|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-239 |
0e+00 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 496.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNIDQIRQKMG 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLF 160
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 161 DEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQDFLNKV 239
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-214 |
1.07e-144 |
|
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: 402.68 E-value: 1.07e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNIDQIRQKMGM 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVI 214
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-236 |
1.31e-135 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 381.46 E-value: 1.31e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNI-TAPDSN-------- 71
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrLKPDRDgelvpadr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 72 --IDQIRQKMGMVFQSFNLFPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIAR 149
Cdd:COG4598 88 rqLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 150 ALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQN 229
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKS 247
|
....*..
gi 498436323 230 SRTQDFL 236
Cdd:COG4598 248 ERLRQFL 254
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-239 |
6.19e-126 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 356.33 E-value: 6.19e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNIDQIRQKMG 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLF 160
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 161 DEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQDFLNKV 239
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-240 |
3.04e-112 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 322.08 E-value: 3.04e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEI------FFEGQNITAPDSNIDQ 74
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditIDTARSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 75 IRQKMGMVFQSFNLFPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMN 154
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 155 PDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQD 234
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242
|
....*.
gi 498436323 235 FLNKVL 240
Cdd:PRK11264 243 FLEKFL 248
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-240 |
3.42e-104 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 305.08 E-value: 3.42e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSF----GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA-PDSNIDQI 75
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 76 RQKMGMVFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNP 155
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVAL-PLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 156 DVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQD 234
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRR 239
|
....*.
gi 498436323 235 FLNKVL 240
Cdd:COG1135 240 FLPTVL 245
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-240 |
1.24e-98 |
|
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: 287.65 E-value: 1.24e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEE-----PTSGEIFFEGQNITAPDSNIDQIR 76
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDIYDKKIDVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 QKMGMVFQSFNLFPhMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGL----KEKADSFPSSLSGGQQQRVAIARALA 152
Cdd:TIGR00972 82 RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 153 MNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKgMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRT 232
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRT 239
|
....*...
gi 498436323 233 QDFLNKVL 240
Cdd:TIGR00972 240 EDYISGRF 247
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-237 |
1.68e-98 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 286.91 E-value: 1.68e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNI----TAPDSNIDQIRQ 77
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 78 KMGMVFQSFNLFPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDV 157
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 158 MLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTpEEIFDHPQNSRTQDFLN 237
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHYLS 241
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
2-240 |
1.08e-97 |
|
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: 285.19 E-value: 1.08e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNIT-----------APDS 70
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYhmpgrngplvpADEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 71 NIDQIRQKMGMVFQSFNLFPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARA 150
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 151 LAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQN 229
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|.
gi 498436323 230 SRTQDFLNKVL 240
Cdd:TIGR03005 241 ERTREFLSKVI 251
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
1.33e-97 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 284.24 E-value: 1.33e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNE----VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA-PDSNIDQI 75
Cdd:COG1136 4 LLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 76 R-QKMGMVFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMN 154
Cdd:COG1136 84 RrRHIGFVFQFFNLLPELTALENVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498436323 155 PDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAkEVADRVIFMADGVIQEE 217
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELA-ARADRVIRLRDGRIVSD 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-236 |
1.20e-96 |
|
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: 282.25 E-value: 1.20e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNIT-APDSNIDQIRQKM 79
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITgLSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFNLFPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVML 159
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498436323 160 FDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPqNSRTQDFL 236
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-237 |
1.20e-95 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 279.59 E-value: 1.20e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNI---TAPDSN-IDQIRQ 77
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKaIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 78 KMGMVFQSFNLFPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDV 157
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 158 MLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTpEEIFDHPQNSRTQDFLN 237
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFKNYLS 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-228 |
2.17e-95 |
|
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: 278.70 E-value: 2.17e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDN----EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA-PDSNIDQI 75
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 76 RQKMGMVFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNP 155
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAL-PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498436323 156 DVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQ 228
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-236 |
6.35e-95 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 281.99 E-value: 6.35e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA--PDsnidqiRQK 78
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlpPE------KRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 79 MGMVFQSFNLFPHMSVLDNLTiTPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVM 158
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVA-FGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 159 LFDEPTSALDP----EMVGEVLAVMQDLakkGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQD 234
Cdd:COG3842 158 LLDEPLSALDAklreEMREELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVAD 234
|
..
gi 498436323 235 FL 236
Cdd:COG3842 235 FI 236
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-240 |
1.44e-93 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 275.31 E-value: 1.44e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNIT-----------APDS 70
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 71 NIDQIRQKMGMVFQSFNLFPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGLKEKA-DSFPSSLSGGQQQRVAIAR 149
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 150 ALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQN 229
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
250
....*....|.
gi 498436323 230 SRTQDFLNKVL 240
Cdd:PRK10619 246 PRLQQFLKGSL 256
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
9.60e-91 |
|
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: 266.28 E-value: 9.60e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDN----EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNIT-APDSNIDQIR 76
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISkLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 -QKMGMVFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNP 155
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVEL-PLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 156 DVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEvADRVIFMADGVI 214
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-223 |
1.55e-89 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 264.61 E-value: 1.55e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSF-GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA-PDSNIDQIRQK 78
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAlRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 79 MGMVFQSFNLFPHMSVLDN-----LTITPV------KIKKEDatkaKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAI 147
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNvlagrLGRTSTwrsllgLFPPED----RERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498436323 148 ARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAK-KGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-229 |
1.44e-86 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 260.39 E-value: 1.44e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNIT--AP-DSNIdqirq 77
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTdlPPkDRNI----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 78 kmGMVFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDV 157
Cdd:COG3839 78 --AMVFQSYALYPHMTVYENIAF-PLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 158 MLFDEPTSALDP----EMVGEVLAVMQDLakkGMTMVVVTHE----MGFakevADRVIFMADGVIQEEGTPEEIFDHPQN 229
Cdd:COG3839 155 FLLDEPLSNLDAklrvEMRAEIKRLHRRL---GTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-235 |
1.11e-85 |
|
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: 254.35 E-value: 1.11e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITaPDSNIDQ--IRQKM 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIS-GLSEAELyrLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFNLFPHMSVLDNLTItPVKIK-KEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVM 158
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAF-PLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498436323 159 LFDEPTSALDPEMVGEVLAVMQDLAK-KGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHpQNSRTQDF 235
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS-DDPLVRQF 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-233 |
1.67e-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: 260.22 E-value: 1.67e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSF-----GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA-PDSNIDQ 74
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 75 IRQKMGMVFQ----SFNlfPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGLKEK-ADSFPSSLSGGQQQRVAIAR 149
Cdd:COG1123 340 LRRRVQMVFQdpysSLN--PRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDlADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 150 ALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQ 228
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
....*
gi 498436323 229 NSRTQ 233
Cdd:COG1123 498 HPYTR 502
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-212 |
7.32e-84 |
|
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: 247.49 E-value: 7.32e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNIDQIRQKMGM 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDNLTItpvkikkedatkakeqamalldqvglkekadsfpsSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL-----------------------------------GLSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 498436323 162 EPTSALDPEMVGEVLAVMQDL-AKKGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-236 |
1.42e-83 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 251.16 E-value: 1.42e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGD-NEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKM 79
Cdd:COG1125 1 MIEFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIR--DLDPVELRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFNLFPHMSVLDNLTITPvKIKKEDATKAKEQAMALLDQVGL--KEKADSFPSSLSGGQQQRVAIARALAMNPDV 157
Cdd:COG1125 79 GYVIQQIGLFPHMTVAENIATVP-RLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 158 MLFDEPTSALDP----EMVGEVLAVMQDLAKkgmTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQ 233
Cdd:COG1125 158 LLMDEPFGALDPitreQLQDELLRLQRELGK---TIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVA 234
|
...
gi 498436323 234 DFL 236
Cdd:COG1125 235 DFV 237
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-218 |
2.90e-83 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 247.66 E-value: 2.90e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSF-GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA-PDSNIDQIRQK 78
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 79 MGMVFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVM 158
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVAL-PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 159 LFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEG 218
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-240 |
3.08e-83 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 251.64 E-value: 3.08e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSF--GDNEV--LKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA-PDSNIDQI 75
Cdd:PRK11153 1 MIELKNISKVFpqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 76 RQKMGMVFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNP 155
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 156 DVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQD 234
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTRE 239
|
....*.
gi 498436323 235 FLNKVL 240
Cdd:PRK11153 240 FIQSTL 245
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-217 |
6.15e-83 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 248.08 E-value: 6.15e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSF----GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNIdqir 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDR---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 qkmGMVFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPD 156
Cdd:COG1116 83 ---GVVFQEPALLPWLTVLDNVAL-GLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498436323 157 VMLFDEPTSALDP----EMVGEVLAVmqdLAKKGMTMVVVTHEMGFAKEVADRVIFMAD--GVIQEE 217
Cdd:COG1116 159 VLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-229 |
1.31e-82 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 251.56 E-value: 1.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDN---------------EVLKS---------IDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSG 56
Cdd:COG4175 3 KIEVRNLYKIFGKRperalklldqgkskdEILEKtgqtvgvndASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 57 EIFFEGQNITA-PDSNIDQIRQ-KMGMVFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFP 134
Cdd:COG4175 83 EVLIDGEDITKlSKKELRELRRkKMSMVFQHFALLPHRTVLENVAF-GLEIQGVPKAERRERAREALELVGLAGWEDSYP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 135 SSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDP----EMVGEVLAVMQDLAKkgmTMVVVTHEMGFAKEVADRVIFMA 210
Cdd:COG4175 162 DELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrEMQDELLELQAKLKK---TIVFITHDLDEALRLGDRIAIMK 238
|
250
....*....|....*....
gi 498436323 211 DGVIQEEGTPEEIFDHPQN 229
Cdd:COG4175 239 DGRIVQIGTPEEILTNPAN 257
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-218 |
1.50e-82 |
|
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: 245.51 E-value: 1.50e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapdsNIDQIRQKMGMVF 83
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT----GVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 84 QSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEP 163
Cdd:cd03259 79 QDYALFPHLTVAENIAF-GLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 164 TSALDP----EMVGEVLAVMQDLakkGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEG 218
Cdd:cd03259 158 LSALDAklreELREELKELQREL---GITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-237 |
2.97e-82 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 246.10 E-value: 2.97e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLL--EEP---TSGEIFFEGQNITAPDSNIDQIR 76
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDIYDPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 QKMGMVFQSFNLFPhMSVLDN----LTITPVKIKKE-DAT--KAKEQAmALLDQVglKEKADSFPSSLSGGQQQRVAIAR 149
Cdd:COG1117 92 RRVGMVFQKPNPFP-KSIYDNvaygLRLHGIKSKSElDEIveESLRKA-ALWDEV--KDRLKKSALGLSGGQQQRLCIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 150 ALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKgMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQN 229
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKD 246
|
....*...
gi 498436323 230 SRTQDFLN 237
Cdd:COG1117 247 KRTEDYIT 254
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-226 |
3.74e-82 |
|
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: 245.56 E-value: 3.74e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDN-EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA-PDSNIDQIRQKM 79
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFNLFPHMSVLDNL------TITPVK-----IKKEDatkaKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIA 148
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlgRRSTWRslfglFPKEE----KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 149 RALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAK-KGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDH 226
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINReEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-240 |
4.63e-82 |
|
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: 245.48 E-value: 4.63e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFG----DNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNidQIR 76
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK--AFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 QKMGMVFQ----SFNlfPHMSVLDNLTiTPVKIKKEDATKakEQAMALLDQVGLKEK-ADSFPSSLSGGQQQRVAIARAL 151
Cdd:COG1124 79 RRVQMVFQdpyaSLH--PRHTVDRILA-EPLRIHGLPDRE--ERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 152 AMNPDVMLFDEPTSALDPEMVGEVLAVMQDL-AKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNS 230
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
250
....*....|
gi 498436323 231 RTQDFLNKVL 240
Cdd:COG1124 234 YTRELLAASL 243
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-223 |
4.65e-82 |
|
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: 244.78 E-value: 4.65e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEE-----PTSGEIFFEGQNITAPDSNIDQIR 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 QKMGMVFQSFNLFPhMSVLDNLTITP--VKIKKEDATKAKEQAmaLLDQVGLKE--KADSFPSSLSGGQQQRVAIARALA 152
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLrlHGIKLKEELDERVEE--ALRKAALWDevKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 153 MNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKgMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-228 |
3.50e-81 |
|
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: 242.62 E-value: 3.50e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSF-GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKMG 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT--KKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQsfN----LFpHMSVLDNLTITPVKIKKEDAtKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPD 156
Cdd:COG1122 79 LVFQ--NpddqLF-APTVEEDVAFGPENLGLPRE-EIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498436323 157 VMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQ 228
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-223 |
6.93e-81 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 241.89 E-value: 6.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapdSNIDQIRQKMGM 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA---RDPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDNLTITpVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFF-ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-239 |
3.17e-80 |
|
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: 241.39 E-value: 3.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDN---------------EVLKS---------IDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGE 57
Cdd:cd03294 1 IKIKGLYKIFGKNpqkafkllakgkskeEILKKtgqtvgvndVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 58 IFFEGQNITA-PDSNIDQIR-QKMGMVFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPS 135
Cdd:cd03294 81 VLIDGQDIAAmSRKELRELRrKKISMVFQSFALLPHRTVLENVAF-GLEVQGVPRAEREERAAEALELVGLEGWEHKYPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 136 SLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEvlavMQDL-----AKKGMTMVVVTHEMGFAKEVADRVIFMA 210
Cdd:cd03294 160 ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE----MQDEllrlqAELQKTIVFITHDLDEALRLGDRIAIMK 235
|
250 260
....*....|....*....|....*....
gi 498436323 211 DGVIQEEGTPEEIFDHPQNSRTQDFLNKV 239
Cdd:cd03294 236 DGRLVQVGTPEEILTNPANDYVREFFRGV 264
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-226 |
1.29e-79 |
|
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: 239.12 E-value: 1.29e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDN-EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNIT-APDSNIDQIRQK 78
Cdd:TIGR02315 1 MLEVENLSKVYPNGkQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITkLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 79 MGMVFQSFNLFPHMSVLDNLTITPVKIK-----------KEDatkaKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAI 147
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGYKptwrsllgrfsEED----KERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 148 ARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDH 226
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-236 |
1.67e-79 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 242.36 E-value: 1.67e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQ----NITAPDSNIdqirq 77
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftNLPPRERRV----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 78 kmGMVFQSFNLFPHMSVLDNLTITPvKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDV 157
Cdd:COG1118 78 --GFVFQHYALFPHMTVAENIAFGL-RVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 158 MLFDEPTSALD----PEMVGEVLAVMQDLakkGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQ 233
Cdd:COG1118 155 LLLDEPFGALDakvrKELRRWLRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVA 231
|
...
gi 498436323 234 DFL 236
Cdd:COG1118 232 RFL 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-236 |
1.49e-77 |
|
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: 233.28 E-value: 1.49e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapdsNIDQIRQKMGM 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT----NLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:cd03300 77 VFQNYALFPHLTVFENIAF-GLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQDFL 236
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-238 |
5.58e-76 |
|
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: 229.88 E-value: 5.58e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNE-VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNidQIRQKMG 80
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV--ELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFPHMSVLDNLTITPvKIKKEDATKAKEQAMALLDQVGLKEK--ADSFPSSLSGGQQQRVAIARALAMNPDVM 158
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 159 LFDEPTSALDP----EMVGEVLAVMQDLAKkgmTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQD 234
Cdd:cd03295 158 LMDEPFGALDPitrdQLQEEFKRLQQELGK---TIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAE 234
|
....
gi 498436323 235 FLNK 238
Cdd:cd03295 235 FVGA 238
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-218 |
2.32e-74 |
|
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: 225.08 E-value: 2.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSF----GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNIDQIR 76
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 QK-MGMVFQ----SFNlfPHMSVLDNLTiTPVKI--KKEDATKAKEQAMALLDQVGLKEK-ADSFPSSLSGGQQQRVAIA 148
Cdd:cd03257 81 RKeIQMVFQdpmsSLN--PRMTIGEQIA-EPLRIhgKLSKKEARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 149 RALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEG 218
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-227 |
5.71e-74 |
|
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: 223.89 E-value: 5.71e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDN----EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSnidqirq 77
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 78 KMGMVFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDV 157
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVAL-GLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498436323 158 MLFDEPTSALDP----EMVGEVLAVmqdLAKKGMTMVVVTHEMGFAKEVADRVIFMAdgviQEEGTPEEIFDHP 227
Cdd:cd03293 153 LLLDEPFSALDAltreQLQEELLDI---WRETGKTVLLVTHDIDEAVFLADRVVVLS----ARPGRIVAEVEVD 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-212 |
1.60e-72 |
|
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: 220.03 E-value: 1.60e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNE--VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKMGM 81
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT--KLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNL-FPHMSVLDNLTITPV--KIKKEDATKAKEQAmalLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVM 158
Cdd:cd03225 80 VFQNPDDqFFGPTVEEEVAFGLEnlGLPEEEIEERVEEA---LELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498436323 159 LFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-236 |
3.69e-71 |
|
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: 217.59 E-value: 3.69e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSnidQIRQkMGM 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERN-VGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDN----LTITPVKiKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDV 157
Cdd:cd03296 79 VFQHYALFRHMTVFDNvafgLRVKPRS-ERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 158 MLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQDFL 236
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-228 |
8.59e-71 |
|
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: 216.53 E-value: 8.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSniDQI-RQKMGMV 82
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP--HEIaRLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 83 FQSFNLFPHMSVLDNLTITPVKIKKEDA---------TKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAM 153
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498436323 154 NPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQ 228
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-228 |
1.31e-70 |
|
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: 218.77 E-value: 1.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFG-DNEVLK---SIDLEVKDGEVVVIIGPSGSGKSTILRC-LNLLEEP--TSGEIFFEGQNITA-PDSNI 72
Cdd:COG0444 1 LLEVRNLKVYFPtRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAiLGLLPPPgiTSGEILFDGEDLLKlSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 73 DQIR-QKMGMVFQ----SFNlfPHMSVLDNLTiTPVKI-KKEDATKAKEQAMALLDQVGL---KEKADSFPSSLSGGQQQ 143
Cdd:COG0444 81 RKIRgREIQMIFQdpmtSLN--PVMTVGDQIA-EPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 144 RVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEE 222
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEE 237
|
....*.
gi 498436323 223 IFDHPQ 228
Cdd:COG0444 238 LFENPR 243
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-225 |
1.77e-70 |
|
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: 216.06 E-value: 1.77e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNidQIRQKMG 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRR--ELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQS----FNL----------FPHMSVLDNLTitpvkikKEDatkaKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVA 146
Cdd:COG1120 79 YVPQEppapFGLtvrelvalgrYPHLGLFGRPS-------AED----REAVEEALERTGLEHLADRPVDELSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 147 IARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAK-KGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFD 225
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
9-239 |
4.20e-69 |
|
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: 216.26 E-value: 4.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 9 KSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNIT--APDSNIDQIRQKMGMVFQSF 86
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMkqSPVELREVRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 87 NLFPHMSVLDNLTITPvKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSA 166
Cdd:TIGR01186 81 ALFPHMTILQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498436323 167 LDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQDFLNKV 239
Cdd:TIGR01186 160 LDPLIRDSMQDELKKLQATlQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-228 |
5.17e-69 |
|
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: 212.59 E-value: 5.17e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNIT--APDSnidqiRQK 78
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITglPPHR-----IAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 79 MGMV--FQSFNLFPHMSVLDNLTI----------------TPVKIKKEDAtkAKEQAMALLDQVGLKEKADSFPSSLSGG 140
Cdd:COG0411 79 LGIArtFQNPRLFPELTVLENVLVaaharlgrgllaallrLPRARREERE--ARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 141 QQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDL-AKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGT 219
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
....*....
gi 498436323 220 PEEIFDHPQ 228
Cdd:COG0411 237 PAEVRADPR 245
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-236 |
5.61e-69 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 211.54 E-value: 5.61e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDneVLKSIDLEVKDGEVVVIIGPSGSGKSTILrclNLL---EEPTSGEIFFEGQNIT--APDsnidqi 75
Cdd:COG3840 1 MLRLDDLTYRYGD--FPLRFDLTIAAGERVAILGPSGAGKSTLL---NLIagfLPPDSGRILWNGQDLTalPPA------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 76 RQKMGMVFQSFNLFPHMSVLDN--LTITP-VKIKKEDatkaKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALA 152
Cdd:COG3840 70 ERPVSMLFQENNLFPHLTVAQNigLGLRPgLKLTAEQ----RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 153 MNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSR 231
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPA 225
|
....*
gi 498436323 232 TQDFL 236
Cdd:COG3840 226 LAAYL 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-222 |
1.17e-68 |
|
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: 210.75 E-value: 1.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNE----VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSniDQI- 75
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE--DARa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 76 ---RQKMGMVFQSFNLFPHMSVLDNLTItPVKIKKEDatKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALA 152
Cdd:COG4181 86 rlrARHVGFVFQSFQLLPTLTALENVML-PLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 153 MNPDVMLFDEPTSALDPEMVGEVLAVMQDL-AKKGMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEE 222
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-239 |
2.15e-68 |
|
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: 214.13 E-value: 2.15e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA-PDSNIDqirqkMG 80
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRlPPQKRD-----YG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFPHMSVLDNLTITpVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLF 160
Cdd:TIGR03265 80 IVFQSYALFPNLTVADNIAYG-LKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 161 DEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQDFLNKV 239
Cdd:TIGR03265 159 DEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEV 238
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-228 |
3.85e-68 |
|
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: 218.23 E-value: 3.85e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSF--GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPT---SGEIFFEGQNITapDSNIDQI 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLL--ELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 76 RQKMGMVFQSFnlfphMSVLDNLTIT-----PVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARA 150
Cdd:COG1123 82 GRRIGMVFQDP-----MTQLNPVTVGdqiaeALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 151 LAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQ 228
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-214 |
3.47e-67 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 206.21 E-value: 3.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKMGMVF 83
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLS--AMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 84 QSFNLFPhMSVLDNLTiTPVKIKKEDATkaKEQAMALLDQVGLKEKA-DSFPSSLSGGQQQRVAIARALAMNPDVMLFDE 162
Cdd:COG4619 81 QEPALWG-GTVRDNLP-FPFQLRERKFD--RERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498436323 163 PTSALDPEMVGEVLAVMQDL-AKKGMTMVVVTHEMGFAKEVADRVIFMADGVI 214
Cdd:COG4619 157 PTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-224 |
4.54e-67 |
|
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: 208.05 E-value: 4.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNE--VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNiTAPDSNIDQIRQKM 79
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD-TLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQS-FNLFPHMSV-------LDNLTITPVKIKK--EDAtkakeqamalLDQVGLKEKADSFPSSLSGGQQQRVAIAR 149
Cdd:TIGR04520 80 GMVFQNpDNQFVGATVeddvafgLENLGVPREEMRKrvDEA----------LKLVGMEDFRDREPHLLSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498436323 150 ALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAK-KGMTMVVVTHEMgfaKEV--ADRVIFMADGVIQEEGTPEEIF 224
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDM---EEAvlADRVIVMNKGKIVAEGTPREIF 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-239 |
1.10e-65 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 207.24 E-value: 1.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNItapdSNIDQIRQKMGM 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV----SRLHARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDN----LTITPVKiKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDV 157
Cdd:PRK10851 79 VFQHYALFRHMTVFDNiafgLTVLPRR-ERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 158 MLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQDFL 236
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFM 237
|
...
gi 498436323 237 NKV 239
Cdd:PRK10851 238 GEV 240
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-232 |
2.09e-65 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 203.01 E-value: 2.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPdsnidqiRQKMG 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-------RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNL---FPhMSVLDnltitpV-------------KIKKEDatkaKEQAMALLDQVGLKEKADSFPSSLSGGQQQR 144
Cdd:COG1121 79 YVPQRAEVdwdFP-ITVRD------VvlmgrygrrglfrRPSRAD----REAVDEALERVGLEDLADRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 145 VAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIqEEGTPEEIF 224
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEEVL 226
|
....*...
gi 498436323 225 DHPQNSRT 232
Cdd:COG1121 227 TPENLSRA 234
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-229 |
2.42e-65 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 207.11 E-value: 2.42e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapdsNIDQIRQKMGM 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT----HVPAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDNLTITpVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498436323 162 EPTSALD----PEMVGEVLAVMQDLakkGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQN 229
Cdd:PRK09452 170 ESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN 238
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-223 |
7.67e-65 |
|
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: 200.74 E-value: 7.67e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNIT--APDsniDQIRQKMGM 81
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglPPH---ERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQvgLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-212 |
6.55e-64 |
|
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: 198.24 E-value: 6.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSF-GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNI-TAPDSNIDQIRQK 78
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVnRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 79 MGMVFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVM 158
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498436323 159 LFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-214 |
3.04e-63 |
|
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: 194.92 E-value: 3.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapdSNIDQIRQKMGM 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK---KEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDNLtitpvkikkedatkakeqamalldqvglkekadsfpsSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:cd03230 78 LPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVI 214
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-228 |
5.01e-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 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: 198.06 E-value: 5.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDN-----EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDS-NIDQI 75
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKkKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 76 RQKMGMVFQsfnlFPHM-----SVLDNLTITPVKIKKEDAtKAKEQAMALLDQVGLKEK-ADSFPSSLSGGQQQRVAIAR 149
Cdd:TIGR04521 81 RKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNLGLSEE-EAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 150 ALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAK-KGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQ 228
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKeKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-223 |
3.75e-61 |
|
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: 191.99 E-value: 3.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapdSNIDQIRQKMG 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR---KEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFPHMSVLDNLTITpVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLF 160
Cdd:COG4555 78 VLPDERGLYDRLTVRENIRYF-AELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498436323 161 DEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-233 |
4.84e-61 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 194.57 E-value: 4.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 20 IDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPD-SNIDQIRQKMGMVFQ----SFNlfPHMSV 94
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgRELRPLRRRMQMVFQdpyaSLN--PRMTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 95 LDNLTiTPVKI-KKEDATKAKEQAMALLDQVGLK-EKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMV 172
Cdd:COG4608 115 GDIIA-EPLRIhGLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQ 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498436323 173 GEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQ 233
Cdd:COG4608 194 AQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPYTQ 255
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-229 |
7.63e-61 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 194.83 E-value: 7.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSF--GDNEV--LKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDS-NIDQIR 76
Cdd:NF040933 3 VRVENVTKIFkkGKKEVvaLDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASPGKiIVPPED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 QKMGMVFQSFNLFPHMSVLDNLTItPVKIKK----EDATKAKEQAMALldqvGLKEKADSFPSSLSGGQQQRVAIARALA 152
Cdd:NF040933 83 RNIGMVFQNWALYPNMTVFDNIAF-PLKIKKvpkdEIEKKVKEVAEIL----GISEVLDRYPRELSGGQQQRVALARALV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498436323 153 MNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQN 229
Cdd:NF040933 158 KNPQVLLLDEPFSNLDARIRDSARALVKKIQRElKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPAN 235
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-231 |
3.98e-60 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 193.01 E-value: 3.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 5 KQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQirQKMGMVFQ 84
Cdd:PRK11432 10 KNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQ--RDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 85 SFNLFPHMSVLDN----LTITPVKiKKEDATKAKEqAMALLDQVGLkekADSFPSSLSGGQQQRVAIARALAMNPDVMLF 160
Cdd:PRK11432 86 SYALFPHMSLGENvgygLKMLGVP-KEERKQRVKE-ALELVDLAGF---EDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498436323 161 DEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPqNSR 231
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP-ASR 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-236 |
9.60e-60 |
|
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: 188.31 E-value: 9.60e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEvLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapdsNIDQIRQKMGM 81
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT----NLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDNLTITpVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQDFL 236
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-218 |
1.19e-59 |
|
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: 187.08 E-value: 1.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNIT---APDSNIdqirqk 78
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTdlpPKDRDI------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 79 mGMVFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVM 158
Cdd:cd03301 75 -AMVFQNYALYPHMTVYDNIAF-GLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498436323 159 LFDEPTSALDP----EMVGEVLAVMQDLakkGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEG 218
Cdd:cd03301 153 LMDEPLSNLDAklrvQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-237 |
4.22e-59 |
|
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: 194.90 E-value: 4.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDN----EVLKSIDLEVKDGEVVVIIGPSGSGKS-TILRCLNLLEEP---TSGEIFFEGQNI-TAPDSN 71
Cdd:COG4172 6 LLSVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLlGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 72 IDQIR-QKMGMVFQ----SFNlfPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGLKE---KADSFPSSLSGGQQQ 143
Cdd:COG4172 86 LRRIRgNRIAMIFQepmtSLN--PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 144 RVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEE 222
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
250
....*....|....*
gi 498436323 223 IFDHPQNSRTQDFLN 237
Cdd:COG4172 244 LFAAPQHPYTRKLLA 258
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-212 |
5.83e-59 |
|
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: 183.60 E-value: 5.83e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSniDQIRQKMGMVF 83
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL--EELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 84 QsfnlfphmsvldnltitpvkikkedatkakeqamalldqvglkekadsfpssLSGGQQQRVAIARALAMNPDVMLFDEP 163
Cdd:cd00267 80 Q----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 498436323 164 TSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-228 |
9.63e-59 |
|
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: 185.57 E-value: 9.63e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSniDQI-RQKM 79
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP--HRIaRLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFNLFPHMSVLDNLTITPVKIKKEDATKA-KEQAMALLDQvgLKEKADSFPSSLSGGQQQRVAIARALAMNPDVM 158
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRAdLERVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 159 LFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQ 228
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-236 |
1.37e-58 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 185.75 E-value: 1.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLL-----EEPTSGEIFFEGQNITAPDSNIDQI 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 76 RQKMGMVFQSFNLFPhMSVLDN----LTITPVKIKK--EDATKAKEQAMALLDQVglKEKADSFPSSLSGGQQQRVAIAR 149
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENvvygLRLKGIKDKQvlDEAVEKSLKGASIWDEV--KDRLHDSALGLSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 150 ALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLaKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQN 229
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
....*..
gi 498436323 230 SRTQDFL 236
Cdd:PRK14239 241 KETEDYI 247
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-223 |
1.68e-58 |
|
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: 196.59 E-value: 1.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNE--VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKM 79
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLR--QIDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFNLFpHMSVLDNLTITpvkikKEDATKakEQAMALLDQVGLKEKADSFP-----------SSLSGGQQQRVAIA 148
Cdd:COG2274 552 GVVLQDVFLF-SGTIRENITLG-----DPDATD--EEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498436323 149 RALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAkKGMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEEI 223
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEEL 696
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-209 |
7.79e-58 |
|
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: 182.43 E-value: 7.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDS--NIDQIRQKMGM 81
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSkkASKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:TIGR03608 81 LFQNFALIENETVEENLDL-GLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMgFAKEVADRVIFM 209
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-214 |
9.11e-58 |
|
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: 182.61 E-value: 9.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEV-LKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA-PDSNIDQIRQKM 79
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVML 159
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAF-ALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 160 FDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHemgfAKEVAD----RVIFMADGVI 214
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH----AKELVDttrhRVIALERGKL 214
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-236 |
1.03e-57 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 183.58 E-value: 1.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLL-----EEPTSGEIFFEGQNITAPDsnIDQIR 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD--VIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 QKMGMVFQSFNLFPHMSVLDNLTITP-----VKIKKEDATKAKE--QAMALLDQVglKEKADSFPSSLSGGQQQRVAIAR 149
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLklnrlVKSKKELQERVRWalEKAQLWDEV--KDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 150 ALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLaKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQN 229
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
....*..
gi 498436323 230 SRTQDFL 236
Cdd:PRK14247 239 ELTEKYV 245
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-218 |
2.80e-57 |
|
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: 179.94 E-value: 2.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSniDQIRQKMGMVF 83
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSP--KELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 84 QSfnlfphmsvldnltitpvkikkedatkakeqamalLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEP 163
Cdd:cd03214 80 QA-----------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 164 TSALDPEMVGEVLAVMQDLAK-KGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEG 218
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
10-222 |
7.92e-57 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 189.99 E-value: 7.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 10 SF---GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKMGMVFQSF 86
Cdd:COG1132 346 SFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR--DLTLESLRRQIGVVPQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 87 NLFpHMSVLDNLTITpvkikKEDATKakEQAMALLDQVGLKEKADSFP-----------SSLSGGQQQRVAIARALAMNP 155
Cdd:COG1132 424 FLF-SGTIRENIRYG-----RPDATD--EEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498436323 156 DVMLFDEPTSALDPEMVGEVLAVMQDLAkKGMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEE 222
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEE 560
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-239 |
2.66e-56 |
|
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: 182.31 E-value: 2.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 32 IIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapdsNIDQIRQKMGMVFQSFNLFPHMSVLDNLTItPVKIKKEDAT 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT----NVPPHLRHINMVFQSYALFPHMTVEENVAF-GLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 112 KAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALD----PEMVGEVLAVMQDLakkGM 187
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQEQL---GI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 498436323 188 TMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQDFLNKV 239
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-214 |
6.08e-56 |
|
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: 177.73 E-value: 6.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapdsnidQIRQKMGMVF 83
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-------KERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 84 QSFNL---FPhMSVLD----NLTITPV---KIKKEDatkaKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAM 153
Cdd:cd03235 75 QRRSIdrdFP-ISVRDvvlmGLYGHKGlfrRLSKAD----KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 154 NPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVI 214
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-223 |
9.95e-56 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 185.22 E-value: 9.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITaPDSNIDQIRQKMGMVF 83
Cdd:COG1129 7 MRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-FRSPRDAQAAGIAIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 84 QSFNLFPHMSVLDNLTIT--PVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:COG1129 86 QELNLVPNLSVAENIFLGrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:COG1129 166 EPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-222 |
1.18e-55 |
|
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: 186.51 E-value: 1.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNE--VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSniDQIRQKM 79
Cdd:COG4987 334 LELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE--DDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFNLFpHMSVLDNLTITpvkikKEDATKakEQAMALLDQVGLKEKADSFP-----------SSLSGGQQQRVAIA 148
Cdd:COG4987 412 AVVPQRPHLF-DTTLRENLRLA-----RPDATD--EELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498436323 149 RALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAkKGMTMVVVTHEMGFAkEVADRVIFMADGVIQEEGTPEE 222
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGTHEE 555
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-229 |
3.49e-55 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 180.61 E-value: 3.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINV--KQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNItapdSNIDQIRQK 78
Cdd:PRK11000 1 MASVtlRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM----NDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 79 MGMVFQSFNLFPHMSVLDNLT--ITPVKIKKEDATKAKEQAMALLDQVGLKEKAdsfPSSLSGGQQQRVAIARALAMNPD 156
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSfgLKLAGAKKEEINQRVNQVAEVLQLAHLLDRK---PKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498436323 157 VMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQN 229
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPAN 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-212 |
6.75e-55 |
|
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: 173.72 E-value: 6.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDN--EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKM 79
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLR--DLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFNLFpHMSVLDNLtitpvkikkedatkakeqamalldqvglkekadsfpssLSGGQQQRVAIARALAMNPDVML 159
Cdd:cd03228 79 AYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498436323 160 FDEPTSALDPEMVGEVLAVMQDLAkKGMTMVVVTHEMGfAKEVADRVIFMADG 212
Cdd:cd03228 120 LDEATSALDPETEALILEALRALA-KGKTVIVIAHRLS-TIRDADRIIVLDDG 170
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-240 |
2.60e-54 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 175.03 E-value: 2.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLL-----EEPTSGEIFFEGQNITAPDSNIDQIR 76
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 QKMGMVFQSFNLFPHMSVLDNLTI-----TPVKIKKE--DATKAKEQAMALLDQVglKEKADSFPSSLSGGQQQRVAIAR 149
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIgvklnGLVKSKKEldERVEWALKKAALWDEV--KDRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 150 ALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLaKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQN 229
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
250
....*....|.
gi 498436323 230 SRTQDFLNKVL 240
Cdd:PRK14267 242 ELTEKYVTGAL 252
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-233 |
4.84e-54 |
|
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: 181.42 E-value: 4.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 7 LSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRC-LNLLeePTSGEIFFEGQNITAPDSNIDQ-IRQKMGMVFQ 84
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLAlLRLI--PSEGEIRFDGQDLDGLSRRALRpLRRRMQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 85 ----SFNlfPHMSVLDnlTIT-PVKIKKEDATKA--KEQAMALLDQVGLKEKA-DSFPSSLSGGQQQRVAIARALAMNPD 156
Cdd:COG4172 370 dpfgSLS--PRMTVGQ--IIAeGLRVHGPGLSAAerRARVAEALEEVGLDPAArHRYPHEFSGGQRQRIAIARALILEPK 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498436323 157 VMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQ 233
Cdd:COG4172 446 LLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTR 523
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-222 |
1.04e-53 |
|
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: 181.11 E-value: 1.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDN-EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKMG 80
Cdd:COG4988 337 IELEDVSFSYPGGrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS--DLDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFpHMSVLDNLTITpvkikKEDATKakEQAMALLDQVGLKEKADSFP-----------SSLSGGQQQRVAIAR 149
Cdd:COG4988 415 WVPQNPYLF-AGTIRENLRLG-----RPDASD--EELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498436323 150 ALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAkKGMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEE 222
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-223 |
1.14e-53 |
|
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: 172.30 E-value: 1.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNE--VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapdSNIDQIRQKMGM 81
Cdd:cd03263 3 IRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR---TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDNLTITpVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:cd03263 80 CPQFDALFDELTVREHLRFY-ARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLaKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-211 |
1.97e-53 |
|
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: 171.12 E-value: 1.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDsniDQIRQKMG 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR---EDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFPHMSVLDNLTITpVKIKKEDATKakEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLF 160
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFW-AALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 498436323 161 DEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTH-EMGFAkevADRVIFMAD 211
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqPLELA---AARVLDLGD 204
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-165 |
2.25e-53 |
|
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: 168.98 E-value: 2.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDsnIDQIRQKMGMVFQSFNLFPHMSVLD 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE--RKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498436323 97 NLtITPVKIKKEDATKAKEQAMALLDQVGL----KEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTS 165
Cdd:pfam00005 79 NL-RLGLLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-234 |
3.38e-52 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 170.26 E-value: 3.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDN-EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNIDQIRQKM 79
Cdd:PRK13639 1 ILETRDLKYSYPDGtEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFN--LFPHmSVLDNLTITP--VKIKKEDATKAKEQAMALLDQVGLKEKAdsfPSSLSGGQQQRVAIARALAMNP 155
Cdd:PRK13639 81 GIVFQNPDdqLFAP-TVEEDVAFGPlnLGLSKEEVEKRVKEALKAVGMEGFENKP---PHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 156 DVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQD 234
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKAN 235
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
6.91e-52 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 169.40 E-value: 6.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNE--VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITApdSNIDQIRQK 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK--ENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 79 MGMVFQS-FNLFPHMSV-------LDNLTITPVKIKK--EDATKakeqamalldQVGLKEKADSFPSSLSGGQQQRVAIA 148
Cdd:PRK13632 85 IGIIFQNpDNQFIGATVeddiafgLENKKVPPKKMKDiiDDLAK----------KVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 149 RALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGM-TMVVVTHEMgfaKEV--ADRVIFMADGVIQEEGTPEEIF 224
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDM---DEAilADKVIVFSEGKLIAQGKPKEIL 230
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-228 |
2.07e-51 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 168.66 E-value: 2.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNID--QIRQKMGMVFQsfnlFPHM-- 92
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKlkPLRKKVGIVFQ----FPEHql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 93 ---SVLDNLTITPVK--IKKEDAtkaKEQAMALLDQVGLKEKA-DSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSA 166
Cdd:PRK13634 99 feeTVEKDICFGPMNfgVSEEDA---KQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498436323 167 LDPEMVGEVLAVMQDLAK-KGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQ 228
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-236 |
3.55e-51 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 167.27 E-value: 3.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 7 LSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEE--PT---SGEIFFEGQNITAPDSNIDQIRQKMGM 81
Cdd:PRK14243 16 LNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYAPDVDPVEVRRRIGM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHmSVLDNLTITP-VKIKKEDATKAKEQAM---ALLDQVglKEKADSFPSSLSGGQQQRVAIARALAMNPDV 157
Cdd:PRK14243 96 VFQKPNPFPK-SIYDNIAYGArINGYKGDMDELVERSLrqaALWDEV--KDKLKQSGLSLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 158 MLFDEPTSALDPEMVGEVLAVMQDLaKKGMTMVVVTHEMGFAKEVADRVIFMA---------DGVIQEEGTPEEIFDHPQ 228
Cdd:PRK14243 173 ILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSPQ 251
|
....*...
gi 498436323 229 NSRTQDFL 236
Cdd:PRK14243 252 QQATRDYV 259
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-214 |
3.87e-51 |
|
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: 165.12 E-value: 3.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDN-EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDsnidqiRQKM-GM 81
Cdd:cd03226 2 IENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE------RRKSiGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQS--FNLFPHmSVLDNLTITpvkikKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVML 159
Cdd:cd03226 76 VMQDvdYQLFTD-SVREELLLG-----LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498436323 160 FDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVI 214
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-236 |
5.93e-51 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 168.60 E-value: 5.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPD-SNIDQIRQKMGMVFQ----SFNlfPH 91
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpEAQKLLRQKIQIVFQnpygSLN--PR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 92 MSVLDNLTiTPVKIKKE-DATKAKEQAMALLDQVGLK-EKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDP 169
Cdd:PRK11308 109 KKVGQILE-EPLLINTSlSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498436323 170 EMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQDFL 236
Cdd:PRK11308 188 SVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALL 255
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-227 |
1.14e-50 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 168.48 E-value: 1.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSF-GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA--P-DSNIdqir 76
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElePaDRDI---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 qkmGMVFQSFNLFPHMSVLDNLTITpVKI----KKEDATKAKEQAMAL-LDQVgLKEKadsfPSSLSGGQQQRVAIARAL 151
Cdd:PRK11650 79 ---AMVFQNYALYPHMSVRENMAYG-LKIrgmpKAEIEERVAEAARILeLEPL-LDRK----PRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 152 AMNPDVMLFDEPTSALDP----EMVGEVLAVMQDLakkGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHP 227
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAklrvQMRLEIQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-218 |
2.42e-50 |
|
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: 163.16 E-value: 2.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSnidqIRQKMGM 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE----ALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDNLTITPVKIKKEdatkaKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLLARLLGIR-----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEG 218
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-226 |
2.91e-50 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 165.19 E-value: 2.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNE--VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKM 79
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS--EETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQS-FNLFPHMSVLDNLT--ITPVKIKKEDATKAKEQAmalLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPD 156
Cdd:PRK13635 84 GMVFQNpDNQFVGATVQDDVAfgLENIGVPREEMVERVDQA---LRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 157 VMLFDEPTSALDPEMVGEVLAVMQDL-AKKGMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEEIFDH 226
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-239 |
7.12e-50 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 167.90 E-value: 7.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA-PDSNIDQIR-QKMGMVFQSFNLFPHMSV 94
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKiSDAELREVRrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 95 LDNlTITPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGE 174
Cdd:PRK10070 124 LDN-TAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 175 VLAVMQDL-AKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQDFLNKV 239
Cdd:PRK10070 203 MQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
17-218 |
1.19e-49 |
|
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: 161.69 E-value: 1.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVK---DGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQniTAPDSNIDQI----RQKMGMVFQSFNLF 89
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT--VLFDSRKKINlppqQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 90 PHMSVLDNLTI-TPVKIKKEDatkaKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALD 168
Cdd:cd03297 88 PHLNVRENLAFgLKRKRNRED----RISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 498436323 169 PEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEG 218
Cdd:cd03297 164 RALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-224 |
1.23e-49 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 163.72 E-value: 1.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNE------VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNiTAPDSNIDQ 74
Cdd:PRK13633 4 MIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 75 IRQKMGMVFQSfnlfPHMSVL------------DNLTITPVKIKK--EDATKAkeqamalldqVGLKEKADSFPSSLSGG 140
Cdd:PRK13633 83 IRNKAGMVFQN----PDNQIVativeedvafgpENLGIPPEEIRErvDESLKK----------VGMYEYRRHAPHLLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 141 QQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGT 219
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGT 227
|
....*
gi 498436323 220 PEEIF 224
Cdd:PRK13633 228 PKEIF 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
1.83e-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: 161.38 E-value: 1.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapdSNIDQIRQKMGM 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV---REPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDNLTITpVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIH-ARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-212 |
2.53e-49 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 161.04 E-value: 2.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFG----DNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITaPDSNIDQI- 75
Cdd:NF038007 1 MLNMQNAEKCYItktiKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVT-NLSYSQKIi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 76 --RQKMGMVFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAM 153
Cdd:NF038007 80 lrRELIGYIFQSFNLIPHLSIFDNVAL-PLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 154 NPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGfAKEVADRVIFMADG 212
Cdd:NF038007 159 NPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDG 216
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-212 |
3.01e-49 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 162.34 E-value: 3.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDN----EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNidqiR 76
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD----R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 qkmGMVFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPD 156
Cdd:COG4525 79 ---GVVFQKDALLPWLNVLDNVAF-GLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 157 VMLFDEPTSALDpEMVGEvlaVMQDL-----AKKGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:COG4525 155 FLLMDEPFGALD-ALTRE---QMQELlldvwQRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-214 |
4.35e-49 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 161.77 E-value: 4.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFfEGqniTAPdsnIDQIRQKMGMVF 83
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-AG---TAP---LAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 84 QSFNLFPHMSVLDNLTItpvKIKKedatKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEP 163
Cdd:PRK11247 88 QDARLLPWKKVIDNVGL---GLKG----QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 164 TSALDPEMVGEvlavMQDL-----AKKGMTMVVVTHEMGFAKEVADRVIFMADGVI 214
Cdd:PRK11247 161 LGALDALTRIE----MQDLieslwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-224 |
5.39e-49 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 162.52 E-value: 5.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNIDQIRQKMGMVFQ--SFNLFPHMSV 94
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQypEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 95 LD------NLTITPVKIKKedatKAKEqAMAL--LDQVGLKEKAdsfPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSA 166
Cdd:PRK13637 103 KDiafgpiNLGLSEEEIEN----RVKR-AMNIvgLDYEDYKDKS---PFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 167 LDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIF 224
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-236 |
7.89e-49 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 161.36 E-value: 7.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTS-----GEIFFEGQNITAPDSNIDQIR 76
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 QKMGMVFQSFNLFPhMSVLDNLTI-------TPvKIKKEDATKAKEQAMALLDQVglKEKADSFPSSLSGGQQQRVAIAR 149
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYgvkivgwRP-KLEIDDIVESALKDADLWDEI--KHKIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 150 ALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLA-KKGMTMVVVTHEMGFAKEVADRVIFMAD-----GVIQEEGTPEEI 223
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKI 243
|
250
....*....|...
gi 498436323 224 FDHPQNSRTQDFL 236
Cdd:PRK14258 244 FNSPHDSRTREYV 256
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-212 |
9.46e-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: 159.91 E-value: 9.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSF-----GDNE--VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCL--NLLeePTSGEIFF--EGQNI---T 66
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYL--PDSGSILVrhDGGWVdlaQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 67 APDSNIDQIRQK-MGMVFQSFNLFPHMSVLDnLTITPVKIKKEDATKAKEQAMALLDQVGLKEK-ADSFPSSLSGGQQQR 144
Cdd:COG4778 82 ASPREILALRRRtIGYVSQFLRVIPRVSALD-VVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498436323 145 VAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-227 |
1.55e-48 |
|
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: 162.96 E-value: 1.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVkQLSKSFGDNEVlkSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQniTAPDSNIDQI----R 76
Cdd:COG4148 2 MLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE--VLQDSARGIFlpphR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 QKMGMVFQSFNLFPHMSVLDNLTITPVKIKKEDATKAKEQAMALLdqvGLKEKADSFPSSLSGGQQQRVAIARALAMNPD 156
Cdd:COG4148 77 RRIGYVFQEARLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498436323 157 VMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGfakEV---ADRVIFMADGVIQEEGTPEEIFDHP 227
Cdd:COG4148 154 LLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLD---EVarlADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-237 |
1.73e-48 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 160.39 E-value: 1.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDN---------EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNI 72
Cdd:COG4167 5 LEVRNLSKTFKYRtglfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLE--YGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 73 DQIRQKMGMVFQ----SFNlfPHMSV---LDnltiTPVKIKKE-DATKAKEQAMALLDQVGL-KEKADSFPSSLSGGQQQ 143
Cdd:COG4167 83 KYRCKHIRMIFQdpntSLN--PRLNIgqiLE----EPLRLNTDlTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 144 RVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDL-AKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEE 222
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELqEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAE 236
|
250
....*....|....*
gi 498436323 223 IFDHPQNSRTQDFLN 237
Cdd:COG4167 237 VFANPQHEVTKRLIE 251
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-214 |
1.81e-48 |
|
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: 156.82 E-value: 1.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNItAPDSNIDQIRQKMGMVF 83
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV-SFASPRDARRAGIAMVY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 84 QsfnlfphmsvldnltitpvkikkedatkakeqamalldqvglkekadsfpssLSGGQQQRVAIARALAMNPDVMLFDEP 163
Cdd:cd03216 82 Q----------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 498436323 164 TSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVI 214
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-239 |
6.08e-48 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 162.31 E-value: 6.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNItapdSNIDQIRQKMG 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL----SHVPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFPHMSVLDNLTItpvKIKKEDATKA--KEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVM 158
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAF---GLKQDKLPKAeiASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 159 LFDEPTSALDPEMVGEV-LAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQDFLN 237
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG 251
|
..
gi 498436323 238 KV 239
Cdd:PRK11607 252 SV 253
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-206 |
6.89e-48 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 164.81 E-value: 6.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNiDQIRQKMG 80
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPR-DAIALGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFPHMSVLDN--LTITPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVM 158
Cdd:COG3845 84 MVHQHFMLVPNLTVAENivLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARIL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498436323 159 LFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRV 206
Cdd:COG3845 164 ILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRV 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
15-214 |
7.51e-48 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 166.82 E-value: 7.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 15 EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSniDQI----RQKMGMVFQSFNLFP 90
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDA--DALaqlrREHFGFIFQRYHLLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 91 HMSVLDNLTITPVKIKKEDATKaKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPE 170
Cdd:PRK10535 100 HLTAAQNVEVPAVYAGLERKQR-LLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 498436323 171 MVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEvADRVIFMADGVI 214
Cdd:PRK10535 179 SGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-212 |
5.75e-47 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 155.03 E-value: 5.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSF-GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA-PDSNIDQIRQK 78
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 79 MGMVFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVM 158
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498436323 159 LFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-228 |
7.70e-47 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 155.19 E-value: 7.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA-PdsnIDQiRQKM 79
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlP---MHK-RARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVF--QSFNLFPHMSVLDNLTITpVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDV 157
Cdd:COG1137 79 GIGYlpQEASIFRKLTVEDNILAV-LELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498436323 158 MLFDEPTSALDPEMVGEVLAVMQDLAKKGMTmVVVT----HEMgfaKEVADRVIFMADGVIQEEGTPEEIFDHPQ 228
Cdd:COG1137 158 ILLDEPFAGVDPIAVADIQKIIRHLKERGIG-VLITdhnvRET---LGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-211 |
1.03e-46 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 154.18 E-value: 1.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLN-LLEEP--TSGEIFFEGQNITApdsnIDQIRQ 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRLTA----LPAEQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 78 KMGMVFQSFNLFPHMSVLDNLTI-TPVKIKKEDAtkaKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPD 156
Cdd:COG4136 77 RIGILFQDDLLFPHLSVGENLAFaLPPTIGRAQR---RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 157 VMLFDEPTSALDPEMVGEVLA-VMQDLAKKGMTMVVVTHEMGFAkEVADRVIFMAD 211
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEEDA-PAAGRVLDLGN 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-218 |
1.09e-46 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 154.19 E-value: 1.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 21 DLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNidqiRQKMGMVFQSFNLFPHMSVLDN--L 98
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA----DRPVSMLFQENNLFAHLTVEQNvgL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 99 TITP-VKIKKEDatkakEQAM-ALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVL 176
Cdd:cd03298 94 GLSPgLKLTAED-----RQAIeVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 498436323 177 AVMQDL-AKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEG 218
Cdd:cd03298 169 DLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-224 |
1.60e-46 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 154.89 E-value: 1.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKMG 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLA--AWSPWELARRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNL-FPhMSVLD--NLTITPVKIKKEDATKAKEQAMAlldQVGLKEKADSFPSSLSGGQQQRVAIARALA----- 152
Cdd:COG4559 79 VLPQHSSLaFP-FTVEEvvALGRAPHGSSAAQDRQIVREALA---LVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwep 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498436323 153 --MNPDVMLFDEPTSALDPemvGEVLAVMQ---DLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIF 224
Cdd:COG4559 155 vdGGPRWLFLDEPTSALDL---AHQHAVLRlarQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVL 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-219 |
1.97e-46 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 154.20 E-value: 1.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 6 QLSKSFGD----NEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDS-NIDQIR-QKM 79
Cdd:PRK11629 10 NLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaAKAELRnQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVML 159
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 160 FDEPTSALDPEMVGEVLAVMQDL-AKKGMTMVVVTHEMGFAKEVaDRVIFMADGVIQEEGT 219
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELS 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-223 |
2.04e-46 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 156.04 E-value: 2.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDsnIDQI----- 75
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED--RRRIgylpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 76 -RqkmGmvfqsfnLFPHMSVLDNLtitpV---KIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARAL 151
Cdd:COG4152 79 eR---G-------LYPKMKVGEQL----VylaRLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498436323 152 AMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
13-222 |
2.96e-46 |
|
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: 153.85 E-value: 2.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 13 DNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILrclNLLE---EPTSGEIFFEGQNITapDSNIDQIRQKMGMVFQSFNLF 89
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVV---SLLErfyDPTSGEILLDGVDIR--DLNLRWLRSQIGLVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 90 PhMSVLDNLTITPVKIKKEDATKAKEQA------MALLD----QVGlkEKAdsfpSSLSGGQQQRVAIARALAMNPDVML 159
Cdd:cd03249 90 D-GTIAENIRYGKPDATDEEVEEAAKKAnihdfiMSLPDgydtLVG--ERG----SQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498436323 160 FDEPTSALDPEMVGEVLAVMqDLAKKGMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEE 222
Cdd:cd03249 163 LDEATSALDAESEKLVQEAL-DRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-223 |
3.22e-46 |
|
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: 155.63 E-value: 3.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 9 KSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapdSNIDQIRQKMGMVFQSFNL 88
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV---REPRKVRRSIGIVPQYASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 89 FPHMSVLDNLTI------TPVKIKKEdatKAKEqamaLLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDE 162
Cdd:TIGR01188 78 DEDLTGRENLEMmgrlygLPKDEAEE---RAEE----LLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 163 PTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:TIGR01188 151 PTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-237 |
5.98e-46 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 154.15 E-value: 5.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA-PDSNIDQIRQKM 79
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFNLFPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVML 159
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 160 FDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPqNSRTQDFLN 237
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQFLD 244
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-226 |
8.65e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 153.75 E-value: 8.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSN--IDQIRQKMGMVFQsfnlFPHMSV 94
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdIKQIRKKVGLVFQ----FPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 95 LDNLTITPVK-------IKKEDATKAKEQAMALldqVGLKEKA-DSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSA 166
Cdd:PRK13649 99 FEETVLKDVAfgpqnfgVSQEEAEALAREKLAL---VGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 167 LDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDH 226
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-222 |
1.15e-45 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 153.00 E-value: 1.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKMG 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA--DWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNL-FPhMSVLD--NLTITPVKIKKEDATKAKEQAMAlldQVGLKEKADSFPSSLSGGQQQRVAIARALA----- 152
Cdd:PRK13548 80 VLPQHSSLsFP-FTVEEvvAMGRAPHGLSRAEDDALVAAALA---QVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498436323 153 -MNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEE 222
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-223 |
1.33e-45 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 151.91 E-value: 1.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 3 NVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNiDQIRQKMGMV 82
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPH-ERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 83 FQSFNLFPHMSVLDNLTITPVKIKKEDaTKAKEQAMALLDQvgLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDE 162
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRS-RKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498436323 163 PTSALDPEMVGEVLAVMQDLAK-KGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAeGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-223 |
1.57e-45 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 151.66 E-value: 1.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 21 DLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQN--ITAPDsnidqiRQKMGMVFQSFNLFPHMSVLDN- 97
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhtTTPPS------RRPVSMLFQENNLFSHLTVAQNi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 98 -LTITPvKIKKEDATKAKEQAMAllDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVL 176
Cdd:PRK10771 93 gLGLNP-GLKLNAAQREKLHAIA--RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498436323 177 AVMQDL-AKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:PRK10771 170 TLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-217 |
2.03e-45 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 151.47 E-value: 2.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNE----VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNID-QI 75
Cdd:PRK10584 6 IVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 76 R-QKMGMVFQSFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMN 154
Cdd:PRK10584 86 RaKHVGFVFQSFMLIPTLNALENVEL-PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498436323 155 PDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEvADRVIFMADGVIQEE 217
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
16-222 |
3.47e-45 |
|
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: 160.12 E-value: 3.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 16 VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDsnIDQIRQKMGMVFQSFNLFPHmSVL 95
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLD--VQAVRRQLGVVLQNGRLMSG-SIF 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 96 DNLTITpvkikkedATKAKEQAMALLDQVGLKEKADSFP-----------SSLSGGQQQRVAIARALAMNPDVMLFDEPT 164
Cdd:TIGR03797 545 ENIAGG--------APLTLDEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRKPRILLFDEAT 616
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498436323 165 SALDPEMVGevlAVMQDLAKKGMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEE 222
Cdd:TIGR03797 617 SALDNRTQA---IVSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDE 670
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-227 |
5.39e-45 |
|
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: 150.39 E-value: 5.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQiRQKMGMVF 83
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT--KLPMHK-RARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 84 --QSFNLFPHMSVLDNLTITpVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:cd03218 80 lpQEASIFRKLTVEENILAV-LEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHP 227
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-237 |
1.85e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 150.27 E-value: 1.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNE---VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITApdSNIDQIRQ 77
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE--ENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 78 KMGMVFQS-FNLFPHMSVLDNLTITpVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPD 156
Cdd:PRK13650 82 KIGMVFQNpDNQFVGATVEDDVAFG-LENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 157 VMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMgfaKEVA--DRVIFMADGVIQEEGTPEEIFdhpqnSRTQ 233
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDL---DEVAlsDRVLVMKNGQVESTSTPRELF-----SRGN 232
|
....
gi 498436323 234 DFLN 237
Cdd:PRK13650 233 DLLQ 236
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-218 |
3.59e-44 |
|
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: 147.70 E-value: 3.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 21 DLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNIT--APdsnidqIRQKMGMVFQSFNLFPHMSVLDN- 97
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTglAP------YQRPVSMLFQENNLFAHLTVRQNi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 98 -LTITP-VKIKKEDatkaKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEV 175
Cdd:TIGR01277 92 gLGLHPgLKLNAEQ----QEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 498436323 176 LAVMQDLA-KKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEG 218
Cdd:TIGR01277 168 LALVKQLCsERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-212 |
7.48e-44 |
|
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: 147.23 E-value: 7.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNidqirqKMgMVFQSFNLFPHMSVLD 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD------RM-VVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 97 NLTITpVKIKKEDATKAKEQAMA--LLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGE 174
Cdd:TIGR01184 74 NIALA-VDRVLPDLSKSERRAIVeeHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 498436323 175 VL-AVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:TIGR01184 153 LQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-222 |
8.39e-44 |
|
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: 147.38 E-value: 8.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 13 DNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKMGMVFQSFNLFpHM 92
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIR--EVTLDSLRRAIGVVPQDTVLF-ND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 93 SVLDNltitpVKIKKEDATKakEQAMALLDQVGLKEKADSFPSS-----------LSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:cd03253 90 TIGYN-----IRYGRPDATD--EEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAkKGMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEE 222
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-199 |
1.42e-43 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 145.26 E-value: 1.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 12 GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNIDQIRQKMGMVFQSFN--LF 89
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQRVGLVFQDPDdqLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 90 pHMSVLDNLTITPVKI--KKEDATKAKEQAMALLDQVGLKEKAdsfPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSAL 167
Cdd:TIGR01166 83 -AADVDQDVAFGPLNLglSEAEVERRVREALTAVGASGLRERP---THCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180 190
....*....|....*....|....*....|..
gi 498436323 168 DPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFA 199
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-223 |
2.07e-43 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 146.77 E-value: 2.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSniDQIRQKMG 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPS--RELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQS--FNL------------FPHmsvldnltiTPVKIKKEDATKAkEQAMALLDqvgLKEKADSFPSSLSGGQQQRVA 146
Cdd:COG4604 79 ILRQEnhINSrltvrelvafgrFPY---------SKGRLTAEDREII-DEAIAYLD---LEDLADRYLDELSGGQRQRAF 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498436323 147 IARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAK-KGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADeLGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-223 |
3.79e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 147.93 E-value: 3.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDN-----EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEI---FFEGQNITAPDS--- 70
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEkek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 71 ----------------NIDQIRQKMGMVFQ--SFNLFpHMSVLDNLTITPVK--IKKEDAtkaKEQAMALLDQVGLKEK- 129
Cdd:PRK13651 83 vleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSmgVSKEEA---KKRAAKYIELVGLDESy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 130 ADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFM 209
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|....
gi 498436323 210 ADGVIQEEGTPEEI 223
Cdd:PRK13651 239 KDGKIIKDGDTYDI 252
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-226 |
4.82e-43 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 146.31 E-value: 4.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLL---EEPTSGEIFFEGQNITAPDS---NIDQ 74
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRlarDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 75 IRQKMGMVFQSFNLFPHMSVLDNLTI-----TPV--KIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAI 147
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLIgalgsTPFwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 148 ARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPE----E 222
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQqfdnE 243
|
....
gi 498436323 223 IFDH 226
Cdd:PRK09984 244 RFDH 247
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-227 |
5.14e-43 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 145.90 E-value: 5.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA-PDSNIdqirQKM 79
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlPGHQI----ARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMV--FQSFNLFPHMSVLDNLTI----------------TPVKIKKEdaTKAKEQAMALLDQVGLKEKADSFPSSLSGGQ 141
Cdd:PRK11300 81 GVVrtFQHVRLFREMTVIENLLVaqhqqlktglfsgllkTPAFRRAE--SEALDRAATWLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 142 QQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTP 220
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
....*..
gi 498436323 221 EEIFDHP 227
Cdd:PRK11300 239 EEIRNNP 245
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-214 |
8.34e-43 |
|
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: 143.96 E-value: 8.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDsnidqiRQKMGM 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA------RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDNLT-ITPVK-IKKEDAtkaKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVML 159
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVyLAQLKgLKKEEA---RRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498436323 160 FDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVI 214
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-218 |
1.17e-42 |
|
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: 144.05 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNE----VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapdSNIDQIR 76
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV---KEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 QKMGMVFQSFNLFPHMSVLDNLTITP--VKIKKEDATKAKEQamaLLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMN 154
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTARENLEYFAglYGLKGDELTARLEE---LADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498436323 155 PDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEG 218
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
1.41e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 145.26 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGD-NEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITApdSNIDQIRQKMG 80
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA--ENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFN--LFPhMSVLDNLTITPVKIKKeDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVM 158
Cdd:PRK13647 83 LVFQDPDdqVFS-STVWDDVAFGPVNMGL-DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498436323 159 LFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPE 221
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-224 |
2.73e-42 |
|
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: 144.07 E-value: 2.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSG---EIFfeGQNITApdSNIDQIRQ 77
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF--GERRGG--EDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 78 KMGMVFQSFNLF--PHMSVLDnLTIT--------PVKIKKEDatkaKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAI 147
Cdd:COG1119 79 RIGLVSPALQLRfpRDETVLD-VVLSgffdsiglYREPTDEQ----RERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 148 ARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKG-MTMVVVTH---EM--GFakevaDRVIFMADGVIQEEGTPE 221
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhveEIppGI-----THVLLLKDGRVVAAGPKE 228
|
...
gi 498436323 222 EIF 224
Cdd:COG1119 229 EVL 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-218 |
3.26e-42 |
|
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: 142.72 E-value: 3.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGeVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITApdsNIDQIRQKMGM 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK---QPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDNLTITPVkIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:cd03264 77 LPQEFGVYPNFTVREFLDYIAW-LKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAkKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEG 218
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-223 |
3.94e-42 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 147.68 E-value: 3.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNidQIRQKMG 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR--AASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQ----SFNL----------FPHMSVLDNLTitpvkikkEDATKAKEQAMallDQVGLKEKADSFPSSLSGGQQQRVA 146
Cdd:PRK09536 81 SVPQdtslSFEFdvrqvvemgrTPHRSRFDTWT--------ETDRAAVERAM---ERTGVAQFADRPVTSLSGGERQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498436323 147 IARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-236 |
4.67e-42 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 143.65 E-value: 4.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEE------PTSGEIFFEGQNITAPDSniDQ 74
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDA--IK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 75 IRQKMGMVFQSFNLFPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGL----KEKADSFPSSLSGGQQQRVAIARA 150
Cdd:PRK14246 88 LRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 151 LAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLaKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNS 230
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNE 246
|
....*.
gi 498436323 231 RTQDFL 236
Cdd:PRK14246 247 LTEKYV 252
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
5.36e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 144.18 E-value: 5.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSF-GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKM 79
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT--KENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFN--LFPhMSVLDNLTITPVKIKKEDATKAKEQAMALlDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDV 157
Cdd:PRK13652 81 GLVFQNPDdqIFS-PTVEQDIAFGPINLGLDEETVAHRVSSAL-HMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 158 MLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHP 227
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-228 |
5.51e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 144.20 E-value: 5.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSN--IDQIRQKMGMVFQsfnlFPHMSV 94
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknLKKLRKKVSLVFQ----FPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 95 LDNLTITPVKIKKED----ATKAKEQAMALLDQVGLKEK-ADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDP 169
Cdd:PRK13641 99 FENTVLKDVEFGPKNfgfsEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 170 EMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQ 228
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
6-223 |
9.81e-42 |
|
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: 145.25 E-value: 9.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 6 QLSKSFGDNEVlkSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNIDQI--RQKMGMVF 83
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPpeKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 84 QSFNLFPHMSVLDNLTitpVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEP 163
Cdd:TIGR02142 82 QEARLFPHLSVRGNLR---YGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 164 TSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
13-225 |
1.21e-41 |
|
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: 141.60 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 13 DNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKMGMVFQSFNLFpHM 92
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVR--DYTLASLRRQIGLVSQDVFLF-ND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 93 SVLDNltitpVKIKKEDATKakEQAMALLDQVGLKEKADSFP-----------SSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:cd03251 91 TVAEN-----IAYGRPGATR--EEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAkKGMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEEIFD 225
Cdd:cd03251 164 EATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-236 |
3.63e-41 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 141.77 E-value: 3.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 7 LSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSG-----EIFFEGQNITAPdSNIDQIRQKMGM 81
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNY-RDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPhMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGL----KEKADSFPSSLSGGQQQRVAIARALAMNPDV 157
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 158 MLFDEPTSALDPEMVGEVLAVMQDLAKKgMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQDFL 236
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-228 |
7.99e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 140.66 E-value: 7.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKMGMVFQ------------ 84
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT--DDNFEKLRKHIGIVFQnpdnqfvgsivk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 85 ---SFNLFPHMSVLDNLtitpvkikkedatkaKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:PRK13648 103 ydvAFGLENHAVPYDEM---------------HRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498436323 162 EPTSALDPEMVGEVLAVMQDL-AKKGMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEEIFDHPQ 228
Cdd:PRK13648 168 EATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-227 |
2.09e-40 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 139.44 E-value: 2.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSF---------GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPD-S 70
Cdd:PRK10419 3 LLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNrA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 71 NIDQIRQKMGMVFQ----SFNlfPHMSVLDNLTiTPVK-IKKEDATKAKEQAMALLDQVGLK-EKADSFPSSLSGGQQQR 144
Cdd:PRK10419 83 QRKAFRRDIQMVFQdsisAVN--PRKTVREIIR-EPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 145 VAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDL-AKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGT--PE 221
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPvgDK 239
|
....*.
gi 498436323 222 EIFDHP 227
Cdd:PRK10419 240 LTFSSP 245
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-214 |
2.81e-40 |
|
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: 136.19 E-value: 2.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNE--VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNidQIRQKM 79
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPN--ELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFNLFPHmSVLDNLtitpvkikkedatkakeqamalldqvglkekadsfpssLSGGQQQRVAIARALAMNPDVML 159
Cdd:cd03246 79 GYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498436323 160 FDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEvADRVIFMADGVI 214
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-227 |
6.07e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 138.58 E-value: 6.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGD-NEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPdSNIDQIRQKM 79
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDF-SKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSfnlfPHMSVL------------DNLTITPVKIKKEdatkaKEQAMAlldQVGLKEKADSFPSSLSGGQQQRVAI 147
Cdd:PRK13644 80 GIVFQN----PETQFVgrtveedlafgpENLCLPPIEIRKR-----VDRALA---EIGLEKYRHRSPKTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 148 ARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGfAKEVADRVIFMADGVIQEEGTPEEIFDHP 227
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-225 |
7.98e-40 |
|
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: 136.97 E-value: 7.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNE-VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKMG 80
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR--DISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFPHmSVLDNLTITPVKIKKEDATKAKEQA------MALLDqvGLKEKADSFPSSLSGGQQQRVAIARALAMN 154
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLGRPNATDEEVIEAAKEAgahdfiMKLPN--GYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 155 PDVMLFDEPTSALDPEMVGEVLAVMQDLaKKGMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEEIFD 225
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-225 |
1.20e-39 |
|
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: 136.85 E-value: 1.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 15 EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNidQIRQKMGMVFQSFNLFpHMSV 94
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPA--WLRRQVGVVLQENVLF-NRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 95 LDNLTITPVKIKKEDATKAKEQAMALLDQVGLKEKADSF----PSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPE 170
Cdd:cd03252 93 RDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIvgeqGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498436323 171 MVGEVLAVMQDLAkKGMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEEIFD 225
Cdd:cd03252 173 SEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
1.25e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 138.06 E-value: 1.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGD-NEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNIDQIRQKM 79
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQS--FNLFPhMSVLDNLTITPVKIK--KEDATKAKEQAMAlldQVGLKEKADSFPSSLSGGQQQRVAIARALAMNP 155
Cdd:PRK13636 85 GMVFQDpdNQLFS-ASVYQDVSFGAVNLKlpEDEVRKRVDNALK---RTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 156 DVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIF 224
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-239 |
1.40e-39 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 137.07 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITApdsnidqirqkmg 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 mvFQSFNLFPHMSVLDNLTITPVKIK--------------------KEDATKAkEQAMAlldQVGLKEKADSFPSSLSGG 140
Cdd:PRK11231 69 --LSSRQLARRLALLPQHHLTPEGITvrelvaygrspwlslwgrlsAEDNARV-NQAME---QTRINHLADRRLTDLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 141 QQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTP 220
Cdd:PRK11231 143 QRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
|
250
....*....|....*....
gi 498436323 221 EEIFdhpqnsrTQDFLNKV 239
Cdd:PRK11231 223 EEVM-------TPGLLRTV 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-223 |
7.57e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 140.54 E-value: 7.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSksfgDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITaPDSNIDQIRQKMGMV- 82
Cdd:COG1129 259 VEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR-IRSPRDAIRAGIAYVp 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 83 --FQSFNLFPHMSVLDNLTIT---------PVKIKKEdatkaKEQAMALLDQVGLKEKADSFP-SSLSGGQQQRVAIARA 150
Cdd:COG1129 334 edRKGEGLVLDLSIRENITLAsldrlsrggLLDRRRE-----RALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 151 LAMNPDVMLFDEPTSALDpemVG---EVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:COG1129 409 LATDPKVLILDEPTRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
1.29e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 136.52 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNE-----VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEI----FFEGQNITAPDS- 70
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 71 ---------NIDQIRQKMGMVFQ--SFNLFPHmSVLDNLTITPV--KIKKEDAtkaKEQAMALLDQVGLKEK-ADSFPSS 136
Cdd:PRK13631 101 tnpyskkikNFKELRRRVSMVFQfpEYQLFKD-TIEKDIMFGPValGVKKSEA---KKLAKFYLNKMGLDDSyLERSPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 137 LSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQE 216
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
....*...
gi 498436323 217 EGTPEEIF 224
Cdd:PRK13631 257 TGTPYEIF 264
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-224 |
2.56e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 134.91 E-value: 2.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 15 EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAP--DSNIDQIRQKMGMVFQsfnlFPHM 92
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkDKYIRPVRKRIGMVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 93 -----SVLDNLTITPvKIKKEDATKAKEQAMALLDQVGL-KEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSA 166
Cdd:PRK13646 97 qlfedTVEREIIFGP-KNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 167 LDPEMVGEVLAVMQDL-AKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIF 224
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-223 |
5.13e-38 |
|
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: 138.78 E-value: 5.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLE--EPTSGEIF----------------FEGQ 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 64 N---------------ITAPDSNIDQIRQKMGMVFQ-SFNLFPHMSVLDNLTITPVKIKKEdATKAKEQAMALLDQVGLK 127
Cdd:TIGR03269 81 PcpvcggtlepeevdfWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYE-GKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 128 EKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAK-KGMTMVVVTHEMGFAKEVADRV 206
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKaSGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*..
gi 498436323 207 IFMADGVIQEEGTPEEI 223
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEV 256
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-223 |
8.28e-38 |
|
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: 138.01 E-value: 8.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFG--DNEVLKSID---LEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFF----EGQNITAPD-S 70
Cdd:TIGR03269 279 IIKVRNVSKRYIsvDRGVVKAVDnvsLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGpD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 71 NIDQIRQKMGMVFQSFNLFPHMSVLDNLTiTPVKIKKEDATkAKEQAMALLDQVGLKEKA-----DSFPSSLSGGQQQRV 145
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLT-EAIGLELPDEL-ARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 146 AIARALAMNPDVMLFDEPTSALDP-EMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPiTKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
16-225 |
1.48e-37 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 138.85 E-value: 1.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 16 VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSniDQIRQKMGMVFQSFNLFpHMSVL 95
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDP--ADLRRNIGYVPQDPRLF-YGTLR 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 96 DNLTItpvkikkeDATKAKEQAM-ALLDQVGLKEKADSFPS-----------SLSGGQQQRVAIARALAMNPDVMLFDEP 163
Cdd:TIGR03375 557 DNIAL--------GAPYADDEEIlRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDEP 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498436323 164 TSALDPEMVGEVLAVMQDLAkKGMTMVVVTHEMGFAkEVADRVIFMADGVIQEEGTPEEIFD 225
Cdd:TIGR03375 629 TSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLL-DLVDRIIVMDNGRIVADGPKDQVLE 688
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-209 |
1.56e-37 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 137.42 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGD-NEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSniDQIRQKMG 80
Cdd:TIGR02857 322 LEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA--DSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFPHmSVLDNltitpVKIKKEDATKAK-EQAmalLDQVGLKEKADSFP-----------SSLSGGQQQRVAIA 148
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAEN-----IRLARPDASDAEiREA---LERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 149 RALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAkKGMTMVVVTHEMGFAkEVADRVIFM 209
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-239 |
1.67e-37 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 133.68 E-value: 1.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSID---LEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNIT-APDSNIDQIRQKMGMVFQ----SFNl 88
Cdd:PRK15079 34 LKAVDgvtLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgMKDDEWRAVRSDIQMIFQdplaSLN- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 89 fPHMSVLDnLTITPVKIKKEDATKA--KEQAMALLDQVGLKEKA-DSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTS 165
Cdd:PRK15079 113 -PRMTIGE-IIAEPLRTYHPKLSRQevKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498436323 166 ALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQDFLNKV 239
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAV 265
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-221 |
3.81e-37 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 130.57 E-value: 3.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCL--NLLEEPTSGEIFFEGQNITapDSNIDQiRQKMG- 80
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDIL--ELSPDE-RARAGi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 -MVFQSFNLFPHMSVLDNLT--ITPVKIKKEDATKAKEQAMALLDQVGLKEkadSFPS-----SLSGGQQQRVAIARALA 152
Cdd:COG0396 80 fLAFQYPVEIPGVSVSNFLRtaLNARRGEELSAREFLKLLKEKMKELGLDE---DFLDryvneGFSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 153 MNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEV-ADRVIFMADGVIQEEGTPE 221
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIkPDFVHVLVDGRIVKSGGKE 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-224 |
3.88e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 131.78 E-value: 3.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKS-----IDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSN--ID 73
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASralfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 74 QIRQKMGMVFQsfnlFPHMSVLDNLTITPVKIKKEDATKAKEQAMAL----LDQVGL-KEKADSFPSSLSGGQQQRVAIA 148
Cdd:PRK13643 81 PVRKKVGVVFQ----FPESQLFEETVLKDVAFGPQNFGIPKEKAEKIaaekLEMVGLaDEFWEKSPFELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 149 RALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIF 224
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-212 |
4.81e-37 |
|
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: 128.82 E-value: 4.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 15 EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLN--LLEEPTSGEIFFEGQNITApdsniDQIRQKMGMVFQSFNLFPHM 92
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDK-----RSFRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 93 SVLDNLTITpvkikkedatkakeqamALLdqvglkekadsfpSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMV 172
Cdd:cd03213 98 TVRETLMFA-----------------AKL-------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 498436323 173 GEVLAVMQDLAKKGMTMVVVTH----EMgFakEVADRVIFMADG 212
Cdd:cd03213 148 LQVMSLLRRLADTGRTIICSIHqpssEI-F--ELFDKLLLLSQG 188
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-212 |
8.10e-37 |
|
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: 127.55 E-value: 8.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 16 VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPdSNIDQIRQKMGMV---FQSFNLFPHM 92
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRR-SPRDAIRAGIAYVpedRKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 93 SVLDNLTItpvkikkedatkakeqamalldqvglkekadsfPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMV 172
Cdd:cd03215 94 SVAENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 498436323 173 GEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:cd03215 141 AEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-236 |
3.88e-36 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 129.86 E-value: 3.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEV-LKSID---LEVKDGEVVVIIGPSGSGKS-TILRCLNLLEEP---TSGEIFFEGQNITAPDSNi 72
Cdd:PRK11022 3 LLNVDKLSVHFGDESApFRAVDrisYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEK- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 73 dQIRQKMG----MVFQ----SFNlfPHMSVLDNLtITPVKIKKEDATKAKEQ-AMALLDQVGLKEKA---DSFPSSLSGG 140
Cdd:PRK11022 82 -ERRNLVGaevaMIFQdpmtSLN--PCYTVGFQI-MEAIKVHQGGNKKTRRQrAIDLLNQVGIPDPAsrlDVYPHQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 141 QQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGT 219
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGK 237
|
250
....*....|....*..
gi 498436323 220 PEEIFDHPQNSRTQDFL 236
Cdd:PRK11022 238 AHDIFRAPRHPYTQALL 254
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-214 |
4.40e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 128.28 E-value: 4.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFG-----DNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA-PDsniDQ 74
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlPE---YK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 75 IRQKMGMVFQ--SFNLFPHMSVLDNLTITPVK---------IKKEDATKAKEQaMALLDQvGLKEKADSFPSSLSGGQQQ 143
Cdd:COG1101 78 RAKYIGRVFQdpMMGTAPSMTIEENLALAYRRgkrrglrrgLTKKRRELFREL-LATLGL-GLENRLDTKVGLLSGGQRQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 144 rvaiARALAM----NPDVMLFDEPTSALDPEMVGEVLAVMQDL-AKKGMTMVVVTHEMGFAKEVADRVIFMADGVI 214
Cdd:COG1101 156 ----ALSLLMatltKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-222 |
5.15e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 133.80 E-value: 5.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNE--VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKM 79
Cdd:PRK11160 339 LTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA--DYSEAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFNLFPHmSVLDNLtitpvKIKKEDATkaKEQAMALLDQVGLKEKADSFPS----------SLSGGQQQRVAIAR 149
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNL-----LLAAPNAS--DEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498436323 150 ALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAkKGMTMVVVTHEMgFAKEVADRVIFMADGVIQEEGTPEE 222
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQE 559
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-222 |
1.15e-35 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 132.11 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFeGQNItapdsNI---DQIRQ 77
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV-----KIgyfDQHQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 78 kmgmvfqsfNLFPHMSVLDNLtitpvkikKEDATKAKEQ-AMALLDQVGLK-EKADSFPSSLSGGQQQRVAIARALAMNP 155
Cdd:COG0488 389 ---------ELDPDKTVLDEL--------RDGAPGGTEQeVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 156 DVMLFDEPTSALDPEMvgevLAVMQD-LAK-KGmTMVVVTHEMGFAKEVADRVIFMADGVIQE-EGTPEE 222
Cdd:COG0488 452 NVLLLDEPTNHLDIET----LEALEEaLDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVREyPGGYDD 516
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-228 |
1.21e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 127.61 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNE--VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGE---IFFEGQNITApdSNIDQIR 76
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTA--KTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 QKMGMVFQS-FNLFPHMSVLDNltitpVKIKKEDATKAKEQAMAL----LDQVGLKEKADSFPSSLSGGQQQRVAIARAL 151
Cdd:PRK13640 84 EKVGIVFQNpDNQFVGATVGDD-----VAFGLENRAVPRPEMIKIvrdvLADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498436323 152 AMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAK-KGMTMVVVTHEMGFAkEVADRVIFMADGVIQEEGTPEEIFDHPQ 228
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-212 |
2.34e-35 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 131.06 E-value: 2.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNIdQIRQKMG 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL-AAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFPHMSVLDNLTITPVKIKKE------DATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMN 154
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIGRHLTKKVcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498436323 155 PDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-226 |
2.49e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 127.61 E-value: 2.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapdSNIDQIRQKMGM 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP---SRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDNLTITPvKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVFG-RYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDH 226
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-212 |
2.51e-35 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 125.97 E-value: 2.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSnidqirqKMG 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-------ERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFPHMSVLDNltitpVKIKKEDATKAKEQ----AMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPD 156
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDN-----VAFGLQLAGVEKMQrleiAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 157 VMLFDEPTSALDP----EMVGEVLAVMQDLAKKgmtMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:PRK11248 149 LLLLDEPFGALDAftreQMQTLLLKLWQETGKQ---VLLITHDIEEAVFMATELVLLSPG 205
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
13-226 |
2.60e-35 |
|
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: 131.76 E-value: 2.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 13 DNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKMGMVFQSFNLFPHm 92
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA--DYTLASLRRQVALVSQDVVLFND- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 93 SVLDNLTIT-PVKIKKEDATKAKEQA--MALLDQV--GLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSAL 167
Cdd:TIGR02203 421 TIANNIAYGrTEQADRAEIERALAAAyaQDFVDKLplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSAL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 168 DPEMVGEVLAVMQDLaKKGMTMVVVTHEMGfAKEVADRVIFMADGVIQEEGTPEEIFDH 226
Cdd:TIGR02203 501 DNESERLVQAALERL-MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-233 |
3.69e-35 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 126.06 E-value: 3.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDN---------EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSN 71
Cdd:PRK15112 4 LLEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 72 IDQirQKMGMVFQ--SFNLFPHMSVLDNLTItPVKIKKEDATKAKEQAM-ALLDQVGLK-EKADSFPSSLSGGQQQRVAI 147
Cdd:PRK15112 84 YRS--QRIRMIFQdpSTSLNPRQRISQILDF-PLRLNTDLEPEQREKQIiETLRQVGLLpDHASYYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 148 ARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDL-AKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDH 226
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
....*..
gi 498436323 227 PQNSRTQ 233
Cdd:PRK15112 241 PLHELTK 247
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-194 |
3.71e-35 |
|
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: 130.94 E-value: 3.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 12 GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSniDQIRQKMGMVFQSFNLFpH 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ--DEVRRRVSVCAQDAHLF-D 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 92 MSVLDNLtitpvKIKKEDATKakEQAMALLDQVGLKEKADSFP-----------SSLSGGQQQRVAIARALAMNPDVMLF 160
Cdd:TIGR02868 423 TTVRENL-----RLARPDATD--EELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....
gi 498436323 161 DEPTSALDPEMVGEVLAVMQDlAKKGMTMVVVTH 194
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
10-222 |
4.17e-35 |
|
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: 131.48 E-value: 4.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 10 SFG---DNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA--PDSnidqIRQKMGMVfq 84
Cdd:COG5265 364 SFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvtQAS----LRAAIGIV-- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 85 sfnlfPHMSVLDNLTITpVKIK--KEDATKAK-EQA--MALLD------------QVG---LKekadsfpssLSGGQQQR 144
Cdd:COG5265 438 -----PQDTVLFNDTIA-YNIAygRPDASEEEvEAAarAAQIHdfieslpdgydtRVGergLK---------LSGGEKQR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 145 VAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVV------VTHemgfakevADRVIFMADGVIQEEG 218
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIahrlstIVD--------ADEILVLEAGRIVERG 574
|
....
gi 498436323 219 TPEE 222
Cdd:COG5265 575 THAE 578
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
15-223 |
4.93e-35 |
|
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: 131.79 E-value: 4.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 15 EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNidQIRQKMGMVFQSFNLFPHmSV 94
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPA--WLRRQMGVVLQENVLFSR-SI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 95 LDNLTITPVKIKKEDATKAKEQAMALLDQVGLKE----KADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPE 170
Cdd:TIGR01846 548 RDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQgyntEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYE 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498436323 171 MVGEVLAVMQDLAkKGMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEEI 223
Cdd:TIGR01846 628 SEALIMRNMREIC-RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEEL 678
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-218 |
1.07e-34 |
|
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: 122.04 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNE--VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDsniDQIRQKM 79
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE---KALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFNLFphmsvldnltitpvkikkeDATkakeqamaLLDQVGLKekadsfpssLSGGQQQRVAIARALAMNPDVML 159
Cdd:cd03247 78 SVLNQRPYLF-------------------DTT--------LRNNLGRR---------FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 160 FDEPTSALDPEMVGEVLAVMQDLAkKGMTMVVVTHEMGfAKEVADRVIFMADGVIQEEG 218
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVL-KDKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-214 |
1.28e-34 |
|
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: 123.08 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 13 DNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSniDQIRQKMGMVFQSFNLFpHM 92
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDP--ADLRRNIGYVPQDVTLF-YG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 93 SVLDNLTITPVKIKKEDATKAKEQAmalldqvGLKEKADSFP-----------SSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:cd03245 93 TLRDNITLGAPLADDERILRAAELA-------GVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAkKGMTMVVVTHEMGFAkEVADRVIFMADGVI 214
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLL-DLVDRIIVMDSGRI 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-207 |
2.17e-34 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 121.57 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 10 SFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEG--------QNITAPDSNIDQIRQKMGM 81
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgarvayvpQRSEVPDSLPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 vfqsfNLFPHMSVLDNLTItpvkikkeDATKAKEQAmalLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:NF040873 81 -----GRWARRGLWRRLTR--------DDRAAVDDA---LERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEvADRVI 207
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCV 189
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-226 |
2.19e-34 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 123.27 E-value: 2.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSF----------------------GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEI 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 59 FFEGqNITAPdsnIDqirqkMGMVFQsfnlfPHMSVLDN---------LTitpvkikkedatkaKEQAMALLDQV----G 125
Cdd:COG1134 84 EVNG-RVSAL---LE-----LGAGFH-----PELTGRENiylngrllgLS--------------RKEIDEKFDEIvefaE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 126 LKEKADSfP-SSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVAD 204
Cdd:COG1134 136 LGDFIDQ-PvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCD 214
|
250 260
....*....|....*....|..
gi 498436323 205 RVIFMADGVIQEEGTPEEIFDH 226
Cdd:COG1134 215 RAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-236 |
2.27e-34 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 128.67 E-value: 2.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSF-----------GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTI-LRCLNLLeePTSGEIFFEGQnitaP 68
Cdd:PRK15134 275 LLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTgLALLRLI--NSQGEIWFDGQ----P 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 69 DSNIDQ-----IRQKMGMVFQSFN--LFPHMSVL----DNLTitpVKIKKEDATKAKEQAMALLDQVGLK-EKADSFPSS 136
Cdd:PRK15134 349 LHNLNRrqllpVRHRIQVVFQDPNssLNPRLNVLqiieEGLR---VHQPTLSAAQREQQVIAVMEEVGLDpETRHRYPAE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 137 LSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQ 215
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
250 260
....*....|....*....|.
gi 498436323 216 EEGTPEEIFDHPQNSRTQDFL 236
Cdd:PRK15134 506 EQGDCERVFAAPQQEYTRQLL 526
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-239 |
2.37e-34 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 129.59 E-value: 2.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 27 GEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNI-TAPDSNIDQIRQKMGMVFQS--FNLFPHMSVLDNLtITPV 103
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdTLSPGKLQALRRDIQFIFQDpyASLDPRQTVGDSI-MEPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 104 KIKK-EDATKAKEQAMALLDQVGLK-EKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQD 181
Cdd:PRK10261 429 RVHGlLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLD 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 182 LAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQDFLNKV 239
Cdd:PRK10261 509 LQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-214 |
2.47e-34 |
|
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: 122.76 E-value: 2.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 16 VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCL-NLLEEP--TSGEIFFEGQnitapDSNIDQIRQKMGMVFQSFNLFPHM 92
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGgtTSGQILFNGQ-----PRKPDQFQKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 93 SVLDNLTITPV---KIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDP 169
Cdd:cd03234 97 TVRETLTYTAIlrlPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498436323 170 EMVGEVLAVMQDLAKKGMTMVVVTHEMG---FakEVADRVIFMADGVI 214
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEI 222
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-233 |
3.10e-34 |
|
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: 128.71 E-value: 3.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 16 VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSniDQIRQKMGMVFQSFNLFPHmSVL 95
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR--EELGRHIGYLPQDVELFDG-TIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 96 DNltitpvkI---KKEDATKAKEQAMAlldqVGLKEKADSFP-----------SSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:COG4618 424 EN-------IarfGDADPEKVVAAAKL----AGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLD 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498436323 162 EPTSALDPEmvGE--VLAVMQDLAKKGMTMVVVTHEMGfAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQ 233
Cdd:COG4618 493 EPNSNLDDE--GEaaLAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVLARLARPAAA 563
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-227 |
3.83e-34 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 129.07 E-value: 3.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 13 DNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNItaPDSNIDQIRQKMGMVFQSFNLFPHm 92
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL--VQYDHHYLHRQVALVGQEPVLFSG- 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 93 SVLDNLTITPVKIKKEDATKAKEQAMA----LLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALD 168
Cdd:TIGR00958 570 SVRENIAYGLTDTPDEEIMAAAKAANAhdfiMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 169 PEMVGevlAVMQDLAKKGMTMVVVTHEMGFAkEVADRVIFMADGVIQEEGTPEEIFDHP 227
Cdd:TIGR00958 650 AECEQ---LLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-237 |
1.90e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 126.36 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSF----GDNEVLKSIDLEVKDGEVVVIIGPSGSGKS-TILRCLNLLEEP----TSGEIFFEGQNIT-APDS 70
Cdd:PRK15134 5 LLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLhASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 71 NIDQIR-QKMGMVFQSfnlfPhMSVLDNLTitpvKIKKEDAT-----------KAKEQAMALLDQVGLKEKA---DSFPS 135
Cdd:PRK15134 85 TLRGVRgNKIAMIFQE----P-MVSLNPLH----TLEKQLYEvlslhrgmrreAARGEILNCLDRVGIRQAAkrlTDYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 136 SLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVI 214
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
250 260
....*....|....*....|...
gi 498436323 215 QEEGTPEEIFDHPQNSRTQDFLN 237
Cdd:PRK15134 236 VEQNRAATLFSAPTHPYTQKLLN 258
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-239 |
3.41e-33 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 122.53 E-value: 3.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFG--DNEVLKSIDL--EVKDGEVVVIIGPSGSGKS-TILRCLNLLEEP--TSGEIFFEGQNI-TAPDSNI 72
Cdd:PRK09473 12 LLDVKDLRVTFStpDGDVTAVNDLnfSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREIlNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 73 DQIR-QKMGMVFQ----SFNlfPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGLKE---KADSFPSSLSGGQQQR 144
Cdd:PRK09473 92 NKLRaEQISMIFQdpmtSLN--PYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 145 VAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
250
....*....|....*.
gi 498436323 224 FDHPQNSRTQDFLNKV 239
Cdd:PRK09473 250 FYQPSHPYSIGLLNAV 265
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-240 |
6.41e-33 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 125.54 E-value: 6.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 15 EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEP---TSGEIFFEGQNITApdsniDQIRQKMGMVFQSFNLFPH 91
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDA-----KEMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 92 MSVLDNLTITP-VKIKKEDATKAKEQAM-ALLDQVGLKEKADS------FPSSLSGGQQQRVAIARALAMNPDVMLFDEP 163
Cdd:TIGR00955 114 LTVREHLMFQAhLRMPRRVTKKEKRERVdEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 164 TSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMG---FakEVADRVIFMADGVIQEEGTPEEIFDH--------PQNSRT 232
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSselF--ELFDKIILMAEGRVAYLGSPDQAVPFfsdlghpcPENYNP 271
|
....*...
gi 498436323 233 QDFLNKVL 240
Cdd:TIGR00955 272 ADFYVQVL 279
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-223 |
7.35e-33 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 125.07 E-value: 7.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKMGMVFQSFNLFpHMSVLD 96
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR--TVTRASLRRNIAVVFQDAGLF-NRSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 97 NLtitpvKIKKEDAT-----KAKEQAMALlDQV-----GLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSA 166
Cdd:PRK13657 428 NI-----RVGRPDATdeemrAAAERAQAH-DFIerkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498436323 167 LDPEMVGEVLAVMqDLAKKGMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEEI 223
Cdd:PRK13657 502 LDVETEAKVKAAL-DELMKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDEL 556
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-240 |
8.20e-33 |
|
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: 119.55 E-value: 8.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPD----SNIDQ-- 74
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELElyqlSEAERrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 75 -IRQKMGMVFQSF--NLFPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGL-KEKADSFPSSLSGGQQQRVAIARA 150
Cdd:TIGR02323 83 lMRTEWGFVHQNPrdGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 151 LAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQN 229
Cdd:TIGR02323 163 LVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQH 242
|
250
....*....|.
gi 498436323 230 SRTQDFLNKVL 240
Cdd:TIGR02323 243 PYTQLLVSSIL 253
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-215 |
1.37e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 123.64 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQnitapdsnidqirQKMGMVF 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-------------LRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 84 QSFNLFPHMSVLDNL-----TITPVKIKKEDATKAKE--------------------------QAMALLDQVGLKEKADS 132
Cdd:COG0488 68 QEPPLDDDLTVLDTVldgdaELRALEAELEELEAKLAepdedlerlaelqeefealggweaeaRAEEILSGLGFPEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 133 FP-SSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVgEVLAvmQDLAKKGMTMVVVTHEMGFAKEVADRVIFMAD 211
Cdd:COG0488 148 RPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESI-EWLE--EFLKNYPGTVLVVSHDRYFLDRVATRILELDR 224
|
....
gi 498436323 212 GVIQ 215
Cdd:COG0488 225 GKLT 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-221 |
2.85e-32 |
|
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: 116.47 E-value: 2.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCL--NLLEEPTSGEIFFEGQNITapDSNIDQiRQKMG- 80
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDIT--DLPPEE-RARLGi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 -MVFQSfnlfPhmsvldnLTITPVKIKKedatkakeqamaLLDQVGLkekadsfpsSLSGGQQQRVAIARALAMNPDVML 159
Cdd:cd03217 80 fLAFQY----P-------PEIPGVKNAD------------FLRYVNE---------GFSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498436323 160 FDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTH-EMGFAKEVADRVIFMADGVIQEEGTPE 221
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-223 |
3.39e-32 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 118.17 E-value: 3.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 5 KQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNidQIRQKMGMVFQ 84
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASK--EVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 85 SFNL--------------FPHMSVLdnltitpVKIKKEDAtKAKEQAMallDQVGLKEKADSFPSSLSGGQQQRVAIARA 150
Cdd:PRK10253 89 NATTpgditvqelvargrYPHQPLF-------TRWRKEDE-EAVTKAM---QATGITHLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498436323 151 LAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAK-KGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNReKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-231 |
6.52e-32 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 116.92 E-value: 6.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNiDQIRQKMGM 81
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH-ARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDNLtITPVKIKKE-DATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLF 160
Cdd:PRK10895 83 LPQEASIFRRLSVYDNL-MAVLQIRDDlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 161 DEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSR 231
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-218 |
1.01e-31 |
|
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: 115.96 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDsnidqiRQKMGMVF 83
Cdd:TIGR03740 3 TKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKD------LHKIGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 84 QSFNLFPHMSVLDNLTITPVKIKKEDATkakeqAMALLDQVGL----KEKADSFpsslSGGQQQRVAIARALAMNPDVML 159
Cdd:TIGR03740 77 ESPPLYENLTARENLKVHTTLLGLPDSR-----IDEVLNIVDLtntgKKKAKQF----SLGMKQRLGIAIALLNHPKLLI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 160 FDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEG 218
Cdd:TIGR03740 148 LDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQG 206
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-225 |
1.07e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 118.78 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITApdsNIDQIRQKMGM 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA---RARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDNLTITPVKIKKedATKAKEQAM-ALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLF 160
Cdd:PRK13536 119 VPQFDNLDLEFTVRENLLVFGRYFGM--STREIEAVIpSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498436323 161 DEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFD 225
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-212 |
2.40e-30 |
|
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: 111.79 E-value: 2.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 8 SKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLnLLE-EPTSGEIFFEGqnitapdsnidqirqKMGMVFQS- 85
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-LGElEKLSGSVSVPG---------------SIAYVSQEp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 86 --FNlfphMSVLDNLTITpvkiKKEDATKAKE-----------QAMALLDQVGLKEKAdsfpSSLSGGQQQRVAIARALA 152
Cdd:cd03250 76 wiQN----GTIRENILFG----KPFDEERYEKvikacalepdlEILPDGDLTEIGEKG----INLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498436323 153 MNPDVMLFDEPTSALDPEmVGEVLA--VMQDLAKKGMTMVVVTHEMGFAKEvADRVIFMADG 212
Cdd:cd03250 144 SDADIYLLDDPLSAVDAH-VGRHIFenCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-214 |
4.85e-30 |
|
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: 111.41 E-value: 4.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 13 DNEVLKSIDLEVKDGEVVVIIGPSGSGKSTilrCLNLLE---EPTSGEIFFEGQNITAPDSNIdqIRQKMGMVFQSFNLF 89
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKST---VVALLEnfyQPQGGQVLLDGKPISQYEHKY--LHSKVSLVGQEPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 90 PHmSVLDN----LTITPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTS 165
Cdd:cd03248 101 AR-SLQDNiaygLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 498436323 166 ALDPEMVGEVLAVMQDlAKKGMTMVVVTHEMGFAkEVADRVIFMADGVI 214
Cdd:cd03248 180 ALDAESEQQVQQALYD-WPERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-239 |
5.16e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 113.18 E-value: 5.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNIDQI---RQKMGMVFQ--SFNLFPH 91
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVkrlRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 92 mSVLDNLTITPVKIKkEDATKAKEQAMALLDQVGL-KEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPE 170
Cdd:PRK13645 107 -TIEKDIAFGPVNLG-ENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 171 MVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHpqnsrtQDFLNKV 239
Cdd:PRK13645 185 GEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN------QELLTKI 248
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-240 |
6.83e-30 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 111.94 E-value: 6.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPD----SNIDQ---IR 76
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalSEAERrrlLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 QKMGMVFQsfN----LFPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGL-KEKADSFPSSLSGGQQQRVAIARAL 151
Cdd:PRK11701 89 TEWGFVHQ--HprdgLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 152 AMNPDVMLFDEPTSALDPEMVGEVLAVMQDL-AKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNS 230
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHP 246
|
250
....*....|
gi 498436323 231 RTQDFLNKVL 240
Cdd:PRK11701 247 YTQLLVSSVL 256
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-219 |
7.41e-30 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 111.51 E-value: 7.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA-PDSNIdqIRQKM 79
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKI--MREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFNLFPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQvgLKEKADSFPSSLSGGQQQRVAIARALAMNPDVML 159
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 160 FDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGT 219
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-207 |
1.64e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 110.19 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 5 KQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITApdSNIDQIRQKMGMVFQ 84
Cdd:PRK10247 11 QNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST--LKPEIYRQQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 85 SFNLFPHmSVLDNLtITPVKIKKEdatKAKEQAM-ALLDQVGLKEKA-DSFPSSLSGGQQQRVAIARALAMNPDVMLFDE 162
Cdd:PRK10247 89 TPTLFGD-TVYDNL-IFPWQIRNQ---QPDPAIFlDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498436323 163 PTSALDPEMVGEVLAVMQDLAK-KGMTMVVVTHEmgfAKEV--ADRVI 207
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVReQNIAVLWVTHD---KDEInhADKVI 208
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
13-224 |
2.35e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.95 E-value: 2.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 13 DNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITApdSNIDQIRQKMGMVFQS-FNLFPH 91
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA--ENVWNLRRKIGMVFQNpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 92 MSVLDNLT--ITPVKIKKEDATKAKEQAMALLDQVGLKEKAdsfPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDP 169
Cdd:PRK13642 97 ATVEDDVAfgMENQGIPREEMIKRVDEALLAVNMLDFKTRE---PARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 170 EMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEEIF 224
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-226 |
2.78e-29 |
|
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: 114.75 E-value: 2.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 16 VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSniDQIRQKMGMVFQSFNLFPHmSVL 95
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDR--ETFGKHIGYLPQDVELFPG-TVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 96 DNltitpvkIKK--EDATKAKEQAMALLDQVglKEKADSFP-----------SSLSGGQQQRVAIARALAMNPDVMLFDE 162
Cdd:TIGR01842 410 EN-------IARfgENADPEKIIEAAKLAGV--HELILRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVLDE 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 163 PTSALDPEmvGE--VLAVMQDLAKKGMTMVVVTHEMGfAKEVADRVIFMADGVIQEEGTPEEIFDH 226
Cdd:TIGR01842 481 PNSNLDEE--GEqaLANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
2-228 |
3.08e-29 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 112.28 E-value: 3.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQlskSFGDNEVlkSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQ--NITAPDSNIDQIRQKM 79
Cdd:PRK11144 4 LNFKQ---QLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlFDAEKGICLPPEKRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFNLFPHMSVLDNLTitpVKIKKEDatkaKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVML 159
Cdd:PRK11144 79 GYVFQDARLFPHYKVRGNLR---YGMAKSM----VAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 160 FDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQ 228
Cdd:PRK11144 152 MDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-212 |
3.87e-29 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 113.87 E-value: 3.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 5 KQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEePT---SGEIFFEGQNITApdSNI-DQIRQKMG 80
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQA--SNIrDTERAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFPHMSVLDNL----TITPVKIKKEDATKAKeqAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPD 156
Cdd:PRK13549 86 IIHQELALVKELSVLENIflgnEITPGGIMDYDAMYLR--AQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 157 VMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-224 |
4.31e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 110.10 E-value: 4.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNIDQIRQKMG 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFPHMSVLDN---LTITPVKIKKEDATKAKEQAMALLDQVGLKEKAdsfPSSLSGGQQQRVAIARALAMNPDV 157
Cdd:PRK13638 81 TVFQDPEQQIFYTDIDSdiaFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQP---IQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498436323 158 MLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIF 224
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-214 |
9.29e-29 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 112.84 E-value: 9.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNIdqiRQKMG 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK---AHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 --MVFQSFNLFPHMSVLDNLTitpVKIKKEDATKAKEQAmaLLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVM 158
Cdd:PRK15439 88 iyLVPQEPLLFPNLSVKENIL---FGLPKRQASMQKMKQ--LLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 159 LFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVI 214
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-239 |
1.06e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 113.41 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNE----VLKSIDLEVKDGEVVVIIGPSGSGKS-TILRCLNLLEEpTSGEIFFEG--------QNITA 67
Cdd:PRK10261 12 VLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKmllrrrsrQVIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 68 PDSNIDQIRQ----KMGMVFQS--FNLFPHMSVLDNLTITPVKIKKEDATKAKEQAMALLDQVGLKEKA---DSFPSSLS 138
Cdd:PRK10261 91 SEQSAAQMRHvrgaDMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 139 GGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMADGVIQEE 217
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
|
250 260
....*....|....*....|..
gi 498436323 218 GTPEEIFDHPQNSRTQDFLNKV 239
Cdd:PRK10261 251 GSVEQIFHAPQHPYTRALLAAV 272
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-212 |
1.59e-28 |
|
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: 105.22 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIffegqnitapdsnidqirqkmgm 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 vfqsfnlfphmSVLDNLTItpvkikkedatkakeqamALLDQvglkekadsfpssLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:cd03221 58 -----------TWGSTVKI------------------GYFEQ-------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 498436323 162 EPTSALDPEMVgEVLAVMqdLAKKGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:cd03221 96 EPTNHLDLESI-EALEEA--LKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
13-236 |
8.13e-28 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 106.32 E-value: 8.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 13 DNEVLKSIDLEVKDGEVVVIIGPSGSGKStiLRCLNLLE------EPTSGEIFFEGQNITAPDsnidqIRQKM-GMVFQ- 84
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPVAPCA-----LRGRKiATIMQn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 85 ---SFNLFPHMSVLDNLTITPVKIKKEDATkakeqAMALLDQVGLKEKA---DSFPSSLSGGQQQRVAIARALAMNPDVM 158
Cdd:PRK10418 88 prsAFNPLHTMHTHARETCLALGKPADDAT-----LTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 159 LFDEPTSALDPEMVGEVLAVMQDL-AKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQDFL 236
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLV 241
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-223 |
9.34e-28 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 106.41 E-value: 9.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNI---------DQ 74
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfarkvaylpQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 75 IRQKMGMVFQ---SFNLFPHMSVLDnltitpvKIKKEDATKAkEQAMALldqVGLKEKADSFPSSLSGGQQQRVAIARAL 151
Cdd:PRK10575 94 LPAAEGMTVRelvAIGRYPWHGALG-------RFGAADREKV-EEAISL---VGLKPLAHRLVDSLSGGERQRAWIAMLV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498436323 152 AMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAK-KGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQeRGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-194 |
5.43e-27 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 103.03 E-value: 5.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPD--SNIDQIRQK 78
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvaEACHYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 79 MGMVfqsfnlfPHMSVLDNLTITpVKIKKEDATkakeQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVM 158
Cdd:PRK13539 82 NAMK-------PALTVAENLEFW-AAFLGGEEL----DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIW 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 498436323 159 LFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTH 194
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-225 |
6.15e-27 |
|
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: 108.67 E-value: 6.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDN-EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNItapdSNID--QIRQK 78
Cdd:TIGR01193 474 IVINDVSYSYGYGsNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL----KDIDrhTLRQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 79 MGMVFQSFNLFPHmSVLDNLTI-TPVKIKKEDATKAKEQAMALLD----QVGLKEKADSFPSSLSGGQQQRVAIARALAM 153
Cdd:TIGR01193 550 INYLPQEPYIFSG-SILENLLLgAKENVSQDEIWAACEIAEIKDDienmPLGYQTELSEEGSSISGGQKQRIALARALLT 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498436323 154 NPDVMLFDEPTSALDpeMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVaDRVIFMADGVIQEEGTPEEIFD 225
Cdd:TIGR01193 629 DSKVLILDESTSNLD--TITEKKIVNNLLNLQDKTIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLD 697
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-212 |
7.16e-27 |
|
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: 107.60 E-value: 7.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEE--PTSGEIFFEGQNITApdSNI-DQIRQ 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKA--SNIrDTERA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 78 KMGMVFQSFNLFPHMSVLDNL----TIT-PVKIKKEDATKAKeqAMALLDQVGLKEKADSFP-SSLSGGQQQRVAIARAL 151
Cdd:TIGR02633 79 GIVIIHQELTLVPELSVAENIflgnEITlPGGRMAYNAMYLR--AKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 152 AMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-226 |
8.91e-27 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 107.80 E-value: 8.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 13 DNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKMGMVFQSFNLFphm 92
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR--DYTLASLRNQVALVSQNVHLF--- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 93 svldNLTI-------TPVKIKKEDATKAKEQAMAL-----LDQvGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLF 160
Cdd:PRK11176 430 ----NDTIanniayaRTEQYSREQIEEAARMAYAMdfinkMDN-GLDTVIGENGVLLSGGQRQRIAIARALLRDSPILIL 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 161 DEPTSALDPEMVGEVLAVMQDLaKKGMTMVVVTHEMGfAKEVADRVIFMADGVIQEEGTPEEIFDH 226
Cdd:PRK11176 505 DEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
4-217 |
1.04e-26 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 102.73 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFG----DNE--VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEgqnitAPDSNIDQIRq 77
Cdd:COG2401 27 VAIVLEAFGvelrVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREA- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 78 kmgmvfqsfnlfphmSVLDNLtitpvkikkeDATKAKEQAMALLDQVGLkekADSF-----PSSLSGGQQQRVAIARALA 152
Cdd:COG2401 101 ---------------SLIDAI----------GRKGDFKDAVELLNAVGL---SDAVlwlrrFKELSTGQKFRFRLALLLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498436323 153 MNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVA-DRVIFMA-DGVIQEE 217
Cdd:COG2401 153 ERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATHHYDVIDDLQpDLLIFVGyGGVPEEK 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-220 |
1.29e-26 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 107.79 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSF--GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNItapDSNIDQIRQKMGM 81
Cdd:TIGR01257 931 VKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI---ETNLDAVRQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDNLTITpVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:TIGR01257 1008 CPQHNILFHHLTVAEHILFY-AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLaKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTP 220
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-220 |
1.87e-26 |
|
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: 101.80 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNE--VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDsnIDQIRQKM 79
Cdd:cd03244 3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG--LHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFNLFPHmSVLDNLtiTPVKIKKEdatkakEQAMALLDQVGLKEKADSFP-----------SSLSGGQQQRVAIA 148
Cdd:cd03244 81 SIIPQDPVLFSG-TIRSNL--DPFGEYSD------EELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 149 RALAMNPDVMLFDEPTSALDPemvgEVLAVMQDLAK---KGMTMVVVTHE----MGFakevaDRVIFMADGVIQEEGTP 220
Cdd:cd03244 152 RALLRKSKILVLDEATASVDP----ETDALIQKTIReafKDCTVLTIAHRldtiIDS-----DRILVLDKGRVVEFDSP 221
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-223 |
1.08e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 104.54 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTILrclNLLEE--PTSGEIFFEGQNITapDSNIDQIRQKMGMVFQSFNLFpHMSV 94
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLL---NALLGflPYQGSLKINGIELR--ELDPESWRKHLSWVGQNPQLP-HGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 95 LDNLTITpvkikKEDATKakEQAMALLDQVGLKEKADSFP-----------SSLSGGQQQRVAIARALAMNPDVMLFDEP 163
Cdd:PRK11174 440 RDNVLLG-----NPDASD--EQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498436323 164 TSALDpeMVGEVLaVMQDL--AKKGMTMVVVTHEMGFAKEVaDRVIFMADGVIQEEGTPEEI 223
Cdd:PRK11174 513 TASLD--AHSEQL-VMQALnaASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAEL 570
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-194 |
1.11e-25 |
|
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: 99.49 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQnitAPDSNIDQIRQKMGMVF 83
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG---PLDFQRDSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 84 QSFNLFPHMSVLDNLTItpvkIKKEDATKAKEQAmalLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEP 163
Cdd:cd03231 80 HAPGIKTTLSVLENLRF----WHADHSDEQVEEA---LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190
....*....|....*....|....*....|.
gi 498436323 164 TSALDPEMVGEVLAVMQDLAKKGMTMVVVTH 194
Cdd:cd03231 153 TTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-194 |
2.00e-25 |
|
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: 98.58 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGqniTAPDSNIDQIRQKMGMVF 83
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG---TPLAEQRDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 84 QSFNLFPHMSVLDNLTITpvkikKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEP 163
Cdd:TIGR01189 80 HLPGLKPELSALENLHFW-----AAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 498436323 164 TSALDPEMVGEVLAVMQDLAKKGMTMVVVTH 194
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-221 |
8.91e-25 |
|
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: 101.80 E-value: 8.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 20 IDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITApdSNIDQIRQKMGMVFQSFNLFPHMSVLDNLT 99
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA--DNREAYRQLFSAVFSDFHLFDRLLGLDGEA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 100 ITpvkikkedatkakEQAMALLDQVGLKEK----ADSFPS-SLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPE---- 170
Cdd:COG4615 429 DP-------------ARARELLERLELDHKvsveDGRFSTtDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrv 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 498436323 171 MVGEVLavmQDLAKKGMTMVVVTH-EMGFakEVADRVIFMADGVIQEEGTPE 221
Cdd:COG4615 496 FYTELL---PELKARGKTVIAISHdDRYF--DLADRVLKMDYGKLVELTGPA 542
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-212 |
1.82e-24 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 100.96 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVkqlSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNiDQIRQKMG 80
Cdd:PRK10982 1 MSNI---SKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSK-EALENGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFPHMSVLDNLTIT--PVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVM 158
Cdd:PRK10982 77 MVHQELNLVLQRSVMDNMWLGryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498436323 159 LFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-218 |
1.86e-24 |
|
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: 97.02 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSF---------------------GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFF 60
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 61 EGQnitAPDSNIDQIRQKMGMVF-QSFNLFPHMSVLDNLTITP--VKIKKEDATKAKEQAMALLDqvgLKEKADSFPSSL 137
Cdd:cd03267 81 AGL---VPWKRRKKFLRRIGVVFgQKTQLWWDLPVIDSFYLLAaiYDLPPARFKKRLDELSELLD---LEELLDTPVRQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 138 SGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDL-AKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQE 216
Cdd:cd03267 155 SLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
..
gi 498436323 217 EG 218
Cdd:cd03267 235 DG 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-218 |
2.34e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 96.45 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSF----------------------GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIF 59
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 60 FEGQnITAPdsnIDqirqkMGMVFQsfnlfPHMSVLDN----LTITPVKiKKEDATKAKEqamaLLDQVGLKEKADSFPS 135
Cdd:cd03220 81 VRGR-VSSL---LG-----LGGGFN-----PELTGRENiylnGRLLGLS-RKEIDEKIDE----IIEFSELGDFIDLPVK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 136 SLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQ 215
Cdd:cd03220 142 TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
...
gi 498436323 216 EEG 218
Cdd:cd03220 222 FDG 224
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
17-216 |
4.06e-24 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 100.05 E-value: 4.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITApdSNIDQIRQKMGMVFQSFNLFPHMsvld 96
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA--EQPEDYRKLFSAVFTDFHLFDQL---- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 97 nltitpvkIKKEDATKAKEQAMALLDQVGLKEK---ADSFPS--SLSGGQQQRVAIARALAMNPDVMLFDEPTSALDP-- 169
Cdd:PRK10522 413 --------LGPEGKPANPALVEKWLERLKMAHKlelEDGRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPhf 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 498436323 170 --EMVGEVLAVMQDlakKGMTMVVVTHEMGFAkEVADRVIFMADGVIQE 216
Cdd:PRK10522 485 rrEFYQVLLPLLQE---MGKTIFAISHDDHYF-IHADRLLEMRNGQLSE 529
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-223 |
5.16e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 99.72 E-value: 5.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLS-KSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPD---------SNID 73
Cdd:COG3845 260 VENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSprerrrlgvAYIP 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 74 QIRQKMGMVfqsfnlfPHMSVLDNLTITpvKIKKE--------DATKAKEQAMALLDQVGLK-EKADSFPSSLSGGQQQR 144
Cdd:COG3845 340 EDRLGRGLV-------PDMSVAENLILG--RYRRPpfsrggflDRKAIRAFAEELIEEFDVRtPGPDTPARSLSGGNQQK 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 145 VAIARALAMNPDVMLFDEPTSALDpemVGEVLAVMQ---DLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPE 221
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLD---VGAIEFIHQrllELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAA 487
|
..
gi 498436323 222 EI 223
Cdd:COG3845 488 EA 489
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-194 |
7.94e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 99.11 E-value: 7.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 16 VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFF-EGQNItapdsnidqirqkmgmvfqsfnLF----P 90
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV----------------------LFlpqrP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 91 HMSV--LDNLTITPvkikKEDATKAKEQAMALLDQVGLKEKADSF------PSSLSGGQQQRVAIARALAMNPDVMLFDE 162
Cdd:COG4178 436 YLPLgtLREALLYP----ATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190
....*....|....*....|....*....|..
gi 498436323 163 PTSALDPEMVGEVLAVMQDlAKKGMTMVVVTH 194
Cdd:COG4178 512 ATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-212 |
8.88e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 98.83 E-value: 8.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 8 SKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPdSNIDQIRQKMGMVFQSFN 87
Cdd:PRK11288 11 GKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFA-STTAALAAGVAIIYQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 88 LFPHMSVLDNLTI--TPVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTS 165
Cdd:PRK11288 90 LVPEMTVAENLYLgqLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498436323 166 ALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:PRK11288 170 SLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-223 |
6.33e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.39 E-value: 6.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 13 DNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITaPDSNIDQIRQKMGMVFQS---FNLF 89
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS-PRSPLDAVKKGMAYITESrrdNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 90 PHMSVLDNLTITP-VKIKKEDAT-----KAKEQAMALLDQVGLKEKADSFP---SSLSGGQQQRVAIARALAMNPDVMLF 160
Cdd:PRK09700 354 PNFSIAQNMAISRsLKDGGYKGAmglfhEVDEQRTAENQRELLALKCHSVNqniTELSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 161 DEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVI------QEEGTPEEI 223
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLtqiltnRDDMSEEEI 502
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
8-214 |
9.06e-23 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 96.49 E-value: 9.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 8 SKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCL--NLLEEPTSGEIFFEGQNITapdsniDQIRQKMGMVFQS 85
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALagRIQGNNFTGTILANNRKPT------KQILKRTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 86 FNLFPHMSVLDNLTIT-----PVKIKKEDATKAKEQAMAlldQVGLKE-----KADSFPSSLSGGQQQRVAIARALAMNP 155
Cdd:PLN03211 149 DILYPHLTVRETLVFCsllrlPKSLTKQEKILVAESVIS---ELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINP 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 156 DVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHemgfakEVADRVIFMADGVI 214
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH------QPSSRVYQMFDSVL 278
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-199 |
9.09e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 91.79 E-value: 9.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDsniDQIRQKMg 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR---DEYHQDL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 mvfqsfnLF--------PHMSVLDNLTITpvkikKEDATKAKEQAM-ALLDQVGLKEKADSFPSSLSGGQQQRVAIARAL 151
Cdd:PRK13538 77 -------LYlghqpgikTELTALENLRFY-----QRLHGPGDDEALwEALAQVGLAGFEDVPVRQLSAGQQRRVALARLW 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498436323 152 AMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGmTMVVVT--HEMGFA 199
Cdd:PRK13538 145 LTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQG-GMVILTthQDLPVA 193
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-223 |
1.02e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 95.75 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 20 IDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITaPDSNIDQIRQkmGMVF-----QSFNLFPHMSV 94
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID-IRSPRDAIRA--GIMLcpedrKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 95 LDNLTITpvkikkedATKAKEQAMALLDQVGLKEKADSF--------PS------SLSGGQQQRVAIARALAMNPDVMLF 160
Cdd:PRK11288 349 ADNINIS--------ARRHHLRAGCLINNRWEAENADRFirslniktPSreqlimNLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498436323 161 DEPTSALDpemVG---EVLAVMQDLAKKGMTMVVVTHE----MGfakeVADRVIFMADGVI-----QEEGTPEEI 223
Cdd:PRK11288 421 DEPTRGID---VGakhEIYNVIYELAAQGVAVLFVSSDlpevLG----VADRIVVMREGRIagelaREQATERQA 488
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-212 |
4.98e-22 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 94.09 E-value: 4.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 5 KQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEePT---SGEIFFEGQNITAPDsnidqIRQ--KM 79
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKD-----IRDseAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVF--QSFNLFPHMSVLDNLTIT--PVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNP 155
Cdd:NF040905 79 GIVIihQELALIPYLSIAENIFLGneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498436323 156 DVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-229 |
2.65e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 89.13 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTILRCL-NLLeePTSGEIFFEGQNITapDSNIDQIRQKMGMVFQSFNLFPHMSVL 95
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMaGLL--PGQGEILLNGRPLS--DWSAAELARHRAYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 96 DNLTITpvkIKKEDATKAKEQAMA-LLDQVGLKEKADSFPSSLSGGQQQRVAIARAL-----AMNPD--VMLFDEPTSAL 167
Cdd:COG4138 88 QYLALH---QPAGASSEAVEQLLAqLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498436323 168 DpemVGEVLAV---MQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDhPQN 229
Cdd:COG4138 165 D---VAQQAALdrlLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT-PEN 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-224 |
2.74e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 92.35 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 13 DNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLnlleeptsgeiffEGQNITAPDSNIDqIRQKMGMVFQSFNLFpHM 92
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM-------------LGELSHAETSSVV-IRGSVAYVPQVSWIF-NA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 93 SVLDNLTITPvKIKKEDATKAkeqamalLDQVGLKEKADSFPS-----------SLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:PLN03232 694 TVRENILFGS-DFESERYWRA-------IDVTALQHDLDLLPGrdlteigergvNISGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVaDRVIFMADGVIQEEGTPEEIF 224
Cdd:PLN03232 766 DPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS 827
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-232 |
3.86e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 89.76 E-value: 3.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSF-------GDNEVLKS--------------IDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIF 59
Cdd:COG4586 1 IIEVENLSKTYrvyekepGLKGALKGlfrreyreveavddISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 60 FEGQNitaPDSNIDQIRQKMGMVF-QSFNLFPHMSVLDNLTITPvKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLS 138
Cdd:COG4586 81 VLGYV---PFKRRKEFARRIGVVFgQRSQLWWDLPAIDSFRLLK-AIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 139 GGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDL-AKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEE 217
Cdd:COG4586 157 LGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYD 236
|
250
....*....|....*
gi 498436323 218 GTPEEIFDHPQNSRT 232
Cdd:COG4586 237 GSLEELKERFGPYKT 251
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
10-223 |
5.50e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 91.34 E-value: 5.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 10 SFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLnLLEEPTsgeifFEGQNITapdsnidqIRQKMGMVFQSFNLF 89
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM-LGELPP-----RSDASVV--------IRGTVAYVPQVSWIF 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 90 pHMSVLDNL----TITPVKIKKEDATKAKEQAMALL---DQVGLKEKAdsfpSSLSGGQQQRVAIARALAMNPDVMLFDE 162
Cdd:PLN03130 692 -NATVRDNIlfgsPFDPERYERAIDVTALQHDLDLLpggDLTEIGERG----VNISGGQKQRVSMARAVYSNSDVYIFDD 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 163 PTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVaDRVIFMADGVIQEEGTPEEI 223
Cdd:PLN03130 767 PLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEEL 826
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-207 |
6.58e-21 |
|
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: 87.85 E-value: 6.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 23 EVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNIT-APDsnidQIRQKMGMVFQSFnlfpHMSVLDNLTIT 101
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSyKPQ----YIKADYEGTVRDL----LSSITKDFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 102 PvKIKKEdatkakeqamaLLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPE---MVGEVLAV 178
Cdd:cd03237 93 P-YFKTE-----------IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlMASKVIRR 160
|
170 180
....*....|....*....|....*....
gi 498436323 179 MQDLAKKgmTMVVVTHEMGFAKEVADRVI 207
Cdd:cd03237 161 FAENNEK--TAFVVEHDIIMIDYLADRLI 187
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-228 |
1.13e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 87.48 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQnitapdsnidqirQKMG 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK-------------LRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFPHM--SVLDNLTITPvKIKKEDATKAKE--QAMALLDQVGLKekadsfpssLSGGQQQRVAIARALAMNPD 156
Cdd:PRK09544 71 YVPQKLYLDTTLplTVNRFLRLRP-GTKKEDILPALKrvQAGHLIDAPMQK---------LSGGETQRVLLARALLNRPQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498436323 157 VMLFDEPTSALDpeMVGEVlaVMQDLAKK-----GMTMVVVTHEMGFAKEVADRVIFMaDGVIQEEGTPEEIFDHPQ 228
Cdd:PRK09544 141 LLVLDEPTQGVD--VNGQV--ALYDLIDQlrrelDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPE 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-223 |
1.19e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 90.18 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITApdSNIDqIRQKMGM 81
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA--GDIA-TRRRVGY 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHMSVLDNLTI------TPvkikkedATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNP 155
Cdd:NF033858 344 MSQAFSLYGELTVRQNLELharlfhLP-------AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKP 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498436323 156 DVMLFDEPTSALDP---EMVGEVLAvmqDLAKK-GMTMVVVTHEMGFAkEVADRVIFMADGVIQEEGTPEEI 223
Cdd:NF033858 417 ELLILDEPTSGVDPvarDMFWRLLI---ELSREdGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAAL 484
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-225 |
1.93e-20 |
|
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: 90.00 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 12 GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDS---NIDQIRQKMgmvfqsfnL 88
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQawiQNDSLRENI--------L 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 89 FPHMSvldnltitpvkikKEDATKAKEQAMALL---------DQVGLKEKAdsfpSSLSGGQQQRVAIARALAMNPDVML 159
Cdd:TIGR00957 721 FGKAL-------------NEKYYQQVLEACALLpdleilpsgDRTEIGEKG----VNLSGGQKQRVSLARAVYSNADIYL 783
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 160 FDEPTSALDPEmVGE-----VLAVMQDLAKKgmTMVVVTHEMGFAKEVaDRVIFMADGVIQEEGTPEEIFD 225
Cdd:TIGR00957 784 FDDPLSAVDAH-VGKhifehVIGPEGVLKNK--TRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-237 |
2.25e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 88.04 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 16 VLKSIDLEVKDGEVVVIIGPSGSGKSTILRC-LNLLEEP---TSGEIFFEGQNITA--PDSNIDQIRQKMGMVFQ--SFN 87
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAiCGITKDNwhvTADRFRWNGIDLLKlsPRERRKIIGREIAMIFQepSSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 88 LFPHMSVLDNL--TITPVKIKK---EDATKAKEQAMALLDQVGLKEKAD---SFPSSLSGGQQQRVAIARALAMNPDVML 159
Cdd:COG4170 102 LDPSAKIGDQLieAIPSWTFKGkwwQRFKWRKKRAIELLHRVGIKDHKDimnSYPHELTEGECQKVMIAMAIANQPRLLI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 160 FDEPTSALDPEMVGEVLAVMQDLAK-KGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDHPQNSRTQDFLN 237
Cdd:COG4170 182 ADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKALLR 260
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
17-223 |
3.22e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 86.14 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTILRCL-NLLeePTSGEIFFEGQNITAPDSNiDQIRQKMGMVFQSFNLFpHMSVL 95
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMaGLL--PGSGSIQFAGQPLEAWSAA-ELARHRAYLSQQQTPPF-AMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 96 DNLTIT-PVKIKKEDATKAKEQamaLLDQVGLKEKADSFPSSLSGGQQQRVAIARAL-----AMNPD--VMLFDEPTSAL 167
Cdd:PRK03695 88 QYLTLHqPDKTRTEAVASALNE---VAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 168 DPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-220 |
3.42e-20 |
|
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: 85.16 E-value: 3.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDN--EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNItapdSNID--QIRQ 77
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI----STIPleDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 78 KMGMVFQSFNLFPHmSVLDNLTI----TPVKIKKedATKAKEQAmalldqvglkekadsfpSSLSGGQQQRVAIARALAM 153
Cdd:cd03369 83 SLTIIPQDPTLFSG-TIRSNLDPfdeySDEEIYG--ALRVSEGG-----------------LNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 154 NPDVMLFDEPTSALDPEMVGEVLAVMQDLAkKGMTMVVVTHEMGfakEVA--DRVIFMADGVIQEEGTP 220
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEF-TNSTILTIAHRLR---TIIdyDKILVMDAGEVKEYDHP 207
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
2-227 |
5.07e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 88.23 E-value: 5.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNItaPDSNIDQIRQKMGM 81
Cdd:PRK10789 316 VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL--TKLQLDSWRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFNLFPHmSVLDNltitpVKIKKEDATKAKEQAMALLDQV---------GLKEKADSFPSSLSGGQQQRVAIARALA 152
Cdd:PRK10789 394 VSQTPFLFSD-TVANN-----IALGRPDATQQEIEHVARLASVhddilrlpqGYDTEVGERGVMLSGGQKQRISIARALL 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498436323 153 MNPDVMLFDEPTSALDPEMVGEVLavmQDLAK--KGMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEEIFDHP 227
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEHQIL---HNLRQwgEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-194 |
2.45e-19 |
|
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: 81.82 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 16 VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIffegqnITAPDSNIDQIRQKmgmvfqsfnlfPHMSvl 95
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI------GMPEGEDLLFLPQR-----------PYLP-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 96 dnltitpvkikkeDATkakeqamaLLDQVglkekadSFPSS--LSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVG 173
Cdd:cd03223 77 -------------LGT--------LREQL-------IYPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|.
gi 498436323 174 EVLAVMQDLakkGMTMVVVTH 194
Cdd:cd03223 129 RLYQLLKEL---GITVISVGH 146
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-196 |
2.68e-19 |
|
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: 86.38 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 25 KDGEVVVIIGPSGSGKSTILRCLnlleeptSGEI---FfeGQNITAPDsnIDQIRQKmgmvFQSFNLFPHMSVLDNLTIT 101
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKIL-------SGELkpnL--GDYDEEPS--WDEVLKR----FRGTELQDYFKKLANGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 102 PV-KIK-------------KEDATKAKEQAMA--LLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTS 165
Cdd:COG1245 162 VAhKPQyvdlipkvfkgtvRELLEKVDERGKLdeLAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190
....*....|....*....|....*....|....
gi 498436323 166 ALDpemVGEVLAV---MQDLAKKGMTMVVVTHEM 196
Cdd:COG1245 242 YLD---IYQRLNVarlIRELAEEGKYVLVVEHDL 272
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-215 |
3.00e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 86.03 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 13 DNEVLKSID---LEVKDGEVVVIIGPSGSGKSTILRCL-NLLEEPTSGEIFFEGQNItAPDSNIDQIRQKMGMVFQS--- 85
Cdd:TIGR02633 269 INPHRKRVDdvsFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPV-DIRNPAQAIRAGIAMVPEDrkr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 86 FNLFPHMSVLDNLTITPVK----IKKEDATKAKEQAMALLDQVGLKEKADSFP-SSLSGGQQQRVAIARALAMNPDVMLF 160
Cdd:TIGR02633 348 HGIVPILGVGKNITLSVLKsfcfKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498436323 161 DEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQ 215
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
55-224 |
9.07e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 85.08 E-value: 9.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 55 SGEIFFEGQNITapDSNIDQIRQKMGMVFQSFNLFpHMSVLDNltitpVKIKKEDATK---AKEQAMALLDQV--GLKEK 129
Cdd:PTZ00265 1276 SGKILLDGVDIC--DYNLKDLRNLFSIVSQEPMLF-NMSIYEN-----IKFGKEDATRedvKRACKFAAIDEFieSLPNK 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 130 ADS----FPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDP---EMVGEVLAVMQDLAKKgmTMVVVTHEMGFAKEV 202
Cdd:PTZ00265 1348 YDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKADK--TIITIAHRIASIKRS 1425
|
170 180
....*....|....*....|....*.
gi 498436323 203 ADRVIF----MADGVIQEEGTPEEIF 224
Cdd:PTZ00265 1426 DKIVVFnnpdRTGSFVQAHGTHEELL 1451
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-224 |
1.19e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 84.38 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSF-GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNIdqIRQKMG 80
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV--LRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSfnlfPHM---SVLDNLTItpvkikKEDATKakEQAMALLDQVGLKEKADSFP-----------SSLSGGQQQRVA 146
Cdd:PRK10790 419 MVQQD----PVVladTFLANVTL------GRDISE--EQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 147 IARALAMNPDVMLFDEPTSALDPemvGEVLAVMQDLA--KKGMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEEIF 224
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDS---GTEQAIQQALAavREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-223 |
2.14e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.44 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 13 DNEVLKSID---LEVKDGEVVVIIGPSGSGKSTILRCL-NLLEEPTSGEIFFEGQNITAPDSNiDQIRQKMGMVFQS--- 85
Cdd:PRK13549 271 VNPHIKRVDdvsFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRNPQ-QAIAQGIAMVPEDrkr 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 86 FNLFPHMSVLDNLTITPVK--IKKEDATKAKEQAMALLDQVGLKEKADSfP----SSLSGGQQQRVAIARALAMNPDVML 159
Cdd:PRK13549 350 DGIVPVMGVGKNITLAALDrfTGGSRIDDAAELKTILESIQRLKVKTAS-PelaiARLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498436323 160 FDEPTSALDpemVG---EVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQ-----EEGTPEEI 223
Cdd:PRK13549 429 LDEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKgdlinHNLTQEQV 497
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-223 |
3.54e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.79 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 15 EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSnidQIRQKMGMVF-----QSFNLF 89
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST---AQRLARGLVYlpedrQSSGLY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 90 PHMSVLDN---LTITP----VKIKKEDATKAKEQAmalldQVGLK-EKADSFPSSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:PRK15439 354 LDAPLAWNvcaLTHNRrgfwIKPARENAVLERYRR-----ALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-212 |
4.24e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 82.74 E-value: 4.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNIDQiRQKMGMVF 83
Cdd:PRK10762 7 LKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQ-EAGIGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 84 QSFNLFPHMSVLDN--LTITPV-KIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLF 160
Cdd:PRK10762 86 QELNLIPQLTIAENifLGREFVnRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 498436323 161 DEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:PRK10762 166 DEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-221 |
6.85e-18 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 79.69 E-value: 6.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRClnLLEEP----TSGEIFFEGQNITAPDSnidQIR 76
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKV--IAGHPaykiLEGDILFKGESILDLEP---EER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 QKMGmVFQSFNlFPhmsvldnLTITPVkiKKED----ATKAKEQAMAL---------------LDQVGLKEkadSFPS-- 135
Cdd:CHL00131 82 AHLG-IFLAFQ-YP-------IEIPGV--SNADflrlAYNSKRKFQGLpeldplefleiinekLKLVGMDP---SFLSrn 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 136 ---SLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVA-DRVIFMAD 211
Cdd:CHL00131 148 vneGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKpDYVHVMQN 227
|
250
....*....|
gi 498436323 212 GVIQEEGTPE 221
Cdd:CHL00131 228 GKIIKTGDAE 237
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-212 |
8.87e-18 |
|
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: 78.91 E-value: 8.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTILrcLNLLEE--PTSGEIFFEGQNITAPDSNIDQIRQKMGMVFQSFN-LFPHMS 93
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLL--LAILGEmqTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKpWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 94 VLDNLTI-TPVKikkedatkaKEQAMALLDQVGLKEKADSFPS-----------SLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:cd03290 95 VEENITFgSPFN---------KQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498436323 162 EPTSALDPEMVGEVL--AVMQDLAKKGMTMVVVTHEMGFAKEvADRVIFMADG 212
Cdd:cd03290 166 DPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-196 |
1.16e-17 |
|
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: 79.33 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 24 VKDGEVVVIIGPSGSGKSTILRCL------NL---LEEPTSGEI--FFEG---QNITAP--DSNIDQIRQKmgmvfQSFN 87
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILagklkpNLgkfDDPPDWDEIldEFRGselQNYFTKllEGDVKVIVKP-----QYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 88 LFPHM---SVLDNLtitpvkiKKEDATKAKEQamaLLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPT 164
Cdd:cd03236 98 LIPKAvkgKVGELL-------KKKDERGKLDE---LVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|..
gi 498436323 165 SALDPEMVGEVLAVMQDLAKKGMTMVVVTHEM 196
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-196 |
5.15e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.47 E-value: 5.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 24 VKDGEVVVIIGPSGSGKSTILRCLnlleeptSGEI---FFEGQNITAPDSNIDQIRqkmGMVFQSfnlfpHMSVLDNLTI 100
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIL-------SGELipnLGDYEEEPSWDEVLKRFR---GTELQN-----YFKKLYNGEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 101 TPV-KI------------------KKEDATKAKEQamaLLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:PRK13409 161 KVVhKPqyvdlipkvfkgkvrellKKVDERGKLDE---VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*...
gi 498436323 162 EPTSALDpemVGEVLAV---MQDLAkKGMTMVVVTHEM 196
Cdd:PRK13409 238 EPTSYLD---IRQRLNVarlIRELA-EGKYVLVVEHDL 271
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-207 |
6.56e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 79.22 E-value: 6.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLN---LLEEptsGEIFFEgQNITAPDSNIDQIRQ 77
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLDD---GRIIYE-QDLIVARLQQDPPRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 78 KMGMVF---------QSFNLFPHMSVLDNLTITPvkikKEDATKAKEQAMALLDQVG--------------LKEKADSFP 134
Cdd:PRK11147 79 VEGTVYdfvaegieeQAEYLKRYHDISHLVETDP----SEKNLNELAKLQEQLDHHNlwqlenrinevlaqLGLDPDAAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498436323 135 SSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLakKGmTMVVVTHEMGFAKEVADRVI 207
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QG-SIIFISHDRSFIRNMATRIV 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-223 |
7.59e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 77.17 E-value: 7.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCL-NLLEEPT-------SGEIFFEGQNITAPDS-N 71
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAIDApR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 72 IDQIRQKMGMVFQ-----------SFNLFPHMSVLDNLTITPVKIKkedatkakEQAMALLDQVGLKEKAdsfPSSLSGG 140
Cdd:PRK13547 81 LARLRAVLPQAAQpafafsareivLLGRYPHARRAGALTHRDGEIA--------WQALALAGATALVGRD---VTTLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 141 QQQRVAIARALAM---------NPDVMLFDEPTSALDPEMVGEVLAVMQDLAKK-GMTMVVVTHEMGFAKEVADRVIFMA 210
Cdd:PRK13547 150 ELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLA 229
|
250
....*....|...
gi 498436323 211 DGVIQEEGTPEEI 223
Cdd:PRK13547 230 DGAIVAHGAPADV 242
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-224 |
1.31e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.85 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNIT-APDSNIDQIRQKMGMVFQSFNL------- 88
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqALQKNLVAYVPQSEEVDWSFPVlvedvvm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 89 ---FPHMSVLdnltitpvKIKKEDATKAKEQAMALLDQVGLKEKAdsfPSSLSGGQQQRVAIARALAMNPDVMLFDEPTS 165
Cdd:PRK15056 103 mgrYGHMGWL--------RRAKKRDRQIVTAALARVDMVEFRHRQ---IGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 166 ALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIfMADGVIQEEGTPEEIF 224
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTF 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
7-207 |
2.46e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.54 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 7 LSKSFGDNEvLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFE------GQNITA-PDSNIDQIRQKM 79
Cdd:PRK13409 346 LTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykPQYIKPdYDGTVEDLLRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSfnlfphmSVLDNLTITPVKIKKedatkakeqamaLLDQvGLKEkadsfpssLSGGQQQRVAIARALAMNPDVML 159
Cdd:PRK13409 425 TDDLGS-------SYYKSEIIKPLQLER------------LLDK-NVKD--------LSGGELQRVAIAACLSRDADLYL 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 498436323 160 FDEPTSALDPEMVGEVLAVMQDLA-KKGMTMVVVTHEMGFAKEVADRVI 207
Cdd:PRK13409 477 LDEPSAHLDVEQRLAVAKAIRRIAeEREATALVVDHDIYMIDYISDRLM 525
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-222 |
2.50e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 77.62 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEI-FFEGQNI--TAPDSNIDqirqkmg 80
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIgyYAQDHAYD------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 mvF-QSFNLFPHMSvldnltitpvKIKKEdatKAKEQAM-----ALL---DQVGLKEKadsfpsSLSGGQQQRVAIARAL 151
Cdd:PRK15064 395 --FeNDLTLFDWMS----------QWRQE---GDDEQAVrgtlgRLLfsqDDIKKSVK------VLSGGEKGRMLFGKLM 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498436323 152 AMNPDVMLFDEPTSALDPEMVgEVLAVMqdLAKKGMTMVVVTHEMGFAKEVADRVI-FMADGVIQEEGTPEE 222
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDMESI-ESLNMA--LEKYEGTLIFVSHDREFVSSLATRIIeITPDGVVDFSGTYEE 522
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
17-233 |
2.60e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 76.76 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSID---LEVKDGEVVVIIGPSGSGKSTILRCLNLLEEptsgeiffEGQNITAPDSNIDQI-------RQK-------M 79
Cdd:PRK15093 20 VKAVDrvsMTLTEGEIRGLVGESGSGKSLIAKAICGVTK--------DNWRVTADRMRFDDIdllrlspRERrklvghnV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSfnlfPHmSVLDnltitPVKIKKEDATKA-----------------KEQAMALLDQVGLKEKAD---SFPSSLSG 139
Cdd:PRK15093 92 SMIFQE----PQ-SCLD-----PSERVGRQLMQNipgwtykgrwwqrfgwrKRRAIELLHRVGIKDHKDamrSFPYELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 140 GQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAK-KGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEG 218
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
250
....*....|....*
gi 498436323 219 TPEEIFDHPQNSRTQ 233
Cdd:PRK15093 242 PSKELVTTPHHPYTQ 256
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
15-218 |
4.18e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 77.13 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 15 EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEgqnitapdsnidqirqkmgmvfQSFNLFPHMSV 94
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE----------------------RSIAYVPQQAW 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 95 LDNLTITP--VKIKKEDATKAKE-----QAMALLDQV--GLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTS 165
Cdd:PTZ00243 732 IMNATVRGniLFFDEEDAARLADavrvsQLEADLAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 166 ALDPEmVGEvlAVMQDL---AKKGMTMVVVTHEMGFAKEvADRVIFMADGVIQEEG 218
Cdd:PTZ00243 812 ALDAH-VGE--RVVEECflgALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSG 863
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-222 |
8.43e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.81 E-value: 8.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNevlksIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITaPDSNIDQIRQkmGM 81
Cdd:PRK10762 258 LKVDNLSGPGVND-----VSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV-TRSPQDGLAN--GI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 VFQSFN-----LFPHMSVLDNLTITPVK--IKKEDATKAKEQAMALLDQVGL----KEKADSFPSSLSGGQQQRVAIARA 150
Cdd:PRK10762 330 VYISEDrkrdgLVLGMSVKENMSLTALRyfSRAGGSLKHADEQQAVSDFIRLfnikTPSMEQAIGLLSGGNQQKVAIARG 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498436323 151 LAMNPDVMLFDEPTSALDpemVG---EVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEE 222
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQ 481
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-195 |
9.52e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.06 E-value: 9.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNItapDSNIDQIRQKMG 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI---KKDLCTYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFPHMSVLDNLTItpvkikkEDATKAKEQAMALLDQVGLKEKADSFPSS-LSGGQQQRVAIARALAMNPDVML 159
Cdd:PRK13540 78 FVGHRSGINPYLTLRENCLY-------DIHFSPGAVGITELCRLFSLEHLIDYPCGlLSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 498436323 160 FDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHE 195
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-194 |
1.01e-15 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 74.06 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLE--EPTSGEIFFEGQNITAPDSNiDQIRQK 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPE-DRAGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 79 MGMVFQSFNLFPHMS--VLDNLTITPVK-------IKKEDATKAKEQAMALLDQvglkeKADSFPSSL----SGGQQQRV 145
Cdd:PRK09580 80 IFMAFQYPVEIPGVSnqFFLQTALNAVRsyrgqepLDRFDFQDLMEEKIALLKM-----PEDLLTRSVnvgfSGGEKKRN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 498436323 146 AIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTH 194
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-203 |
1.34e-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: 75.36 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 5 KQLSKSFGDN-EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFfegqnitaPDSNIdqirqKMGMVF 83
Cdd:TIGR03719 8 NRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR--------PQPGI-----KVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 84 QSFNLFPHMSVLDNLTITPVKIKK--------------EDA---TKAKEQA--MALLDQVGLK------EKA-------- 130
Cdd:TIGR03719 75 QEPQLDPTKTVRENVEEGVAEIKDaldrfneisakyaePDAdfdKLAAEQAelQEIIDAADAWdldsqlEIAmdalrcpp 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498436323 131 -DSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLakKGmTMVVVTHEMGFAKEVA 203
Cdd:TIGR03719 155 wDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PG-TVVAVTHDRYFLDNVA 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
7-207 |
1.38e-15 |
|
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: 75.21 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 7 LSKSFGDNEvLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFE------GQNITaPDSNI---DQIRQ 77
Cdd:COG1245 347 LTKSYGGFS-LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykPQYIS-PDYDGtveEFLRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 78 KMGMVFQSfnlfphmSVLDNLTITPVKIKKedatkakeqamaLLDQvGLKEkadsfpssLSGGQQQRVAIARALAMNPDV 157
Cdd:COG1245 425 ANTDDFGS-------SYYKTEIIKPLGLEK------------LLDK-NVKD--------LSGGELQRVAIAACLSRDADL 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 498436323 158 MLFDEPTSALDPEMVGEVLAVMQDLA-KKGMTMVVVTHEMGFAKEVADRVI 207
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFAeNRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-223 |
1.41e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 75.82 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 24 VKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapdSNIDQIRQKMGMVfqsfnlfPHMSVLDNLTITP- 102
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---TNISDVHQNMGYC-------PQFDAIDDLLTGRe 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 103 -----VKIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLA 177
Cdd:TIGR01257 2032 hlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWN 2111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 498436323 178 VMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:TIGR01257 2112 TIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-223 |
1.41e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 75.15 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPDSNiDQIRQKMGMVFQ---SFNLFPHMS 93
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAN-EAINHGFALVTEerrSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 94 VLDNLTITPVKIKKE-----DATKAKEQAMALLDQVGLKEKADSFP-SSLSGGQQQRVAIARALAMNPDVMLFDEPTSAL 167
Cdd:PRK10982 343 IGFNSLISNIRNYKNkvgllDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 168 DPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADG-----VIQEEGTPEEI 223
Cdd:PRK10982 423 DVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGlvagiVDTKTTTQNEI 483
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
8-212 |
1.45e-15 |
|
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: 72.68 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 8 SKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPT---SGEIFFEGQNItapDSNIDQIRQKMGMVFQ 84
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY---KEFAEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 85 SFNLFPHMSVldnltitpvkikkedatkakEQamaLLDQVgLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPT 164
Cdd:cd03233 91 EDVHFPTLTV--------------------RE---TLDFA-LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498436323 165 SALDPEMVGEVLAVMQDLAK--KGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:cd03233 147 RGLDSSTALEILKCIRTMADvlKTTTFVSLYQASDEIYDLFDKVLVLYEG 196
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
7-231 |
2.68e-15 |
|
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: 71.45 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 7 LSKSFGDNEVLKSIDlEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapdsnidqirqkmgmvfqsf 86
Cdd:cd03222 6 CVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 87 nlfphmsvldnltITPVKIKkedatkakeqamalldqvglkekadsfpssLSGGQQQRVAIARALAMNPDVMLFDEPTSA 166
Cdd:cd03222 65 -------------YKPQYID------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAY 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 167 LDPEMVGEVLAVMQDLAKKGM-TMVVVTHEMGFAKEVADRVIfmadgVIQEEGTPEEIFDHPQNSR 231
Cdd:cd03222 102 LDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIH-----VFEGEPGVYGIASQPKGTR 162
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
13-168 |
4.80e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.91 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 13 DNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFF-EGQNITapDSNIDQIRQKMGMVFQSFNLFPH 91
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLK--DINLKWWRSKIGVVSQDPLLFSN 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 92 mSVLDNLTITPVKIK---------KEDATKAKEQA-----------------MALLDQVGLKEKADSF------------ 133
Cdd:PTZ00265 475 -SIKNNIKYSLYSLKdlealsnyyNEDGNDSQENKnkrnscrakcagdlndmSNTTDSNELIEMRKNYqtikdsevvdvs 553
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498436323 134 -----------------------PSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALD 168
Cdd:PTZ00265 554 kkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
7-194 |
4.85e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 71.42 E-value: 4.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 7 LSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQnitaPDSNIDQIRQkMGMVFQSF 86
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK----TATRGDRSRF-MAYLGHLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 87 NLFPHMSVLDNLTItpvkIKKEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSA 166
Cdd:PRK13543 92 GLKADLSTLENLHF----LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
170 180
....*....|....*....|....*...
gi 498436323 167 LDPEMVGEVLAVMQDLAKKGMTMVVVTH 194
Cdd:PRK13543 168 LDLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-223 |
5.02e-15 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 74.21 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 16 VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKMGMVFQSFNLFphmSVL 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA--KIGLHDLRFKITIIPQDPVLF---SGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 96 DNLTITPVkikkedATKAKEQAMALLDQVGLKEKADSFPS-----------SLSGGQQQRVAIARALAMNPDVMLFDEPT 164
Cdd:TIGR00957 1376 LRMNLDPF------SQYSDEEVWWALELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 165 SALDPEMVGEVLAVMQDLAKKgMTMVVVTHEMGFAKEVAdRVIFMADGVIQEEGTPEEI 223
Cdd:TIGR00957 1450 AAVDLETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-170 |
6.65e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 70.35 E-value: 6.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFeGQniTAPDSNIDQIRQkmgm 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GE--TVKLAYVDQSRD---- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 vfqsfNLFPHMSV-------LDNLTITPVKIkkedatkakeQAMALLDQVGLKeKADS--FPSSLSGGQQQRVAIARALA 152
Cdd:TIGR03719 396 -----ALDPNKTVweeisggLDIIKLGKREI----------PSRAYVGRFNFK-GSDQqkKVGQLSGGERNRVHLAKTLK 459
|
170
....*....|....*...
gi 498436323 153 MNPDVMLFDEPTSALDPE 170
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVE 477
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-219 |
1.01e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 69.38 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEePTSGEIFFEGQNITApdsNIDQIRQKMGM 81
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G-PDAGRRPWRF*TWCA---NRRALRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 -------VFQSF----NLFPHMSVLDnltitpvkIKKEDAtkaKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARA 150
Cdd:NF000106 90 hrpvr*gRRESFsgreNLYMIGR*LD--------LSRKDA---RARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAAS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498436323 151 LAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVA------DRVIFMADGVIQEEGT 219
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAheltviDRGRVIADGKVDELKT 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-240 |
1.03e-13 |
|
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: 70.32 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 16 VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPD-SNIDQIRQKMGMVFQ-SFNLFPHMS 93
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQtSWIMPGTIKDNIIFGlSYDEYRYTS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 94 VLDNLTItpvkikKEDATKAKEQAMALLDQVGLkekadsfpsSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVG 173
Cdd:TIGR01271 521 VIKACQL------EEDIALFPEKDKTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498436323 174 EVL--AVMQDLAKKgmTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTpeeiFDHPQNSRTqDFLNKVL 240
Cdd:TIGR01271 586 EIFesCLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEGVCYFYGT----FSELQAKRP-DFSSLLL 646
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-228 |
2.34e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.04 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 16 VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITApdSNIDQIRQKMGMVFQSFNLFPHmSVL 95
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGA--YGLRELRRQFSMIPQDPVLFDG-TVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 96 DNLtiTPVKikkeDATKAkeQAMALLDQVGLKEKADSFP-----------SSLSGGQQQRVAIARA-LAMNPDVMLFDEP 163
Cdd:PTZ00243 1402 QNV--DPFL----EASSA--EVWAALELVGLRERVASESegidsrvleggSNYSVGQRQLMCMARAlLKKGSGFILMDEA 1473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498436323 164 TSALDPEMVGEVLA-VMQdlAKKGMTMVVVTHEMgfaKEVA--DRVIFMADGVIQEEGTPEEIFDHPQ 228
Cdd:PTZ00243 1474 TANIDPALDRQIQAtVMS--AFSAYTVITIAHRL---HTVAqyDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-240 |
5.11e-13 |
|
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: 66.80 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 14 NEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITAPD-SNIDQIRQKMGMVFQ-SFNLFPH 91
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQfSWIMPGTIKENIIFGvSYDEYRY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 92 MSVLDNLTItpvkikKEDATKAKEQAMALLDQVGLkekadsfpsSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEM 171
Cdd:cd03291 130 KSVVKACQL------EEDITKFPEKDNTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 172 VGEVL--AVMQDLAKKgmTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTpeeiFDHPQNSRTqDFLNKVL 240
Cdd:cd03291 195 EKEIFesCVCKLMANK--TRILVTSKMEHLKK-ADKILILHEGSSYFYGT----FSELQSLRP-DFSSKLM 257
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-194 |
5.62e-13 |
|
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: 67.85 E-value: 5.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 14 NEVL-KSIDLEVKDGEVVVIIGPSGSGKSTILRCLN--------LLEEPTSGEIFFEGQ-----------NITAPDSNID 73
Cdd:TIGR00954 464 GDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFYVPQrpymtlgtlrdQIIYPDSSED 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 74 QIRQkmGMVFQSFnlfphMSVLDNLTITPVkikkedatkakeqamaLLDQVGLKEKADsFPSSLSGGQQQRVAIARALAM 153
Cdd:TIGR00954 544 MKRR--GLSDKDL-----EQILDNVQLTHI----------------LEREGGWSAVQD-WMDVLSGGEKQRIAMARLFYH 599
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 498436323 154 NPDVMLFDEPTSALDPEMVGevlAVMQDLAKKGMTMVVVTH 194
Cdd:TIGR00954 600 KPQFAILDECTSAVSVDVEG---YMYRLCREFGITLFSVSH 637
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
17-220 |
8.60e-13 |
|
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: 65.71 E-value: 8.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTIL---------RCLNLLEEPTSGEIFFEG-QNIT------------APDSN--- 71
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHLKKEQPGNHDRIEGlEHIDkvividqspigrTPRSNpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 72 ----IDQIRQKMGMVFQS--FN------LFPHMSVLDNLTITPVKIKK--EDATKAKEQaMALLDQVGLKEKADSFPSS- 136
Cdd:cd03271 91 ytgvFDEIRELFCEVCKGkrYNretlevRYKGKSIADVLDMTVEEALEffENIPKIARK-LQTLCDVGLGYIKLGQPATt 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 137 LSGGQQQRVAIARALAM---NPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKeVADRVIFM---- 209
Cdd:cd03271 170 LSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK-CADWIIDLgpeg 248
|
250
....*....|...
gi 498436323 210 --ADGVIQEEGTP 220
Cdd:cd03271 249 gdGGGQVVASGTP 261
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-169 |
1.66e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.19 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 10 SFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCL---------NLL----EEPTSGEiffegqnitapdsNIDQIR 76
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysNDLtlfgRRRGSGE-------------TIWDIK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 QKMGMVFQSFnlfpHMSVLDNLTITPV-------KIKKEDATKAKEQ--AMALLDQVGL-KEKADSFPSSLSGGQQQRVA 146
Cdd:PRK10938 336 KHIGYVSSSL----HLDYRVSTSVRNVilsgffdSIGIYQAVSDRQQklAQQWLDILGIdKRTADAPFHSLSWGQQRLAL 411
|
170 180
....*....|....*....|...
gi 498436323 147 IARALAMNPDVMLFDEPTSALDP 169
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDP 434
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-212 |
2.11e-12 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 63.50 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTIlrCLNLLEEptSGEIFFEGQNITAPDSNIDQIRQkmgmvfqsfnlfphMSVLD 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYA--SGKARLISFLPKFSRNKLIFIDQ--------------LQFLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 97 NLTITPVKIkkedatkakEQAMalldqvglkekadsfpSSLSGGQQQRVAIARALAMNPD--VMLFDEPTSALDPEMVGE 174
Cdd:cd03238 73 DVGLGYLTL---------GQKL----------------STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQ 127
|
170 180 190
....*....|....*....|....*....|....*...
gi 498436323 175 VLAVMQDLAKKGMTMVVVTHEMGFAKEvADRVIFMADG 212
Cdd:cd03238 128 LLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPG 164
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-181 |
3.31e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.53 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 5 KQLSKSFGDN-EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFegqnitAPDSNIdqirqkmGMVF 83
Cdd:PRK11819 10 NRVSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP------APGIKV-------GYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 84 QSFNLFPHMSVLDNLT--ITPVKIKKE----------------DATkAKEQA--MALLDQVGLK------EKA------- 130
Cdd:PRK11819 77 QEPQLDPEKTVRENVEegVAEVKAALDrfneiyaayaepdadfDAL-AAEQGelQEIIDAADAWdldsqlEIAmdalrcp 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498436323 131 --DSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMV-----------GEVLAVMQD 181
Cdd:PRK11819 156 pwDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVawleqflhdypGTVVAVTHD 219
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-208 |
4.09e-12 |
|
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: 62.01 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 27 GEVVVIIGPSGSGKSTILRCL-NLLEEPTSGEIFFEGQNItapdsnidqirqkmgmvfqsfnlfphmsvldnltitpvki 105
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDI---------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 106 kkedatkakeqaMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPEMVGEVLA------VM 179
Cdd:smart00382 42 ------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLL 109
|
170 180
....*....|....*....|....*....
gi 498436323 180 QDLAKKGMTMVVVTHEMGFAKEVADRVIF 208
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-223 |
1.28e-11 |
|
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: 63.88 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 136 SLSGGQQQRVAIARAL---AMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKeVADRVIFM--- 209
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIK-TADYIIDLgpe 907
|
90
....*....|....*..
gi 498436323 210 ---ADGVIQEEGTPEEI 223
Cdd:TIGR00630 908 ggdGGGTVVASGTPEEV 924
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-212 |
1.48e-11 |
|
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: 61.49 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKsfgdnEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEP--TSGEIFFEGQNITapdsniDQIRQKM 79
Cdd:cd03232 13 VPVKGGKR-----QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLD------KNFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFNLFPHMSVLDNLTITpvkikkedatkakeqamALLdqvglkekadsfpSSLSGGQQQRVAIARALAMNPDVML 159
Cdd:cd03232 82 GYVEQQDVHSPNLTVREALRFS-----------------ALL-------------RGLSVEQRKRLTIGVELAAKPSILF 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 160 FDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMG---FakEVADRVIFMADG 212
Cdd:cd03232 132 LDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSasiF--EKFDRLLLLKRG 185
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-212 |
1.76e-11 |
|
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: 61.89 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTIlrclnlleepTSGEIFFEGQ----------------NITAPD-SNID------ 73
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL----------AFDTIYAEGQrryveslsayarqflgQMDKPDvDSIEglspai 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 74 QIRQKmgmvfqSFNLFPHMSVLdnlTITPV--KIKKEDATKAKEQAMALLDQVGLKE-KADSFPSSLSGGQQQRVAIARA 150
Cdd:cd03270 81 AIDQK------TTSRNPRSTVG---TVTEIydYLRLLFARVGIRERLGFLVDVGLGYlTLSRSAPTLSGGEAQRIRLATQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498436323 151 LAMNPDVML--FDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEvADRVIFMADG 212
Cdd:cd03270 152 IGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVIDIGPG 214
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
9-207 |
1.85e-11 |
|
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: 61.47 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 9 KSFGDNEVlksIDLevkDGEVVVIIGPSGSGKSTILRCLNLleePTSGEiffegqniTAPDSNIDQIRQKMGMVfqsfnl 88
Cdd:cd03240 10 RSFHERSE---IEF---FSPLTLIVGQNGAGKTTIIEALKY---ALTGE--------LPPNSKGGAHDPKLIRE------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 89 fphmsvldNLTITPVKIKKEDATKAK---EQAMALLDQVGLKEKADSF------PSSLSGGQQQ------RVAIARALAM 153
Cdd:cd03240 67 --------GEVRAQVKLAFENANGKKytiTRSLAILENVIFCHQGESNwplldmRGRCSGGEKVlasliiRLALAETFGS 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 154 NPDVMLFDEPTSALDPEMVGEVLAVMQDLAK--KGMTMVVVTHEMGFaKEVADRVI 207
Cdd:cd03240 139 NCGILALDEPTTNLDEENIEESLAEIIEERKsqKNFQLIVITHDEEL-VDAADHIY 193
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-224 |
2.06e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 16 VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITapDSNIDQIRQKMGMVFQSFNLFphmSVL 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA--KFGLTDLRRVLSIIPQSPVLF---SGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 96 DNLTITPVKIKKE-DATKAKEQAMaLLDQV-----GLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDP 169
Cdd:PLN03232 1326 VRFNIDPFSEHNDaDLWEALERAH-IKDVIdrnpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDV 1404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498436323 170 EMVGEVLAVMQDlAKKGMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEEIF 224
Cdd:PLN03232 1405 RTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELL 1457
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-223 |
2.11e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.22 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 16 VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITApdSNIDQIRQKMGMVFQSFNLFPHmSVL 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISK--FGLMDLRKVLGIIPQAPVLFSG-TVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 96 DNLTitPVKIKKE-DATKAKEQAMaLLDQV-----GLKEKADSFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDp 169
Cdd:PLN03130 1331 FNLD--PFNEHNDaDLWESLERAH-LKDVIrrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD- 1406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498436323 170 emVGeVLAVMQDLAK---KGMTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEEI 223
Cdd:PLN03130 1407 --VR-TDALIQKTIReefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENL 1459
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-169 |
2.41e-11 |
|
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: 63.01 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSF--GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRC-LNLLEepTSGEIFFEGqnITAPDSNIDQIRQK 78
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAlLRLLS--TEGEIQIDG--VSWNSVTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 79 MGMVFQSF---------NLFPHMSVLDnltitpvkikkedatkakEQAMALLDQVGLKEKADSFPSSL-----------S 138
Cdd:TIGR01271 1294 FGVIPQKVfifsgtfrkNLDPYEQWSD------------------EEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlS 1355
|
170 180 190
....*....|....*....|....*....|.
gi 498436323 139 GGQQQRVAIARALAMNPDVMLFDEPTSALDP 169
Cdd:TIGR01271 1356 NGHKQLMCLARSILSKAKILLLDEPSAHLDP 1386
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-170 |
3.01e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.44 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFeGQniTAPDSNIDQIRQkmgm 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE--TVKLAYVDQSRD---- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 82 vfqsfNLFPHMSV-------LDNLTITpvkiKKEDATKA-------KEQamallDQ---VGLkekadsfpssLSGGQQQR 144
Cdd:PRK11819 398 -----ALDPNKTVweeisggLDIIKVG----NREIPSRAyvgrfnfKGG-----DQqkkVGV----------LSGGERNR 453
|
170 180
....*....|....*....|....*.
gi 498436323 145 VAIARALAMNPDVMLFDEPTSALDPE 170
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-169 |
1.37e-10 |
|
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: 59.87 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSF--GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRC-LNLLEepTSGEIFFEGQNITApdSNIDQIRQK 78
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAfLRLLN--TEGDIQIDGVSWNS--VPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 79 MGMVFQSFNLFPHmSVLDNLtitpvkikKEDATKAKEQAMALLDQVGLKEKADSFPSS-----------LSGGQQQRVAI 147
Cdd:cd03289 79 FGVIPQKVFIFSG-TFRKNL--------DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCL 149
|
170 180
....*....|....*....|..
gi 498436323 148 ARALAMNPDVMLFDEPTSALDP 169
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDP 171
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
12-212 |
1.58e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.51 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 12 GDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNllEEPTSGEIffEGQNITAPDSNIDQIRQK-MGMVFQSFNLFP 90
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVI--TGGDRLVNGRPLDSSFQRsIGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 91 HMSVLDNLTIT-----PVKIKKEDATKAKEQAMALLDQVGLKEKADSFPSS-LSGGQQQRVAIARALAMNPDVMLF-DEP 163
Cdd:TIGR00956 850 TSTVRESLRFSaylrqPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLFlDEP 929
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 498436323 164 TSALDPEMVGEVLAVMQDLAKKGMTMVVVTHE---MGFAKevADRVIFMADG 212
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsaILFEE--FDRLLLLQKG 979
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-223 |
2.17e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITApdSNIDQIRQKMG 80
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITR--LSFEQLQKLVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFN---LFPHMsvlDNLTITPVKIKkEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDV 157
Cdd:PRK10938 81 DEWQRNNtdmLSPGE---DDTGRTTAEII-QDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498436323 158 MLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEI 223
Cdd:PRK10938 157 LILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
136-223 |
2.37e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.80 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 136 SLSGGQQQRVAIARALAMNPDVMLFDEPTSALDpemVG---EVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEG 480
|
90
....*....|....*.
gi 498436323 213 VI-----QEEGTPEEI 223
Cdd:NF040905 481 RItgelpREEASQERI 496
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-239 |
3.03e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 16 VLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNL----LEEPTSGEIFFEGqniTAPDsniDQIRQKMGMVF---QSFNL 88
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDG---ITPE---EIKKHYRGDVVynaETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 89 FPHMSVLDNLTI-----TPVK-----IKKEDATKAKEQAMALLdqvGLKEKADS-----FPSSLSGGQQQRVAIARALAM 153
Cdd:TIGR00956 150 FPHLTVGETLDFaarckTPQNrpdgvSREEYAKHIADVYMATY---GLSHTRNTkvgndFVRGVSGGERKRVSIAEASLG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 154 NPDVMLFDEPTSALDPEMVGEVLAVMQdlakkgmTMVVVTHEMGF---------AKEVADRVIFMADGVIQEEGTPEEI- 223
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSATALEFIRALK-------TSANILDTTPLvaiyqcsqdAYELFDKVIVLYEGYQIYFGPADKAk 299
|
250 260
....*....|....*....|...
gi 498436323 224 -------FDHPQNSRTQDFLNKV 239
Cdd:TIGR00956 300 qyfekmgFKCPDRQTTADFLTSL 322
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
4-226 |
4.22e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.13 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNE---VLKSIDLEVKDGEVVVIIGPSGSGKSTIlrcLNLLeeptsgeiffegQNITAPDSNIDQIRQKMG 80
Cdd:PRK13545 24 LKDLFFRSKDGEyhyALNNISFEVPEGEIVGIIGLNGSGKSTL---SNLI------------AGVTMPNKGTVDIKGSAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFPHMSVLDNLTITPVK--IKKEdatKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVM 158
Cdd:PRK13545 89 LIAISSGLNGQLTGIENIELKGLMmgLTKE---KIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498436323 159 LFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDH 226
Cdd:PRK13545 166 VIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-170 |
8.74e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 56.42 E-value: 8.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFgDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEgqnitapDSNIDQIRQK-M 79
Cdd:PRK13541 1 MLSLHQLQFNI-EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYK-------NCNINNIAKPyC 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 80 GMVFQSFNLFPHMSVLDNLTITpvkikkEDATKAKEQAMALLDQVGLKEKADSFPSSLSGGQQQRVAIARALAMNPDVML 159
Cdd:PRK13541 73 TYIGHNLGLKLEMTVFENLKFW------SEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWL 146
|
170
....*....|.
gi 498436323 160 FDEPTSALDPE 170
Cdd:PRK13541 147 LDEVETNLSKE 157
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-195 |
1.30e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.93 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 15 EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLnlLEEPTSGEIffEGQ-NITAPDSNIDQIRQKMGMVFQSFNLFPHMS 93
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVL--AGRKTGGYI--EGDiRISGFPKKQETFARISGYCEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 94 VLDNLTIT-----PVKIKKEDATKAKEQAMALLDQVGLKEKADSFP--SSLSGGQQQRVAIARALAMNPDVMLFDEPTSA 166
Cdd:PLN03140 970 VRESLIYSaflrlPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180
....*....|....*....|....*....
gi 498436323 167 LDPEMVGEVLAVMQDLAKKGMTMVVVTHE 195
Cdd:PLN03140 1050 LDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
135-240 |
1.61e-09 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 57.73 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 135 SSLSGGQQQRVAIARALAM---NPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKeVADRVIfmaD 211
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVIK-TADWII---D 900
|
90 100 110
....*....|....*....|....*....|....*...
gi 498436323 212 ---------GVIQEEGTPEEIFDHPqNSRTQDFLNKVL 240
Cdd:COG0178 901 lgpeggdggGEIVAEGTPEEVAKVK-ASYTGRYLKEYL 937
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
137-240 |
1.68e-09 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 57.39 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 137 LSGGQQQRVAIARALAMNPD---VMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKeVADRVIfmaD-- 211
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVIK-TADWII---Dlg 906
|
90 100 110
....*....|....*....|....*....|....*.
gi 498436323 212 -------GVIQEEGTPEEIFDHPqNSRTQDFLNKVL 240
Cdd:PRK00349 907 peggdggGEIVATGTPEEVAKVE-ASYTGRYLKPVL 941
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
9-194 |
1.94e-09 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 55.79 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 9 KSFGDNEVlksIDLevkDGEVVVIIGPSGSGKSTILRCLNLL-------------------EEPTSGEIFFEGQN----I 65
Cdd:COG0419 11 RSYRDTET---IDF---DDGLNLIVGPNGAGKSTILEAIRYAlygkarsrsklrsdlinvgSEEASVELEFEHGGkryrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 66 TAPDSNIDQI-----RQKMGMVFQSFNLfphmSVLDNLtITPVKIKKEDATKAKEQAMAL--LDQVGLKEKADSFP-SSL 137
Cdd:COG0419 85 ERRQGEFAEFleakpSERKEALKRLLGL----EIYEEL-KERLKELEEALESALEELAELqkLKQEILAQLSGLDPiETL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498436323 138 SGGQQQRVAIARALAmnpdvMLFDepTSALDPEMVGEVLAVMQDLAkkgmtmvVVTH 194
Cdd:COG0419 160 SGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-226 |
3.55e-09 |
|
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: 55.69 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 2 INVKQLSKSFGDN--EVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQNITA-PdsnIDQIRQK 78
Cdd:cd03288 20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlP---LHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 79 MGMVFQS---------FNLFPHMSVLDNLTITPVKIkkedaTKAKEQAMAL---LDQVgLKEKADSFpsslSGGQQQRVA 146
Cdd:cd03288 97 LSIILQDpilfsgsirFNLDPECKCTDDRLWEALEI-----AQLKNMVKSLpggLDAV-VTEGGENF----SVGQRQLFC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 147 IARALAMNPDVMLFDEPTSALDpeMVGEVL---AVMQDLAKKgmTMVVVTHEMGFAKEvADRVIFMADGVIQEEGTPEEI 223
Cdd:cd03288 167 LARAFVRKSSILIMDEATASID--MATENIlqkVVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENL 241
|
...
gi 498436323 224 FDH 226
Cdd:cd03288 242 LAQ 244
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-209 |
1.11e-08 |
|
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: 54.62 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGeVVVIIGPSGSGKSTILRCLNLLEEPTSG-----EIFFEGQNITAPD---------------------- 69
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSrkfdeEDFYLGDDPDLPEieieltfgsllsrllrlllkee 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 70 ------SNIDQIRQKMGMVFQSFN-----LFPHMSVLDNLTITPVKIKKEDatkakeqamaLLDQVGLK-EKADSFPSSL 137
Cdd:COG3593 93 dkeeleEALEELNEELKEALKALNellseYLKELLDGLDLELELSLDELED----------LLKSLSLRiEDGKELPLDR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 138 SG-GQQQRVAIARALAM-------NPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEV-ADRVIF 208
Cdd:COG3593 163 LGsGFQRLILLALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVpLENIRR 242
|
.
gi 498436323 209 M 209
Cdd:COG3593 243 L 243
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-209 |
2.34e-08 |
|
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: 51.98 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 26 DGEVVVIIGPSGSGKSTILRCLNLLEeptsgeiffegqnitapdsnidqirqkmgmVFQSFNLFPHMSVLDNLTITPVKI 105
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIGLAL------------------------------GGAQSATRRRSGVKAGCIVAAVSA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 106 kkedatkakeQAMALLDQvglkekadsfpssLSGGQQQRVAIARALA---MNPDVM-LFDEPTSALDPEMVGEVLAVMQD 181
Cdd:cd03227 70 ----------ELIFTRLQ-------------LSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAEAILE 126
|
170 180
....*....|....*....|....*...
gi 498436323 182 LAKKGMTMVVVTHEMGFAkEVADRVIFM 209
Cdd:cd03227 127 HLVKGAQVIVITHLPELA-ELADKLIHI 153
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-190 |
3.23e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.71 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 20 IDLEVKdgevVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGqnitapdsnidqiRQKMGMVFQSfnlfpHMSVLDnLT 99
Cdd:PLN03073 532 IDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVFRSA-------------KVRMAVFSQH-----HVDGLD-LS 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 100 ITPVKIKKEDATKAKEQAM-ALLDQVGLKEKADSFPS-SLSGGQQQRVAIARALAMNPDVMLFDEPTSALDpemVGEVLA 177
Cdd:PLN03073 589 SNPLLYMMRCFPGVPEQKLrAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD---LDAVEA 665
|
170
....*....|....*
gi 498436323 178 VMQDLA--KKGMTMV 190
Cdd:PLN03073 666 LIQGLVlfQGGVLMV 680
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-238 |
5.33e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 53.29 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 135 SSLSGGQQQRVAIARAL---AMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKeVADRVIFMA- 210
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYVLELGp 886
|
90 100 110
....*....|....*....|....*....|....*
gi 498436323 211 -----DGVIQEEGTPEEIF--DHPQNSRTQDFLNK 238
Cdd:PRK00635 887 eggnlGGYLLASCSPEELIhlHTPTAKALRPYLSS 921
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-223 |
5.48e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.82 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILrclNLLeeptSG-EIFFEGQnITAPDSNIDQIR------ 76
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL---SLI----AGaRKIQQGR-VEVLGGDMADARhrravc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 77 -------QKMGMvfqsfNLFPHMSVLDNLtitpvkikkE--------DATKAKEQAMALLDQVGLkekaDSFPS----SL 137
Cdd:NF033858 76 priaympQGLGK-----NLYPTLSVFENL---------DffgrlfgqDAAERRRRIDELLRATGL----APFADrpagKL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 138 SGGQQQRVAIARALAMNPDVMLFDEPTSALDP-------EMVGEVLAvmqdlAKKGMTMVVVTHEMgfakEVADR---VI 207
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPlsrrqfwELIDRIRA-----ERPGMSVLVATAYM----EEAERfdwLV 208
|
250
....*....|....*.
gi 498436323 208 FMADGVIQEEGTPEEI 223
Cdd:NF033858 209 AMDAGRVLATGTPAEL 224
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
109-209 |
8.89e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 109 DATKAKEQAMALLdqVGLKEKAD---SFPSSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDpemVGEVLAVMQDLAKK 185
Cdd:PLN03073 316 DAYTAEARAASIL--AGLSFTPEmqvKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKW 390
|
90 100
....*....|....*....|....
gi 498436323 186 GMTMVVVTHEMGFAKEVADRVIFM 209
Cdd:PLN03073 391 PKTFIVVSHAREFLNTVVTDILHL 414
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
84-238 |
1.16e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.14 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 84 QSFNLFPHMSvLDNL-----TITPVKIKKEDATKAKEQAMALLDQVGLK----EKAdsfPSSLSGGQQQRVAIARALA-- 152
Cdd:PRK00635 419 KTFAEFQQMS-LQELfiflsQLPSKSLSIEEVLQGLKSRLSILIDLGLPyltpERA---LATLSGGEQERTALAKHLGae 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 153 MNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEmgfakevaDRVIFMADGVIqEEGTPEEIFDHPQ--NS 230
Cdd:PRK00635 495 LIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD--------EQMISLADRII-DIGPGAGIFGGEVlfNG 565
|
....*...
gi 498436323 231 RTQDFLNK 238
Cdd:PRK00635 566 SPREFLAK 573
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-211 |
1.57e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFegqnitapDSNidqirQKMG 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL--------DPN-----ERLG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQSFNLFPHMSVLDNLTITPV---KIKKE----------------------------DATKAKEQAMALLDQVGLKEK 129
Cdd:PRK15064 68 KLRQDQFAFEEFTVLDTVIMGHTelwEVKQErdriyalpemseedgmkvadlevkfaemDGYTAEARAGELLLGVGIPEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 130 ADSFP-SSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDpemVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRvif 208
Cdd:PRK15064 148 QHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD---INTIRWLEDVLNERNSTMIIISHDRHFLNSVCTH--- 221
|
...
gi 498436323 209 MAD 211
Cdd:PRK15064 222 MAD 224
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-212 |
6.79e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 6.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 1 MINVKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFeGQNItapdsnidqirqKMG 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGI------------KLG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 81 MVFQsfnlfpHMSVLDNLTITPVKIKKEDATKAKEQAMA-LLDQVGLK-EKADSFPSSLSGGQQQRVAIARALAMNPDVM 158
Cdd:PRK10636 379 YFAQ------HQLEFLRADESPLQHLARLAPQELEQKLRdYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLL 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498436323 159 LFDEPTSALDPEMVGevlAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADG 212
Cdd:PRK10636 453 LLDEPTNHLDLDMRQ---ALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDG 503
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-216 |
1.58e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 4 VKQLSKSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLnlLEE--PTSGEI---------FFegqnitapdsni 72
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM--LGQlqADSGRIhcgtklevaYF------------ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 73 DQIRQkmgmvfqsfNLFPHMSVLDNLTitpvKIKKEDATKAKEQ-AMALLDQVGLKEKADSFP-SSLSGGQQQRVAIARA 150
Cdd:PRK11147 388 DQHRA---------ELDPEKTVMDNLA----EGKQEVMVNGRPRhVLGYLQDFLFHPKRAMTPvKALSGGERNRLLLARL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498436323 151 LAMNPDVMLFDEPTSALDPEMVgEVLAVMqdLAKKGMTMVVVTHEMGFA-KEVADRVIFMADGVIQE 216
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVETL-ELLEEL--LDSYQGTVLLVSHDRQFVdNTVTECWIFEGNGKIGR 518
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
135-237 |
1.66e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.47 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 135 SSLSGGQQQRVAIARALAMN-PDVM-LFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGfAKEVADRVIFMADG 212
Cdd:TIGR00630 487 GTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED-TIRAADYVIDIGPG 565
|
90 100 110
....*....|....*....|....*....|.
gi 498436323 213 V------IQEEGTPEEIFDHPqNSRTQDFLN 237
Cdd:TIGR00630 566 AgehggeVVASGTPEEILANP-DSLTGQYLS 595
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-226 |
1.13e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.19 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLLEEPTSGEIFFEGQ--------NITAPDSNIDQIRQKM-GMVF---Q 84
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvsviaisaGLSGQLTGIENIEFKMlCMGFkrkE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 85 SFNLFPHM---SVLDNLTITPVKikkedatkakeqamalldqvglkekadsfpsSLSGGQQQRVAIARALAMNPDVMLFD 161
Cdd:PRK13546 120 IKAMTPKIiefSELGEFIYQPVK-------------------------------KYSSGMRAKLGFSINITVNPDILVID 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498436323 162 EPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEVADRVIFMADGVIQEEGTPEEIFDH 226
Cdd:PRK13546 169 EALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
109-207 |
1.66e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 109 DATKAKEQAMALLDQVGLKEKADSFP-SSLSGGQQQRVAIARALAMNPDVMLFDEPTSALDpemVGEVLAVMQDLAKKGM 187
Cdd:PRK10636 121 DAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQG 197
|
90 100
....*....|....*....|
gi 498436323 188 TMVVVTHEMGFAKEVADRVI 207
Cdd:PRK10636 198 TLILISHDRDFLDPIVDKII 217
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
135-237 |
1.92e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.40 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 135 SSLSGGQQQRVAIARALAMN-PDVM-LFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEmgfaKEV---ADRVIfm 209
Cdd:COG0178 484 GTLSGGEAQRIRLATQIGSGlVGVLyVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHD----EDTiraADYII-- 557
|
90 100 110
....*....|....*....|....*....|....*..
gi 498436323 210 aD---------GVIQEEGTPEEIFDHPqNSRTQDFLN 237
Cdd:COG0178 558 -DigpgagehgGEVVAQGTPEEILKNP-DSLTGQYLS 592
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
18-50 |
6.36e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.38 E-value: 6.36e-05
10 20 30
....*....|....*....|....*....|....
gi 498436323 18 KSI-DLEVKDGEVVVIIGPSGSGKSTILRCLNLL 50
Cdd:COG4637 11 KSLrDLELPLGPLTVLIGANGSGKSNLLDALRFL 44
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
13-77 |
1.16e-04 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 42.87 E-value: 1.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498436323 13 DNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILR--CLNLLEEPTSGE----IFFEGQNITAPDSNIDQIRQ 77
Cdd:COG5635 166 RIESLKRLELLEAKKKRLLILGEPGSGKTTLLRylALELAERYLDAEdpipILIELRDLAEEASLEDLLAE 236
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
17-42 |
1.27e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 1.27e-04
10 20
....*....|....*....|....*.
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKST 42
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSS 41
|
|
| ABC_ATPase |
pfam09818 |
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. ... |
138-211 |
3.12e-04 |
|
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: 41.04 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 138 SGGQQQRVAIARALAMNPDVMLFDEPTSA-----LDPEMVGEVLA-----------VMQDLAKKGMTMVVVTHEMGFAKE 201
Cdd:pfam09818 159 SGSTSQAANIMEALEAGASLLLIDEDTSAtnfmiRDERMQALVSKdkepitpfvdrVRSLYDDLGVSTILVVGGSGDYLD 238
|
90
....*....|
gi 498436323 202 VADRVIFMAD 211
Cdd:pfam09818 239 VADTVILMDE 248
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
29-83 |
3.45e-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: 40.84 E-value: 3.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 29 VVVIIGPSGSGKSTILRCLNLL-----EEPTSGEIFFEGQNITAPDSNIDQIRQKMGMVF 83
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLadfdaLVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEF 60
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
17-43 |
3.86e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 3.86e-04
10 20
....*....|....*....|....*..
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKSTI 43
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
134-194 |
6.77e-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: 40.07 E-value: 6.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498436323 134 PSSLSGGQQQ---RVAIARALAMNPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTH 194
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
19-50 |
8.95e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.60 E-value: 8.95e-04
10 20 30
....*....|....*....|....*....|..
gi 498436323 19 SIDLEVKDGeVVVIIGPSGSGKSTILRCLNLL 50
Cdd:COG3950 18 EIDFDNPPR-LTVLVGENGSGKTTLLEAIALA 48
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
15-47 |
1.66e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 38.62 E-value: 1.66e-03
10 20 30
....*....|....*....|....*....|....
gi 498436323 15 EVLKSIDLEVKDGE-VVVIIGPSGSGKSTILRCL 47
Cdd:COG3267 30 EALARLEYALAQGGgFVVLTGEVGTGKTTLLRRL 63
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
137-208 |
1.80e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 1.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498436323 137 LSGGQQQRVAIARALAM------NPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFaKEVADRVIF 208
Cdd:PRK03918 789 LSGGERIALGLAFRLALslylagNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHDEEL-KDAADYVIR 865
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
26-63 |
2.17e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 37.87 E-value: 2.17e-03
10 20 30
....*....|....*....|....*....|....*...
gi 498436323 26 DGEVVVIIGPSGSGKSTILRCLnLLEEPTSGEIFFEGQ 63
Cdd:pfam13191 23 RPPSVLLTGEAGTGKTTLLREL-LRALERDGGYFLRGK 59
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-212 |
2.29e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 135 SSLSGGQQQRVAIARALAM---NPDVMLFDEPTSALDPEMVGEVLAVMQDLAKKGMTMVVVTHEMGFAKEvADRVIFMAD 211
Cdd:PRK00635 1698 SSLSLSEKIAIKIAKFLYLppkHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQ-ADYLIEMGP 1776
|
.
gi 498436323 212 G 212
Cdd:PRK00635 1777 G 1777
|
|
| PRK05416 |
PRK05416 |
RNase adapter RapZ; |
28-47 |
3.24e-03 |
|
RNase adapter RapZ;
Pssm-ID: 235450 Cd Length: 288 Bit Score: 37.77 E-value: 3.24e-03
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
17-42 |
3.60e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.13 E-value: 3.60e-03
10 20
....*....|....*....|....*.
gi 498436323 17 LKSIDLEVKDGEVVVIIGPSGSGKST 42
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSS 41
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
29-47 |
3.95e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 36.36 E-value: 3.95e-03
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
17-194 |
3.98e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 37.64 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 17 LKSIDLEVKDgeVVVIIGPSGSGKSTILRCLNLLEEptSGEIFFEGQNITAPDSNIDQIRQKMGMVFQSFNLFPHMSVLD 96
Cdd:COG4938 12 FKEAELELKP--LTLLIGPNGSGKSTLIQALLLLLQ--SNFIYLPAERSGPARLYPSLVRELSDLGSRGEYTADFLAELE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498436323 97 NLTITPVKIKK---------EDATKAKEQAMALLDQVGL----KEKADSFPSSLSG-GQQQRVAIARALAM---NPDVML 159
Cdd:COG4938 88 NLEILDDKSKElleqveewlEKIFPGKVEVDASSDLVRLvfrpSGNGKRIPLSNVGsGVSELLPILLALLSaakPGSLLI 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 498436323 160 FDEPTSALDPEM---VGEVLAvmqDLAKKGMTMVVVTH 194
Cdd:COG4938 168 IEEPEAHLHPKAqsaLAELLA---ELANSGVQVIIETH 202
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
27-80 |
4.97e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 36.35 E-value: 4.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 498436323 27 GEVVVIIGPSGSGKSTILRclnlleeptsgEIFFEGQNItapdsNIDQIRQKMG 80
Cdd:COG4639 2 LSLVVLIGLPGSGKSTFAR-----------RLFAPTEVV-----SSDDIRALLG 39
|
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
27-47 |
4.99e-03 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 36.97 E-value: 4.99e-03
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
9-44 |
6.15e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 36.67 E-value: 6.15e-03
10 20 30
....*....|....*....|....*....|....*.
gi 498436323 9 KSFGDNevlksIDLEVKDGeVVVIIGPSGSGKSTIL 44
Cdd:cd03278 10 KSFADK-----TTIPFPPG-LTAIVGPNGSGKSNII 39
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
9-50 |
6.48e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 36.95 E-value: 6.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 498436323 9 KSFGDNEVLKSIDLEVKDGEVVVIIGPSGSGKSTILRCLNLL 50
Cdd:COG1106 11 RSFKDELTLSMVASGLRLLRVNLIYGANASGKSNLLEALYFL 52
|
|
| COG3911 |
COG3911 |
Predicted ATPase [General function prediction only]; |
30-58 |
6.76e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443117 Cd Length: 180 Bit Score: 36.33 E-value: 6.76e-03
10 20
....*....|....*....|....*....
gi 498436323 30 VVIIGPSGSGKSTILRCLNLLEEPTSGEI 58
Cdd:COG3911 6 IVITGGPGSGKTTLLNALARRGYACVPEA 34
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
21-44 |
7.07e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.11 E-value: 7.07e-03
|
| AAA_23 |
pfam13476 |
AAA domain; |
9-49 |
7.77e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 36.32 E-value: 7.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 498436323 9 KSFGDnevlKSIDLEVKdgeVVVIIGPSGSGKSTILRCLNL 49
Cdd:pfam13476 7 RSFRD----QTIDFSKG---LTLITGPNGSGKTTILDAIKL 40
|
|
| |
