVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525903658 175 QAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMG---FarEVADRVVVLDQGELIEQG 237
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIVYSG 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
21-248 |
7.39e-29 |
|
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: 114.43 E-value: 7.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 21 DLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdSERNIARQRRDIGM 100
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL-------------ADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 101 VFQRFNLFPHmTALENIIEAPIHVLGTPRAEALEQARGLLARVGLADKANHYP-----SMLSGGQQQRVAIARALAMKPQ 175
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPigengVLLSGGQRQRLAIARALLKDAP 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525903658 176 AMLFDEPTSALDPETVGEVLQVMKELaEEGMTMVVVTHEMGfAREVADRVVVLDQGELIEQGPPEQIFSHPSH 248
Cdd:TIGR02203 490 ILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLARNGL 560
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
7-256 |
2.36e-28 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 108.72 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 7 ELIIDAQDLHKSF---------GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRE 77
Cdd:PRK15112 2 ETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 78 RSDGSlvrdserniarQRrdIGMVFQ--RFNLFPHMTaLENIIEAPIHVLGTPRAEALEQA-RGLLARVGL-ADKANHYP 153
Cdd:PRK15112 82 YSYRS-----------QR--IRMIFQdpSTSLNPRQR-ISQILDFPLRLNTDLEPEQREKQiIETLRQVGLlPDHASYYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 154 SMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGE 232
Cdd:PRK15112 148 HMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGE 227
|
250 260
....*....|....*....|....
gi 1525903658 233 LIEQGPPEQIFSHPSHPRTRAFLS 256
Cdd:PRK15112 228 VVERGSTADVLASPLHELTKRLIA 251
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
8-244 |
8.42e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.02 E-value: 8.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 8 LIIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgSLVRDS 87
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDK----------PISMLS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 ERNIARQrrdIGMVFQRfNLFPHMTALENIIE---APiHV-----LGTPRAEALEQArglLARVGLADKANHYPSMLSGG 159
Cdd:PRK11231 71 SRQLARR---LALLPQH-HLTPEGITVRELVAygrSP-WLslwgrLSAEDNARVNQA---MEQTRINHLADRRLTDLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 160 QQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPP 239
Cdd:PRK11231 143 QRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
|
....*
gi 1525903658 240 EQIFS 244
Cdd:PRK11231 223 EEVMT 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
10-242 |
1.35e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 108.38 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSdgslvrdser 89
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARL---------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 niARQRrdIGMVFQRFNLFPHMTALENI-------------IEAPIHVLgtpraeaLEQARgllarvgLADKANHYPSML 156
Cdd:PRK13536 112 --ARAR--IGVVPQFDNLDLEFTVRENLlvfgryfgmstreIEAVIPSL-------LEFAR-------LESKADARVSDL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 157 SGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQ 236
Cdd:PRK13536 174 SGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAE 253
|
....*.
gi 1525903658 237 GPPEQI 242
Cdd:PRK13536 254 GRPHAL 259
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
13-237 |
3.48e-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: 104.40 E-value: 3.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 13 QDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrERSDgslvrdsernia 92
Cdd:TIGR03740 4 KNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPW---TRKD------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 93 rqRRDIGMVFQRFNLFPHMTALENIieaPIH--VLGTPRAEALEqargLLARVGLADKANHYPSMLSGGQQQRVAIARAL 170
Cdd:TIGR03740 69 --LHKIGSLIESPPLYENLTARENL---KVHttLLGLPDSRIDE----VLNIVDLTNTGKKKAKQFSLGMKQRLGIAIAL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525903658 171 AMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQG 237
Cdd:TIGR03740 140 LNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQG 206
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-249 |
4.53e-27 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 109.37 E-value: 4.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 23 QILKGISLQVRRGEVVVLIGASGSGKTTFIRCI--NLLEDIQG-GRIRVNGRAMGyrersdgslvrdserniARQRRDIG 99
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafRSPKGVKGsGSVLLNGMPID-----------------AKEMRAIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 100 MVFQRFNLF-PHMTALENII-----EAPIHVLGTPRAEALEQargLLARVGLADKAN------HYPSMLSGGQQQRVAIA 167
Cdd:TIGR00955 102 AYVQQDDLFiPTLTVREHLMfqahlRMPRRVTKKEKRERVDE---VLQALGLRKCANtrigvpGRVKGLSGGERKRLAFA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 168 RALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMG---FarEVADRVVVLDQGELIEQGPPEQ--- 241
Cdd:TIGR00955 179 SELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSselF--ELFDKIILMAEGRVAYLGSPDQavp 256
|
....*...
gi 1525903658 242 IFSHPSHP 249
Cdd:TIGR00955 257 FFSDLGHP 264
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-228 |
1.24e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 102.31 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 18 SFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCI-NLLEDIQGGRIRVNGRAMGY---RERSDGSLVrdserniAR 93
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLaGVLRPTSGTVRRAGGARVAYvpqRSEVPDSLP-------LT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 94 QRRDIGMvfqrfNLFPHMTALeniieapihvlGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMK 173
Cdd:NF040873 74 VRDLVAM-----GRWARRGLW-----------RRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 174 PQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREvADRVVVL 228
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
13-240 |
2.20e-26 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 102.84 E-value: 2.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 13 QDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCI--NLLEDIQGGRIRVNGR---AMGYRERSdgslvrds 87
Cdd:COG0396 4 KNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEdilELSPDERA-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 erniarqRRDIGMVFQR---------FNLFphMTALENIIEAPIhvlgtPRAEALEQARGLLARVGLAdkanhyPSML-- 156
Cdd:COG0396 76 -------RAGIFLAFQYpveipgvsvSNFL--RTALNARRGEEL-----SAREFLKLLKEKMKELGLD------EDFLdr 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 157 ------SGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHemgFAR----EVADRVV 226
Cdd:COG0396 136 yvnegfSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH---YQRildyIKPDFVH 212
|
250
....*....|....
gi 1525903658 227 VLDQGELIEQGPPE 240
Cdd:COG0396 213 VLVDGRIVKSGGKE 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-235 |
4.10e-26 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 106.03 E-value: 4.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTfircinLLEDIQG--------GRIRVNGRAMGYRErsd 80
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKST------LMKVLSGvyphgsyeGEILFDGEVCRFKD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 81 gslVRDSERniarqrRDIGMVFQRFNLFPHMTALENIIeapihvLGTPRA--------EALEQARGLLARVGLADKANHY 152
Cdd:NF040905 72 ---IRDSEA------LGIVIIHQELALIPYLSIAENIF------LGNERAkrgvidwnETNRRARELLAKVGLDESPDTL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 153 PSMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGE 232
Cdd:NF040905 137 VTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
...
gi 1525903658 233 LIE 235
Cdd:NF040905 217 TIE 219
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
24-245 |
4.92e-26 |
|
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: 106.37 E-value: 4.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSD-----GSLVRDSE-------RNI 91
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgrhiGYLPQDVElfdgtiaENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 92 ARqrrdigmvfqrfnlFPHMTAlENIIEApihvlgtprAEA-------LEQARGLLARVGLADkanhypSMLSGGQQQRV 164
Cdd:COG4618 427 AR--------------FGDADP-EKVVAA---------AKLagvhemiLRLPDGYDTRIGEGG------ARLSGGQRQRI 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 165 AIARALAMKPQAMLFDEPTSALDPEtvGE--VLQVMKELAEEGMTMVVVTHEMGfAREVADRVVVLDQGELIEQGPPEQI 242
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDDE--GEaaLAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEV 553
|
...
gi 1525903658 243 FSH 245
Cdd:COG4618 554 LAR 556
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
9-244 |
6.50e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 101.51 E-value: 6.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCInllediqggrirvngraMGYRERSDGSLVRDSE 88
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMV-----------------VGIVPRDAGNIIIDDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 rNI------ARQRRDIGMVFQRFNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQ 162
Cdd:PRK10895 66 -DIsllplhARARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 163 RVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQI 242
Cdd:PRK10895 145 RVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
..
gi 1525903658 243 FS 244
Cdd:PRK10895 225 LQ 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-246 |
7.15e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.96 E-value: 7.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 2 AHKSDELIIDAQDLHKSF---GDLQILKGISLQVRRGEVVVLIGASGSGKTTfirCINLLEDI---QGGRIRVNGramgy 75
Cdd:TIGR00958 471 APLNLEGLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNLyqpTGGQVLLDG----- 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 76 rersdgslVRDSERNIARQRRDIGMVFQRFNLFPHmTALENIIEApihVLGTPRAEALEQARGLLARVGLADKANHYP-- 153
Cdd:TIGR00958 543 --------VPLVQYDHHYLHRQVALVGQEPVLFSG-SVRENIAYG---LTDTPDEEIMAAAKAANAHDFIMEFPNGYDte 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 154 -----SMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPEtVGEVLQVMKELAeeGMTMVVVTHEMGFAREvADRVVVL 228
Cdd:TIGR00958 611 vgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE-CEQLLQESRSRA--SRTVLLIAHRLSTVER-ADQILVL 686
|
250
....*....|....*...
gi 1525903658 229 DQGELIEQGPPEQIFSHP 246
Cdd:TIGR00958 687 KKGSVVEMGTHKQLMEDQ 704
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
10-237 |
7.58e-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: 99.69 E-value: 7.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFG--DLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGramgyrersdgSLVRDS 87
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG-----------VPVSDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 ERNIARQrrdIGMVFQRFNLFpHMTALENiieapihvLGTPraealeqargllarvgladkanhypsmLSGGQQQRVAIA 167
Cdd:cd03247 70 EKALSSL---ISVLNQRPYLF-DTTLRNN--------LGRR---------------------------FSGGERQRLALA 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 168 RALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEgMTMVVVTHEMGfAREVADRVVVLDQGELIEQG 237
Cdd:cd03247 111 RILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
13-240 |
1.38e-25 |
|
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: 99.52 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 13 QDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLED--IQGGRIRVNGR---AMGYRERSdgslvrds 87
Cdd:cd03217 4 KDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEditDLPPEERA-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 erniarqRRDIGMVFQRfnlfphmtaleniieaPIHVLGTPRAEALeqaRGLlaRVGLadkanhypsmlSGGQQQRVAIA 167
Cdd:cd03217 76 -------RLGIFLAFQY----------------PPEIPGVKNADFL---RYV--NEGF-----------SGGEKKRNEIL 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 168 RALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTH-EMGFAREVADRVVVLDQGELIEQGPPE 240
Cdd:cd03217 117 QLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-234 |
2.45e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 99.95 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 19 FGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIrcinllediqggrirvnGRAMGYRERSDGSLVRD----SERNIAR- 93
Cdd:PRK11614 15 YGKIQALHEVSLHINQGEIVTLIGANGAGKTTLL-----------------GTLCGDPRATSGRIVFDgkdiTDWQTAKi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 94 QRRDIGMVFQRFNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLLARvgLADKANHYPSMLSGGQQQRVAIARALAMK 173
Cdd:PRK11614 78 MREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525903658 174 PQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELI 234
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-231 |
1.12e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 102.17 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSDGSlvrdser 89
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAA------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 niarqRRDIGMVFQRFNLFPHMTALENII--EAPIH-VLGTP---RAEALEQARGLLARVGLADKANHYPSMLSGGQQQR 163
Cdd:PRK09700 79 -----QLGIGIIYQELSVIDELTVLENLYigRHLTKkVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525903658 164 VAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQG 231
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-234 |
1.18e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 101.93 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 17 KSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRcinLLEDIQ-----GGRIRVNGRAMGYRErsdgslVRDSERNi 91
Cdd:PRK13549 13 KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMK---VLSGVYphgtyEGEIIFEGEELQASN------IRDTERA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 92 arqrrDIGMVFQRFNLFPHMTALENII--EAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARA 169
Cdd:PRK13549 83 -----GIAIIHQELALVKELSVLENIFlgNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELI 234
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-235 |
1.57e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 101.78 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 21 DLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSDGslVRDSERNIARQRRDIGm 100
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDA--VKKGMAYITESRRDNG- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 101 vfqrfnLFPHMTALENIIEAPIHVLG---------TPRAEA--LEQARGLLARVglADKANHYPSMLSGGQQQRVAIARA 169
Cdd:PRK09700 352 ------FFPNFSIAQNMAISRSLKDGgykgamglfHEVDEQrtAENQRELLALK--CHSVNQNITELSGGNQQKVLISKW 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIE 235
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
23-244 |
3.71e-24 |
|
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: 100.97 E-value: 3.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 23 QILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGyrersdgslvrdsERNIARQRRDIGMVF 102
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLA-------------IADPAWLRRQMGVVL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 103 QRFNLFPHMTAlENI--------IEAPIHVLGTPRAEA--LEQARGLLARVGladkanHYPSMLSGGQQQRVAIARALAM 172
Cdd:TIGR01846 538 QENVLFSRSIR-DNIalcnpgapFEHVIHAAKLAGAHDfiSELPQGYNTEVG------EKGANLSGGQRQRIAIARALVG 610
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525903658 173 KPQAMLFDEPTSALDPETVGEVLQVMKELAeEGMTMVVVTHEMGFAREvADRVVVLDQGELIEQGPPEQIFS 244
Cdd:TIGR01846 611 NPRILIFDEATSALDYESEALIMRNMREIC-RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELLA 680
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
24-241 |
3.97e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.65 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAmgyrersdgslvrdserniarqrrdiGMVF- 102
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA--------------------------RVLFl 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 103 -QRfnlfPHMtaleniieaPIHVL-------GTPRAEALEQARGLLARVGLA------DKANHYPSMLSGGQQQRVAIAR 168
Cdd:COG4178 432 pQR----PYL---------PLGTLreallypATAEAFSDAELREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFAR 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525903658 169 ALAMKPQAMLFDEPTSALDPETVGEVLQVMKElAEEGMTMVVVTHEMGFAReVADRVVVLDQGELIEQGPPEQ 241
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLAA-FHDRVLELTGDGSWQLLPAEA 569
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
9-238 |
5.20e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 100.08 E-value: 5.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYrersDGSlvRDSe 88
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTF----NGP--KSS- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 rniarQRRDIGMVFQRFNLFPHMTALENII--EAPIHVLGTPR-AEALEQARGLLARVGLADKANHYPSMLSGGQQQRVA 165
Cdd:PRK10762 77 -----QEAGIGIIHQELNLIPQLTIAENIFlgREFVNRFGRIDwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 166 IARALAMKPQAMLFDEPTSAL-DPETvgEVL-QVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGP 238
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALtDTET--ESLfRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAERE 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-233 |
7.39e-24 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 96.00 E-value: 7.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 21 DLQILKGISLQVRRGEVVVLIGASGSGKTTfirCINLLEDI---QGGRIRVNGRAMG-YRERSdgslvrdserniarQRR 96
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKST---VVALLENFyqpQGGQVLLDGKPISqYEHKY--------------LHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 97 DIGMVFQRFNLFPHmTALENIIEApihVLGTPRAEALEQARGLLARVGLADKANHYP-------SMLSGGQQQRVAIARA 169
Cdd:cd03248 89 KVSLVGQEPVLFAR-SLQDNIAYG---LQSCSFECVKEAAQKAHAHSFISELASGYDtevgekgSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKElAEEGMTMVVVTHEMGFArEVADRVVVLDQGEL 233
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-244 |
1.04e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 96.06 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTfircinLLEDIQG-----GRIRVNGRAMgyrerSDGSLvrdseRNIARQRrdiG 99
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKST------LLARMAGllpgqGEILLNGRPL-----SDWSA-----AELARHR---A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 100 MVFQRFNLFPHMTALENIieaPIHVLGTPRAEALEQARGLLA-RVGLADKANHYPSMLSGGQQQRVAIARAL-----AMK 173
Cdd:COG4138 73 YLSQQQSPPFAMPVFQYL---ALHQPAGASSEAVEQLLAQLAeALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTIN 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525903658 174 PQA--MLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFS 244
Cdd:COG4138 150 PEGqlLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
10-237 |
1.63e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.15 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLH-KSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIrciNLLediQG-----GRIRVNGRAMgyrersdgsl 83
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLL---NAL---LGflpyqGSLKINGIEL---------- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 84 vrdSERNIARQRRDIGMVFQRFNLFpHMTALENIieapihVLGTPRAEAlEQARGLLARVGLADKANHYP---------- 153
Cdd:PRK11174 414 ---RELDPESWRKHLSWVGQNPQLP-HGTLRDNV------LLGNPDASD-EQLQQALENAWVSEFLPLLPqgldtpigdq 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 154 -SMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKElAEEGMTMVVVTHEMGFAREVaDRVVVLDQGE 232
Cdd:PRK11174 483 aAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQ 560
|
....*
gi 1525903658 233 LIEQG 237
Cdd:PRK11174 561 IVQQG 565
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-213 |
1.97e-23 |
|
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: 98.59 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 5 SDELIIDAQDLHKSFGDLQI-LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGramgyrerSDGSL 83
Cdd:TIGR02868 330 LGKPTLELRDLSAGYPGAPPvLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG--------VPVSS 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 84 VRDSErniarQRRDIGMVFQRFNLFpHMTALENIIeapihvLGTPRAeALEQARGLLARVGLADKANHYP---------- 153
Cdd:TIGR02868 402 LDQDE-----VRRRVSVCAQDAHLF-DTTVRENLR------LARPDA-TDEELWAALERVGLADWLRALPdgldtvlgeg 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525903658 154 -SMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKElAEEGMTMVVVTH 213
Cdd:TIGR02868 469 gARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
24-232 |
3.52e-23 |
|
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: 93.30 E-value: 3.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCInLLE-DIQGGRIRVNGRaMGYRERS----DGSlVRDserNIArqrrdI 98
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-LGElEKLSGSVSVPGS-IAYVSQEpwiqNGT-IRE---NIL-----F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 99 GMVF--QRFNlfphmtaleniieapiHVLgtpRAEALEQ-----ARGLLARVGlaDKAnhypSMLSGGQQQRVAIARALA 171
Cdd:cd03250 89 GKPFdeERYE----------------KVI---KACALEPdleilPDGDLTEIG--EKG----INLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525903658 172 MKPQAMLFDEPTSALDPETVGEVLQ--VMKELAeEGMTMVVVTHEMGFAREvADRVVVLDQGE 232
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIFEncILGLLL-NNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
9-242 |
3.70e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.81 E-value: 3.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAmgyrersdgsLVRDSE 88
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNP----------CARLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 rNIARQrRDIGMVFQRFNLFPHMTALENIIeapihvLGTPR-AEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIA 167
Cdd:PRK15439 81 -AKAHQ-LGIYLVPQEPLLFPNLSVKENIL------FGLPKrQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 168 RALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQI 242
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-242 |
8.85e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 96.63 E-value: 8.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 2 AHKSDELIIDAQDLH-KSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGyrersd 80
Cdd:COG3845 250 PAEPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDIT------ 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 81 gslvrdseRNIARQRRDIGMVF-----QRFNLFPHMTALENIIeapihvLGTPRAEALeQARGLLARVGLADKANH---- 151
Cdd:COG3845 324 --------GLSPRERRRLGVAYipedrLGRGLVPDMSVAENLI------LGRYRRPPF-SRGGFLDRKAIRAFAEEliee 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 152 ----YPS------MLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREV 221
Cdd:COG3845 389 fdvrTPGpdtparSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILAL 468
|
250 260
....*....|....*....|.
gi 1525903658 222 ADRVVVLDQGELIEQGPPEQI 242
Cdd:COG3845 469 SDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-237 |
9.58e-23 |
|
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: 93.17 E-value: 9.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 16 HKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRaMGYRERSdgslvrdserniaRQR 95
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRK-------------KFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 96 RDIGMVF-QRFNLFPHMTALENiIEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKP 174
Cdd:cd03267 94 RRIGVVFgQKTQLWWDLPVIDS-FYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 175 QAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQG 237
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-237 |
1.01e-22 |
|
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: 92.60 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 20 GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersDGSLVrdserniarqrrDIG 99
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR--------VSSLL------------GLG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 100 MVFQrfnlfPHMTALENI-IEAPIhvLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAML 178
Cdd:cd03220 93 GGFN-----PELTGRENIyLNGRL--LGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1525903658 179 FDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQG 237
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-242 |
1.41e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 93.31 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRersdgslvrdSERNIARQrrdIGMVFQ 103
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW----------SSKAFARK---VAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 RFNLFPHMTALE--NIIEAPIH-VLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAMLFD 180
Cdd:PRK10575 93 QLPAAEGMTVRElvAIGRYPWHgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525903658 181 EPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQI 242
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
10-232 |
1.78e-22 |
|
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: 89.82 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCInllediqggrirvngraMGYRERSDGSLVRDSER 89
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI-----------------AGELEPDEGIVTWGSTV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIARqrrdigmvfqrfnlfphmtaleniieapihvlgtpraeaLEQargllarvgladkanhypsmLSGGQQQRVAIARA 169
Cdd:cd03221 64 KIGY---------------------------------------FEQ--------------------LSGGEKMRLALAKL 84
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVgEVLQVMkeLAEEGMTMVVVTHEMGFAREVADRVVVLDQGE 232
Cdd:cd03221 85 LLENPNLLLLDEPTNHLDLESI-EALEEA--LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
28-255 |
2.08e-22 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 94.10 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 28 ISLQVRRGEVVVLIGASGSGKTTFIRCInllediqGGRIRVNGRAMGYRER-SDGSLVRDSerniARQRR-----DIGMV 101
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAI-------CGVTKDNWRVTADRMRfDDIDLLRLS----PRERRklvghNVSMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 102 FQRFN--LFPHMTALENIIEA-P--------IHVLGTPRAEALEqargLLARVGLADKAN---HYPSMLSGGQQQRVAIA 167
Cdd:PRK15093 95 FQEPQscLDPSERVGRQLMQNiPgwtykgrwWQRFGWRKRRAIE----LLHRVGIKDHKDamrSFPYELTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 168 RALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAE-EGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSHP 246
Cdd:PRK15093 171 IALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
....*....
gi 1525903658 247 SHPRTRAFL 255
Cdd:PRK15093 251 HHPYTQALI 259
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-234 |
1.86e-21 |
|
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: 92.97 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 17 KSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLL--EDIQGGRIRVNGRAMgyrersDGSLVRDSERniarq 94
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPL------KASNIRDTER----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 95 rRDIGMVFQRFNLFPHMTALENII---EAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSM-LSGGQQQRVAIARAL 170
Cdd:TIGR02633 78 -AGIVIIHQELTLVPELSVAENIFlgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 171 AMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELI 234
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-237 |
3.31e-21 |
|
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: 92.50 E-value: 3.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 3 HKSDELI-----IDAQDLHKSFG-DLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyr 76
Cdd:TIGR01193 462 KKRTELNnlngdIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF----- 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 77 ersdgsLVRDSERNIARQRrdIGMVFQRFNLFPHmTALENIIeapihvLGTPRAEALEQARGLLARVGLADKANHYP--- 153
Cdd:TIGR01193 537 ------SLKDIDRHTLRQF--INYLPQEPYIFSG-SILENLL------LGAKENVSQDEIWAACEIAEIKDDIENMPlgy 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 154 --------SMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEgmTMVVVTHEMGFAREVaDRV 225
Cdd:TIGR01193 602 qtelseegSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQS-DKI 678
|
250
....*....|..
gi 1525903658 226 VVLDQGELIEQG 237
Cdd:TIGR01193 679 IVLDHGKIIEQG 690
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
25-237 |
3.85e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 92.00 E-value: 3.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVngramgyrersDGSLVRDSErnIARQRRDIGMVFQR 104
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL-----------DGHDLRDYT--LASLRNQVALVSQN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 105 FNLFpHMTALENIIEApihVLGTPRAEALEQARGLLARVGLADKANH--------YPSMLSGGQQQRVAIARALAMKPQA 176
Cdd:PRK11176 426 VHLF-NDTIANNIAYA---RTEQYSREQIEEAARMAYAMDFINKMDNgldtvigeNGVLLSGGQRQRIAIARALLRDSPI 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525903658 177 MLFDEPTSALDPETVGEVLQVMKELaEEGMTMVVVTHEMGfAREVADRVVVLDQGELIEQG 237
Cdd:PRK11176 502 LILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLS-TIEKADEILVVEDGEIVERG 560
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-235 |
4.29e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.90 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 17 KSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRErsdgslVRDS-ERNIArqr 95
Cdd:PRK11288 12 KTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAS------TTAAlAAGVA--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 96 rdigMVFQRFNLFPHMTALENII--EAPiHVLG-TPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAM 172
Cdd:PRK11288 83 ----IIYQELHLVPEMTVAENLYlgQLP-HKGGiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525903658 173 KPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIE 235
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
24-245 |
7.19e-21 |
|
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: 91.26 E-value: 7.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSD-----GSLVRDSE-------RNI 91
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgkhiGYLPQDVElfpgtvaENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 92 ARQRRDIGMvfqrfnlfphmtalENIIEAPihvlgtpraeALEQARGLLARVgladkANHYPSM-------LSGGQQQRV 164
Cdd:TIGR01842 413 ARFGENADP--------------EKIIEAA----------KLAGVHELILRL-----PDGYDTVigpggatLSGGQRQRI 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 165 AIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGfAREVADRVVVLDQGELIEQGPPEQIFS 244
Cdd:TIGR01842 464 ALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLA 542
|
.
gi 1525903658 245 H 245
Cdd:TIGR01842 543 K 543
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
24-239 |
1.07e-20 |
|
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: 87.16 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersDGSLVRdseRNIARQRrdIGMVFQ 103
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGV--------DISKIG---LHDLRSR--ISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 ---------RFNLFPHMTALENIIEapihvlgtpraEALEQArGLLARV-----GLADKANHYPSMLSGGQQQRVAIARA 169
Cdd:cd03244 86 dpvlfsgtiRSNLDPFGEYSDEELW-----------QALERV-GLKEFVeslpgGLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKElAEEGMTMVVVTHE----MGFarevaDRVVVLDQGELIEQGPP 239
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRldtiIDS-----DRILVLDKGRVVEFDSP 221
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-251 |
1.53e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 88.61 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSF-------GDLQILKG--------------ISLQVRRGEVVVLIGASGSGKTTFIRcinLLEDI---QGG 64
Cdd:COG4586 1 IIEVENLSKTYrvyekepGLKGALKGlfrreyreveavddISFTIEPGEIVGFIGPNGAGKSTTIK---MLTGIlvpTSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 65 RIRVNGRAmGYRERsdgslvrdserniARQRRDIGMVF-QRFNLFPHMTALE--NIIEApihVLGTPRAEA---LEQARG 138
Cdd:COG4586 78 EVRVLGYV-PFKRR-------------KEFARRIGVVFgQRSQLWWDLPAIDsfRLLKA---IYRIPDAEYkkrLDELVE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 139 LLarvGLADKANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGF 217
Cdd:COG4586 141 LL---DLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDD 217
|
250 260 270
....*....|....*....|....*....|....
gi 1525903658 218 AREVADRVVVLDQGELIEQGPPEQIFSHPSHPRT 251
Cdd:COG4586 218 IEALCDRVIVIDHGRIIYDGSLEELKERFGPYKT 251
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
24-235 |
3.63e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 85.78 E-value: 3.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCInllediqggrirvngrAMGYRERSDGSLVRDSERNIARQRrdigmvfq 103
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL----------------AGALKGTPVAGCVDVPDNQFGREA-------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 rfnlfphmtaleNIIEApihvlgTPRAEALEQARGLLARVGLADKANHY--PSMLSGGQQQRVAIARALAMKPQAMLFDE 181
Cdd:COG2401 101 ------------SLIDA------IGRKGDFKDAVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1525903658 182 PTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVA-DRVVVLDQGELIE 235
Cdd:COG2401 163 FCSHLDRQTAKRVARNLQKLARRaGITLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-244 |
3.72e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.96 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 13 QDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgSLVRDSERNIA 92
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGE----------HIQHYASKEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 93 RQrrdIGMVFQRFNLFPHMTALENIIEA--PIHVLGTP-RAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARA 169
Cdd:PRK10253 81 RR---IGLLAQNATTPGDITVQELVARGryPHQPLFTRwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525903658 170 LAMKPQAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFS 244
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
25-244 |
1.42e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 85.32 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRCInllediqggrirvngraMGYRERSDGSL-VRDSERNIARQRRDIGMVFQ 103
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKAL-----------------MGFVRLASGKIsILGQPTRQALQKNLVAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 RFNL---FPHMtaLENIIE----APIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQA 176
Cdd:PRK15056 86 SEEVdwsFPVL--VEDVVMmgryGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525903658 177 MLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLdQGELIEQGPPEQIFS 244
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTFT 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
36-239 |
1.74e-19 |
|
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: 87.76 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 36 EVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgslvrDSERNIARQRRDIGMVFQRFNLFPHMTALE 115
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK--------------DIETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 116 NIIEAPiHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVL 195
Cdd:TIGR01257 1023 HILFYA-QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1525903658 196 QVMKELaEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPP 239
Cdd:TIGR01257 1102 DLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
14-237 |
1.81e-19 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 87.24 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 14 DLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCInllediqGGRIRVNGRAmgyrersdgSLVRDSERNIAR 93
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQGNNFT---------GTILANNRKPTK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 94 Q-RRDIGMVFQRFNLFPHMTALENIIEAPIhvLGTPRA----EALEQARGLLARVGLAD-----KANHYPSMLSGGQQQR 163
Cdd:PLN03211 137 QiLKRTGFVTQDDILYPHLTVRETLVFCSL--LRLPKSltkqEKILVAESVISELGLTKcentiIGNSFIRGISGGERKR 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 164 VAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHE-MGFAREVADRVVVLDQGELIEQG 237
Cdd:PLN03211 215 VSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-237 |
1.84e-19 |
|
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: 83.47 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 17 KSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLledIQGGRIRVNG--RAMGYrersdgslvrDSERNIARQ 94
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGdiHYNGI----------PYKEFAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 95 RRDIGMVFQRFNLFPHMTAleniieapihvlgtprAEALEQARGLlarvgladKANHYPSMLSGGQQQRVAIARALAMKP 174
Cdd:cd03233 82 PGEIIYVSEEDVHFPTLTV----------------RETLDFALRC--------KGNEFVRGISGGERKRVSIAEALVSRA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 175 QAMLFDEPTSALDPETVGEVLQVMKELA-EEGMT-MVVVTHEMGFAREVADRVVVLDQGELIEQG 237
Cdd:cd03233 138 SVLCWDNSTRGLDSSTALEILKCIRTMAdVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-213 |
2.07e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.38 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 20 GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGramgyrERSDGSLVRDSERNIARQrrdig 99
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG------GDIDDPDVAEACHYLGHR----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 100 mvfqrfN-LFPHMTALENIiEAPIHVLGTPRAEALEQarglLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAML 178
Cdd:PRK13539 82 ------NaMKPALTVAENL-EFWAAFLGGEELDIAAA----LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|....*
gi 1525903658 179 FDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTH 213
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
28-235 |
3.87e-19 |
|
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: 86.39 E-value: 3.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 28 ISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdSERNIARQRRDIGMVFQRFNL 107
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV-------------TADNREAYRQLFSAVFSDFHL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 108 FPhmtaleniieapiHVLGTPRAEALEQARGLLARVGLADK---ANHYPSM--LSGGQQQRVAIARALAMKPQAMLFDEP 182
Cdd:COG4615 418 FD-------------RLLGLDGEADPARARELLERLELDHKvsvEDGRFSTtdLSQGQRKRLALLVALLEDRPILVFDEW 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1525903658 183 TSALDPE------TvgEVLQvmkELAEEGMTMVVVTHEMGFArEVADRVVVLDQGELIE 235
Cdd:COG4615 485 AADQDPEfrrvfyT--ELLP---ELKARGKTVIAISHDDRYF-DLADRVLKMDYGKLVE 537
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-230 |
8.58e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.77 E-value: 8.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 27 GISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGramgyrersdgslvrdseRNIARQRRDigmvFQRFN 106
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG------------------EPIRRQRDE----YHQDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 107 LF--------PHMTALENI-IEAPIHvlGTPRAEALEQArglLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAM 177
Cdd:PRK13538 77 LYlghqpgikTELTALENLrFYQRLH--GPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1525903658 178 LFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQ 230
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVASDKVRKLRLGQ 204
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-213 |
2.88e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 80.10 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 12 AQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAmgyrersdgslvrdsernI 91
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP------------------L 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 92 ARQR----RDIGMVFQRFNLFPHMTALENI-IEAPIHvlgTPRAEALEQArglLARVGLADKANHYPSMLSGGQQQRVAI 166
Cdd:TIGR01189 65 AEQRdephENILYLGHLPGLKPELSALENLhFWAAIH---GGAQRTIEDA---LAAVGLTGFEDLPAAQLSAGQQRRLAL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1525903658 167 ARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTH 213
Cdd:TIGR01189 139 ARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-242 |
4.09e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.75 E-value: 4.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 28 ISLQVRRGEVVVLIGASGSGKTTFIRCI-NLLEdiQGGRIRVNGRAMgyRERSDGSLVRDSERNIARQRRDIGM-VFQRF 105
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMaGLLP--GSGSIQFAGQPL--EAWSAAELARHRAYLSQQQTPPFAMpVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 106 NLfpHMTAleniieapihvlGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARAL-----AMKP--QAML 178
Cdd:PRK03695 91 TL--HQPD------------KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 179 FDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQI 242
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-214 |
6.60e-18 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 82.85 E-value: 6.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 20 GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLED---IQGGRIRVNGRAM--------GYRERSD----GSLV 84
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLdssfqrsiGYVQQQDlhlpTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 85 RDSERNIARQRRDigmvfQRFNLFPHMTALENIIEapihVLG-TPRAEALeqargllarVGLADKAnhypsmLSGGQQQR 163
Cdd:TIGR00956 854 RESLRFSAYLRQP-----KSVSKSEKMEYVEEVIK----LLEmESYADAV---------VGVPGEG------LNVEQRKR 909
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1525903658 164 VAIARALAMKPQAMLF-DEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHE 214
Cdd:TIGR00956 910 LTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
24-213 |
1.14e-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: 77.58 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIrvngramgyrersdgslvrdsernIARQRRDIGMVFQ 103
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI------------------------GMPEGEDLLFLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 RfnlfPHMTAleniieapihvlGTPRaealEQargllarvgLAdkanhYP--SMLSGGQQQRVAIARALAMKPQAMLFDE 181
Cdd:cd03223 72 R----PYLPL------------GTLR----EQ---------LI-----YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|..
gi 1525903658 182 PTSALDPETVGEVLQVMKelaEEGMTMVVVTH 213
Cdd:cd03223 118 ATSALDEESEDRLYQLLK---ELGITVISVGH 146
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
23-239 |
1.61e-17 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 78.22 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 23 QILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersDGSLVrdserNIARQRRDIGMVF 102
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI--------DISTI-----PLEDLRSSLTIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 103 QRFNLFphMTALENIIEAPIHVLGTPRAEALEQARGllarvGLAdkanhypsmLSGGQQQRVAIARALAMKPQAMLFDEP 182
Cdd:cd03369 89 QDPTLF--SGTIRSNLDPFDEYSDEEIYGALRVSEG-----GLN---------LSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1525903658 183 TSALDPETVGEVLQVMKELAeEGMTMVVVTHEMgfaREVA--DRVVVLDQGELIEQGPP 239
Cdd:cd03369 153 TASIDYATDALIQKTIREEF-TNSTILTIAHRL---RTIIdyDKILVMDAGEVKEYDHP 207
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
10-242 |
2.16e-17 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 80.55 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIR------VNGRAMgYRERSDGSL 83
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWrf*twcANRRAL-RRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 84 VRDSERNIARQRRDIGMVFQRFNLfphmtaleniieapihvlgtPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQR 163
Cdd:NF000106 93 VR*GRRESFSGRENLYMIGR*LDL--------------------SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1525903658 164 VAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQI 242
Cdd:NF000106 153 LDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
10-213 |
2.24e-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: 77.92 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYrersdgslVRDS-E 88
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF--------QRDSiA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 RNIARQRRDIGMVfqrfnlfPHMTALENI-IEAPIHvlgtpRAEALEQArglLARVGLA---DKANHYpsmLSGGQQQRV 164
Cdd:cd03231 73 RGLLYLGHAPGIK-------TTLSVLENLrFWHADH-----SDEQVEEA---LARVGLNgfeDRPVAQ---LSAGQQRRV 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1525903658 165 AIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTH 213
Cdd:cd03231 135 ALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-231 |
1.75e-16 |
|
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: 75.36 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 20 GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLED--IQGGRIRVNGRamgyrersdgslvrdsERNIARQRRd 97
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGR----------------PLDKNFQRS- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 98 IGMVFQRFNLFPHMTALENIieapihvlgtpRAEALeqARGLlarvgladkanhypsmlSGGQQQRVAIARALAMKPQAM 177
Cdd:cd03232 81 TGYVEQQDVHSPNLTVREAL-----------RFSAL--LRGL-----------------SVEQRKRLTIGVELAAKPSIL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1525903658 178 LFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMG---FarEVADRVVVLDQG 231
Cdd:cd03232 131 FLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSasiF--EKFDRLLLLKRG 185
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
28-233 |
2.17e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 78.33 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 28 ISLQVRRGEVVVLIGASGSGKTTFIRCI-NLLEDIQGGRIRVNGRAMGYRERSDGslVRDSERNIARQRRDIGMVfqrfn 106
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNPAQA--IRAGIAMVPEDRKRHGIV----- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 107 lfPHMTALENIIEAPIH---VLGTPRAEALEQA-RGLLARVGLADKANHYP-SMLSGGQQQRVAIARALAMKPQAMLFDE 181
Cdd:TIGR02633 352 --PILGVGKNITLSVLKsfcFKMRIDAAAELQIiGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1525903658 182 PTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGEL 233
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
25-235 |
2.33e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 78.09 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdSERNIARQRRDIGMVFQR 104
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV-------------TAEQPEDYRKLFSAVFTD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 105 FNLFPHMTALEniieapihvlGTPRAEALEQArgLLARVGLADKANHYPSM-----LSGGQQQRVAIARALAMKPQAMLF 179
Cdd:PRK10522 406 FHLFDQLLGPE----------GKPANPALVEK--WLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEERDILLL 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1525903658 180 DEPTSALDPETVGEVLQV-MKELAEEGMTMVVVTHEMGFArEVADRVVVLDQGELIE 235
Cdd:PRK10522 474 DEWAADQDPHFRREFYQVlLPLLQEMGKTIFAISHDDHYF-IHADRLLEMRNGQLSE 529
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-233 |
4.66e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 77.26 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 28 ISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRErsdgslVRDSER-NIA---RQRRDIGMVfq 103
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRS------PRDAIRaGIMlcpEDRKAEGII-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 rfnlfPHMTALENI-IEAPIH-----VLGTPRAEAlEQARGLLARVGLADKANHYPSM-LSGGQQQRVAIARALAMKPQA 176
Cdd:PRK11288 344 -----PVHSVADNInISARRHhlragCLINNRWEA-ENADRFIRSLNIKTPSREQLIMnLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 177 MLFDEPTSALDpetVG---EVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGEL 233
Cdd:PRK11288 418 ILLDEPTRGID---VGakhEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-242 |
4.98e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.47 E-value: 4.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 2 AHKSDELIIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdg 81
Cdd:NF033858 259 ADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-------- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 82 slvrDSeRNIARQRRdIGMVFQRFNLFPHMTALENIieapihVL-----GTPRAEALEQARGLLARVGLADKANHYPSML 156
Cdd:NF033858 331 ----DA-GDIATRRR-VGYMSQAFSLYGELTVRQNL------ELharlfHLPAAEIAARVAEMLERFDLADVADALPDSL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 157 SGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELA-EEGMTMVVVTHEMGFArEVADRVVVLDQGELIE 235
Cdd:NF033858 399 PLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSrEDGVTIFISTHFMNEA-ERCDRISLMHAGRVLA 477
|
....*..
gi 1525903658 236 QGPPEQI 242
Cdd:NF033858 478 SDTPAAL 484
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-246 |
5.57e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 77.06 E-value: 5.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgYRERSDgslvrdserniaRQRRDIGMVFQ 103
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL-TKLQLD------------SWRSRLAVVSQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 RFNLFPHMTAlENIieapihVLGTPRA--EALEQArGLLARV---------GLADKANHYPSMLSGGQQQRVAIARALAM 172
Cdd:PRK10789 397 TPFLFSDTVA-NNI------ALGRPDAtqQEIEHV-ARLASVhddilrlpqGYDTEVGERGVMLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 173 KPQAMLFDEPTSALDPETVGEVLQVMKELAeEGMTMVVVTHEMGFAREvADRVVVLDQGELIEQGPPEQIFSHP 246
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
10-243 |
6.82e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.68 E-value: 6.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 10 IDAQDLHKSFGDLQ-ILKGISLQVRRGEVVVLIGASGSGKTTFIrciNLLED---IQGGRIRVNGRAMGyrERSDGSLvr 85
Cdd:PRK10790 341 IDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLA---SLLMGyypLTEGEIRLDGRPLS--SLSHSVL-- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 86 dserniarqRRDIGMVFQRfnlfPHMTA---LENIieapihVLGTPRAEalEQARGLLARVGLADKANHYP--------- 153
Cdd:PRK10790 414 ---------RQGVAMVQQD----PVVLAdtfLANV------TLGRDISE--EQVWQALETVQLAELARSLPdglytplge 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 154 --SMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEgMTMVVVTHEMGFAREvADRVVVLDQG 231
Cdd:PRK10790 473 qgNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLSTIVE-ADTILVLHRG 550
|
250
....*....|..
gi 1525903658 232 ELIEQGPPEQIF 243
Cdd:PRK10790 551 QAVEQGTHQQLL 562
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-242 |
7.26e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.63 E-value: 7.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 28 ISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGR---AMGYRERSDGSLVRDSERniaRQRRDI------ 98
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKeinALSTAQRLARGLVYLPED---RQSSGLyldapl 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 99 -----GMVFQRFNLFPHMTALENIIEAPIHVLGTPRAEALEQARGLlarvgladkanhypsmlSGGQQQRVAIARALAMK 173
Cdd:PRK15439 359 awnvcALTHNRRGFWIKPARENAVLERYRRALNIKFNHAEQAARTL-----------------SGGNQQKVLIAKCLEAS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1525903658 174 PQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQI 242
Cdd:PRK15439 422 PQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-234 |
1.20e-15 |
|
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: 76.13 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 23 QILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLE-DIQGGRIRVNGRAMGYRERS---DGSL-VRDserNIARQRRD 97
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDkDFNGEARPQPGIKVGYLPQEpqlDPTKtVRE---NVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 98 IGMVFQRFN---------------LFPHMTALENIIEApihVLGTPRAEALEQARGLLaRV--GLADKANhypsmLSGGQ 160
Cdd:TIGR03719 96 IKDALDRFNeisakyaepdadfdkLAAEQAELQEIIDA---ADAWDLDSQLEIAMDAL-RCppWDADVTK-----LSGGE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 161 QQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELaeEGmTMVVVTHEMGFAREVADRVVVLDQGELI 234
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PG-TVVAVTHDRYFLDNVAGWILELDRGRGI 237
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-228 |
3.03e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 72.44 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 13 QDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdSERNIA 92
Cdd:PRK10247 11 QNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI-------------STLKPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 93 RQRRDIGMVFQRFNLFPHmTALENIIeAPIHVLG-TPRAEALeqaRGLLARVGLADKANHYP-SMLSGGQQQRVAIARAL 170
Cdd:PRK10247 78 IYRQQVSYCAQTPTLFGD-TVYDNLI-FPWQIRNqQPDPAIF---LDDLERFALPDTILTKNiAELSGGEKQRISLIRNL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525903658 171 AMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEmgfAREV--ADRVVVL 228
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHD---KDEInhADKVITL 210
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-233 |
6.82e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.88 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSDG---SLVRDSERniarQRRD---I 98
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlanGIVYISED----RKRDglvL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 99 GM-VFQRFNLfphmTALENIIEAPIHVLGTPRAEALEQARGLLarvgladkaN-HYPSM------LSGGQQQRVAIARAL 170
Cdd:PRK10762 344 GMsVKENMSL----TALRYFSRAGGSLKHADEQQAVSDFIRLF---------NiKTPSMeqaiglLSGGNQQKVAIARGL 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525903658 171 AMKPQAMLFDEPTSALDpetVG---EVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGEL 233
Cdd:PRK10762 411 MTRPKVLILDEPTRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
18-246 |
1.24e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.30 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 18 SFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCInllediqggrirvngraMGYRERSDGSLVRDserniarQRRD 97
Cdd:PRK09544 13 SFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVV-----------------LGLVAPDEGVIKRN-------GKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 98 IGMVFQRFNLFPHMtaleniieaPIHVL-------GTPRAEALEQarglLARVGLADKANHYPSMLSGGQQQRVAIARAL 170
Cdd:PRK09544 69 IGYVPQKLYLDTTL---------PLTVNrflrlrpGTKKEDILPA----LKRVQAGHLIDAPMQKLSGGETQRVLLARAL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525903658 171 AMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDQgELIEQGPPEQIFSHP 246
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHP 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
28-233 |
1.97e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.27 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 28 ISLQVRRGEVVVLIGASGSGKTTFIRCInlLEDIQG---GRIRVNGRAMGyrersdgslVRDSERNIarqRRDIGMVFQ- 103
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCL--FGAYPGrweGEIFIDGKPVK---------IRNPQQAI---AQGIAMVPEd 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 --RFNLFPHMTALENIIEAPIHVLGTPRA--EALEQ--ARGLLARvgLADKANHyPSM----LSGGQQQRVAIARALAMK 173
Cdd:PRK13549 347 rkRDGIVPVMGVGKNITLAALDRFTGGSRidDAAELktILESIQR--LKVKTAS-PELaiarLSGGNQQKAVLAKCLLLN 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525903658 174 PQAMLFDEPTSALDpetVG---EVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGEL 233
Cdd:PRK13549 424 PKILILDEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
9-248 |
3.00e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 70.63 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCinLLEDIQG----------GRIRVNGRAMGYRE- 77
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKA--LAGDLTGggaprgarvtGDVTLNGEPLAAIDa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 78 ----RSDGSLVRDSERNIARQRRDIGMVfqrfNLFPHMTALeniieapihvlGTPRAEALEQARGLLARVGLADKANHYP 153
Cdd:PRK13547 79 prlaRLRAVLPQAAQPAFAFSAREIVLL----GRYPHARRA-----------GALTHRDGEIAWQALALAGATALVGRDV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 154 SMLSGGQQQRVAIARALAM---------KPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVAD 223
Cdd:PRK13547 144 TTLSGGELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHAD 223
|
250 260
....*....|....*....|....*
gi 1525903658 224 RVVVLDQGELIEQGPPEQIFShPSH 248
Cdd:PRK13547 224 RIAMLADGAIVAHGAPADVLT-PAH 247
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-228 |
5.46e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 70.97 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 33 RRGEVVVLIGASGSGKTTFIRcinlledIQGGRIRVN-GRAmgyrersdgslvrDSERniarqrrDIGMVFQRFN---LF 108
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALK-------ILSGELKPNlGDY-------------DEEP-------SWDEVLKRFRgteLQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 109 PHMTALEN-----------IIEAPIHVLGTPRaEALEQA--RGLLA----RVGLADKANHYPSMLSGGQQQRVAIARALA 171
Cdd:COG1245 150 DYFKKLANgeikvahkpqyVDLIPKVFKGTVR-ELLEKVdeRGKLDelaeKLGLENILDRDISELSGGELQRVAIAAALL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 172 MKPQAMLFDEPTSALDpetVGE---VLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVL 228
Cdd:COG1245 229 RDADFYFFDEPSSYLD---IYQrlnVARLIRELAEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-244 |
1.33e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 70.36 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgslvrdserNIArqrrDIGMVFQ 103
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGL------------------NIA----KIGLHDL 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 RFNLfphmtaleNII-EAPIHVLGTPRAE--------------ALEQARGLLARVGLADKANHYPSM----LSGGQQQRV 164
Cdd:TIGR00957 1359 RFKI--------TIIpQDPVLFSGSLRMNldpfsqysdeevwwALELAHLKTFVSALPDKLDHECAEggenLSVGQRQLV 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 165 AIARALAMKPQAMLFDEPTSALDPETvGEVLQVMKELAEEGMTMVVVTHEMGFAREVAdRVVVLDQGELIEQGPPEQIFS 244
Cdd:TIGR00957 1431 CLARALLRKTKILVLDEATAAVDLET-DNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-240 |
1.67e-13 |
|
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: 68.20 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 32 VRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRER-----SDGSlVRDserniarqrrdigMVFQRFN 106
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQyikadYEGT-VRD-------------LLSSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 107 LFPHMTALENIIEAPIHVLGTPRAEALEqargllarvgladkanhypsmLSGGQQQRVAIARALAMKPQAMLFDEPTSAL 186
Cdd:cd03237 88 DFYTHPYFKTEIAKPLQIEQILDREVPE---------------------LSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1525903658 187 DPETVGEVLQVMKELAEEG-MTMVVVTHEMGFAREVADRVVVLDqGELIEQG---PPE 240
Cdd:cd03237 147 DVEQRLMASKVIRRFAENNeKTAFVVEHDIIMIDYLADRLIVFE-GEPSVNGvanPPQ 203
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-234 |
5.26e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.44 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 18 SFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCIN---LLEDiqgGRIRVNGRAMGYRersdgsLVRDSERN---- 90
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLDD---GRIIYEQDLIVAR------LQQDPPRNvegt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 91 ----IARQRRDIGMVFQRFNLFPHMTALENIiEAPIHVLGTPRaEALEQARG---------LLARVGL-ADKAnhyPSML 156
Cdd:PRK11147 83 vydfVAEGIEEQAEYLKRYHDISHLVETDPS-EKNLNELAKLQ-EQLDHHNLwqlenrineVLAQLGLdPDAA---LSSL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525903658 157 SGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELaeEGmTMVVVTHEMGFAREVADRVVVLDQGELI 234
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QG-SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
8-234 |
8.48e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.61 E-value: 8.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 8 LIIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCinLLEDIQ--GGRIRVNGRA-MGYrersdgsLV 84
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRT--LVGELEpdSGTVKWSENAnIGY-------YA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 85 RDSERNIArqrRDIgmvfqrfNLFPHMTALEniieapihvlgtpRAEALEQA-RGLLARVGL-ADKANHYPSMLSGGQQQ 162
Cdd:PRK15064 389 QDHAYDFE---NDL-------TLFDWMSQWR-------------QEGDDEQAvRGTLGRLLFsQDDIKKSVKVLSGGEKG 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525903658 163 RVAIARALAMKPQAMLFDEPTSALDPETVgEVLQVMKELAEEgmTMVVVTHEMGFAREVADRVVVLDQGELI 234
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMDMESI-ESLNMALEKYEG--TLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-247 |
9.56e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.88 E-value: 9.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGR---AMGYRErsdgslvrdserniarQRRDIGM 100
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGReigAYGLRE----------------LRRQFSM 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 101 VFQ---------RFNLFPHMTALENIIEAPIHVLGTpRAEALEQARGLLARVgLADKANHypsmlSGGQQQRVAIARALA 171
Cdd:PTZ00243 1389 IPQdpvlfdgtvRQNVDPFLEASSAEVWAALELVGL-RERVASESEGIDSRV-LEGGSNY-----SVGQRQLMCMARALL 1461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1525903658 172 MKPQA-MLFDEPTSALDPeTVGEVLQVMKELAEEGMTMVVVTHEMgfaREVA--DRVVVLDQGELIEQGPPEQIFSHPS 247
Cdd:PTZ00243 1462 KKGSGfILMDEATANIDP-ALDRQIQATVMSAFSAYTVITIAHRL---HTVAqyDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-217 |
1.13e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.28 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 2 AHKSDELIIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCinLLEDIQ--GGRIRVnGRAM------ 73
Cdd:PRK11147 312 ASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKL--MLGQLQadSGRIHC-GTKLevayfd 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 74 GYRERSDGSlvRDSERNIARQRRDIgMV----------FQRFnLFPHMTALeniieapihvlgTPRaealeqargllarv 143
Cdd:PRK11147 389 QHRAELDPE--KTVMDNLAEGKQEV-MVngrprhvlgyLQDF-LFHPKRAM------------TPV-------------- 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 144 gladKAnhypsmLSGGQQQRVAIARaLAMKPQAML-FDEPTSALDPETVgEVLQVMkeLAEEGMTMVVVTHEMGF 217
Cdd:PRK11147 439 ----KA------LSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLDVETL-ELLEEL--LDSYQGTVLLVSHDRQF 499
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-231 |
1.22e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyRERSDGSLVRDSERNIARQRRDIGMVFQ- 103
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI--NNHNANEAINHGFALVTEERRSTGIYAYl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 --RFN-LFPHMTALENiieaPIHVLGTPRAEALEQARGLLARVGLADKANHYPSmLSGGQQQRVAIARALAMKPQAMLFD 180
Cdd:PRK10982 342 diGFNsLISNIRNYKN----KVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGS-LSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1525903658 181 EPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQG 231
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-238 |
1.46e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.06 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 23 QILKGISLQVRRGEVVVLIGASGSGKTTFIRCINllEDIQGGRIRVNGRAmgyreRSDGSLVRDSERniaRQRRDIGMVF 102
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIA--SNTDGFHIGVEGVI-----TYDGITPEEIKK---HYRGDVVYNA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 103 QRFNLFPHMTALENIIEAP------IHVLGTPRAEALEQARGLLARV-GLADK-----ANHYPSMLSGGQQQRVAIARAL 170
Cdd:TIGR00956 145 ETDVHFPHLTVGETLDFAArcktpqNRPDGVSREEYAKHIADVYMATyGLSHTrntkvGNDFVRGVSGGERKRVSIAEAS 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 171 AMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVT--HEMGFAREVADRVVVLDQGELIEQGP 238
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQIYFGP 294
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-231 |
1.48e-12 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 65.04 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 21 DLQILKGISLQVRRGEVVVLIGASGSGKTTfircinLLEDIQGGRIRVNGRAMGYRERSDGSLVRDSErniARQRRDIGM 100
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSS------LLLAILGEMQTLEGKVHWSNKNESEPSFEATR---SRNRYSVAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 101 VFQRFNLFpHMTALENIIeapihvLGTP----RAEALEQARGL-----LARVGLADKANHYPSMLSGGQQQRVAIARALA 171
Cdd:cd03290 84 AAQKPWLL-NATVEENIT------FGSPfnkqRYKAVTDACSLqpdidLLPFGDQTEIGERGINLSGGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525903658 172 MKPQAMLFDEPTSALDPETVGEVLQ--VMKELAEEGMTMVVVTHEMGFAREvADRVVVLDQG 231
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
14-232 |
1.95e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.37 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 14 DLHKSFGD--LQILKGislQVRRGEVVVLIGASGSGKTTFIRcinlledIQGGRIrvngramgyrERSDGSLvrDSERNI 91
Cdd:PRK13409 345 DLTKKLGDfsLEVEGG---EIYEGEVIGIVGPNGIGKTTFAK-------LLAGVL----------KPDEGEV--DPELKI 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 92 A----RQRRDIGMVFQRFnlfphmtaLENIIEApihvLGTP--RAEaleqargLLARVGLADKANHYPSMLSGGQQQRVA 165
Cdd:PRK13409 403 SykpqYIKPDYDGTVEDL--------LRSITDD----LGSSyyKSE-------IIKPLQLERLLDKNVKDLSGGELQRVA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525903658 166 IARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDqGE 232
Cdd:PRK13409 464 IAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLMVFE-GE 530
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
9-213 |
2.97e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.10 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRERSdgslvrdse 88
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 rniarqrRDIGMVFQRFNLFPHMTALENiieapIHVLGTPRAEALEQARG-LLARVGLADKANHYPSMLSGGQQQRVAIA 167
Cdd:PRK13543 82 -------RFMAYLGHLPGLKADLSTLEN-----LHFLCGLHGRRAKQMPGsALAIVGLAGYEDTLVRQLSAGQKKRLALA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1525903658 168 RaLAMKPQAM-LFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTH 213
Cdd:PRK13543 150 R-LWLSPAPLwLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-222 |
6.56e-12 |
|
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: 64.96 E-value: 6.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 7 ELIIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVngramgyrersdGSLVrd 86
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI------------GETV-- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 87 serniarqrrDIGMVFQ-RFNLFPHMTALENIIE-APIHVLGTPRAealeQARGLLARVGL--ADKaNHYPSMLSGGQQQ 162
Cdd:TIGR03719 386 ----------KLAYVDQsRDALDPNKTVWEEISGgLDIIKLGKREI----PSRAYVGRFNFkgSDQ-QKKVGQLSGGERN 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525903658 163 RVAIARALAMKPQAMLFDEPTSALDPETvgevLQVMKE-LAEEGMTMVVVTHEMGFAREVA 222
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVET----LRALEEaLLNFAGCAVVISHDRWFLDRIA 507
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-231 |
7.97e-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: 65.03 E-value: 7.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 32 VRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdserniarqRRDIGMVFQRFNLFPHM 111
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI---------------------LTNISDVHQNMGYCPQF 2020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 112 TALENIIEAPIHVL------GTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEPTSA 185
Cdd:TIGR01257 2021 DAIDDLLTGREHLYlyarlrGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTG 2100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1525903658 186 LDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQG 231
Cdd:TIGR01257 2101 MDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-238 |
8.41e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.97 E-value: 8.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 20 GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGrAMGYRERSdGSLVRDSERniarqrrdig 99
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYVPQQ-AWIQNDSLR---------- 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 100 mvfqrfnlfphmtalENIIEApiHVLGTPRAEALEQARGLLA---------RVGLADKANHypsmLSGGQQQRVAIARAL 170
Cdd:TIGR00957 717 ---------------ENILFG--KALNEKYYQQVLEACALLPdleilpsgdRTEIGEKGVN----LSGGQKQRVSLARAV 775
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525903658 171 AMKPQAMLFDEPTSALDPETVGEVLQvmKELAEEGM----TMVVVTHEMGFAREVaDRVVVLDQGELIEQGP 238
Cdd:TIGR00957 776 YSNADIYLFDDPLSAVDAHVGKHIFE--HVIGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGS 844
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-242 |
8.80e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.37 E-value: 8.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 14 DLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMGYRErSDGSLvrdserniar 93
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKS-SKEAL---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 94 qRRDIGMVFQRFNLFPHMTALENII--EAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALA 171
Cdd:PRK10982 72 -ENGISMVHQELNLVLQRSVMDNMWlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525903658 172 MKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQI 242
Cdd:PRK10982 151 YNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-237 |
1.48e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.74 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 4 KSDELIIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCI--NLLEDIQGGRIRVNGRAMgyrersdg 81
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESI-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 82 sLVRDSErniARQRRDIGMVFQrfnlFP-------HMTALENIIEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPS 154
Cdd:CHL00131 74 -LDLEPE---ERAHLGIFLAFQ----YPieipgvsNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 155 M-----LSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHemgFARE----VADRV 225
Cdd:CHL00131 146 RnvnegFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH---YQRLldyiKPDYV 222
|
250
....*....|..
gi 1525903658 226 VVLDQGELIEQG 237
Cdd:CHL00131 223 HVMQNGKIIKTG 234
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
14-232 |
2.83e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.88 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 14 DLHKSFGD--LQILKGislQVRRGEVVVLIGASGSGKTTFIRcinlledIQGGRIrvngramgyrERSDGSLvrDSERNI 91
Cdd:COG1245 346 DLTKSYGGfsLEVEGG---EIREGEVLGIVGPNGIGKTTFAK-------ILAGVL----------KPDEGEV--DEDLKI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 92 ARQRrdigmvfQRFNLFPHMTALENIIEAPIHVLGTPRAEAlEQARGL-LARvgLADKanhYPSMLSGGQQQRVAIARAL 170
Cdd:COG1245 404 SYKP-------QYISPDYDGTVEEFLRSANTDDFGSSYYKT-EIIKPLgLEK--LLDK---NVKDLSGGELQRVAIAACL 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525903658 171 AMKPQAMLFDEPTSALDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFAREVADRVVVLDqGE 232
Cdd:COG1245 471 SRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLMVFE-GE 532
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-244 |
4.61e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.34 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 22 LQILKGI------------SLQVRRGEVVVLIGASGSGKTTFIRCInllediQGGRIRVNGRamgyRERSDGSLVRDSer 89
Cdd:PRK10938 4 LQISQGTfrlsdtktlqlpSLTLNAGDSWAFVGANGSGKSALARAL------AGELPLLSGE----RQSQFSHITRLS-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 nIARQRRDIGMVFQRFN---LFPH-----MTALENIIEapiHVLGTPRAEALEQARGLLArvgLADKANHYpsmLSGGQQ 161
Cdd:PRK10938 72 -FEQLQKLVSDEWQRNNtdmLSPGeddtgRTTAEIIQD---EVKDPARCEQLAQQFGITA---LLDRRFKY---LSTGET 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 162 QRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQ 241
Cdd:PRK10938 142 RKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREE 221
|
...
gi 1525903658 242 IFS 244
Cdd:PRK10938 222 ILQ 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
156-242 |
5.90e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.45 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 156 LSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQvmKELAEE--GMTMVVVTHEMGFAREVaDRVVVLDQGEL 233
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDElrGKTRVLVTNQLHFLSQV-DRIILVHEGMI 817
|
....*....
gi 1525903658 234 IEQGPPEQI 242
Cdd:PLN03130 818 KEEGTYEEL 826
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
20-234 |
1.03e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.29 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 20 GDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLE-DIQGGRIRVNGRAMGYRERS---DGSL-VRDserNIARQ 94
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDkEFEGEARPAPGIKVGYLPQEpqlDPEKtVRE---NVEEG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 95 RRDIGMVFQRFN---------------LFPHMTALENIIEApihvlgtprAEA------LEQARGLL------ARVGLad 147
Cdd:PRK11819 95 VAEVKAALDRFNeiyaayaepdadfdaLAAEQGELQEIIDA---------ADAwdldsqLEIAMDALrcppwdAKVTK-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 148 kanhypsmLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVgEVLQvmKELAEEGMTMVVVTHEMGFAREVADRVVV 227
Cdd:PRK11819 164 --------LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV-AWLE--QFLHDYPGTVVAVTHDRYFLDNVAGWILE 232
|
....*..
gi 1525903658 228 LDQGELI 234
Cdd:PRK11819 233 LDRGRGI 239
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-258 |
1.32e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.53 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRamgyrersdgslvrdserniarqrrDIGmvfq 103
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDC-------------------------DVA---- 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 RFNLFPHMTALENIIEAPIHVLGTPRA--------------EALEQA--RGLLAR--VGLADKANHYPSMLSGGQQQRVA 165
Cdd:PLN03232 1302 KFGLTDLRRVLSIIPQSPVLFSGTVRFnidpfsehndadlwEALERAhiKDVIDRnpFGLDAEVSEGGENFSVGQRQLLS 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 166 IARALAMKPQAMLFDEPTSALDPETVGEVLQVMKElAEEGMTMVVVTHEMGFAREvADRVVVLDQGELIEQGPPEQIFSH 245
Cdd:PLN03232 1382 LARALLRRSKILVLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSR 1459
|
250
....*....|...
gi 1525903658 246 pshpRTRAFLSRV 258
Cdd:PLN03232 1460 ----DTSAFFRMV 1468
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-228 |
1.39e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 32 VRRGEVVVLIGASGSGKTTFIRcinlledIQGGRIRVN-GRAmgyrersdgslvrDSERNIARqrrdigmVFQRFN---L 107
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVK-------ILSGELIPNlGDY-------------EEEPSWDE-------VLKRFRgteL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 108 FPHMTALEN-----------IIEAPIHVLGTPRaEALEQA--RG----LLARVGLADKANHYPSMLSGGQQQRVAIARAL 170
Cdd:PRK13409 149 QNYFKKLYNgeikvvhkpqyVDLIPKVFKGKVR-ELLKKVdeRGkldeVVERLGLENILDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525903658 171 AMKPQAMLFDEPTSALDpetVGE---VLQVMKELAeEGMTMVVVTHEMGFAREVADRVVVL 228
Cdd:PRK13409 228 LRDADFYFFDEPTSYLD---IRQrlnVARLIRELA-EGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
9-214 |
1.88e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.81 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvrdsE 88
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI--------------K 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 RNIARQRRDIGMVFQRFNLFPHMTALENIIeAPIHVLGTpraeALEQARglLARVGLADKANHYP-SMLSGGQQQRVAIA 167
Cdd:PRK13540 67 KDLCTYQKQLCFVGHRSGINPYLTLRENCL-YDIHFSPG----AVGITE--LCRLFSLEHLIDYPcGLLSSGQKRQVALL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1525903658 168 RALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHE 214
Cdd:PRK13540 140 RLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
9-237 |
1.97e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.42 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 9 IIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLED--IQGGRIRVNGRAMGYRERSDgslvrd 86
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPED------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 87 serniaRQRRDIGMVFQR-------FNLFPHMTAL-----------------ENIIEAPIHVLGTPraealeqaRGLLAR 142
Cdd:PRK09580 75 ------RAGEGIFMAFQYpveipgvSNQFFLQTALnavrsyrgqepldrfdfQDLMEEKIALLKMP--------EDLLTR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 143 ---VGladkanhypsmLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAR 219
Cdd:PRK09580 141 svnVG-----------FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILD 209
|
250
....*....|....*....
gi 1525903658 220 EVA-DRVVVLDQGELIEQG 237
Cdd:PRK09580 210 YIKpDYVHVLYQGRIVKSG 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-243 |
2.15e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.76 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTFIRC-INLLEDIQGGRIRVNGrAMGYRERSD---GSLVRDserNIArqrrdIGM 100
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVIRG-SVAYVPQVSwifNATVRE---NIL-----FGS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 101 VFQ--RFNLFPHMTALENIIEApihVLGTPRAEALEqaRGLlarvgladkanhypsMLSGGQQQRVAIARALAMKPQAML 178
Cdd:PLN03232 704 DFEseRYWRAIDVTALQHDLDL---LPGRDLTEIGE--RGV---------------NISGGQKQRVSMARAVYSNSDIYI 763
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 179 FDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVaDRVVVLDQGELIEQGPPEQIF 243
Cdd:PLN03232 764 FDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS 827
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-244 |
2.27e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.52 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNG---RAMGyrersdgslvrdsernIARQRRDIGM 100
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiSKFG----------------LMDLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 101 VFQ---------RFNLFP---HMTAleniieapihvlgtPRAEALEQA----------RGLLARVGLADKAnhypsmLSG 158
Cdd:PLN03130 1318 IPQapvlfsgtvRFNLDPfneHNDA--------------DLWESLERAhlkdvirrnsLGLDAEVSEAGEN------FSV 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 159 GQQQRVAIARALAMKPQAMLFDEPTSALDpetVGEVLQVMKELAEE--GMTMVVVTHEMGFAREvADRVVVLDQGELIEQ 236
Cdd:PLN03130 1378 GQRQLLSLARALLRRSKILVLDEATAAVD---VRTDALIQKTIREEfkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEF 1453
|
....*...
gi 1525903658 237 GPPEQIFS 244
Cdd:PLN03130 1454 DTPENLLS 1461
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
154-228 |
4.62e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.53 E-value: 4.62e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 154 SMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVL 228
Cdd:cd03236 138 DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
22-238 |
5.38e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.47 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 22 LQILKGISLQVRRGEVVVLIGASGSGKTTfircinlLEDIQGGR---------IRVNG---------RAMGYRERSD--- 80
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTT-------LMDVLAGRktggyiegdIRISGfpkkqetfaRISGYCEQNDihs 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 81 -GSLVRDSerniarqrrdigMVFQRFnlfphmtaleniIEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSM--LS 157
Cdd:PLN03140 966 pQVTVRES------------LIYSAF------------LRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVtgLS 1021
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 158 GGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGF-AREVADRVVVLDQ-GELIE 235
Cdd:PLN03140 1022 TEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLMKRgGQVIY 1101
|
...
gi 1525903658 236 QGP 238
Cdd:PLN03140 1102 SGP 1104
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-231 |
6.22e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.41 E-value: 6.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIrvngramgYRERSdgslvrdserniarqrrdIGMVFQ 103
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------WAERS------------------IAYVPQ 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 RFNLFpHMTALENII----EAPIHVLGTPRAEALEQARGLLARvGLADKANHYPSMLSGGQQQRVAIARALAMKPQAMLF 179
Cdd:PTZ00243 729 QAWIM-NATVRGNILffdeEDAARLADAVRVSQLEADLAQLGG-GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 180 DEPTSALDPEtVGEvlQVMKEL---AEEGMTMVVVTHEMGFArEVADRVVVLDQG 231
Cdd:PTZ00243 807 DDPLSALDAH-VGE--RVVEECflgALAGKTRVLATHQVHVV-PRADYVVALGDG 857
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-232 |
6.53e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 21 DLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNG------------------------------ 70
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdinlkwwrskigvvsqdpllfsnsi 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 71 --------------RAMGYRERSDGSlvrDSERNIARQRRDIGMVFQRFNLFPHMTALENIIEAPIHVLGTPRAEALEQA 136
Cdd:PTZ00265 477 knnikyslyslkdlEALSNYYNEDGN---DSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQTIKDSEVVDVS 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 137 RGLLAR---VGLADK----ANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKEL-AEEGMTM 208
Cdd:PTZ00265 554 KKVLIHdfvSALPDKyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRIT 633
|
250 260
....*....|....*....|....
gi 1525903658 209 VVVTHEMGFAReVADRVVVLDQGE 232
Cdd:PTZ00265 634 IIIAHRLSTIR-YANTIFVLSNRE 656
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
154-237 |
8.40e-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: 56.56 E-value: 8.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 154 SMLSGGQQQRVAIARALAMKPQAMLF--DEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREvADRVVVL--- 228
Cdd:cd03238 86 STLSGGELQRVKLASELFSEPPGTLFilDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFgpg 164
|
90
....*....|..
gi 1525903658 229 ---DQGELIEQG 237
Cdd:cd03238 165 sgkSGGKVVFSG 176
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
156-239 |
1.12e-09 |
|
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: 57.24 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 156 LSGGQQQRVAIARALAMK---PQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAReVADRVVVLDQ-- 230
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK-CADWIIDLGPeg 248
|
90
....*....|...
gi 1525903658 231 ----GELIEQGPP 239
Cdd:cd03271 249 gdggGQVVASGTP 261
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
156-259 |
1.45e-09 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 58.11 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 156 LSGGQQQRVAIARALAMKPQA---MLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMgfarEV---ADRVVVL- 228
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTGktlYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNL----DViktADWIIDLg 902
|
90 100 110
....*....|....*....|....*....|....*..
gi 1525903658 229 ----DQ-GELIEQGPPEQIFSHP-SHprTRAFLSRVL 259
Cdd:COG0178 903 peggDGgGEIVAEGTPEEVAKVKaSY--TGRYLKEYL 937
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
152-244 |
1.65e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 152 YPSMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEG-MTMVVVTHEMGFAREvADRVVVLDQ 230
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKR-SDKIVVFNN 1433
|
90
....*....|....*....
gi 1525903658 231 ----GELIE-QGPPEQIFS 244
Cdd:PTZ00265 1434 pdrtGSFVQaHGTHEELLS 1452
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
156-229 |
1.74e-09 |
|
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: 55.66 E-value: 1.74e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 156 LSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGM-TMVVVTHEMGFAREVADRVVVLD 229
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-234 |
4.63e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.34 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 16 HKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCI-------NLlediqGGRIRVNGRAMgyrersDGSLVRDSE 88
Cdd:NF040905 267 HPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrsygrNI-----SGTVFKDGKEV------DVSTVSDAI 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 89 RN-IA---RQRRDIGMVfqrfnlfphmtaLENIIEAPIHVLGTPRaealeqarglLARVGLADK------ANHY------ 152
Cdd:NF040905 336 DAgLAyvtEDRKGYGLN------------LIDDIKRNITLANLGK----------VSRRGVIDEneeikvAEEYrkkmni 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 153 --PSM------LSGGQQQRVAIARALAMKPQAMLFDEPTSALDpetVG---EVLQVMKELAEEGMTMVVVTHEMGFAREV 221
Cdd:NF040905 394 ktPSVfqkvgnLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGM 470
|
250
....*....|...
gi 1525903658 222 ADRVVVLDQGELI 234
Cdd:NF040905 471 CDRIYVMNEGRIT 483
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
156-242 |
5.27e-09 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 56.56 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 156 LSGGQQQRVAIARALAMK---PQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAReVADRVVVLDQ-- 230
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIK-TADYIIDLGPeg 908
|
90
....*....|....*.
gi 1525903658 231 ----GELIEQGPPEQI 242
Cdd:TIGR00630 909 gdggGTVVASGTPEEV 924
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-190 |
5.58e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 5.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 8 LIIDAQDLHKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVngramgyrersdGSLVRds 87
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI------------GETVK-- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 88 erniarqrrdIGMVFQ-RFNLFPHMTALENIIE-APIHVLGtpRAEAleQARGLLARVGL--AD---KAnhypSMLSGGQ 160
Cdd:PRK11819 389 ----------LAYVDQsRDALDPNKTVWEEISGgLDIIKVG--NREI--PSRAYVGRFNFkgGDqqkKV----GVLSGGE 450
|
170 180 190
....*....|....*....|....*....|
gi 1525903658 161 QQRVAIARALAMKPQAMLFDEPTSALDPET 190
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-232 |
1.30e-08 |
|
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: 54.48 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRaMGYRERSDGSLVRDSERNIArqrrdIGMVFQ 103
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISFSSQFSWIMPGTIKENII-----FGVSYD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 RFNLFPHMTAL---ENIIEAPihvlgtpraealEQARGLLARVGLadkanhypsMLSGGQQQRVAIARALAMKPQAMLFD 180
Cdd:cd03291 126 EYRYKSVVKACqleEDITKFP------------EKDNTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 181 EPTSALDPETVGEVLQ--VMKELAEEgmTMVVVTHEMGFAREvADRVVVLDQGE 232
Cdd:cd03291 185 SPFGYLDVFTEKEIFEscVCKLMANK--TRILVTSKMEHLKK-ADKILILHEGS 235
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
28-213 |
3.37e-08 |
|
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: 53.98 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 28 ISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRA----------MGYRERSDGSLVRDSERNIarQRRD 97
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGklfyvpqrpyMTLGTLRDQIIYPDSSEDM--KRRG 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 98 IGMvfqrfnlfphmTALENIIEapihvlgtpraeaLEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAM 177
Cdd:TIGR00954 549 LSD-----------KDLEQILD-------------NVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFA 604
|
170 180 190
....*....|....*....|....*....|....*.
gi 1525903658 178 LFDEPTSALDPETVGEVLQVMKELaeeGMTMVVVTH 213
Cdd:TIGR00954 605 ILDECTSAVSVDVEGYMYRLCREF---GITLFSVSH 637
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
25-226 |
3.64e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 52.65 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTfircinLLEDI---QGGRIRVNGRAMGYRERSdGSLVRDSERNIARQRRDIGMV 101
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSS------LAFDTiyaEGQRRYVESLSAYARQFL-GQMDKPDVDSIEGLSPAIAID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 102 FQRFNLFPHMTaleniieapihvLGTpRAEALEQARGLLARVGLADKAN-------HYPSM------LSGGQQQRVAIAR 168
Cdd:cd03270 84 QKTTSRNPRST------------VGT-VTEIYDYLRLLFARVGIRERLGflvdvglGYLTLsrsaptLSGGEAQRIRLAT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 169 ALAMKPQAML--FDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREvADRVV 226
Cdd:cd03270 151 QIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVI 209
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-231 |
3.90e-08 |
|
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: 53.76 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRaMGYRERSDGSLVRDSERNIArqrrdIGMVFQ 103
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-ISFSPQTSWIMPGTIKDNII-----FGLSYD 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 RFNLFPHMTALEniIEAPIHVLGtpraealEQARGLLARVGLAdkanhypsmLSGGQQQRVAIARALAMKPQAMLFDEPT 183
Cdd:TIGR01271 515 EYRYTSVIKACQ--LEEDIALFP-------EKDKTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1525903658 184 SALDPETVGEVLQ--VMKELAEEgmTMVVVTHEMGFAREvADRVVVLDQG 231
Cdd:TIGR01271 577 THLDVVTEKEIFEscLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
24-245 |
5.86e-08 |
|
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: 52.22 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGramgyrersdgslVRDSERNIARQRRDIGMVFQ 103
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG-------------IDISKLPLHTLRSRLSIILQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 ---------RFNLFPHMTALENIIeapihvlgtprAEALE--QARGLLARV--GLADKANHYPSMLSGGQQQRVAIARAL 170
Cdd:cd03288 103 dpilfsgsiRFNLDPECKCTDDRL-----------WEALEiaQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAF 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525903658 171 AMKPQAMLFDEPTSALDPETvGEVLQ--VMKELAEEgmTMVVVTHEMGFAREvADRVVVLDQGELIEQGPPEQIFSH 245
Cdd:cd03288 172 VRKSSILIMDEATASIDMAT-ENILQkvVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ 244
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
156-259 |
6.36e-08 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 53.15 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 156 LSGGQQQRVAIARALAMKPQA---MLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMgfarEV---ADRVVVL- 228
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTGktlYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNL----DViktADWIIDLg 906
|
90 100 110
....*....|....*....|....*....|....*..
gi 1525903658 229 ----DQ-GELIEQGPPEQIFSHP-SHprTRAFLSRVL 259
Cdd:PRK00349 907 peggDGgGEIVATGTPEEVAKVEaSY--TGRYLKPVL 941
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-213 |
8.35e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 18 SFGDLQILKGISLQVRRGEVVVLIGASGSGKTTfircinLLEDIQGGRirvngrAMGY--------RERSDGSLVRDSER 89
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKST------LLSLITGDH------PQGYsndltlfgRRRGSGETIWDIKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 90 NIarqrrdiGMVFQRFnlfpHM------TALENIIEAPIHVLGTPRA--EALEQ-ARGLLARVGLADK-ANHYPSMLSGG 159
Cdd:PRK10938 337 HI-------GYVSSSL----HLdyrvstSVRNVILSGFFDSIGIYQAvsDRQQKlAQQWLDILGIDKRtADAPFHSLSWG 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 160 QQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMT-MVVVTH 213
Cdd:PRK10938 406 QQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSH 460
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
156-256 |
1.39e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 51.94 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 156 LSGGQQQRVAIARALAMKPQAMLF--DEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREvADRVVVLDQ--- 230
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRA-ADYVIDIGPgag 567
|
90 100
....*....|....*....|....*....
gi 1525903658 231 ---GELIEQGPPEQIFSHPsHPRTRAFLS 256
Cdd:TIGR00630 568 ehgGEVVASGTPEEILANP-DSLTGQYLS 595
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
156-255 |
1.79e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.75 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 156 LSGGQQQRVAIARALAMKPQAMLF--DEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFArEVADRVVVLDQ--- 230
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGITYilDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRIIDIGPgag 555
|
90 100
....*....|....*....|....*...
gi 1525903658 231 ---GELIEQGPPEQiFSHPSHPRTRAFL 255
Cdd:PRK00635 556 ifgGEVLFNGSPRE-FLAKSDSLTAKYL 582
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-242 |
4.32e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.51 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 19 FGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNGRAMgyrersdgslvRDserniARQRRDI 98
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM-----------AD-----ARHRRAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 99 GmvfQRF---------NLFPHMTALENiIEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARA 169
Cdd:NF033858 75 C---PRIaympqglgkNLYPTLSVFEN-LDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 170 LAMKPQAMLFDEPTSALDP-------ETVGEVLQvmkelAEEGMTMVVVTHEMGFArEVADRVVVLDQGELIEQGPPEQI 242
Cdd:NF033858 151 LIHDPDLLILDEPTTGVDPlsrrqfwELIDRIRA-----ERPGMSVLVATAYMEEA-ERFDWLVAMDAGRVLATGTPAEL 224
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-232 |
5.72e-07 |
|
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: 47.75 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 34 RGEVVVLIGASGSGKTTFIRCI-NLLEDIQGGRIRVNGramgyrersdgslvrdserniarqrrdigmvfqrfnlfphmt 112
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 113 aleniieapihvlgtpraealEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVG 192
Cdd:smart00382 39 ---------------------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEA 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1525903658 193 EVLQ------VMKELAEEGMTMVVVTHEMGF-----AREVADRVVVLDQGE 232
Cdd:smart00382 98 LLLLleelrlLLLLKSEKNLTVILTTNDEKDlgpalLRRRFDRRIVLLLIL 148
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
118-238 |
5.78e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.21 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 118 IEAPIHVLGTPRAEALEQARGLlarvgladkanhypSMLSGGQQQRVAIARAL---AMKPQAMLFDEPTSALDPETVGEV 194
Cdd:PRK00635 786 IHEKIHALCSLGLDYLPLGRPL--------------SSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKAL 851
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1525903658 195 LQVMKELAEEGMTMVVVTHEMGFAReVADRVvvldqgelIEQGP 238
Cdd:PRK00635 852 IYVLQSLTHQGHTVVIIEHNMHVVK-VADYV--------LELGP 886
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
37-213 |
8.00e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.47 E-value: 8.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 37 VVVLIGASGSGKTTFIRCINLL-----------------EDIQGGRIRVNGRAMGYR---ERSDGSLVRDSERNIARQRR 96
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAIRYAlygkarsrsklrsdlinVGSEEASVELEFEHGGKRyriERRQGEFAEFLEAKPSERKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 97 DIGMVFQ--RF-NLFPHMTALENIIEAPIHVLGtpRAEALEQARgLLARVGLADkanhyPSMLSGGQQQRVAIARALamk 173
Cdd:COG0419 105 ALKRLLGleIYeELKERLKELEEALESALEELA--ELQKLKQEI-LAQLSGLDP-----IETLSGGERLRLALADLL--- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1525903658 174 pqAMLFDepTSALDPETVGEVLQVMKELAeegmtmvVVTH 213
Cdd:COG0419 174 --SLILD--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
25-245 |
1.36e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.27 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 25 LKGISLQVRRGEVVVLIGASGSGKTTfircinlLEDIQGGRIrvngramgyrERSDGSLVRDSERNIarqrrdigmVFQR 104
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKST-------LSNIIGGSL----------SPTVGKVDRNGEVSV---------IAIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 105 FNLFPHMTALENIiEAPIHVLGTPRAEALEQARGLLARVGLADKANHYPSMLSGGQQQRVAIARALAMKPQAMLFDEPTS 184
Cdd:PRK13546 94 AGLSGQLTGIENI-EFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525903658 185 ALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREVADRVVVLDQGELIEQGPPEQIFSH 245
Cdd:PRK13546 173 VGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-257 |
3.45e-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: 47.30 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 17 KSFGDLQIlkgiSLQvrrGEVVVLIGASGSGKTTFIRCINLL-----------------EDIQGGRIRVNGR-----AMG 74
Cdd:COG3593 12 RSIKDLSI----ELS---DDLTVLVGENNSGKSSILEALRLLlgpsssrkfdeedfylgDDPDLPEIEIELTfgsllSRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 75 YRERSDGSLVRDSERNIARQRRDIGMVFQRFN--LFPHMTALENIIEAPIHVLGTPRAEALEQARgllarVGLADKANHY 152
Cdd:COG3593 85 LRLLLKEEDKEELEEALEELNEELKEALKALNelLSEYLKELLDGLDLELELSLDELEDLLKSLS-----LRIEDGKELP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 153 PSMLSGGQQQRVAIA--RALAMKPQA-----MLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREV-ADR 224
Cdd:COG3593 160 LDRLGSGFQRLILLAllSALAELKRApanpiLLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVpLEN 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1525903658 225 VVVLDQGE-------LIEQGPPEQ--IFSHPSHPRTRAFLSR 257
Cdd:COG3593 240 IRRLRRDSggttstkLIDLDDEDLrkLLRYLGVTRSELLFAR 281
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
157-226 |
5.03e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 5.03e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 157 SGGQQQRVAIARALAMKPQAMLFDEPTSALDpetVGEVLQVMKELAEEGMTMVVVTHemgfAREVADRVV 226
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSH----AREFLNTVV 408
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
40-233 |
7.92e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 40 LIGASGSGKTTFIRcinlledIQGG---------RIRVNGRaMG--------YRERS--DGSLVRDSERNIARQRRDigm 100
Cdd:PRK15064 32 LIGANGCGKSTFMK-------ILGGdlepsagnvSLDPNER-LGklrqdqfaFEEFTvlDTVIMGHTELWEVKQERD--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 101 vfqRFNLFPHMTAleniiEAPIHV--LGTPRAE-----ALEQARGLLARVGLADKaNHYPSM--LSGGQQQRVAIARALA 171
Cdd:PRK15064 101 ---RIYALPEMSE-----EDGMKVadLEVKFAEmdgytAEARAGELLLGVGIPEE-QHYGLMseVAPGWKLRVLLAQALF 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525903658 172 MKPQAMLFDEPTSALDPETVGEVLQVmkeLAEEGMTMVVVTHEMGFAREVADRVVVLDQGEL 233
Cdd:PRK15064 172 SNPDILLLDEPTNNLDINTIRWLEDV---LNERNSTMIIISHDRHFLNSVCTHMADLDYGEL 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-200 |
8.14e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.83 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDIQGgRIRVNGramgyrersdgslVRDSERNIARQRRDIGMVFQ 103
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEG-EIQIDG-------------VSWNSVTLQTWRKAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 104 ---------RFNLFPHMTALENIIEAPIHVLGTprAEALEQARGLLARVgLADKAnhypSMLSGGQQQRVAIARALAMKP 174
Cdd:TIGR01271 1300 kvfifsgtfRKNLDPYEQWSDEEIWKVAEEVGL--KSVIEQFPDKLDFV-LVDGG----YVLSNGHKQLMCLARSILSKA 1372
|
170 180
....*....|....*....|....*.
gi 1525903658 175 QAMLFDEPTSALDPETVGEVLQVMKE 200
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
156-226 |
2.30e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.50 E-value: 2.30e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525903658 156 LSGGQQQRVAIARALA---MKP-QAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFArEVADRVV 226
Cdd:cd03227 78 LSGGEKELSALALILAlasLKPrPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELA-ELADKLI 151
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-233 |
3.46e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 19 FGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCI-NLLEDIQGGRIRVNGRAMGYRERSDGSLVRDSERNIArqrrd 97
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLaGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQ----- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 98 igmvfqrfnlfpHMTALeniieAPihvlgtprAEALEQARGLLARVGL-ADKANHYPSMLSGGQQQRVAIARALAMKPQA 176
Cdd:PRK10636 397 ------------HLARL-----AP--------QELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525903658 177 MLFDEPTSALDpetvgevLQVMKELAE-----EGmTMVVVTHEMGFAREVADRVVVLDQGEL 233
Cdd:PRK10636 452 LLLDEPTNHLD-------LDMRQALTEalidfEG-ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
24-250 |
3.57e-05 |
|
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: 44.07 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 24 ILKGISLQVRRGEVVVLIGASGSGKTT----FIRCINLLEDIQggrirvngramgyrerSDGslVRDSERNIARQRRDIG 99
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLNTEGDIQ----------------IDG--VSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 100 MVFQRFNLFphmtaleniiEAPIHVLGTPRAEALEQARGLLA-RVGLADKANHYPS-----------MLSGGQQQRVAIA 167
Cdd:cd03289 81 VIPQKVFIF----------SGTFRKNLDPYGKWSDEEIWKVAeEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 168 RALAMKPQAMLFDEPTSALDPETVGEVLQVMKElAEEGMTMVVVTHEMGFAREvADRVVVLDQGELIEQGPPEQIFSHPS 247
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNEKS 228
|
...
gi 1525903658 248 HPR 250
Cdd:cd03289 229 HFK 231
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
138-256 |
5.37e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.25 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 138 GLLARVGLadkanHYPSM------LSGGQQQRVAIARALAMKPQAMLF--DEPTSALDPETVGEVLQVMKELAEEGMTMV 209
Cdd:COG0178 467 GFLVDVGL-----DYLTLdrsagtLSGGEAQRIRLATQIGSGLVGVLYvlDEPSIGLHQRDNDRLIETLKRLRDLGNTVI 541
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1525903658 210 VVTHEmgfaREV---ADRVVvlD--------QGELIEQGPPEQIFSHP-SHprTRAFLS 256
Cdd:COG0178 542 VVEHD----EDTiraADYII--DigpgagehGGEVVAQGTPEEILKNPdSL--TGQYLS 592
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
135-235 |
1.36e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 135 QARGLLARVGLADKANHYP-SMLSGGQQQRVAIARALAMKPQAMLFDEPTSALDpetVGEVLQVMKELAEEGMTMVVVTH 213
Cdd:PRK10636 128 RAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILISH 204
|
90 100
....*....|....*....|..
gi 1525903658 214 EMGFAREVADRVVVLDQGELIE 235
Cdd:PRK10636 205 DRDFLDPIVDKIIHIEQQSLFE 226
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
156-209 |
1.95e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 1.95e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1525903658 156 LSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKeLAEEGMTMV 209
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV-LFQGGVLMV 680
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
138-226 |
2.70e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.27 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 138 GLLARVGLADKANHYPSMLSGGQQQRVAIARALAM---KPQAM-LFDEPTSALDPETVGEVLQVMKELAEEgMTMVVVTH 213
Cdd:pfam02463 1060 GIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIqkyKPAPFyLLDEIDAALDDQNVSRVANLLKELSKN-AQFIVISL 1138
|
90
....*....|...
gi 1525903658 214 EMGFArEVADRVV 226
Cdd:pfam02463 1139 REEML-EKADKLV 1150
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
156-213 |
3.44e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.22 E-value: 3.44e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525903658 156 LSGGQQQ---RVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTH 213
Cdd:pfam13304 237 LSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
34-53 |
4.51e-04 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 39.43 E-value: 4.51e-04
|
| Twinkle_C |
cd01122 |
C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid ... |
17-52 |
4.97e-04 |
|
C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid localization, also known as C10orf2, PEO1, SCA8, ATXN8, IOSCA, PEOA3 or SANDO) is a homohexameric DNA helicases which unwinds short stretches of double-stranded DNA in the 5' to 3' direction and, along with mitochondrial single-stranded DNA binding protein and mtDNA polymerase gamma, is thought to play a key role in mtDNA replication. Mutations in the human gene cause infantile onset spinocerebellar ataxia (IOSCA) and progressive external ophthalmoplegia (PEO) and are also associated with several mitochondrial depletion syndromes. This group also contains viral GP4-like and related bacterial helicases.
Pssm-ID: 410867 Cd Length: 266 Bit Score: 40.68 E-value: 4.97e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1525903658 17 KSFGDL-QILKGIslqvRRGEVVVLIGASGSGKTTFI 52
Cdd:cd01122 28 KRFPSLnKLLKGH----RRGELTIFTGPTGSGKTTFL 60
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
16-61 |
8.95e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 40.03 E-value: 8.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1525903658 16 HKSFGDLQILKGISLQVRRGEVVVLIGASGSGKTTFIRCINLLEDI 61
Cdd:COG1106 10 FRSFKDELTLSMVASGLRLLRVNLIYGANASGKSNLLEALYFLRNL 55
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
156-258 |
8.96e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.60 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 156 LSGGQQQRVAIARALAMKPQAMLFDEPTSALDPETVGEVLQVMKELAE--EGMTMVVVTHEMGFAREVADRVVVLDQGEL 233
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHltEATVLMSLLQPAPETFDLFDDIILLSEGQI 416
|
90 100 110
....*....|....*....|....*....|...
gi 1525903658 234 IEQGPPEQI--------FSHPSHPRTRAFLSRV 258
Cdd:PLN03140 417 VYQGPRDHIleffescgFKCPERKGTADFLQEV 449
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
156-214 |
9.09e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.51 E-value: 9.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 156 LSGGQQQRVAIARALAMkpqAMLF---------DEPTSALDPETVGEVL-QVMKELAEEG-MTMVVVTHE 214
Cdd:cd03240 116 CSGGEKVLASLIIRLAL---AETFgsncgilalDEPTTNLDEENIEESLaEIIEERKSQKnFQLIVITHD 182
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
37-70 |
1.22e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.68 E-value: 1.22e-03
10 20 30
....*....|....*....|....*....|....
gi 1525903658 37 VVVLIGASGSGKTTFIRCINLLEDIQGGRIRVNG 70
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTD 34
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
234-256 |
2.66e-03 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 35.45 E-value: 2.66e-03
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
17-67 |
2.80e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 38.37 E-value: 2.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1525903658 17 KSFGDLQIlkgiSLqvrrGEVVVLIGASGSGKTTFIRCINLLEDIQGGRIR 67
Cdd:COG4637 11 KSLRDLEL----PL----GPLTVLIGANGSGKSNLLDALRFLSDAARGGLQ 53
|
|
| ABC_ATPase |
pfam09818 |
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. ... |
157-230 |
2.86e-03 |
|
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. This entry also includes MRB1590 from Trypanosoma brucei brucei has a central ATPase domain homologous to this domain.
Pssm-ID: 462914 Cd Length: 282 Bit Score: 38.35 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 157 SGGQQQRVAIARALAMKPQAMLFDEPTSA---------------LDPETVGEVLQVMKELAEE-GMTMVVVTHEMGFARE 220
Cdd:pfam09818 159 SGSTSQAANIMEALEAGASLLLIDEDTSAtnfmirdermqalvsKDKEPITPFVDRVRSLYDDlGVSTILVVGGSGDYLD 238
|
90
....*....|
gi 1525903658 221 VADRVVVLDQ 230
Cdd:pfam09818 239 VADTVILMDE 248
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
154-244 |
6.22e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 154 SMLSGGQQQRVAIARALAMKPQA---MLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTHEMGFAREvADRVVVLDQ 230
Cdd:PRK00635 1698 SSLSLSEKIAIKIAKFLYLPPKHptlFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQ-ADYLIEMGP 1776
|
90 100
....*....|....*....|
gi 1525903658 231 ------GELIEQGPPEQIFS 244
Cdd:PRK00635 1777 gsgktgGKILFSGPPKDISA 1796
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-252 |
6.27e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525903658 139 LLARVGLAD-KANHYPSMLSGGQQQRVAIARALA--MKPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTmVVVTHEM 215
Cdd:PRK00635 1370 FIDKVGLSYiTLGQEQDTLSDGEHYRLHLAKKISsnLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNT-VIATDRS 1448
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1525903658 216 GFAREVADRVVVLD-----QGELIEQGPPEQIfSHPSHPRTR 252
Cdd:PRK00635 1449 GSLAEHADHLIHLGpgsgpQGGYLLSTSALKQ-SQPDLHNTR 1489
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
156-213 |
7.24e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 36.86 E-value: 7.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525903658 156 LSGGQQQRVAIARALAM----------KPQAMLFDEPTSALDPETVGEVLQVMKELAEEGMTMVVVTH 213
Cdd:cd03279 124 LSGGETFLASLSLALALsevlqnrggaRLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISH 191
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
38-66 |
9.01e-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: 9.01e-03
10 20
....*....|....*....|....*....
gi 1525903658 38 VVLIGASGSGKTTFIRCINLLEDIQGGRI 66
Cdd:cd01127 2 TLVLGTTGSGKTTSIVIPLLDQAARGGSV 30
|
|
| |
