|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-257 |
6.13e-177 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 486.78 E-value: 6.13e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNKLNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDGQLK 80
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 81 VADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQR 160
Cdd:PRK10619 81 VADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALF 240
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
250
....*....|....*..
gi 1709668069 241 GAPKSPRLQQFLKGSLK 257
Cdd:PRK10619 241 GNPQSPRLQQFLKGSLK 257
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-257 |
6.62e-170 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 468.90 E-value: 6.62e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDN---KLNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDG 77
Cdd:COG4598 1 MTDTappALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 78 QLKVADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQ 157
Cdd:COG4598 81 ELVPADRRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRD-AYPAHLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPD 237
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPA 239
|
250 260
....*....|....*....|
gi 1709668069 238 ALFGAPKSPRLQQFLKGSLK 257
Cdd:COG4598 240 EVFGNPKSERLRQFLSSSLK 259
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-253 |
1.85e-140 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 393.59 E-value: 1.85e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgqlkvADKN 85
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVvviigpsgsgKSTLLRCINLLEEPDSGTITVDGEDLT-----------DSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIAR 165
Cdd:COG1126 71 DINKLRRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKAD-AYPAQLSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPKS 245
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
....*...
gi 1709668069 246 PRLQQFLK 253
Cdd:COG1126 230 ERTRAFLS 237
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-230 |
3.06e-119 |
|
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: 339.12 E-value: 3.06e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgqlkvADKN 85
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-----------DDKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIAR 165
Cdd:cd03262 70 NINELRQKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKAD-AYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709668069 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-253 |
1.87e-100 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 292.77 E-value: 1.87e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 13 KRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdKDGQLKVadknqlRLLRT 92
Cdd:PRK09493 9 KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-----NDPKVDE------RLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 93 RLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARALAMEPE 172
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAH-HYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPKSPRLQQFL 252
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
.
gi 1709668069 253 K 253
Cdd:PRK09493 237 Q 237
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
8-256 |
6.04e-91 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 268.93 E-value: 6.04e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 8 VIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDGQlkvadKNQL 87
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQ-----KGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 88 RLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARAL 167
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKET-SYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPKSPR 247
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPR 239
|
....*....
gi 1709668069 248 LQQFLKGSL 256
Cdd:PRK11264 240 TRQFLEKFL 248
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
8-253 |
1.57e-86 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 257.25 E-value: 1.57e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 8 VIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDkdgqlkvADKNQL 87
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQK-------PSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 88 RLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARAL 167
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKAD-RFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGhpDA-LFGAPKSP 246
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG--DAsHFTQPQTE 234
|
....*..
gi 1709668069 247 RLQQFLK 253
Cdd:COG4161 235 AFAHYLS 241
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
11-253 |
8.42e-85 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 253.01 E-value: 8.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 11 LHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDkdgqlkvADKNQLRLL 90
Cdd:PRK11124 8 INCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKT-------PSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 91 RTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARALAME 170
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYAD-RFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDAlFGAPKSPRLQQ 250
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAFKN 238
|
...
gi 1709668069 251 FLK 253
Cdd:PRK11124 239 YLS 241
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
10-253 |
3.50e-81 |
|
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: 243.97 E-value: 3.50e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDGQLKVADKNQLRL 89
Cdd:TIGR03005 5 DVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNGPLVPADEKHLRQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 90 LRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARALAM 169
Cdd:TIGR03005 85 MRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKAD-HMPAQLSGGQQQRVAIARALAM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPKSPRL 248
Cdd:TIGR03005 164 RPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDlTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKEERT 243
|
....*
gi 1709668069 249 QQFLK 253
Cdd:TIGR03005 244 REFLS 248
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-253 |
6.21e-77 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 236.13 E-value: 6.21e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 8 VIDLHKRY----GEHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgQLkvaD 83
Cdd:COG1135 4 LENLSKTFptkgGPVTALDDVSLTIEKGEIfgiigysgagKSTLIRCINLLERPTSGSVLVDGVDLT-------AL---S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 84 KNQLRLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSI 163
Cdd:COG1135 74 ERELRAARRKIGMIFQHFNLLSSRTVAENV-ALPLEIAGVPKAEIRKRVAELLELVGLSDKAD-AYPSQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGA 242
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFAN 231
|
250
....*....|.
gi 1709668069 243 PKSPRLQQFLK 253
Cdd:COG1135 232 PQSELTRRFLP 242
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
10-244 |
6.00e-72 |
|
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: 219.76 E-value: 6.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRYGEH----EVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKdgqlkvadkn 85
Cdd:cd03258 6 NVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGK---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIAR 165
Cdd:cd03258 76 ELRKARRRIGMIFQHFNLLSSRTVFENVA-LPLEIAGVPKAEIEERVLELLELVGLEDKAD-AYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPK 244
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-252 |
2.39e-69 |
|
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: 213.30 E-value: 2.39e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNKLNVIDLHKRYGEHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgqlk 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEIlaiiggsgsgKSVLLKLIIGLLRPDSGEILVDGQDIT---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 81 VADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQR 160
Cdd:COG1127 71 GLSEKELYELRRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAAD-KMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDAL 239
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
250
....*....|...
gi 1709668069 240 FgAPKSPRLQQFL 252
Cdd:COG1127 230 L-ASDDPWVRQFL 241
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-235 |
3.89e-67 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 207.20 E-value: 3.89e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYG----EHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgQLKV 81
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFvaivgpsgsgKSTLLNILGGLDRPTSGEVLIDGQDIS-------SLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 82 ADKNQLRllRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRV 161
Cdd:COG1136 78 RELARLR--RRHIGFVFQFFNLLPELTALENVA-LPLLLAGVSRKERRERARELLERVGLGDRLD-HRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709668069 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGH 235
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSDER 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-229 |
3.06e-66 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 203.57 E-value: 3.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDkdgqlkvadkn 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLED----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEApiqvlglskqeareravkylakvgiderqqvkypvhLSGGQQQRVSIAR 165
Cdd:cd03229 70 ELPPLRRRIGMVFQDFALFPHLTVLENIALG------------------------------------LSGGQQQRVALAR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709668069 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGK 229
Cdd:cd03229 114 ALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
5-254 |
1.13e-65 |
|
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: 204.45 E-value: 1.13e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 5 KLNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEK--PS---EGTIVVSGQNIglvrdkdgql 79
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvPGvriEGKVLFDGQDI---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 80 kVADKNQLRLLRTRLTMVFQHFNLWShMTVLENVMEAPiQVLGL-SKQEARERAVKYLAKVGI-DErqqVK-----YPVH 152
Cdd:TIGR00972 71 -YDKKIDVVELRRRVGMVFQKPNPFP-MSIYDNIAYGP-RLHGIkDKKELDEIVEESLKKAALwDE---VKdrlhdSALG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
Cdd:TIGR00972 145 LSGGQQQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVE 223
|
250 260
....*....|....*....|..
gi 1709668069 233 EGHPDALFGAPKSPRLQQFLKG 254
Cdd:TIGR00972 224 YGPTEQIFTNPKEKRTEDYISG 245
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
10-230 |
1.49e-64 |
|
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: 200.41 E-value: 1.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRYG----EHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqLKVADKN 85
Cdd:cd03255 5 NLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDI---------SKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIAR 165
Cdd:cd03255 76 LAAFRRRHIGFVFQSFNLLPDLTALENVE-LPLLLAGVPKKERRERAEELLERVGLGDRLN-HYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709668069 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSShVIFLHQGKI 230
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADR-IIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-251 |
7.54e-63 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 196.57 E-value: 7.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 8 VIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDgqlkvadknqL 87
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAE----------L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 88 RLLRTRLTMVFQHFNLWSHMTVLENVMeAPI-QVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARA 166
Cdd:cd03261 73 YRLRRRMGMLFQSGALFDSLTVFENVA-FPLrEHTRLSEEEIREIVLEKLEAVGLRGAED-LYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPkS 245
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-D 229
|
....*.
gi 1709668069 246 PRLQQF 251
Cdd:cd03261 230 PLVRQF 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-244 |
1.93e-62 |
|
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: 195.63 E-value: 1.93e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRY-GEHEVLKGVSLQAK------------AGdvisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIglv 72
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEkgefvaiigpngSG------------KSTLLRLLNGLLKPTSGEVLVDGKDI--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 73 rdkdgqlkvaDKNQLRLLRTRLTMVFQH-----FNlwshMTVLENVMEAPIQvLGLSKQEARERAVKYLAKVGIDERQQv 147
Cdd:COG1122 66 ----------TKKNLRELRRKVGLVFQNpddqlFA----PTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLAD- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 148 KYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQ 227
Cdd:COG1122 130 RPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDD 209
|
250
....*....|....*..
gi 1709668069 228 GKIEEEGHPDALFGAPK 244
Cdd:COG1122 210 GRIVADGTPREVFSDYE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-246 |
2.69e-62 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 203.60 E-value: 2.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRY-----GEHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDgqlk 80
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETlglvgesgsgKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRS---- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 81 vadknqLRLLRTRLTMVFQH----FNlwSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQVKYPVHLSGG 156
Cdd:COG1123 337 ------LRELRRRVQMVFQDpyssLN--PRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGH 235
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGP 488
|
250
....*....|.
gi 1709668069 236 PDALFGAPKSP 246
Cdd:COG1123 489 TEEVFANPQHP 499
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
10-235 |
1.46e-61 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 192.96 E-value: 1.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRY-GEHEVLKGVSLQAK------------AGdvisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKd 76
Cdd:COG2884 6 NVSKRYpGGREALSDVSLEIEkgefvfltgpsgAG------------KSTLLKLLYGEERPTSGQVLVNGQDLSRLKRR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 77 gqlkvadknQLRLLRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGG 156
Cdd:COG2884 73 ---------EIPYLRRRIGVVFQDFRLLPDRTVYENVA-LPLRVTGKSRKEIRRRVREVLDLVGLSDKAK-ALPHELSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGH 235
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-246 |
7.70e-60 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 192.62 E-value: 7.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNKLNVIDLHKRYGEHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNI-GLVRDKdgql 79
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFvallgpsgcgKTTLLRMIAGFETPDSGRILLDGRDVtGLPPEK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 80 kvadknqlrllRtRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQ 159
Cdd:COG3842 77 -----------R-NVGMVFQDYALFPHLTVAENV-AFGLRMRGVPKAEIRARVAELLELVGLEGLAD-RYPHQLSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 160 RVSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRIMQQLaeeGKTMVVVTH--EMGFArhVSSHVIFLHQGKIEEE 233
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAklreEMREELRRLQREL---GITFIYVTHdqEEALA--LADRIAVMNDGRIEQV 217
|
250
....*....|...
gi 1709668069 234 GHPDALFGAPKSP 246
Cdd:COG3842 218 GTPEEIYERPATR 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
10-256 |
1.68e-59 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 191.55 E-value: 1.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRY----GEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdGQLkvaDKN 85
Cdd:PRK11153 6 NISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDL-------TAL---SEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVmeA-PIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIA 164
Cdd:PRK11153 76 ELRKARRQIGMIFQHFNLLSSRTVFDNV--AlPLELAGTPKAEIKARVTELLELVGLSDKAD-RYPAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAP 243
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
250
....*....|...
gi 1709668069 244 KSPRLQQFLKGSL 256
Cdd:PRK11153 233 KHPLTREFIQSTL 245
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-239 |
4.66e-58 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 184.88 E-value: 4.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRY-GEHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKdgqlkvadk 84
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFvaligpsgagKSTLLRCLNGLVEPTSGEILVDGQDVTALRGR--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 85 nQLRLLRTRLTMVFQHFNLWSHMTVLENVM------EAPIQ-VLGLSKQEARERAVKYLAKVGIDER--QQVKYpvhLSG 155
Cdd:COG3638 74 -ALRRLRRRIGMIFQQFNLVPRLSVLTNVLagrlgrTSTWRsLLGLFPPEDRERALEALERVGLADKayQRADQ---LSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
Cdd:COG3638 150 GQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDG 229
|
....*
gi 1709668069 235 HPDAL 239
Cdd:COG3638 230 PPAEL 234
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-256 |
3.01e-56 |
|
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: 180.38 E-value: 3.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGE----HEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDgqlkv 81
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 82 adknqlrlLRTRLTMVFQH----FNlwSHMTVLENVMEaPIQVLGLskQEARERAVKYLAKVGIDERQQVKYPVHLSGGQ 157
Cdd:COG1124 77 --------FRRRVQMVFQDpyasLH--PRHTVDRILAE-PLRIHGL--PDREERIAELLEQVGLPPSFLDRYPHQLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHP 236
Cdd:COG1124 144 RQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTV 223
|
250 260
....*....|....*....|
gi 1709668069 237 DALFGAPKSPRLQQFLKGSL 256
Cdd:COG1124 224 ADLLAGPKHPYTRELLAASL 243
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-239 |
4.75e-56 |
|
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: 179.69 E-value: 4.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGE-HEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDgqlkvadk 84
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 85 nqLRLLRTRLTMVFQHFNLWSHMTVLENVMEA------PIQVL-GLSKQEARERAVKYLAKVGIDER--QQVKYpvhLSG 155
Cdd:cd03256 73 --LRQLRRQIGMIFQQFNLIERLSVLENVLSGrlgrrsTWRSLfGLFPKEEKQRALAALERVGLLDKayQRADQ---LSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDG 227
|
....*
gi 1709668069 235 HPDAL 239
Cdd:cd03256 228 PPAEL 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-239 |
5.57e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 179.10 E-value: 5.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvadKN 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIfgllgpngagKTTTIRMLLGLLRPTSGEVRVLGEDV--------------AR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTRLTMVFQHFNLWSHMTVLENV-MEAPIQvlGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIA 164
Cdd:COG1131 67 DPAEVRRRIGYVPQEPALYPDLTVRENLrFFARLY--GLPRKEARERIDELLELFGLTDAAD-RKVGTLSGGMKQRLGLA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709668069 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDAL 239
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-239 |
9.20e-56 |
|
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: 179.03 E-value: 9.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGE-HEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDgqlkvadk 84
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKK-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 85 nqLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPI-------QVLGLSKQEARERAVKYLAKVGIDER--QQVKYpvhLSG 155
Cdd:TIGR02315 74 --LRKLRRRIGMIFQHYNLIERLTVLENVLHGRLgykptwrSLLGRFSEEDKERALSALERVGLADKayQRADQ---LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
Cdd:TIGR02315 149 GQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDG 228
|
....*
gi 1709668069 235 HPDAL 239
Cdd:TIGR02315 229 APSEL 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-239 |
8.41e-55 |
|
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: 175.83 E-value: 8.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEK-----PSEGTIVVSGQNIglvrdkdgqlk 80
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDI----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 81 VADKNQLRLLRTRLTMVFQHFNLWsHMTVLENVmeapiqVLGL------SKQEARERAVKYLAKVGIDERqqVK---YPV 151
Cdd:cd03260 70 YDLDVDVLELRRRVGMVFQKPNPF-PGSIYDNV------AYGLrlhgikLKEELDERVEEALRKAALWDE--VKdrlHAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
Cdd:cd03260 141 GLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
....*...
gi 1709668069 232 EEGHPDAL 239
Cdd:cd03260 220 EFGPTEQI 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-234 |
9.07e-55 |
|
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: 175.40 E-value: 9.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvadkN 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV---------------T 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVmeA-PIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIA 164
Cdd:cd03259 66 GVPPERRNIGMVFQDYALFPHLTVAENI--AfGLKLRGVPKAEIRARVRELLELVGLEGLLN-RYPHELSGGQQQRVALA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709668069 165 RALAMEPEVLLFDEPTSALDP----ELVGEVLRImqqLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAklreELREELKEL---QRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-234 |
2.53e-54 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 174.62 E-value: 2.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRY----GEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKdgqlkv 81
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRR------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 82 adknQLRLLRTRLTMVFQH----FNlwSHMTVLENVMEAPIQVLGLSKQEARERAVKYLA-KVGIDERQQVKYPVHLSGG 156
Cdd:cd03257 76 ----LRKIRRKEIQMVFQDpmssLN--PRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLvGVGLPEEVLNRYPHELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
10-254 |
1.88e-53 |
|
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: 173.98 E-value: 1.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqLKVADKNQLRL 89
Cdd:cd03294 29 EILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDI---------AAMSRKELREL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 90 LRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARALAM 169
Cdd:cd03294 100 RRKKISMVFQSFALLPHRTVLENV-AFGLEVQGVPRAEREERAAEALELVGLEGWEH-KYPDELSGGMQQRVGLARALAV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 170 EPEVLLFDEPTSALDP----ELVGEVLRIMqqlAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPKS 245
Cdd:cd03294 178 DPDILLMDEAFSALDPlirrEMQDELLRLQ---AELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPAN 254
|
....*....
gi 1709668069 246 PRLQQFLKG 254
Cdd:cd03294 255 DYVREFFRG 263
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-254 |
4.68e-53 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 172.53 E-value: 4.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 2 SDNKLNVIDLHKRYGEHEVLKGVSLQAKA------------GdvisiigssgsgKSTFLRCINFL--EKPS---EGTIVV 64
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPEnkvtaligpsgcG------------KSTLLRCLNRMndLIPGarvEGEILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 65 SGQNIglvRDKDgqlkvADKNQLRllrTRLTMVFQHFNLWShMTVLENVmeapiqVLGL------SKQEARERAVKYLAK 138
Cdd:COG1117 76 DGEDI---YDPD-----VDVVELR---RRVGMVFQKPNPFP-KSIYDNV------AYGLrlhgikSKSELDEIVEESLRK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 139 VGI-DErqqVK-----YPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPelvGEVLRI---MQQLAEEgKTMVVVT 209
Cdd:COG1117 138 AALwDE---VKdrlkkSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDP---ISTAKIeelILELKKD-YTIVIVT 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1709668069 210 HEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPKSPRLQQFLKG 254
Cdd:COG1117 211 HNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYITG 255
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-252 |
1.67e-52 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 173.79 E-value: 1.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSdnkLNVIDLHKRYGEHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGqniglvRDKDGQLK 80
Cdd:COG1118 1 MS---IEVRNISKRFGSFTLLDDVSLEIASGELvallgpsgsgKTTLLRIIAGLETPDSGRIVLNG------RDLFTNLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 81 VADKnqlrllrtRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQR 160
Cdd:COG1118 72 PRER--------RVGFVFQHYALFPHMTVAENIAFGL-RVRPPSKAEIRARVEELLELVQLEGLAD-RYPSQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 161 VSIARALAMEPEVLLFDEPTSALD----PELVGEVLRImqqLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHP 236
Cdd:COG1118 142 VALARALAVEPEVLLLDEPFGALDakvrKELRRWLRRL---HDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTP 218
|
250
....*....|....*.
gi 1709668069 237 DALFGAPKSPRLQQFL 252
Cdd:COG1118 219 DEVYDRPATPFVARFL 234
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-210 |
2.83e-52 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 170.66 E-value: 2.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNKLNVIDLHKRY----GEHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkd 76
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFvalvgpsgcgKSTLLRLIAGLEKPTSGEVLVDGKPV------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 77 gqlkvadknqlRLLRTRLTMVFQHFNL--WshMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLS 154
Cdd:COG1116 76 -----------TGPGPDRGVVFQEPALlpW--LTVLDNVA-LGLELRGVPKAERRERARELLELVGLAGFED-AYPHQLS 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRImqqLAEEGKTMVVVTH 210
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTH 197
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-229 |
8.98e-52 |
|
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: 167.64 E-value: 8.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRYGEHE--VLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvaDKNQL 87
Cdd:cd03225 4 NLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL-------------TKLSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 88 RLLRTRLTMVFQH-----FNLwshmTVLENVMEAPIQvLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVS 162
Cdd:cd03225 71 KELRRKVGLVFQNpddqfFGP----TVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRD-RSPFTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709668069 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
44-210 |
2.19e-51 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 171.82 E-value: 2.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgqlkVADKNQLRLLR-TRLTMVFQHFNLWSHMTVLENVmEAPIQVLG 122
Cdd:COG4175 66 KSTLVRCLNRLIEPTAGEVLIDGEDIT----------KLSKKELRELRrKKMSMVFQHFALLPHRTVLENV-AFGLEIQG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 123 LSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRIMQQL 198
Cdd:COG4175 135 VPKAERRERAREALELVGLAGWED-SYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrEMQDELLELQAKL 213
|
170
....*....|..
gi 1709668069 199 aeeGKTMVVVTH 210
Cdd:COG4175 214 ---KKTIVFITH 222
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-253 |
1.02e-50 |
|
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: 166.86 E-value: 1.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 17 EHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlKVADKNQLRLLRTRLTM 96
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDI----------TAKKKKKLKDLRKKVGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 97 VFQH-----FNLwshmTVLENVMEAPIQvLGLSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARALAMEP 171
Cdd:TIGR04521 87 VFQFpehqlFEE----TVYKDIAFGPKN-LGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 172 EVLLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALF---------- 240
Cdd:TIGR04521 162 EVLILDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFsdvdelekig 241
|
250
....*....|....
gi 1709668069 241 -GAPKSPRLQQFLK 253
Cdd:TIGR04521 242 lDVPEITELARKLK 255
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-253 |
6.73e-50 |
|
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: 164.01 E-value: 6.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRYGE-HEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvADKNQLR 88
Cdd:cd03295 5 NVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI------------REQDPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 89 LlRTRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERQQV-KYPVHLSGGQQQRVSIARAL 167
Cdd:cd03295 73 L-RRKIGYVIQQIGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLDPAEFAdRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 168 AMEPEVLLFDEPTSALDP----ELVGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAP 243
Cdd:cd03295 151 AADPPLLLMDEPFGALDPitrdQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
250
....*....|
gi 1709668069 244 KSPRLQQFLK 253
Cdd:cd03295 228 ANDFVAEFVG 237
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-245 |
4.27e-49 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 164.86 E-value: 4.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDnkLNVIDLHKRYGEHEVLKGVSLQAK------------AGdvisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQN 68
Cdd:COG3839 1 MAS--LELENVSKSYGGVEALKDIDLDIEdgeflvllgpsgCG------------KSTLLRMIAGLEDPTSGEILIGGRD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 69 IGlvrdkdgQLKVADKNqlrllrtrLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERaVKYLAK-VGIDERQQv 147
Cdd:COG3839 67 VT-------DLPPKDRN--------IAMVFQSYALYPHMTVYEN-IAFPLKLRKVPKAEIDRR-VREAAElLGLEDLLD- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 148 KYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRIMQQLaeeGKTMVVVTHE----MGFArhvs 219
Cdd:COG3839 129 RKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAklrvEMRAEIKRLHRRL---GTTTIYVTHDqveaMTLA---- 201
|
250 260
....*....|....*....|....*.
gi 1709668069 220 SHVIFLHQGKIEEEGHPDALFGAPKS 245
Cdd:COG3839 202 DRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-252 |
4.72e-49 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 161.74 E-value: 4.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 8 VIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgQLKVADKNql 87
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT-------DVPVQERN-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 88 rllrtrLTMVFQHFNLWSHMTVLENV---MEAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIA 164
Cdd:cd03296 76 ------VGFVFQHYALFRHMTVFDNVafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLAD-RYPAQLSGGQRQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAP 243
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
....*....
gi 1709668069 244 KSPRLQQFL 252
Cdd:cd03296 229 ASPFVYSFL 237
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
10-252 |
1.14e-48 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 162.57 E-value: 1.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRYGE-HEVLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIglvRDKDgqlkvadknqLR 88
Cdd:COG1125 6 NVTKRYPDgTVAVDDLSLTIPAGEFtvlvgpsgcgKTTTLRMINRLIEPTSGRILIDGEDI---RDLD----------PV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 89 LLRTRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERQQV-KYPVHLSGGQQQRVSIARAL 167
Cdd:COG1125 73 ELRRRIGYVIQQIGLFPHMTVAENIATVP-RLLGWDKERIRARVDELLELVGLDPEEYRdRYPHELSGGQQQRVGVARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 168 AMEPEVLLFDEPTSALDP----ELVGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAP 243
Cdd:COG1125 152 AADPPILLMDEPFGALDPitreQLQDELLRLQREL---GKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANP 228
|
....*....
gi 1709668069 244 KSPRLQQFL 252
Cdd:COG1125 229 ANDFVADFV 237
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-238 |
2.76e-48 |
|
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: 159.52 E-value: 2.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgQLKVADKN 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT-------GLPPHEIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTrltmvFQHFNLWSHMTVLENVMEAPIQVLGLS---------KQEARERAVKYLAKVGIDERQQVkyPVH-LSG 155
Cdd:cd03219 74 RLGIGRT-----FQIPRLFPELTVLENVMVAAQARTGSGlllararreEREARERAEELLERVGLADLADR--PAGeLSY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGH 235
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
...
gi 1709668069 236 PDA 238
Cdd:cd03219 227 PDE 229
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-239 |
5.22e-48 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 158.87 E-value: 5.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvadKN 85
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV--------------RK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTRLTMVFQHFNLWSHMTVLENV-MEAPIQvlGLSKQEARERAVKYLAKVGIDERQQVKYpVHLSGGQQQRVSIA 164
Cdd:COG4555 68 EPREARRQIGVLPDERGLYDRLTVRENIrYFAELY--GLFDEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVALA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709668069 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDAL 239
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-245 |
7.53e-48 |
|
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: 165.46 E-value: 7.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRY--GEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPS---EGTIVVSGQNIGLVRDkdgqlk 80
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 81 vadknqlRLLRTRLTMVFQH----FNLwshMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGG 156
Cdd:COG1123 79 -------ALRGRRIGMVFQDpmtqLNP---VTVGDQIAEA-LENLGLSRAEARARVLELLEAVGLERRLD-RYPHQLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGH 235
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
250
....*....|
gi 1709668069 236 PDALFGAPKS 245
Cdd:COG1123 227 PEEILAAPQA 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
10-233 |
7.68e-48 |
|
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: 158.02 E-value: 7.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRYG----EHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQniglvrdkdgqlkvadkn 85
Cdd:cd03293 5 NVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE------------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIAR 165
Cdd:cd03293 67 PVTGPGPDRGYVFQQDALLPWLTVLDNVA-LGLELQGVPKAEARERAEELLELVGLSGFEN-AYPHQLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709668069 166 ALAMEPEVLLFDEPTSALDP----ELVGEVLRImqqLAEEGKTMVVVTHEMGFARHVSSHVIFLHQ--GKIEEE 233
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDAltreQLQEELLDI---WRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-246 |
1.27e-46 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 157.52 E-value: 1.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRY----GEHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCI-NFLEKP--SEGTIVVSGQNIglvrdkdgq 78
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETlglvgesgsgKSTLARAIlGLLPPPgiTSGEILFDGEDL--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 79 LKvADKNQLRLLRTR-LTMVFQH----FNlwSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQV--KYPV 151
Cdd:COG0444 73 LK-LSEKELRKIRGReIQMIFQDpmtsLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRldRYPH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
250
....*....|....*.
gi 1709668069 231 EEEGHPDALFGAPKSP 246
Cdd:COG0444 230 VEEGPVEELFENPRHP 245
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-238 |
1.79e-46 |
|
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: 154.90 E-value: 1.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNKLNVIDLHKRY--GEHEV--LKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkd 76
Cdd:COG4181 4 SSAPIIELRGLTKTVgtGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 77 gQLkvaDKNQL-RLLRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSkqEARERAVKYLAKVGIDERQQvKYPVHLSG 155
Cdd:COG4181 78 -AL---DEDARaRLRARHVGFVFQSFQLLPTLTALENVM-LPLELAGRR--DARARARALLERVGLGHRLD-HYPAQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPElVGEvlRIMQQL----AEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIE 231
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAA-TGE--QIIDLLfelnRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLV 225
|
....*..
gi 1709668069 232 EEGHPDA 238
Cdd:COG4181 226 EDTAATA 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-240 |
7.10e-46 |
|
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: 153.66 E-value: 7.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDgqlkvadkn 85
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVtallgpngsgKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 qlrlLRTRLTMVFQHFNLWSHMTVLENVM--EAP-IQVLGLSKQEARERAVKYLAKVGIDE-RQQvkyPVH-LSGGQQQR 160
Cdd:COG1120 73 ----LARRIAYVPQEPPAPFGLTVRELVAlgRYPhLGLFGRPSAEDREAVEEALERTGLEHlADR---PVDeLSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDAL 239
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
.
gi 1709668069 240 F 240
Cdd:COG1120 226 L 226
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
11-229 |
8.54e-46 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 152.40 E-value: 8.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 11 LHKRY-GEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKdgqlkvadknQLRL 89
Cdd:TIGR02673 7 VSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGR----------QLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 90 LRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERQQVkYPVHLSGGQQQRVSIARALAM 169
Cdd:TIGR02673 77 LRRRIGVVFQDFRLLPDRTVYENV-ALPLEVRGKKEREIQRRVGAALRQVGLEHKADA-FPEQLSGGEQQRVAIARAIVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
Cdd:TIGR02673 155 SPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-245 |
1.19e-45 |
|
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: 152.78 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 13 KRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvadkNQLRLLRT 92
Cdd:cd03300 8 KFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI---------------TNLPPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 93 RLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARALAMEPE 172
Cdd:cd03300 73 PVNTVFQNYALFPHLTVFENIA-FGLRLKKLPKAEIKERVAEALDLVQLEGYAN-RKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709668069 173 VLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPKS 245
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPAN 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6-238 |
5.41e-45 |
|
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: 151.73 E-value: 5.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAK------------AGdvisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIGlvr 73
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVErgeivgligpngAG------------KTTLFNLITGFYRPTSGRILFDGRDIT--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 74 dkdgQLKVADKNQLRLLRTrltmvFQHFNLWSHMTVLENVMEAPIQVLGLS--------------KQEARERAVKYLAKV 139
Cdd:COG0411 70 ----GLPPHRIARLGIART-----FQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreEREARERAEELLERV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 140 GIDERQQvKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHV 218
Cdd:COG0411 141 GLADRAD-EPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGL 219
|
250 260
....*....|....*....|
gi 1709668069 219 SSHVIFLHQGKIEEEGHPDA 238
Cdd:COG0411 220 ADRIVVLDFGRVIAEGTPAE 239
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-230 |
2.62e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 148.43 E-value: 2.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvaDKN 85
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-------------SAM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTRLTMVFQHFNLWsHMTVLENvMEAPIQVLGlsKQEARERAVKYLAKVGIDER---QQVKypvHLSGGQQQRVS 162
Cdd:COG4619 68 PPPEWRRQVAYVPQEPALW-GGTVRDN-LPFPFQLRE--RKFDRERALELLERLGLPPDildKPVE---RLSGGERQRLA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
Cdd:COG4619 141 LIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
44-246 |
1.33e-43 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 150.27 E-value: 1.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgqlkVADKNQLRLLRTRLTMVFQH----FNlwSHMTVLENVMEaPIQ 119
Cdd:COG4608 57 KSTLGRLLLRLEEPTSGEILFDGQDIT----------GLSGRELRPLRRRMQMVFQDpyasLN--PRMTVGDIIAE-PLR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 120 VLGL-SKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL 198
Cdd:COG4608 124 IHGLaSKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDL 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1709668069 199 AEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPKSP 246
Cdd:COG4608 204 QDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHP 252
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-230 |
2.88e-43 |
|
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: 144.46 E-value: 2.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvadKN 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIygllgpngagKTTLIKIILGLLKPDSGEIKVLGKDI--------------KK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVmeapiqvlglskqeareravkylakvgiderqqvkypvHLSGGQQQRVSIAR 165
Cdd:cd03230 67 EPEEVKRRIGYLPEEPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQ 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709668069 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
Cdd:cd03230 109 ALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-251 |
5.65e-43 |
|
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: 149.03 E-value: 5.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 2 SDNKLNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkv 81
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDI------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 82 adknqlrllrTRLT-------MVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDErQQVKYPVHLS 154
Cdd:TIGR03265 69 ----------TRLPpqkrdygIVFQSYALFPNLTVADNI-AYGLKNRGMGRAEVAERVAELLDLVGLPG-SERKYPGQLS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPE----LVGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
Cdd:TIGR03265 137 GGQQQRVALARALATSPGLLLLDEPLSALDARvrehLRTEIRQLQRRL---GVTTIMVTHDQEEALSMADRIVVMNHGVI 213
|
250 260
....*....|....*....|.
gi 1709668069 231 EEEGHPDALFGAPKSPRLQQF 251
Cdd:TIGR03265 214 EQVGTPQEIYRHPATPFVADF 234
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-225 |
6.32e-43 |
|
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: 144.68 E-value: 6.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 8 VIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqLKVADKNQL 87
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQET---------PPLNSKKAS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 88 RLLRTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARAL 167
Cdd:TIGR03608 72 KFRREKLGYLFQNFALIENETVEEN-LDLGLKYKKLSKKEKREKKKEALEKVGLNLKLK-QKIYELSGGEQQRVALARAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1709668069 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARhVSSHVIFL 225
Cdd:TIGR03608 150 LKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAK-QADRVIEL 206
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-241 |
1.26e-42 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 146.04 E-value: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 8 VIDLHKRYGEHE--VLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGqniglvrdkdgqLKVADKN 85
Cdd:TIGR04520 3 VENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG------------LDTLDEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTRLTMVFQH-FNLWSHMTV-------LENvmeapiqvLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQ 157
Cdd:TIGR04520 71 NLWEIRKKVGMVFQNpDNQFVGATVeddvafgLEN--------LGVPREEMRKRVDEALKLVGMEDFRD-REPHLLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGHP 236
Cdd:TIGR04520 142 KQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTP 220
|
....*
gi 1709668069 237 DALFG 241
Cdd:TIGR04520 221 REIFS 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-230 |
2.75e-42 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 143.32 E-value: 2.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 9 IDLHKRYGEHEV-LKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRdkdgqlkvadKNQL 87
Cdd:cd03292 4 INVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLR----------GRAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 88 RLLRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARAL 167
Cdd:cd03292 74 PYLRRKIGVVFQDFRLLPDRNVYENVA-FALEVTGVPPREIRKRVPAALELVGLSHKHR-ALPAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709668069 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-240 |
3.57e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 144.08 E-value: 3.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNK-LNVIDLHKRYGEHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDkdgql 79
Cdd:COG1121 1 MMMMPaIELENLTVSYGGRPVLEDVSLTIPPGEFvaivgpngagKSTLLKAILGLLPPTSGTVRLFGKPPRRARR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 80 kvadknqlrllrtRLTMVFQHFNL-WS-HMTVLENVM---EAPIQVLGLSKQEARERAVKYLAKVGIDE--RQQVKypvH 152
Cdd:COG1121 76 -------------RIGYVPQRAEVdWDfPITVRDVVLmgrYGRRGLFRRPSRADREAVDEALERVGLEDlaDRPIG---E 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIeE 232
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV-A 218
|
....*...
gi 1709668069 233 EGHPDALF 240
Cdd:COG1121 219 HGPPEEVL 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-253 |
4.64e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 140.66 E-value: 4.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHevLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgQLKVADkn 85
Cdd:COG3840 2 LRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT-------ALPPAE-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 qlrllrtR-LTMVFQHFNLWSHMTVLENVmeapiqVLGLSK-----QEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQ 159
Cdd:COG3840 71 -------RpVSMLFQENNLFPHLTVAQNI------GLGLRPglkltAEQRAQVEQALERVGLAGLLD-RLPGQLSGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDA 238
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
250
....*....|....*
gi 1709668069 239 LFGAPKSPRLQQFLK 253
Cdd:COG3840 217 LLDGEPPPALAAYLG 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-254 |
2.00e-40 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 147.18 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 19 EVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVrdkdgqlkvaDKNQL-RLLRTRLTMV 97
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATL----------DADALaQLRREHFGFI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 98 FQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERqqVKY-PVHLSGGQQQRVSIARALAMEPEVLLF 176
Cdd:PRK10535 92 FQRYHLLSHLTAAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLEDR--VEYqPSQLSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 177 DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKI----------EEEGHPDALfgAPKSP 246
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIvrnppaqekvNVAGGTEPV--VNTAS 245
|
....*...
gi 1709668069 247 RLQQFLKG 254
Cdd:PRK10535 246 GWRQFVSG 253
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-236 |
2.28e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 140.99 E-value: 2.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 17 EHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDGQLKVADKNQLRL------- 89
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKtrfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 90 ----LRTRLTMVFQ--HFNLWSHmTVLENVMEAPIQvLGLSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSI 163
Cdd:PRK13651 99 kikeIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVS-MGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709668069 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHP 236
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDT 249
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
13-252 |
1.56e-39 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 140.22 E-value: 1.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 13 KRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDgqlkvadknqlrllrT 92
Cdd:PRK10851 10 KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---------------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 93 RLTMVFQHFNLWSHMTVLENVmeapiqVLGLSKQEARER----AVKYLAKVGIDERQ----QVKYPVHLSGGQQQRVSIA 164
Cdd:PRK10851 75 KVGFVFQHYALFRHMTVFDNI------AFGLTVLPRRERpnaaAIKAKVTQLLEMVQlahlADRYPAQLSGGQKQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAP 243
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
....*....
gi 1709668069 244 KSPRLQQFL 252
Cdd:PRK10851 229 ATRFVLEFM 237
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
13-254 |
1.99e-39 |
|
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: 139.99 E-value: 1.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 13 KRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVrdkdgqlkvaDKNQLRLLRT 92
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQ----------SPVELREVRR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 93 R-LTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARALAMEP 171
Cdd:TIGR01186 71 KkIGMVFQQFALFPHMTILQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEH-RYPDELSGGMQQRVGLARALAAEP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 172 EVLLFDEPTSALDP----ELVGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPKSPR 247
Cdd:TIGR01186 149 DILLMDEAFSALDPlirdSMQDELKKLQATL---QKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEY 225
|
....*..
gi 1709668069 248 LQQFLKG 254
Cdd:TIGR01186 226 VEEFIGK 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
10-234 |
2.16e-39 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 135.85 E-value: 2.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQnigLVRDkdgqLKVADKNqlrl 89
Cdd:cd03301 5 NVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR---DVTD----LPPKDRD---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 90 lrtrLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERaVKYLAKV-GIDERQQvKYPVHLSGGQQQRVSIARALA 168
Cdd:cd03301 74 ----IAMVFQNYALYPHMTVYDN-IAFGLKLRKVPKDEIDER-VREVAELlQIEHLLD-RKPKQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 169 MEPEVLLFDEPTSALDP----ELVGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
Cdd:cd03301 147 REPKVFLMDEPLSNLDAklrvQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
44-240 |
2.53e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 138.83 E-value: 2.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCINFLEKPSEGTI----VVSGQNIGLVRDKDGQLKVADKNQLRLlRTRLTMVFQ--HFNLWSHmTVLENVMEAP 117
Cdd:PRK13631 65 KSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNPYSKKIKNFKEL-RRRVSMVFQfpEYQLFKD-TIEKDIMFGP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 118 IQvLGLSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQ 197
Cdd:PRK13631 143 VA-LGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD 221
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1709668069 198 LAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALF 240
Cdd:PRK13631 222 AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
44-257 |
2.59e-39 |
|
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: 142.90 E-value: 2.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCINFLEkPSEGTIVVSGQNI-GLvrdkdgqlkvaDKNQLRLLRTRLTMVFQ----HFNlwSHMTVLENVMEaPI 118
Cdd:COG4172 325 KSTLGLALLRLI-PSEGEIRFDGQDLdGL-----------SRRALRPLRRRMQVVFQdpfgSLS--PRMTVGQIIAE-GL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 119 QVL--GLSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQ 196
Cdd:COG4172 390 RVHgpGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLR 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709668069 197 QL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPKSPRLQQFLKGSLK 257
Cdd:COG4172 470 DLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPL 531
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-229 |
2.87e-39 |
|
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: 133.91 E-value: 2.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 8 VIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgqlkvadKNQL 87
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA-------------KLPL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 88 RLLRTRLTMVFQhfnlwshmtvlenvmeapiqvlglskqeareravkylakvgiderqqvkypvhLSGGQQQRVSIARAL 167
Cdd:cd00267 69 EELRRRIGYVPQ-----------------------------------------------------LSGGQRQRVALARAL 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709668069 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
Cdd:cd00267 96 LLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-252 |
5.05e-39 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 138.17 E-value: 5.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNKLNVIDLHKRY--------GEHEV--LKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNig 70
Cdd:PRK11308 1 SQQPLLQAIDLKKHYpvkrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 71 lvrdkdgqLKVADKNQLRLLRTRLTMVFQ--HFNLWSHMTVlENVMEAPIQV-LGLSKQEARERAVKYLAKVGIDERQQV 147
Cdd:PRK11308 79 --------LLKADPEAQKLLRQKIQIVFQnpYGSLNPRKKV-GQILEEPLLInTSLSAAERREKALAMMAKVGLRPEHYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 148 KYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLH 226
Cdd:PRK11308 150 RYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMY 229
|
250 260
....*....|....*....|....*.
gi 1709668069 227 QGKIEEEGHPDALFGAPKSPRLQQFL 252
Cdd:PRK11308 230 LGRCVEKGTKEQIFNNPRHPYTQALL 255
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-252 |
5.86e-39 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 138.70 E-value: 5.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNKLNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNiglvrdkdgqlk 80
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 81 VADknqlRLLRTR-LTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKV---GIDERqqvkYPVHLSGG 156
Cdd:PRK11432 70 VTH----RSIQQRdICMVFQSYALFPHMSLGENV-GYGLKMLGVPKEERKQRVKEALELVdlaGFEDR----YVDQISGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 157 QQQRVSIARALAMEPEVLLFDEPTSALDPEL---VGEVLRIMQQlaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
Cdd:PRK11432 141 QQQRVALARALILKPKVLLFDEPLSNLDANLrrsMREKIRELQQ--QFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQI 218
|
250
....*....|....*....
gi 1709668069 234 GHPDALFGAPKSPRLQQFL 252
Cdd:PRK11432 219 GSPQELYRQPASRFMASFM 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-256 |
1.13e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 135.43 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 4 NKLNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFL-----EKPSEGTIVVSGQNIGlvrdkdgq 78
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIF-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 79 lkvadKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAP-IQVLGLSKQEARERAVKYLAKVGI-DE-RQQVKYPV-HLS 154
Cdd:PRK14247 74 -----KMDVIELRRRVQMVFQIPNPIPNLSIFENVALGLkLNRLVKSKKELQERVRWALEKAQLwDEvKDRLDAPAgKLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
Cdd:PRK14247 149 GGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
250 260
....*....|....*....|..
gi 1709668069 235 HPDALFGAPKSPRLQQFLKGSL 256
Cdd:PRK14247 228 PTREVFTNPRHELTEKYVTGRL 249
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-230 |
3.71e-38 |
|
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: 132.66 E-value: 3.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDG---QLKVADKNq 86
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGyvpQRRSIDRD- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 87 lrllrtrltmvfqhFNLwshmTVLENVMEAPIQVLGLSK---QEARERAVKYLAKVGIDE--RQQVKypvHLSGGQQQRV 161
Cdd:cd03235 83 --------------FPI----SVRDVVLMGLYGHKGLFRrlsKADKAKVDEALERVGLSElaDRQIG---ELSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
44-252 |
1.37e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 133.61 E-value: 1.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkVADKNQ--LRLLRTRLTMVFQ--HFNLWSHmTVLENVMEAPIQ 119
Cdd:PRK13634 46 KSTLLQHLNGLLQPTSGTVTIGERVI-----------TAGKKNkkLKPLRKKVGIVFQfpEHQLFEE-TVEKDICFGPMN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 120 vLGLSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL- 198
Cdd:PRK13634 114 -FGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLh 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709668069 199 AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALF-----------GAPKSPRLQQFL 252
Cdd:PRK13634 193 KEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFadpdeleaiglDLPETVKFKRAL 257
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-239 |
9.74e-37 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 129.09 E-value: 9.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvADKN 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI------------TGLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEAR-ERAVKYLAKvgIDER--QQVKypvHLSGGQQQRVS 162
Cdd:cd03224 69 PHERARAGIGYVPEGRRIFPELTVEEN-LLLGAYARRRAKRKARlERVYELFPR--LKERrkQLAG---TLSGGEQQMLA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709668069 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDAL 239
Cdd:cd03224 143 IARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-247 |
1.58e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 130.20 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGE-HEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLvrDKDGQLKVadk 84
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY--DKKSLLEV--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 85 nqlrllRTRLTMVFQHFN--LWSHmTVLENVMEAPIQvLGLSKQEARERAVKYLAKVGIdERQQVKYPVHLSGGQQQRVS 162
Cdd:PRK13639 77 ------RKTVGIVFQNPDdqLFAP-TVEEDVAFGPLN-LGLSKEEVEKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGA 242
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
....*
gi 1709668069 243 PKSPR 247
Cdd:PRK13639 228 IETIR 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-256 |
2.47e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 129.19 E-value: 2.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 4 NKLNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFL-----EKPSEGTIVVSGQNIglvrdkdgq 78
Cdd:PRK14267 3 FAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNI--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 79 lKVADKNQLRLlRTRLTMVFQHFNLWSHMTVLENV-MEAPIQVLGLSKQEARERAVKYLAKVGIDErqQVK-----YPVH 152
Cdd:PRK14267 74 -YSPDVDPIEV-RREVGMVFQYPNPFPHLTIYDNVaIGVKLNGLVKSKKELDERVEWALKKAALWD--EVKdrlndYPSN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
250 260
....*....|....*....|....
gi 1709668069 233 EGHPDALFGAPKSPRLQQFLKGSL 256
Cdd:PRK14267 229 VGPTRKVFENPEHELTEKYVTGAL 252
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
44-244 |
2.91e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 129.95 E-value: 2.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgQLKVADKNqLRLLRTRLTMVFQ--HFNLWSHmTVLENVMEAPIQvL 121
Cdd:PRK13641 46 KSTLMQHFNALLKPSSGTITIAGYHI--------TPETGNKN-LKKLRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKN-F 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 122 GLSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE 201
Cdd:PRK13641 115 GFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA 194
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1709668069 202 GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPK 244
Cdd:PRK13641 195 GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-230 |
5.32e-36 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 126.01 E-value: 5.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgQLKVADKNQlrl 89
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA-------SLSPKELAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 90 lrtrltmvfqhfnlwsHMTVLENVMEApiqvLGLSkqeareravkYLAKVGIDErqqvkypvhLSGGQQQRVSIARALAM 169
Cdd:cd03214 74 ----------------KIAYVPQALEL----LGLA----------HLADRPFNE---------LSGGERQRVLLARALAQ 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709668069 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
Cdd:cd03214 115 EPPILLLDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-246 |
1.20e-35 |
|
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: 132.89 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNKLNVIDLHKRYG----EHEVLKGVSLQAKAGDVISIIGSSGSGKS-TFLRCINFLEKPS---EGTIVVSGQNIglv 72
Cdd:COG4172 2 MSMPLLSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 73 rdkdgqLKvADKNQLRLLR-TRLTMVFQH----FNlwSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDE-RQQ 146
Cdd:COG4172 79 ------LG-LSERELRRIRgNRIAMIFQEpmtsLN--PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDpERR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 147 VK-YPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIF 224
Cdd:COG4172 150 LDaYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAV 229
|
250 260
....*....|....*....|..
gi 1709668069 225 LHQGKIEEEGHPDALFGAPKSP 246
Cdd:COG4172 230 MRQGEIVEQGPTAELFAAPQHP 251
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
20-210 |
3.48e-35 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 125.22 E-value: 3.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 20 VLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgQLKVADKNQLRllRTRLTMVFQ 99
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVT-------NLSYSQKIILR--RELIGYIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 100 HFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERQQVKyPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
Cdd:NF038007 91 SFNLIPHLSIFDNV-ALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHK-PMQLSGGQQQRVAIARAMVSNPALLLADEP 168
|
170 180 190
....*....|....*....|....*....|.
gi 1709668069 180 TSALDPELVGEVLRIMQQLAEEGKTMVVVTH 210
Cdd:NF038007 169 TGNLDSKNARAVLQQLKYINQKGTTIIMVTH 199
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-215 |
3.87e-35 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 124.07 E-value: 3.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 16 GEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLvrdkdgqlkvaDKNQLRLLRTRLT 95
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDY-----------SRKGLLERRQRVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 96 MVFQHFN--LWShMTVLENVMEAPIQvLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARALAMEPEV 173
Cdd:TIGR01166 72 LVFQDPDdqLFA-ADVDQDVAFGPLN-LGLSEAEVERRVREALTAVGASGLRE-RPTHCLSGGEKKRVAIAGAVAMRPDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1709668069 174 LLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFA 215
Cdd:TIGR01166 149 LLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-240 |
9.14e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 126.01 E-value: 9.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 17 EHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlKVADKNQ-LRLLRTRLT 95
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLI----------TSTSKNKdIKQIRKKVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 96 MVFQ--HFNLWSHmTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARALAMEPEV 173
Cdd:PRK13649 89 LVFQfpESQLFEE-TVLKDVAFGP-QNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709668069 174 LLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALF 240
Cdd:PRK13649 167 LVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
10-244 |
1.12e-34 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 127.76 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRdkdgqlkvADKnqlRL 89
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP--------AEN---RH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 90 LRTrltmVFQHFNLWSHMTVLENVmeapiqVLGL-----SKQEARERAVKYLAKVGIDERQQVKyPVHLSGGQQQRVSIA 164
Cdd:PRK09452 88 VNT----VFQSYALFPHMTVFENV------AFGLrmqktPAAEITPRVMEALRMVQLEEFAQRK-PHQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 165 RALAMEPEVLLFDEPTSALDPELvgevLRIMQ----QLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDAL 239
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKL----RKQMQnelkALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
....*
gi 1709668069 240 FGAPK 244
Cdd:PRK09452 233 YEEPK 237
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-240 |
1.22e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 125.55 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 17 EHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvADKN-QLRLLRTRLT 95
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI------------TDKKvKLSDIRKKVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 96 MVFQH--FNLWSHmTVLENVMEAPIQvLGLSKQEARERAVKYLAKVGID-ERQQVKYPVHLSGGQQQRVSIARALAMEPE 172
Cdd:PRK13637 87 LVFQYpeYQLFEE-TIEKDIAFGPIN-LGLSEEEIENRVKRAMNIVGLDyEDYKDKSPFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALF 240
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-252 |
1.58e-34 |
|
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: 123.99 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEvLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvadkN 85
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI---------------T 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEaRERAVKYLAKV-GIDERQQvKYPVHLSGGQQQRVSIA 164
Cdd:cd03299 65 NLPPEKRDISYVPQNYALFPHMTVYKNI-AYGLKKRKVDKKE-IERKVLEIAEMlGIDHLLN-RKPETLSGGEQQRVAIA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAP 243
Cdd:cd03299 142 RALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
....*....
gi 1709668069 244 KSPRLQQFL 252
Cdd:cd03299 222 KNEFVAEFL 230
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
13-239 |
1.66e-34 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 125.58 E-value: 1.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 13 KRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglVRDKDGqlkvadknqlrlLRT 92
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV--VREPRK------------VRR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 93 RLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDE--RQQVKYpvhLSGGQQQRVSIARALAME 170
Cdd:TIGR01188 67 SIGIVPQYASVDEDLTGREN-LEMMGRLYGLPKDEAEERAEELLELFELGEaaDRPVGT---YSGGMRRRLDIAASLIHQ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDAL 239
Cdd:TIGR01188 143 PDVLFLDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-212 |
2.97e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 128.60 E-value: 2.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRYGEHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQniglvrdkdgqlKVADKNQLRL 89
Cdd:COG1129 9 GISKSFGGVKALDGVSLELRPGEVhallgengagKSTLMKILSGVYQPDSGEILLDGE------------PVRFRSPRDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 90 LRTRLTMVFQHFNLWSHMTVLENVMeapiqvLG--------LSKQEARERAVKYLAKVG--IDERQQVKypvHLSGGQQQ 159
Cdd:COG1129 77 QAAGIAIIHQELNLVPNLSVAENIF------LGreprrgglIDWRAMRRRARELLARLGldIDPDTPVG---DLSVAQQQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1709668069 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM 212
Cdd:COG1129 148 LVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRL 200
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
44-181 |
3.83e-34 |
|
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: 120.45 E-value: 3.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvaDKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEaPIQVLGL 123
Cdd:pfam00005 24 KSTLLKLIAGLLSPTEGTILLDGQDL-------------TDDERKSLRKEIGYVFQDPQLFPRLTVRENLRL-GLLLKGL 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709668069 124 SKQEARERAVKYLAKVGIDE---RQQVKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTS 181
Cdd:pfam00005 90 SKREKDARAEEALEKLGLGDladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-254 |
3.90e-34 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 123.35 E-value: 3.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNKLNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFL-----EKPSEGTIVVSGQNIGLVRdk 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 76 dgqlkvADKNQLRllrTRLTMVFQHFNLWShMTVLENVMEApIQVLGLSKQEARERAV-KYLAKVGI-DErqqVKYPVH- 152
Cdd:PRK14239 79 ------TDTVDLR---KEIGMVFQQPNPFP-MSIYENVVYG-LRLKGIKDKQVLDEAVeKSLKGASIwDE---VKDRLHd 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 ----LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQG 228
Cdd:PRK14239 145 salgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDG 223
|
250 260
....*....|....*....|....*.
gi 1709668069 229 KIEEEGHPDALFGAPKSPRLQQFLKG 254
Cdd:PRK14239 224 DLIEYNDTKQMFMNPKHKETEDYISG 249
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
16-235 |
6.06e-34 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 122.29 E-value: 6.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 16 GEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKdgqlkvadknQLRLLRTRLT 95
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNR----------EVPFLRRQIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 96 MVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARALAMEPEVLL 175
Cdd:PRK10908 83 MIFQDHHLLMDRTVYDNV-AIPLIIAGASGDDIRRRVSAALDKVGLLDKAK-NFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 176 FDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGH 235
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVG 220
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
44-245 |
2.78e-33 |
|
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: 122.99 E-value: 2.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKdgqlkvadknqlrllRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGL 123
Cdd:TIGR01187 9 KTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH---------------LRHINMVFQSYALFPHMTVEENV-AFGLKMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 124 SKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVG----EVLRIMQQLa 199
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQLEEFAD-RKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDqmqlELKTIQEQL- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1709668069 200 eeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPKS 245
Cdd:TIGR01187 151 --GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPAN 194
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-246 |
4.47e-33 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 122.51 E-value: 4.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 22 KGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqLKVADKnQLRLLRTRLTMVFQH- 100
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL---------LGMKDD-EWRAVRSDIQMIFQDp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 101 -FNLWSHMTVLENVMEaPIQVL--GLSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
Cdd:PRK15079 108 lASLNPRMTIGEIIAE-PLRTYhpKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 178 EPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPKSP 246
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHP 256
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
44-250 |
7.27e-33 |
|
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: 122.52 E-value: 7.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCINFLEKPSEGTIVVsgqniglvrdkDGQLKVADKNQLRLL--RTRLTMVFQHFNLWSHMTVLENVMeapiqvL 121
Cdd:COG4148 38 KTTLLRAIAGLERPDSGRIRL-----------GGEVLQDSARGIFLPphRRRIGYVFQEARLFPHLSVRGNLL------Y 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 122 GLSKQEARERAVKyLAKV----GID---ERqqvkYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRI 194
Cdd:COG4148 101 GRKRAPRAERRIS-FDEVvellGIGhllDR----RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPY 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1709668069 195 MQQLAEEGKT-MVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPKSPRLQQ 250
Cdd:COG4148 176 LERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-254 |
1.26e-32 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 122.83 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 21 LKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgqlKVADKNQLRLLRTRLTMVFQH 100
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIA---------KISDAELREVRRKKIAMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 101 FNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
Cdd:PRK10070 115 FALMPHMTVLDNTAFG-MELAGINAEERREKALDALRQVGLENYAH-SYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709668069 181 SALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPKSPRLQQFLKG 254
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-229 |
1.87e-32 |
|
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: 116.71 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYG--EHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvaD 83
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKvaivgpsgsgKSTLLKLLLRLYDPTSGEILIDGVDL-------------R 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 84 KNQLRLLRTRLTMVFQHFNLWShMTVLENVmeapiqvlglskqeareravkylakvgiderqqvkypvhLSGGQQQRVSI 163
Cdd:cd03228 68 DLDLESLRKNIAYVPQDPFLFS-GTIRENI---------------------------------------LSGGQRQRIAI 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709668069 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHVsSHVIFLHQGK 229
Cdd:cd03228 108 ARALLRDPPILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-239 |
1.93e-32 |
|
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: 118.55 E-value: 1.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgQLKVAdkn 85
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIvallgrngagKTTLLKAISGLLPPRSGSIRFDGEDIT-------GLPPH--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 qlRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEAR-ERAVKY---LAkvgidER--QQVKYpvhLSGGQQQ 159
Cdd:COG0410 74 --RIARLGIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADlERVYELfprLK-----ERrrQRAGT---LSGGEQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDAL 239
Cdd:COG0410 144 MLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-239 |
3.06e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.07 E-value: 3.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 3 DNKLNVIDLHKRYGE-HEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQniglvrdkdgqlKV 81
Cdd:PRK13647 2 DNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGR------------EV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 82 ADKNQlRLLRTRLTMVFQHFN--LWShMTVLENVMEAPIQvLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQ 159
Cdd:PRK13647 70 NAENE-KWVRSKVGLVFQDPDdqVFS-STVWDDVAFGPVN-MGLDKDEVERRVEEALKAVRMWDFRD-KPPYHLSYGQKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDAL 239
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-234 |
4.04e-32 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 117.21 E-value: 4.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 5 KLNVIdlhkRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgQLKVADK 84
Cdd:cd03298 2 RLDKI----RFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT-------AAPPADR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 85 NqlrllrtrLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEaRERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIA 164
Cdd:cd03298 71 P--------VSMLFQENNLFAHLTVEQNVGLGLSPGLKLTAED-RQAIEVALARVGLAGLEK-RLPGELSGGERQRVALA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709668069 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
10-239 |
1.04e-31 |
|
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: 116.32 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglVRDKDGqlkvadknqlrl 89
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV--VREPRE------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 90 LRTRLTMVFQHFNLWSHMTVLENV-MEAPIQvlGLSKQEARERAVKYLAKVGIDER--QQVKYpvhLSGGQQQRVSIARA 166
Cdd:cd03265 71 VRRRIGIVFQDLSVDDELTGWENLyIHARLY--GVPGAERRERIDELLDFVGLLEAadRLVKT---YSGGMRRRLEIARS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709668069 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDAL 239
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-239 |
1.16e-31 |
|
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: 122.64 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRYGEHE--VLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgQLKVADknql 87
Cdd:COG2274 478 NVSFRYPGDSppVLDNISLTIKPGERvaivgrsgsgKSTLLKLLLGLYEPTSGRILIDGIDLR-------QIDPAS---- 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 88 rlLRTRLTMVFQHFNLWShMTVLENVMeapiqvlgLSKQEARERAVKYLAK-VGIDE-----RQQVKYPVH-----LSGG 156
Cdd:COG2274 547 --LRRQIGVVLQDVFLFS-GTIRENIT--------LGDPDATDEEIIEAARlAGLHDfiealPMGYDTVVGeggsnLSGG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGHP 236
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDGTH 693
|
...
gi 1709668069 237 DAL 239
Cdd:COG2274 694 EEL 696
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-254 |
1.53e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 116.89 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYG----EHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNI---Glvrdkdgq 78
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpG-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 79 lkvADKNqlrllrtrltMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQ 158
Cdd:COG4525 76 ---ADRG----------VVFQKDALLPWLNVLDNV-AFGLRLRGVPKAERRARAEELLALVGLADFAR-RRIWQLSGGMR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 159 QRVSIARALAMEPEVLLFDEPTSALDpELVGEVlriMQQL-----AEEGKTMVVVTHEMGFARHVSSHVIFL--HQGKIE 231
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALD-ALTREQ---MQELlldvwQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIV 216
|
250 260
....*....|....*....|...
gi 1709668069 232 EEGHPDalFGapksprlQQFLKG 254
Cdd:COG4525 217 ERLELD--FS-------RRFLAG 230
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-239 |
3.49e-31 |
|
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: 114.93 E-value: 3.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgqlkvADKN 85
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDIT-----------KLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLlRTRLTMVFQHFNLWSHMTVLENVMeapiqvLGLSKQEARERAvkylakvgIDERQQVKYPV----------HLSG 155
Cdd:TIGR03410 70 HERA-RAGIAYVPQGREIFPRLTVEENLL------TGLAALPRRSRK--------IPDEIYELFPVlkemlgrrggDLSG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
Cdd:TIGR03410 135 GQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASG 214
|
....*
gi 1709668069 235 HPDAL 239
Cdd:TIGR03410 215 AGDEL 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-225 |
3.66e-31 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 114.84 E-value: 3.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHE-------VLKGVSLQAKAGDVISIIGSSGSGKSTFLRCI--NFLekPSEGTIvvsgqnigLVRDKD 76
Cdd:COG4778 5 LEVENLSKTFTLHLqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYL--PDSGSI--------LVRHDG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 77 GQLKVADKNQ---LRLLRTRLTMVFQHFNLWSHMTVLENVMEaPIQVLGLSKQEARERAVKYLAKVGIDERQQVKYPVHL 153
Cdd:COG4778 75 GWVDLAQASPreiLALRRRTIGYVSQFLRVIPRVSALDVVAE-PLLERGVDREEARARARELLARLNLPERLWDLPPATF 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709668069 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFL 225
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-219 |
5.78e-31 |
|
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: 113.73 E-value: 5.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKdgqlkvadkn 85
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 qlrlLRTRLTMVFQHFNLWSHMTVLENV-MEApiQVLGLSKQEARERAVkyLAKVGIDERQQVkyPV-HLSGGQQQRVSI 163
Cdd:COG4133 73 ----YRRRLAYLGHADGLKPELTVRENLrFWA--ALYGLRADREAIDEA--LEAVGLAGLADL--PVrQLSAGQKRRVAL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTH---EMGFARHVS 219
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqplELAAARVLD 201
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-239 |
8.64e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 119.88 E-value: 8.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 14 RY-GEHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIglvRDkdgqLKVADknqlrlLRT 92
Cdd:COG1132 348 SYpGDRPVLKDISLTIPPGETvalvgpsgsgKSTLVNLLLRFYDPTSGRILIDGVDI---RD----LTLES------LRR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 93 RLTMVFQHFNLWsHMTVLENvmeapiqvLGLSKQEA-RERAVKYLAKVGIDERQQvKYP-----------VHLSGGQQQR 160
Cdd:COG1132 415 QIGVVPQDTFLF-SGTIREN--------IRYGRPDAtDEEVEEAAKAAQAHEFIE-ALPdgydtvvgergVNLSGGQRQR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGHPDAL 239
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRNA-DRILVLDDGRIVEQGTHEEL 561
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-230 |
9.16e-31 |
|
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: 113.53 E-value: 9.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQniglvrdkdgQLKVADKN 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK----------PLDIAARN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRtrltmvfQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERQQVKYPvHLSGGQQQRVSIAR 165
Cdd:cd03269 71 RIGYLP-------EERGLYPKMKVIDQLVYLA-QLKGLKKEEARRRIDEWLERLELSEYANKRVE-ELSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709668069 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-240 |
1.44e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.94 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNKLNVIDLHKRYGE-HEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDkdGQL 79
Cdd:PRK13636 1 MEDYILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRK--GLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 80 KvadknqlrlLRTRLTMVFQH--FNLWShMTVLENVMEAPIQvLGLSKQEARERAVKYLAKVGIDERQQvkYPVH-LSGG 156
Cdd:PRK13636 79 K---------LRESVGMVFQDpdNQLFS-ASVYQDVSFGAVN-LKLPEDEVRKRVDNALKRTGIEHLKD--KPTHcLSFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGH 235
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN 225
|
....*
gi 1709668069 236 PDALF 240
Cdd:PRK13636 226 PKEVF 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-230 |
1.72e-30 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 114.00 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKdgqlkvadkn 85
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 qlrllrTRltMVFQHFNLWSHMTVLENVMeapiqvLGLsKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIAR 165
Cdd:PRK11247 83 ------TR--LMFQDARLLPWKKVIDNVG------LGL-KGQWRDAALQALAAVGLADRAN-EWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709668069 166 ALAMEPEVLLFDEPTSALDPelvgeVLRI-MQQLAE-----EGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDA-----LTRIeMQDLIEslwqqHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
44-212 |
2.11e-30 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 112.77 E-value: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCINFLEKPSEGTIVVSGQNIglvrdKDGQLKVADKNQLRllrtRLTMVFQHFNLWSHMTVLENVMEApiqVLGL 123
Cdd:cd03297 36 KSTLLRCIAGLEKPDGGTIVLNGTVL-----FDSRKKINLPPQQR----KIGLVFQQYALFPHLNVRENLAFG---LKRK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 124 SKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-G 202
Cdd:cd03297 104 RNREDRISVDELLDLLGLDHLLN-RYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNlN 182
|
170
....*....|
gi 1709668069 203 KTMVVVTHEM 212
Cdd:cd03297 183 IPVIFVTHDL 192
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-250 |
2.15e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 114.01 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEH---------EVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkd 76
Cdd:PRK10419 4 LNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLA------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 77 gQLkvaDKNQLRLLRTRLTMVFQH----FNlwSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQVKYPVH 152
Cdd:PRK10419 78 -KL---NRAQRKAFRRDIQMVFQDsisaVN--PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKT-MVVVTHEMGFARHVSSHVIFLHQGKIE 231
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQIV 231
|
250 260
....*....|....*....|..
gi 1709668069 232 EE---GHPDAlFGAPKSPRLQQ 250
Cdd:PRK10419 232 ETqpvGDKLT-FSSPAGRVLQN 252
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-229 |
2.20e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.82 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNKLNVIDLHKRYGEHEVLKGVSLQAK------------AGdvisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQn 68
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRpgeihallgengAG------------KSTLMKILYGLYQPDSGEILIDGK- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 69 iglvrdkdgqlKVADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGID---E 143
Cdd:COG3845 68 -----------PVRIRSPRDAIALGIGMVHQHFMLVPNLTVAENIVlgLEPTKGGRLDRKAARARIRELSERYGLDvdpD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 144 RqqvkyPVH-LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHV 222
Cdd:COG3845 137 A-----KVEdLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRV 211
|
....*..
gi 1709668069 223 IFLHQGK 229
Cdd:COG3845 212 TVLRRGK 218
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-233 |
3.61e-30 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 113.36 E-value: 3.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEH---------EVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkd 76
Cdd:TIGR02769 3 LEVRDVTHTYRTGglfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDL------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 77 GQLkvaDKNQLRLLRTRLTMVFQH----FNlwSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQVKYPVH 152
Cdd:TIGR02769 76 YQL---DRKQRRAFRRDVQLVFQDspsaVN--PRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
Cdd:TIGR02769 151 LSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
..
gi 1709668069 232 EE 233
Cdd:TIGR02769 231 EE 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-234 |
4.28e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 114.05 E-value: 4.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAK------------AGdvisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIGL-V 72
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPkgeifgllgpngAG------------KTTTIRIILGILAPDSGEVLWDGEPLDPeD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 73 RDKDG----------QLKVADknQLRLLrTRLTmvfqhfnlwshmtvlenvmeapiqvlGLSKQEARERAVKYLAKVGID 142
Cdd:COG4152 70 RRRIGylpeerglypKMKVGE--QLVYL-ARLK--------------------------GLSKAEAKRRADEWLERLGLG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 143 ERQQVKypVH-LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSH 221
Cdd:COG4152 121 DRANKK--VEeLSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDR 198
|
250
....*....|...
gi 1709668069 222 VIFLHQGKIEEEG 234
Cdd:COG4152 199 IVIINKGRKVLSG 211
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-240 |
4.42e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 113.68 E-value: 4.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 24 VSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqLKVADKNQLRLLRTRLTMVFQ--HF 101
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVV---------SSTSKQKEIKPVRKKVGVVFQfpES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 102 NLWSHmTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTS 181
Cdd:PRK13643 96 QLFEE-TVLKDVAFGP-QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 182 ALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALF 240
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-240 |
8.46e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.87 E-value: 8.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 17 EHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGqniglvrdkdgqLKVADKNQLRLLRTRLTM 96
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG------------LDTSDEENLWDIRNKAGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 97 VFQH-FNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERQqvKYPVH-LSGGQQQRVSIARALAMEPEVL 174
Cdd:PRK13633 90 VFQNpDNQIVATIVEEDVAFGP-ENLGIPPEEIRERVDESLKKVGMYEYR--RHAPHlLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709668069 175 LFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGHPDALF 240
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-237 |
1.64e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 111.36 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvADKN 85
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPL------------AAWS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTRLTMVfQHfnlwSHM----TVLENVMeapiqvLGL-----SKQEARERAVKYLAKVGIDERQQVKYPvHLSGG 156
Cdd:COG4559 70 PWELARRRAVLP-QH----SSLafpfTVEEVVA------LGRaphgsSAAQDRQIVREALALVGLAHLAGRSYQ-TLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 157 QQQRVSIARALA-------MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
Cdd:COG4559 138 EQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGR 217
|
....*...
gi 1709668069 230 IEEEGHPD 237
Cdd:COG4559 218 LVAQGTPE 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-230 |
1.64e-29 |
|
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: 108.67 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQniglvrdkdgqlkvadkn 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 qlrllrtrltmvfqhfnlwshmtvlenvmeapiQVLGLSKQEARERavkylakvGIderqqvkYPVH-LSGGQQQRVSIA 164
Cdd:cd03216 63 ---------------------------------EVSFASPRDARRA--------GI-------AMVYqLSVGERQMVEIA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709668069 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-236 |
1.96e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.40 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdGQLKVADkn 85
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPL-------ADWSPAE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 qlrlLRTRLTMVFQHFNLWSHMTVLEnVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQVKYPvHLSGGQQQRVSIAR 165
Cdd:PRK13548 74 ----LARRRAVLPQHSSLSFPFTVEE-VVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYP-QLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709668069 166 ALA------MEPEVLLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHP 236
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-252 |
2.24e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 115.57 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 11 LHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKST----FLRCINflekpSEGTIVVSGQniglvrdkdgQLKVADKNQ 86
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQ----------PLHNLNRRQ 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 87 LRLLRTRLTMVFQHFN--LWSHMTVLENVMEApIQV--LGLSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVS 162
Cdd:PRK15134 357 LLPVRHRIQVVFQDPNssLNPRLNVLQIIEEG-LRVhqPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFG 241
Cdd:PRK15134 436 IARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFA 515
|
250
....*....|.
gi 1709668069 242 APKSPRLQQFL 252
Cdd:PRK15134 516 APQQEYTRQLL 526
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-230 |
2.35e-29 |
|
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: 109.65 E-value: 2.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 8 VIDLHKRYGEH-EVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLvrdkdgqlkvadknq 86
Cdd:cd03226 2 IENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA--------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 87 lRLLRTRLTMVFQH--FNLWSHmTVLENvmeapiqvLGLSKQEA---RERAVKYLAKVGIDERQQvKYPVHLSGGQQQRV 161
Cdd:cd03226 67 -KERRKSIGYVMQDvdYQLFTD-SVREE--------LLLGLKELdagNEQAETVLKDLDLYALKE-RHPLSLSGGQKQRL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
Cdd:cd03226 136 AIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-239 |
2.40e-29 |
|
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: 115.63 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRY-GEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCI-NFLEkPSEGTIVVSGQNIGlvrdkdgQLKVADknql 87
Cdd:COG4988 341 DVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLlGFLP-PYSGSILINGVDLS-------DLDPAS---- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 88 rlLRTRLTMVFQH---FnlwsHMTVLENvmeapiqvLGLSKQEARERAVKY-LAKVGIDE-----RQQVKYPVH-----L 153
Cdd:COG4988 409 --WRRQIAWVPQNpylF----AGTIREN--------LRLGRPDASDEELEAaLEAAGLDEfvaalPDGLDTPLGeggrgL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEE 233
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDGRIVEQ 552
|
....*.
gi 1709668069 234 GHPDAL 239
Cdd:COG4988 553 GTHEEL 558
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
9-256 |
4.34e-29 |
|
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: 112.51 E-value: 4.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 9 IDLHKRYGEHEVlkGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdKDGQLKVadknQLR 88
Cdd:TIGR02142 3 ARFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL-----FDSRKGI----FLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 89 LLRTRLTMVFQHFNLWSHMTVLENVmeapiqVLGLSKQEARERAV---KYLAKVGIDERQQvKYPVHLSGGQQQRVSIAR 165
Cdd:TIGR02142 72 PEKRRIGYVFQEARLFPHLSVRGNL------RYGMKRARPSERRIsfeRVIELLGIGHLLG-RLPGRLSGGEKQRVAIGR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPK 244
Cdd:TIGR02142 145 ALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
250
....*....|..
gi 1709668069 245 SPRLQQFLKGSL 256
Cdd:TIGR02142 225 LPWLAREDQGSL 236
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
21-243 |
6.10e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 110.46 E-value: 6.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 21 LKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgqlkvaDKNQLRLLRTRLTMVFQH 100
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG------------DFSKLQGIRKLVGIVFQN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 101 FNL-WSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIdERQQVKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
Cdd:PRK13644 86 PETqFVGRTVEEDLAFGP-ENLCLPPIEIRKRVDRALAEIGL-EKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709668069 180 TSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGfARHVSSHVIFLHQGKIEEEGHPDALFGAP 243
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-222 |
1.10e-28 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 108.75 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGE----HEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdGQLKV 81
Cdd:PRK11629 6 LQCDNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPM-------SKLSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 82 ADKNQLRllRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERQQVKyPVHLSGGQQQRV 161
Cdd:PRK11629 79 AAKAELR--NQKLGFIYQFHHLLPDFTALENV-AMPLLIGKKKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709668069 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHV 222
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
6-246 |
1.12e-28 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 109.54 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEH---------EVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQniglvrdkd 76
Cdd:COG4167 5 LEVRNLSKTFKYRtglfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 77 gQLKVAD-KNQLRLLRtrltMVFQHFN--LWSHMTVLEnVMEAPIQVL-GLSKQEARERAVKYLAKVGIDERQQVKYPVH 152
Cdd:COG4167 76 -KLEYGDyKYRCKHIR----MIFQDPNtsLNPRLNIGQ-ILEEPLRLNtDLTAEEREERIFATLRLVGLLPEHANFYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
250
....*....|....*
gi 1709668069 232 EEGHPDALFGAPKSP 246
Cdd:COG4167 230 EYGKTAEVFANPQHE 244
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-241 |
1.53e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.48 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 17 EHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgQLKVADKnQLRLLRTRLTM 96
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITI--------THKTKDK-YIRPVRKRIGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 97 VFQhfnlWSHMTVLENVMEAPIQV----LGLSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARALAMEPE 172
Cdd:PRK13646 90 VFQ----FPESQLFEDTVEREIIFgpknFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 173 VLLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFG 241
Cdd:PRK13646 166 IIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-234 |
2.53e-28 |
|
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: 106.89 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGdVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKdgqlkvadkn 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 qlrlLRTRLTMVFQHFNLWSHMTVLENVmeAPIQVL-GLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIA 164
Cdd:cd03264 70 ----LRRRIGYLPQEFGVYPNFTVREFL--DYIAWLkGIPSKEVKARVDEVLELVNLGDRAK-KKIGSLSGGMRRRVGIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-234 |
4.60e-28 |
|
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: 106.15 E-value: 4.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDGQLKVadkn 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 qlrllrtrltmVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEAREravkYLAKVGIDERQQVKYPvHLSGGQQQRVSIAR 165
Cdd:cd03268 77 -----------LIEAPGFYPNLTAREN-LRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVK-GFSLGMKQRLGIAL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-234 |
1.74e-27 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 105.14 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRY----GEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGqnIGLVRDKdgqlkv 81
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 82 adknqlRLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERQQVKYPvHLSGGQQQRV 161
Cdd:cd03266 74 ------AEARRRLGFVSDSTGLYDRLTARENL-EYFAGLYGLKGDELTARLEELADRLGMEELLDRRVG-GFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709668069 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-228 |
2.02e-27 |
|
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: 105.24 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 21 LKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrDKDGQLKVadknqlrllrtrltMVFQH 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI----TEPGPDRM--------------VVFQN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 101 FNLWSHMTVLENVMEAPIQVL-GLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
Cdd:TIGR01184 63 YSLLPWLTVRENIALAVDRVLpDLSKSERRAIVEEHIALVGLTEAAD-KRPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1709668069 180 TSALDP----ELVGEVLRIMQqlaEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
Cdd:TIGR01184 142 FGALDAltrgNLQEELMQIWE---EHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-234 |
2.45e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 105.87 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFL---EKPSEGTIVVSGQNIglvrDKDGQLKva 82
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTV----QREGRLA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 83 dkNQLRLLRTRLTMVFQHFNLWSHMTVLENVMeapIQVLGLS----------KQEARERAVKYLAKVGIDE--RQQVKYp 150
Cdd:PRK09984 79 --RDIRKSRANTGYIFQQFNLVNRLSVLENVL---IGALGSTpfwrtcfswfTREQKQRALQALTRVGMVHfaHQRVST- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 151 vhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRIMQQlaEEGKTMVVVTHEMGFARHVSSHVIFLHQ 227
Cdd:PRK09984 153 --LSGGQQQRVAIARALMQQAKVILADEPIASLDPEsarIVMDTLRDINQ--NDGITVVVTLHQVDYALRYCERIVALRQ 228
|
....*..
gi 1709668069 228 GKIEEEG 234
Cdd:PRK09984 229 GHVFYDG 235
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
14-234 |
3.26e-27 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 104.17 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 14 RYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIvvsgqniglvrdkdgqlKVADKNQLRLLRTR 93
Cdd:TIGR01277 7 RYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSI-----------------KVNDQSHTGLAPYQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 94 --LTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEaRERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARALAMEP 171
Cdd:TIGR01277 70 rpVSMLFQENNLFAHLTVRQNIGLGLHPGLKLNAEQ-QEKVVDAAQQVGIADYLD-RLPEQLSGGQRQRVALARCLVRPN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709668069 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
Cdd:TIGR01277 148 PILLLDEPFSALDPLLREEMLALVKQLCSERQrTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-253 |
5.53e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.10 E-value: 5.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNKLNVIDLHKRYGEHE--VLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQ--NIGLVRDkd 76
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlSEETVWD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 77 gqlkvadknqlrlLRTRLTMVFQH-FNLWSHMTV-------LENVmeapiqvlGLSKQEARERAVKYLAKVGIDERQQvK 148
Cdd:PRK13635 79 -------------VRRQVGMVFQNpDNQFVGATVqddvafgLENI--------GVPREEMVERVDQALRQVGMEDFLN-R 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 149 YPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHvSSHVIFLHQ 227
Cdd:PRK13635 137 EPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNK 215
|
250 260 270
....*....|....*....|....*....|....*..
gi 1709668069 228 GKIEEEGHPDALF-----------GAPKSPRLQQFLK 253
Cdd:PRK13635 216 GEILEEGTPEEIFksghmlqeiglDVPFSVKLKELLK 252
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-254 |
6.91e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 105.18 E-value: 6.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFL-EKPS----EGTIVVSGQNIGLVRDkdgqlk 80
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSgyrySGDVLLGGRSIFNYRD------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 81 vadknqLRLLRTRLTMVFQHFNLWShMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQVKY---PVHLSGGQ 157
Cdd:PRK14271 96 ------VLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPD 237
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTE 247
|
250
....*....|....*..
gi 1709668069 238 ALFGAPKSPRLQQFLKG 254
Cdd:PRK14271 248 QLFSSPKHAETARYVAG 264
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-245 |
7.43e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 106.84 E-value: 7.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDkdgqlkvadkn 85
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP----------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 qlrlLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVlGLSKQEARERAVKYLAKVGIDERQQVKyPVHLSGGQQQRVSIAR 165
Cdd:PRK11607 89 ----YQRPINMMFQSYALFPHMTVEQNIAFGLKQD-KLPKAEIASRVNEMLGLVHMQEFAKRK-PHQLSGGQRQRVALAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 166 ALAMEPEVLLFDEPTSALDPELVG----EVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFG 241
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKKLRDrmqlEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
....
gi 1709668069 242 APKS 245
Cdd:PRK11607 240 HPTT 243
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-252 |
8.36e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 104.35 E-value: 8.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFL-----EKPSEGTIVVSGQNIglvrdkdgqlk 80
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNI----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 81 VADKNQLRLLRTRLTMVFQHFNLWShMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGiDERQQVKYPVH-----LSG 155
Cdd:PRK14258 77 YERRVNLNRLRRQVSMVHPKPNLFP-MSVYDNVAYG-VKIVGWRPKLEIDDIVESALKDA-DLWDEIKHKIHksaldLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQ-----GK 229
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFFKGnenriGQ 233
|
250 260
....*....|....*....|...
gi 1709668069 230 IEEEGHPDALFGAPKSPRLQQFL 252
Cdd:PRK14258 234 LVEFGLTKKIFNSPHDSRTREYV 256
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-230 |
8.43e-27 |
|
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: 103.35 E-value: 8.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHE--VLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvad 83
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 84 KNQLRLLRTRLTMVFQHFNLWSHMTVLENVM-EAPIQvlGLSKQEARERAVKYLAKVGIdeRQQVKYPVH-LSGGQQQRV 161
Cdd:cd03263 67 RTDRKAARQSLGYCPQFDALFDELTVREHLRfYARLK--GLPKSEIKEEVELLLRVLGL--TDKANKRARtLSGGMKRKL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
Cdd:cd03263 143 SLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-245 |
8.63e-27 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 106.08 E-value: 8.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 5 KLNVIDLHKRY-GEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgQLKVAD 83
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN-------ELEPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 84 KNqlrllrtrLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERaVKYLAKV-GIDERQQVKyPVHLSGGQQQRVS 162
Cdd:PRK11650 76 RD--------IAMVFQNYALYPHMSVREN-MAYGLKIRGMPKAEIEER-VAEAARIlELEPLLDRK-PRELSGGQRQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 163 IARALAMEPEVLLFDEPTSALDPELVG----EVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDA 238
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLDAKLRVqmrlEIQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVE 221
|
....*..
gi 1709668069 239 LFGAPKS 245
Cdd:PRK11650 222 VYEKPAS 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-243 |
1.03e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.50 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 12 HKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvaDKNQLRLLR 91
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI-------------TKENIREVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 92 TRLTMVFQHFN--LWShMTVLENVMEAPIQvLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARALAM 169
Cdd:PRK13652 78 KFVGLVFQNPDdqIFS-PTVEQDIAFGPIN-LGLDEETVAHRVSSALHMLGLEELRD-RVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709668069 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAP 243
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
6-249 |
3.08e-26 |
|
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: 102.60 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVsgqniglvRDKDGQ----LKV 81
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATY--------IMRSGAelelYQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 82 ADKNQLRLLRTRLTMVFQHFNLWSHMTVLE--NVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQ 159
Cdd:TIGR02323 76 SEAERRRLMRTEWGFVHQNPRDGLRMRVSAgaNIGERLMAIGARHYGNIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDA 238
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQ 235
|
250
....*....|.
gi 1709668069 239 LFGAPKSPRLQ 249
Cdd:TIGR02323 236 VLDDPQHPYTQ 246
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-254 |
3.83e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 102.55 E-value: 3.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 2 SDNKLNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEK--PS---EGTIVVSGQNIglvrdKD 76
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNL-----YA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 77 GQLKVADknqlrlLRTRLTMVFQHFNLWSHmTVLENVMEAPiQVLGLSKQ--EARERAVKYLA---KVGIDERQQvkyPV 151
Cdd:PRK14243 82 PDVDPVE------VRRRIGMVFQKPNPFPK-SIYDNIAYGA-RINGYKGDmdELVERSLRQAAlwdEVKDKLKQS---GL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLH----- 226
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNvelte 229
|
250 260 270
....*....|....*....|....*....|..
gi 1709668069 227 ----QGKIEEEGHPDALFGAPKSPRLQQFLKG 254
Cdd:PRK14243 230 gggrYGYLVEFDRTEKIFNSPQQQATRDYVSG 261
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-239 |
5.71e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 101.99 E-value: 5.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNKLNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNI-GLvrdkDGQl 79
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeGL----PGH- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 80 KVADKNqlrLLRTrltmvFQHFNLWSHMTVLENVMEAPIQVL------GL--------SKQEARERAVKYLAKVGIDE-- 143
Cdd:PRK11300 76 QIARMG---VVRT-----FQHVRLFREMTVIENLLVAQHQQLktglfsGLlktpafrrAESEALDRAATWLERVGLLEha 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 144 -RQqvkyPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSH 221
Cdd:PRK11300 148 nRQ----AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDR 223
|
250
....*....|....*...
gi 1709668069 222 VIFLHQGKIEEEGHPDAL 239
Cdd:PRK11300 224 IYVVNQGTPLANGTPEEI 241
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
8-243 |
6.56e-26 |
|
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: 101.70 E-value: 6.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 8 VIDLHK---RYGEHEVLKGVSLQAK------------AGdvisiigssgsgKSTFLRCINFLEKPSEG-TIVVSGQNIGL 71
Cdd:COG1119 3 LLELRNvtvRRGGKTILDDISWTVKpgehwailgpngAG------------KSTLLSLITGDLPPTYGnDVRLFGERRGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 72 VRdkdgqlkVADknqlrlLRTRLTMV--FQHFNLWSHMTVLENVMEAPIQVLGLSKQ---EARERAVKYLAKVGIDERQQ 146
Cdd:COG1119 71 ED-------VWE------LRKRIGLVspALQLRFPRDETVLDVVLSGFFDSIGLYREptdEQRERARELLELLGLAHLAD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 147 VKYPvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEG-KTMVVVTHemgfarHVS------ 219
Cdd:COG1119 138 RPFG-TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTH------HVEeippgi 210
|
250 260 270
....*....|....*....|....*....|...
gi 1709668069 220 SHVIFLHQGKIEEEGHPD---------ALFGAP 243
Cdd:COG1119 211 THVLLLKDGRVVAAGPKEevltsenlsEAFGLP 243
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
8-240 |
7.53e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 101.99 E-value: 7.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 8 VIDLHKRYGEHE--VLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGqniglvrdkdgqlKVADKN 85
Cdd:PRK13632 10 VENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG-------------ITISKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTRLTMVFQH-FNLWSHMTV-------LENVMEAPiqvlglskQEARERAVKYLAKVGIDERQQvKYPVHLSGGQ 157
Cdd:PRK13632 77 NLKEIRKKIGIIFQNpDNQFIGATVeddiafgLENKKVPP--------KKMKDIIDDLAKKVGMEDYLD-KEPQNLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEG-KTMVVVTHEMGFARhVSSHVIFLHQGKIEEEGHP 236
Cdd:PRK13632 148 KQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKP 226
|
....
gi 1709668069 237 DALF 240
Cdd:PRK13632 227 KEIL 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-253 |
8.83e-26 |
|
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: 105.62 E-value: 8.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRY--GEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDgqlkvad 83
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 84 knqlrlLRTRLTMVFQHFNLWsHMTVLENvmeapiqvLGLSKQEA-RERAVKYLAKVGIDE-----RQQVKYPVH----- 152
Cdd:COG4987 407 ------LRRRIAVVPQRPHLF-DTTLREN--------LRLARPDAtDEELWAALERVGLGDwlaalPDGLDTWLGeggrr 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEE 232
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGLERM-DRILVLEDGRIVE 549
|
250 260
....*....|....*....|.
gi 1709668069 233 EGHPDALfgAPKSPRLQQFLK 253
Cdd:COG4987 550 QGTHEEL--LAQNGRYRQLYQ 568
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-240 |
1.62e-25 |
|
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: 100.31 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNI-GLVRDKdgqlkvadk 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMHK--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 85 nqlrllRTRLTMVF--QHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDE-RQQVKYpvHLSGGQQQRV 161
Cdd:cd03218 72 ------RARLGIGYlpQEASIFRKLTVEENIL-AVLEIRGLSKKEREEKLEELLEEFHITHlRKSKAS--SLSGGERRRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALF 240
Cdd:cd03218 143 EIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-239 |
1.98e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 101.81 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNKLNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlk 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 81 vadKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERQQVKYPvHLSGGQQQR 160
Cdd:PRK13537 72 ---PSRARHARQRVGVVPQFDNLDPDFTVRENLLVFG-RYFGLSAAAARALVPPLLEFAKLENKADAKVG-ELSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 161 VSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRimqQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPD 237
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQarhLMWERLR---SLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPH 223
|
..
gi 1709668069 238 AL 239
Cdd:PRK13537 224 AL 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-256 |
2.47e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.51 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 2 SDNKLNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDkdgqlkV 81
Cdd:PRK14246 7 AEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKD------I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 82 ADKNQLRLlRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLS-KQEARERAVKYLAKVGI--DERQQVKYPV-HLSGGQ 157
Cdd:PRK14246 81 FQIDAIKL-RKEVGMVFQQPNPFPHLSIYDNI-AYPLKSHGIKeKREIKKIVEECLRKVGLwkEVYDRLNSPAsQLSGGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPD 237
Cdd:PRK14246 159 QQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSN 237
|
250
....*....|....*....
gi 1709668069 238 ALFGAPKSPRLQQFLKGSL 256
Cdd:PRK14246 238 EIFTSPKNELTEKYVIGRI 256
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
10-237 |
5.94e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 99.39 E-value: 5.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDgqlkvadknqlrl 89
Cdd:COG4604 6 NVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRE------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 90 LRTRLTMVFQ--HFNlwSHMTVLENVMeapiqvLG--------LSK--QEARERAVKYLAKVGIDERqqvkYPVHLSGGQ 157
Cdd:COG4604 73 LAKRLAILRQenHIN--SRLTVRELVA------FGrfpyskgrLTAedREIIDEAIAYLDLEDLADR----YLDELSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHP 236
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTP 220
|
.
gi 1709668069 237 D 237
Cdd:COG4604 221 E 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-202 |
6.25e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 98.95 E-value: 6.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 5 KLNVIDLHKRYGEHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvadk 84
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIvgllgpngagKTTTFYMIVGLVKPDSGRIFLDGEDI--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 85 nqlrllrTRLTM----------------VFQHfnlwshMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERQQVK 148
Cdd:COG1137 68 -------THLPMhkrarlgigylpqeasIFRK------LTVEDNIL-AVLELRKLSKKEREERLEELLEEFGITHLRKSK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1709668069 149 yPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEG 202
Cdd:COG1137 134 -AYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERG 186
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-241 |
6.61e-25 |
|
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: 102.96 E-value: 6.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRY-----GEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVsgqniglvRDKDGQLK 80
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV--------RVGDEWVD 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 81 VADKNQLrlLRTRLT----MVFQHFNLWSHMTVLENVMEApIQvLGLSKQEARERAVKYLAKVGIDERQQV----KYPVH 152
Cdd:TIGR03269 352 MTKPGPD--GRGRAKryigILHQEYDLYPHRTVLDNLTEA-IG-LELPDELARMKAVITLKMVGFDEEKAEeildKYPDE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR-IMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
250
....*....|
gi 1709668069 232 EEGHPDALFG 241
Cdd:TIGR03269 508 KIGDPEEIVE 517
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
13-244 |
1.08e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 100.87 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 13 KRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvadkNQLRLLRT 92
Cdd:PRK11000 11 KAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM---------------NDVPPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 93 RLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERaVKYLAKV----GIDERQqvkyPVHLSGGQQQRVSIARALA 168
Cdd:PRK11000 76 GVGMVFQSYALYPHLSVAEN-MSFGLKLAGAKKEEINQR-VNQVAEVlqlaHLLDRK----PKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 169 MEPEVLLFDEPTSALDPEL----VGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPK 244
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALrvqmRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
7-241 |
1.33e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 99.04 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 7 NVIDLHK---RYG---EHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQniglvrdkdgqlK 80
Cdd:PRK13650 3 NIIEVKNltfKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD------------L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 81 VADKNQLRLlRTRLTMVFQH-FNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQ 159
Cdd:PRK13650 71 LTEENVWDI-RHKIGMVFQNpDNQFVGATVEDDVAFG-LENKGIPHEEMKERVNEALELVGMQDFKE-REPARLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEGHPDA 238
Cdd:PRK13650 148 RVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRE 226
|
...
gi 1709668069 239 LFG 241
Cdd:PRK13650 227 LFS 229
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
79-253 |
1.68e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 99.43 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 79 LKVADKNQLRLLRTRLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDE---RQQVkYPVHL 153
Cdd:PRK11022 76 QRISEKERRNLVGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpasRLDV-YPHQL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
170 180
....*....|....*....|.
gi 1709668069 233 EGHPDALFGAPKSPRLQQFLK 253
Cdd:PRK11022 235 TGKAHDIFRAPRHPYTQALLR 255
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-237 |
2.45e-24 |
|
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: 101.03 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLE--KPSEGTIVVsgqNIGL--------VRDK 75
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIY---HVALcekcgyveRPSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 76 DGQ----------LKVAD-----KNQLRLLRTRLTMVFQH-FNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKV 139
Cdd:TIGR03269 78 VGEpcpvcggtlePEEVDfwnlsDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEA-LEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 140 GIDERQqvkypVH----LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRimQQLAEEGKTMVVVTHEM 212
Cdd:TIGR03269 157 QLSHRI-----THiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtakLVHNALE--EAVKASGISMVLTSHWP 229
|
250 260
....*....|....*....|....*
gi 1709668069 213 GFARHVSSHVIFLHQGKIEEEGHPD 237
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIKEEGTPD 254
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-254 |
2.56e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 97.91 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 2 SDNKLNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlKV 81
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI----------PA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 82 ADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQVKyPVHLSGGQQQRV 161
Cdd:PRK11831 74 MSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLM-PSELSGGMARRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALF 240
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQ 232
|
250
....*....|....
gi 1709668069 241 GAPkSPRLQQFLKG 254
Cdd:PRK11831 233 ANP-DPRVRQFLDG 245
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
15-250 |
2.91e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.39 E-value: 2.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 15 YGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDgqlkvadknqlrlLRTRL 94
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-------------LARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 95 TMVFQHFNLWSHMTVLENVM--EAPIQVL-GLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARALAMEP 171
Cdd:PRK11231 79 ALLPQHHLTPEGITVRELVAygRSPWLSLwGRLSAEDNARVNQAMEQTRINHLAD-RRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFgapkSPRLQQ 250
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM----TPGLLR 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-237 |
3.91e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.08 E-value: 3.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQniglvrdkdgqlKVADKN 85
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK------------PVEGPG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRllrtrlTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIAR 165
Cdd:PRK11248 70 AER------GVVFQNEGLLPWRNVQDNV-AFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEK-RYIWQLSGGQRQRVGIAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709668069 166 ALAMEPEVLLFDEPTSALDP---ELVGEVLriMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLH--QGKIEEEGHPD 237
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALDAftrEQMQTLL--LKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVERLPLN 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
10-239 |
5.92e-24 |
|
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: 96.15 E-value: 5.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRYGEH-EVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVrdkdgqlkvadknQLR 88
Cdd:cd03253 5 NVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV-------------TLD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 89 LLRTRLTMVFQHFNLWsHMTVLENVMEAPIQVLGLSKQEARERAV----------KYLAKVGidERQqvkypVHLSGGQQ 158
Cdd:cd03253 72 SLRRAIGVVPQDTVLF-NDTIGYNIRYGRPDATDEEVIEAAKAAQihdkimrfpdGYDTIVG--ERG-----LKLSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGHPDA 238
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
.
gi 1709668069 239 L 239
Cdd:cd03253 222 L 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-216 |
6.70e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.99 E-value: 6.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 14 RYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVS-GQNIGLVRDkdgQLKVADKNQLRLLRT 92
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAgGARVAYVPQ---RSEVPDSLPLTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 93 rLTM-VFQHFNLWSHMTvlenvmeapiqvlglskQEARERAVKYLAKVGID--ERQQVKypvHLSGGQQQRVSIARALAM 169
Cdd:NF040873 78 -VAMgRWARRGLWRRLT-----------------RDDRAAVDDALERVGLAdlAGRQLG---ELSGGQRQRALLAQGLAQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1709668069 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFAR 216
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVR 183
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-240 |
1.42e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 96.62 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 17 EHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLekpsegTIVVSGQNIglVRDKDGQLKVADKNQLRLLRTRLTM 96
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGL------IISETGQTI--VGDYAIPANLKKIKEVKRLRKEIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 97 VFQ--HFNLWSHmTVLENVMEAPIQvLGLSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARALAMEPEVL 174
Cdd:PRK13645 95 VFQfpEYQLFQE-TIEKDIAFGPVN-LGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709668069 175 LFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALF 240
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
13-237 |
1.71e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.15 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 13 KRYGEHEVLKGVSLQAKAGDVisiigssgSGKSTFLRCINFLEKPSEGTIVVSGqniglvrdkdgqlKVADknqlrLLrt 92
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESvgiigrngAGKSTLLKLIAGILEPTSGRVEVNG-------------RVSA-----LL-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 93 RLTMVFQhfnlwSHMTVLENV-MEApiQVLGLSKQEARER--AVKYLAKVG--IDerQQVKypvHLSGGQQQRVSIARAL 167
Cdd:COG1134 94 ELGAGFH-----PELTGRENIyLNG--RLLGLSRKEIDEKfdEIVEFAELGdfID--QPVK---TYSSGMRARLAFAVAT 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPD 237
Cdd:COG1134 162 AVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
85-246 |
2.10e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 96.72 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 85 NQLRLLRT-RLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDE-RQQVK-YPVHLSGGQQQ 159
Cdd:PRK09473 89 KELNKLRAeQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEaRKRMKmYPHEFSGGMRQ 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKT-MVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDA 238
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
....*...
gi 1709668069 239 LFGAPKSP 246
Cdd:PRK09473 249 VFYQPSHP 256
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
44-252 |
2.46e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.39 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCINFLEKPSEGTIVVSGQNIGLVRDkdgqlkvadkNQLRLLRTRLTMVFQ--HFNLWSHMTVLENVMEaPIQVL 121
Cdd:PRK10261 363 KSTTGRALLRLVESQGGEIIFNGQRIDTLSP----------GKLQALRRDIQFIFQdpYASLDPRQTVGDSIME-PLRVH 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 122 GL-SKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE 200
Cdd:PRK10261 432 GLlPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQR 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1709668069 201 E-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPKSPRLQQFL 252
Cdd:PRK10261 512 DfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-233 |
3.90e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 94.08 E-value: 3.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 2 SDNKLNVIDLHKRYGEHE----VLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNiglvrdkdg 77
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 78 qLKVADKNQLRLLRTR-LTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGG 156
Cdd:PRK10584 74 -LHQMDEEARAKLRAKhVGFVFQSFMLIPTLNALENV-ELPALLRGESSRQSRNGAKALLEQLGLGKRLD-HLPAQLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709668069 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHvIFLHQGKIEEE 233
Cdd:PRK10584 151 EQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRR-LRLVNGQLQEE 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-252 |
4.65e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.47 E-value: 4.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 17 EHEVLKGVSLQAKAGDVISIIGSSGSGKS-TFLRCINFLEKPS----EGTIVVSGQNiglvrdkdgqLKVADKNQLRLLR 91
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGES----------LLHASEQTLRGVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 92 -TRLTMVFQHfnLWSHMTVLENVMEAPIQVL----GLSKQEARERAVKYLAKVGIdeRQQVK----YPVHLSGGQQQRVS 162
Cdd:PRK15134 91 gNKIAMIFQE--PMVSLNPLHTLEKQLYEVLslhrGMRREAARGEILNCLDRVGI--RQAAKrltdYPHQLSGGERQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFG 241
Cdd:PRK15134 167 IAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFS 246
|
250
....*....|.
gi 1709668069 242 APKSPRLQQFL 252
Cdd:PRK15134 247 APTHPYTQKLL 257
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-243 |
1.30e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 95.29 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDGQLKVADKN 85
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QlrllRTRLTMVFQ-----------HFNLWSHMTvlenvmeapiqvlglskqEARERAV-KYLAKVGIDerQQVKYPV-H 152
Cdd:PRK09536 84 Q----DTSLSFEFDvrqvvemgrtpHRSRFDTWT------------------ETDRAAVeRAMERTGVA--QFADRPVtS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
Cdd:PRK09536 140 LSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRA 219
|
250
....*....|.
gi 1709668069 233 EGHPDALFGAP 243
Cdd:PRK09536 220 AGPPADVLTAD 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-249 |
1.65e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 92.68 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIvvsgqnigLVRDKDGQLK----V 81
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV--------HYRMRDGQLRdlyaL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 82 ADKNQLRLLRTRLTMVFQHFNLWSHMTVLE--NVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQ 159
Cdd:PRK11701 79 SEAERRRLLRTEWGFVHQHPRDGLRMQVSAggNIGERLMAVGARHYGDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDA 238
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQ 238
|
250
....*....|.
gi 1709668069 239 LFGAPKSPRLQ 249
Cdd:PRK11701 239 VLDDPQHPYTQ 249
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-240 |
1.87e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 93.15 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLvrdkdgqlkvaDKN 85
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY-----------SKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDE-RQQvkyPVH-LSGGQQQRVSI 163
Cdd:PRK13638 71 GLLALRQQVATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHfRHQ---PIQcLSHGQKKRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709668069 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALF 240
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-239 |
2.77e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 93.74 E-value: 2.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNKLNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVsgqniglvrdkdgqLK 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV--------------LG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 81 VADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEArERAVKYLAKVGIDERQQVKYPVHLSGGQQQR 160
Cdd:PRK13536 103 VPVPARARLARARIGVVPQFDNLDLEFTVRENLLVFG-RYFGMSTREI-EAVIPSLLEFARLESKADARVSDLSGGMKRR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 161 VSIARALAMEPEVLLFDEPTSALDP---ELVGEVLRimqQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPD 237
Cdd:PRK13536 181 LTLARALINDPQLLILDEPTTGLDPharHLIWERLR---SLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPH 257
|
..
gi 1709668069 238 AL 239
Cdd:PRK13536 258 AL 259
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-239 |
3.14e-22 |
|
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: 91.83 E-value: 3.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 17 EHEVLKGVSLQAKAGDVISIIGSSGSGKSTflrCINFLEK---PSEGTIVVSGQNIglvRDkdgqlkvadkNQLRLLRTR 93
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERfydPTSGEILLDGVDI---RD----------LNLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 94 LTMVFQHFNLWShMTVLENVmeapiqVLGL--SKQEARERAVKylaKVGIDE---------RQQV-KYPVHLSGGQQQRV 161
Cdd:cd03249 79 IGLVSQEPVLFD-GTIAENI------RYGKpdATDEEVEEAAK---KANIHDfimslpdgyDTLVgERGSQLSGGQKQRI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709668069 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGHPDAL 239
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDEL 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-239 |
3.20e-22 |
|
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: 91.78 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 14 RYG--EHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVrdkdgqlkvaDKNQLRllr 91
Cdd:cd03252 9 RYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA----------DPAWLR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 92 TRLTMVFQHfNLWSHMTVLENV--------MEAPIQVLGLSKQEA--RERAVKYLAKVGidERQqvkypVHLSGGQQQRV 161
Cdd:cd03252 76 RQVGVVLQE-NVLFNRSIRDNIaladpgmsMERVIEAAKLAGAHDfiSELPEGYDTIVG--EQG-----AGLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709668069 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGHPDAL 239
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
86-252 |
3.86e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 94.92 E-value: 3.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLR-TRLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQV--KYPVHLSGGQQQR 160
Cdd:PRK10261 97 QMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTIlsRYPHQLSGGMRQR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLHQGKIEEEGHPDAL 239
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIfITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
170
....*....|...
gi 1709668069 240 FGAPKSPRLQQFL 252
Cdd:PRK10261 257 FHAPQHPYTRALL 269
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
44-239 |
5.30e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 90.80 E-value: 5.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCINFLEKPSEGTIVVSGQniglvrdkdgqlkvaDKNQLRLLRTRLTMVFQHFNLWSHMTVLENVmeapiqVLGL 123
Cdd:PRK10771 38 KSTLLNLIAGFLTPASGSLTLNGQ---------------DHTTTPPSRRPVSMLFQENNLFSHLTVAQNI------GLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 124 S-----KQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL 198
Cdd:PRK10771 97 NpglklNAAQREKLHAIARQMGIEDLLA-RLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1709668069 199 AEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDAL 239
Cdd:PRK10771 176 CQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
107-230 |
6.01e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 94.31 E-value: 6.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 107 MTVLENVMEAPIQVLG----LSKQEARERAVKYLAKVGI---DERQQVKypvHLSGGQQQRVSIARALAMEPEVLLFDEP 179
Cdd:COG1129 345 LSIRENITLASLDRLSrgglLDRRRERALAEEYIKRLRIktpSPEQPVG---NLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1709668069 180 TSALDpelVG---EVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
Cdd:COG1129 422 TRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-230 |
7.08e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 7.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 8 VIDLHKRYGEHEVLKGVSLQAKAGDvisiigssgsgKSTFLRCINFLEKPSEGTIVVSGQniglvrdkdgqlkvadknql 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDriglvgrngagKSTLLKILAGELEPDSGEVSIPKG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 88 rllrTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQ-------------------------------EARERAVKYL 136
Cdd:COG0488 61 ----LRIGYLPQEPPLDDDLTVLDTVLDGDAELRALEAEleeleaklaepdedlerlaelqeefealggwEAEARAEEIL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 137 AKVGIDERQQVKyPV-HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLRimQQLAEEGKTMVVVTHEMGFA 215
Cdd:COG0488 137 SGLGFPEEDLDR-PVsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESI-EWLE--EFLKNYPGTVLVVSHDRYFL 212
|
250
....*....|....*
gi 1709668069 216 RHVSSHVIFLHQGKI 230
Cdd:COG0488 213 DRVATRILELDRGKL 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-240 |
9.43e-22 |
|
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: 90.36 E-value: 9.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 16 GEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdKDGQLKVadknqlrlLRTRLT 95
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI-----RDISRKS--------LRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 96 MVFQHFNLWSHmTVLENVMeapiqvlgLSKQEARERAVKYLAK-VGIDE--RQQVK----YPVH----LSGGQQQRVSIA 164
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIR--------LGRPNATDEEVIEAAKeAGAHDfiMKLPNgydtVLGEnggnLSQGERQLLAIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 165 RALAMEPEVLLFDEPTSALDPE---LVGE-VLRIMqqlaeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGHPDALF 240
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTEtekLIQEaLEKLM-----KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
44-240 |
1.02e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.97 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvaDKNQLRLLRTRLTMVFQH-FNLWSHMTV-------LENVMe 115
Cdd:PRK13648 48 KSTIAKLMIGIEKVKSGEIFYNNQAI-------------TDDNFEKLRKHIGIVFQNpDNQFVGSIVkydvafgLENHA- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 116 apiqvlgLSKQEARERAVKYLAKVGIDERQQVKyPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIM 195
Cdd:PRK13648 114 -------VPYDEMHRRVSEALKQVDMLERADYE-PNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLV 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1709668069 196 QQLAEEGK-TMVVVTHEMGFARHvSSHVIFLHQGKIEEEGHPDALF 240
Cdd:PRK13648 186 RKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
20-239 |
2.33e-21 |
|
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: 92.71 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 20 VLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvaDKNQLRLLRTRLTMVFQ 99
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDL-------------AGLDVQAVRRQLGVVLQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 100 HFNLWSHmTVLENVMEAPIqvlgLSKQEARERAvkylAKVGIDER-QQVKYPVH---------LSGGQQQRVSIARALAM 169
Cdd:TIGR03797 535 NGRLMSG-SIFENIAGGAP----LTLDEAWEAA----RMAGLAEDiRAMPMGMHtvisegggtLSGGQRQRLLIARALVR 605
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709668069 170 EPEVLLFDEPTSALDPELVGEVlriMQQLAEEGKTMVVVTHEMGFARHvsSHVIF-LHQGKIEEEGHPDAL 239
Cdd:TIGR03797 606 KPRILLFDEATSALDNRTQAIV---SESLERLKVTRIVIAHRLSTIRN--ADRIYvLDAGRVVQQGTYDEL 671
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-250 |
2.70e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 90.24 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNKLNVIDLHKRYGEHE--VLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKP---SEGTIVVSGQNIGlvrdk 75
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLT----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 76 dgQLKVADknqlrlLRTRLTMVFQH-FNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERQQVKyPVHLS 154
Cdd:PRK13640 76 --AKTVWD------IREKVGIVFQNpDNQFVGATVGDDVAFG-LENRAVPRPEMIKIVRDVLADVGMLDYIDSE-PANLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSShVIFLHQGKIEEE 233
Cdd:PRK13640 146 GGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANMADQ-VLVLDDGKLLAQ 224
|
250
....*....|....*..
gi 1709668069 234 GHPDALFgaPKSPRLQQ 250
Cdd:PRK13640 225 GSPVEIF--SKVEMLKE 239
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-230 |
2.94e-21 |
|
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: 88.80 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 17 EHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgQLKVADknqlrlLRTRLTM 96
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIR-------QLDPAD------LRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 97 VFQHFNLWSHmTVLENVMeapiqvlgLSKQEARERAVKYLAKV-GID----------ERQQVKYPVHLSGGQQQRVSIAR 165
Cdd:cd03245 83 VPQDVTLFYG-TLRDNIT--------LGAPLADDERILRAAELaGVTdfvnkhpnglDLQIGERGRGLSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709668069 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHVsSHVIFLHQGKI 230
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLLDLV-DRIIVMDSGRI 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-210 |
7.45e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 91.19 E-value: 7.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 16 GEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgQLKVADknqlrlLRTRLT 95
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA-------DADADS------WRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 96 MVFQHFNLWSHmTVLENVmeapiqvlGLSKQEARERAVK-YLAKVGIDERQQV----------KYPVHLSGGQQQRVSIA 164
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENI--------RLARPDASDAEIReALERAGLDEFVAAlpqgldtpigEGGAGLSGGQAQRLALA 470
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1709668069 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTH 210
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTH 515
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-242 |
9.88e-21 |
|
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: 87.67 E-value: 9.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 14 RYGEHE--VLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvRDKdgqlkvadknQLRLLR 91
Cdd:cd03251 9 RYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV---RDY----------TLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 92 TRLTMVFQHFNLWSHmTVLENVMEApiqVLGLSKQEARERAVKYLAKVGIDERQQvKYP-------VHLSGGQQQRVSIA 164
Cdd:cd03251 76 RQIGLVSQDVFLFND-TVAENIAYG---RPGATREEVEEAARAANAHEFIMELPE-GYDtvigergVKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709668069 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGHPDALFGA 242
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
17-247 |
2.54e-20 |
|
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: 89.93 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 17 EHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgQLKVADknqlrlLRTRLTM 96
Cdd:TIGR03375 477 ETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIR-------QIDPAD------LRRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 97 VFQHFNLWsHMTVLEN-VMEAPiqvlGLSKQEAReRAVKyLAKVG-------------IDERQQvkypvHLSGGQQQRVS 162
Cdd:TIGR03375 544 VPQDPRLF-YGTLRDNiALGAP----YADDEEIL-RAAE-LAGVTefvrrhpdgldmqIGERGR-----SLSGGQRQAVA 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGHPDALFGA 242
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLLDLV-DRIIVMDNGRIVADGPKDQVLEA 689
|
....*
gi 1709668069 243 PKSPR 247
Cdd:TIGR03375 690 LRKGR 694
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-234 |
3.98e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 85.66 E-value: 3.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 12 HKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRdkdgqlkvadknqlrllr 91
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG------------------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 92 trLTMVFQhfnlwSHMTVLENV-MEAPIqvLGLSKQE--ARERAVKYLAKVG--IDerQQVKypvHLSGGQQQRVSIARA 166
Cdd:cd03220 91 --LGGGFN-----PELTGRENIyLNGRL--LGLSRKEidEKIDEIIEFSELGdfID--LPVK---TYSSGMKARLAFAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709668069 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
Cdd:cd03220 157 TALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
150-230 |
1.20e-19 |
|
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: 83.25 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 150 PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
Cdd:cd03215 102 SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
.
gi 1709668069 230 I 230
Cdd:cd03215 182 I 182
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-210 |
1.70e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 83.69 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCIN-FLEKP--SEGTIVVSGQNIglvrdkdgqlkva 82
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRL------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 83 dkNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEApiqvL--GLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQR 160
Cdd:COG4136 69 --TALPAEQRRIGILFQDDLLFPHLSVGENLAFA----LppTIGRAQRRARVEQALEEAGLAGFAD-RDPATLSGGQRAR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1709668069 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLR-IMQQLAEEGKTMVVVTH 210
Cdd:COG4136 142 VALLRALLAEPRALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTH 192
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-230 |
2.02e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 84.75 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYG-----EHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlk 80
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 81 vadknqlrllrTRLTM---------VFQhfn--lwSHMTVLENVMEA-------PIQvLGLSKQEaRERAVKYLAKVGID 142
Cdd:COG1101 71 -----------TKLPEykrakyigrVFQdpmmgtaPSMTIEENLALAyrrgkrrGLR-RGLTKKR-RELFRELLATLGLG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 143 ERQQVKYPV-HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSS 220
Cdd:COG1101 138 LENRLDTKVgLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGN 217
|
250
....*....|
gi 1709668069 221 HVIFLHQGKI 230
Cdd:COG1101 218 RLIMMHEGRI 227
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
14-239 |
3.95e-19 |
|
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: 86.33 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 14 RYGEH--EVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLvrdkdgqlkvADKNQLRllr 91
Cdd:TIGR01846 464 RYAPDspEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAI----------ADPAWLR--- 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 92 TRLTMVFQHFNLWSHmTVLENVmeapiqvlGLSKQEARERAVKYLAKVG-----IDERQQ------VKYPVHLSGGQQQR 160
Cdd:TIGR01846 531 RQMGVVLQENVLFSR-SIRDNI--------ALCNPGAPFEHVIHAAKLAgahdfISELPQgyntevGEKGANLSGGQRQR 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 161 VSIARALAMEPEVLLFDEPTSALDPElvGEVLrIMQQLAE--EGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGHPDA 238
Cdd:TIGR01846 602 IAIARALVGNPRILIFDEATSALDYE--SEAL-IMRNMREicRGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEE 677
|
.
gi 1709668069 239 L 239
Cdd:TIGR01846 678 L 678
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-212 |
4.18e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.12 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 21 LKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQniglvrdkdgqlKVADKNQLRLLRTRLTMVFQH 100
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ------------EMRFASTTAALAAGVAIIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 101 FNLWSHMTVLENVMeapiqvLG--------LSKQEARERAVKYLAKVG--IDERQQVKYpvhLSGGQQQRVSIARALAME 170
Cdd:PRK11288 88 LHLVPEMTVAENLY------LGqlphkggiVNRRLLNYEAREQLEHLGvdIDPDTPLKY---LSIGQRQMVEIAKALARN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1709668069 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM 212
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRM 200
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-232 |
4.95e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.89 E-value: 4.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDvisiigssgsgKSTFLRCINFLEKPSEGTIVVsGQNiglvrdkdgqLKVA--D 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDrigligpngagKSTLLKLLAGELEPDSGTVKL-GET----------VKIGyfD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 84 KNQlrllrtrltmvfQHFNLwsHMTVLENVME-APiqvlGLSKQEAReravKYLAKVGIDERQQVKyPVH-LSGGQQQRV 161
Cdd:COG0488 385 QHQ------------EELDP--DKTVLDELRDgAP----GGTEQEVR----GYLGRFLFSGDDAFK-PVGvLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709668069 162 SIARALAMEPEVLLFDEPTSALDPELVgEVLriMQQLAE-EGkTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETL-EAL--EEALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-230 |
8.39e-19 |
|
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: 80.72 E-value: 8.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 14 RYG--EHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRdkdgqlkvadknqLRLLR 91
Cdd:cd03246 9 RYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD-------------PNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 92 TRLTMVFQHFNLWSHmTVLENVmeapiqvlglskqeareravkylakvgiderqqvkypvhLSGGQQQRVSIARALAMEP 171
Cdd:cd03246 76 DHVGYLPQDDELFSG-SIAENI---------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709668069 172 EVLLFDEPTSALDPElvGE--VLRIMQQLAEEGKTMVVVTHEMGFARHVSShVIFLHQGKI 230
Cdd:cd03246 116 RILVLDEPNSHLDVE--GEraLNQAIAALKAAGATRIVIAHRPETLASADR-ILVLEDGRV 173
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
44-210 |
1.15e-18 |
|
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: 81.06 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCInflekpsegtivvSGQNIGLvRDKdGQLKVADKNQ-LRLLRTRLTMVFQHFNLWSHMTVLENVMeapiqvlg 122
Cdd:cd03213 48 KSTLLNAL-------------AGRRTGL-GVS-GEVLINGRPLdKRSFRKIIGYVPQDDILHPTLTVRETLM-------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 123 lskqeareravkYLAKVgideRQqvkypvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEG 202
Cdd:cd03213 105 ------------FAAKL----RG-------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTG 161
|
....*...
gi 1709668069 203 KTMVVVTH 210
Cdd:cd03213 162 RTIICSIH 169
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-210 |
2.18e-18 |
|
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: 83.95 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRY-GEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDgqlkvadk 84
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE-------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 85 nqlrlLRTRLTMVFQHFNLWsHMTVLENVMeapiqvlgLSKQEARERAV-KYLAKVG----IDERQQ-VKYPVH-----L 153
Cdd:TIGR02868 407 -----VRRRVSVCAQDAHLF-DTTVRENLR--------LARPDATDEELwAALERVGladwLRALPDgLDTVLGeggarL 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1709668069 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTH 210
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-242 |
4.31e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.19 E-value: 4.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 15 YGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgqlKVADKNQLRllrtRL 94
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ---------HYASKEVAR----RI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 95 TMVFQHFNLWSHMTVLENVMEA--PIQVLGLSKQEARERAV-KYLAKVGIDE--RQQVKYpvhLSGGQQQRVSIARALAM 169
Cdd:PRK10253 84 GLLAQNATTPGDITVQELVARGryPHQPLFTRWRKEDEEAVtKAMQATGITHlaDQSVDT---LSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709668069 170 EPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGA 242
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-234 |
4.37e-18 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 79.28 E-value: 4.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHE--VLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDkdgqlkvad 83
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 84 knqlrLLRTRLTMVFQHFNLWShMTVLENVMEapiqvlglskqeareravkylakvgiderqqvkypvHLSGGQQQRVSI 163
Cdd:cd03247 72 -----ALSSLISVLNQRPYLFD-TTLRNNLGR------------------------------------RFSGGERQRLAL 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709668069 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEG 234
Cdd:cd03247 110 ARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-243 |
8.18e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.22 E-value: 8.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 19 EVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQniglvrdkdgQLKVADknqLRLLRTRLTMVF 98
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH----------PLHFGD---YSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 99 QH-FNLWSHMTVLENVMEAPIQV-LGLSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARALAMEPEVLLF 176
Cdd:PRK15112 94 QDpSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709668069 177 DEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAP 243
Cdd:PRK15112 174 DEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
7-241 |
1.31e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.14 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 7 NVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvaDKNQ 86
Cdd:PRK13642 9 NLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELL-------------TAEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 87 LRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQqVKYPVHLSGGQQQRVSIARA 166
Cdd:PRK13642 76 VWNLRRKIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFK-TREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709668069 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHvSSHVIFLHQGKIEEEGHPDALFG 241
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-251 |
2.29e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.02 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRY--GEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDgqlkvad 83
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA------- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 84 knqlrlLRTRLTMVFQHFNLWSHmTVLENvmeapiqvLGLSKQEAR-ERAVKYLAKVGIDE----------------RQq 146
Cdd:PRK11160 412 ------LRQAISVVSQRVHLFSA-TLRDN--------LLLAAPNASdEALIEVLQQVGLEKlleddkglnawlgeggRQ- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 147 vkypvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEM-GFARHvsSHVIFL 225
Cdd:PRK11160 476 ------LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLtGLEQF--DRICVM 546
|
250 260
....*....|....*....|....*.
gi 1709668069 226 HQGKIEEEGHPDALFGapKSPRLQQF 251
Cdd:PRK11160 547 DNGQIIEQGTHQELLA--QQGRYYQL 570
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
5-240 |
2.55e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 78.38 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 5 KLNVIDLHkrYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvADK 84
Cdd:PRK11614 7 SFDKVSAH--YGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI------------TDW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 85 NQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVlglSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIA 164
Cdd:PRK11614 73 QTAKIMREAVAIVPEGRRVFSRMTVEENLAMGGFFA---ERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709668069 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALF 240
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
97-234 |
3.76e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 79.53 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 97 VFQHFNLWSHMTVLENVMeapiqvLGLSKQEARE--RAVKYLakvGIdERQQVKYPVHLSGGQQQRVSIARALAMEPEVL 174
Cdd:PRK11144 81 VFQDARLFPHYKVRGNLR------YGMAKSMVAQfdKIVALL---GI-EPLLDRYPGSLSGGEKQRVAIGRALLTAPELL 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709668069 175 LFDEPTSALDPELVGEVLRIMQQLAEEGKT-MVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
Cdd:PRK11144 151 LMDEPLASLDLPRKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-239 |
4.33e-17 |
|
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: 80.15 E-value: 4.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 14 RYG--EHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRdkdgqlkvadknqLRLLR 91
Cdd:TIGR02203 339 RYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT-------------LASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 92 TRLTMVFQHFNLWSHmTVLENV-MEAPIQVlglSKQEARERAVKYLAKVGIDE-----RQQV-KYPVHLSGGQQQRVSIA 164
Cdd:TIGR02203 406 RQVALVSQDVVLFND-TIANNIaYGRTEQA---DRAEIERALAAAYAQDFVDKlplglDTPIgENGVLLSGGQRQRLAIA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 165 RALAMEPEVLLFDEPTSALDPE---LVGEVL-RIMQqlaeeGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEG-HPDAL 239
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNEserLVQAALeRLMQ-----GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGtHNELL 555
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-230 |
5.10e-17 |
|
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: 77.31 E-value: 5.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 20 VLKGVSLQAKAGDVISIIGSSGSGKSTFLRCI-NFLEKPS--EGTIVVSGQNiglvRDKDgqlkvadknqlrLLRTRLTM 96
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGGttSGQILFNGQP----RKPD------------QFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 97 VFQHFNLWSHMTVLENVMEAPIQVLG--LSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARALAMEPEVL 174
Cdd:cd03234 86 VRQDDILLPGLTVRETLTYTAILRLPrkSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 175 LFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMG---FarHVSSHVIFLHQGKI 230
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEI 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-250 |
8.06e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.52 E-value: 8.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 20 VLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDGQLKVAdknqlrllrtrltMVFQ 99
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVA-------------YLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 100 HFNLWSHMTVLENVM--EAPIQ-VLGLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARALAMEPEVLLF 176
Cdd:PRK10575 93 QLPAAEGMTVRELVAigRYPWHgALGRFGAADREKVEEAISLVGLKPLAH-RLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709668069 177 DEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFgapKSPRLQQ 250
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM---RGETLEQ 243
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
121-246 |
1.53e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 76.66 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 121 LGLSKQEARERAVKYLAKVGIDERQQV--KYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL 198
Cdd:PRK10418 107 LALGKPADDATLTAALEAVGLENAARVlkLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESI 186
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1709668069 199 AEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPKSP 246
Cdd:PRK10418 187 VQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
153-229 |
1.59e-16 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 75.58 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElVGEvlRIMQQL----AEEGKTMVVVTHEMGFARHVsSHVIFLHQG 228
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH-VGR--HIFENCilglLLNNKTRILVTHQLQLLPHA-DQIVVLDNG 203
|
.
gi 1709668069 229 K 229
Cdd:cd03250 204 R 204
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-228 |
2.04e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.29 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 13 KRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGqniglvRDKDgQLKVADKNQLRLlrt 92
Cdd:PRK09700 13 KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN------INYN-KLDHKLAAQLGI--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 93 rlTMVFQHFNLWSHMTVLEN--VMEAPI-QVLGLSK---QEARERAVKYLAKVGI--DERQQVKypvHLSGGQQQRVSIA 164
Cdd:PRK09700 83 --GIIYQELSVIDELTVLENlyIGRHLTkKVCGVNIidwREMRVRAAMMLLRVGLkvDLDEKVA---NLSISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709668069 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
44-236 |
2.27e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 78.52 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvadKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPiQVLGL 123
Cdd:TIGR01257 969 KTTTLSILTGLLPPTSGTVLVGGKDI--------------ETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYA-QLKGR 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 124 SKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaEEGK 203
Cdd:TIGR01257 1034 SWEEAQLEMEAMLEDTGLHHKRN-EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGR 1111
|
170 180 190
....*....|....*....|....*....|...
gi 1709668069 204 TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHP 236
Cdd:TIGR01257 1112 TIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-230 |
3.08e-16 |
|
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: 75.20 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 17 EHEVLKGVSLQAKAGDVISIIGSSGSGKSTflrCINFLEK---PSEGTIVVSGQNIGLVRDKdgqlkvadknqlrLLRTR 93
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKST---VVALLENfyqPQGGQVLLDGKPISQYEHK-------------YLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 94 LTMVFQHFNLWSHmTVLENVMEAPIQVlglSKQEARERAVKYLAKVGIDERQQVKYP------VHLSGGQQQRVSIARAL 167
Cdd:cd03248 90 VSLVGQEPVLFAR-SLQDNIAYGLQSC---SFECVKEAAQKAHAHSFISELASGYDTevgekgSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709668069 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKI 230
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-239 |
3.73e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.45 E-value: 3.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 20 VLKGVSLQAKAGDVISIIGSSGSGKSTflrCINFLE---KPSEGTIVVSGQNIglvrdkdgqlkvaDKNQLRLLRTRLTM 96
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQnlyQPTGGQVLLDGVPL-------------VQYDHHYLHRQVAL 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 97 VFQHFNLWSHmTVLENVmeapiqVLGLS---KQEARERAVKYLAKVGIDERQQVKYPV------HLSGGQQQRVSIARAL 167
Cdd:TIGR00958 560 VGQEPVLFSG-SVRENI------AYGLTdtpDEEIMAAAKAANAHDFIMEFPNGYDTEvgekgsQLSGGQKQRIAIARAL 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709668069 168 AMEPEVLLFDEPTSALDpelvGEVLRIMQQLAE-EGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGHPDAL 239
Cdd:TIGR00958 633 VRKPRVLILDEATSALD----AECEQLLQESRSrASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-234 |
4.67e-16 |
|
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: 74.74 E-value: 4.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvaDKN 85
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPW-------------TRK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRllrtRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEAREraVKYLAKVGIDERQQVKypvHLSGGQQQRVSIAR 165
Cdd:TIGR03740 68 DLH----KIGSLIESPPLYENLTAREN-LKVHTTLLGLPDSRIDE--VLNIVDLTNTGKKKAK---QFSLGMKQRLGIAI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
Cdd:TIGR03740 138 ALLNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQG 206
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-237 |
5.36e-16 |
|
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: 74.10 E-value: 5.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLE--KPSEGTIVVSGQNIGlvrdkdgQLKVAD 83
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDIT-------DLPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 84 KNqlrllRTRLTMVFQHfnlwshmtvlenvmeaPIQVLGLSKQEareravkYLAKVGiderqqvkypVHLSGGQQQRVSI 163
Cdd:cd03217 74 RA-----RLGIFLAFQY----------------PPEIPGVKNAD-------FLRYVN----------EGFSGGEKKRNEI 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709668069 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIF-LHQGKIEEEGHPD 237
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHvLYDGRIVKSGDKE 190
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
151-234 |
5.78e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.09 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKI 230
Cdd:PLN03130 739 VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMI 817
|
....
gi 1709668069 231 EEEG 234
Cdd:PLN03130 818 KEEG 821
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
153-237 |
7.18e-16 |
|
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: 76.71 E-value: 7.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvGE--VLRIMQQLAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKI 230
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDE--GEaaLAAAIRALKARGATVVVITHRPSLLAAV-DKLLVLRDGRV 544
|
....*..
gi 1709668069 231 EEEGHPD 237
Cdd:COG4618 545 QAFGPRD 551
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-248 |
1.79e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.39 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLvrdkdgqLKVADKn 85
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISL-------LPLHAR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 qlrlLRTRLTMVFQHFNLWSHMTVLENVMeAPIQVL-GLSKQEARERAVKYLAKVGIDERQQvKYPVHLSGGQQQRVSIA 164
Cdd:PRK10895 76 ----ARRGIGYLPQEASIFRRLSVYDNLM-AVLQIRdDLSAEQREDRANELMEEFHIEHLRD-SMGQSLSGGERRRVEIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPK 244
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
....
gi 1709668069 245 SPRL 248
Cdd:PRK10895 230 VKRV 233
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-230 |
2.44e-15 |
|
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: 73.14 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 12 HKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQniglvrdkdgqlkVADKNQLRLLR 91
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-------------VPWKRRKKFLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 92 tRLTMVF-QHFNLWSHMTVLE--NVMEApiqVLGLSKQEARERaVKYLAKVgIDERQQVKYPV-HLSGGQQQRVSIARAL 167
Cdd:cd03267 95 -RIGVVFgQKTQLWWDLPVIDsfYLLAA---IYDLPPARFKKR-LDELSEL-LDLEELLDTPVrQLSLGQRMRAEIAAAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709668069 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVT-HEMGFARHVSSHVIFLHQGKI 230
Cdd:cd03267 169 LHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTsHYMKDIEALARRVLVIDKGRL 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
13-237 |
5.07e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.31 E-value: 5.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 13 KRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPS---EGTIVVSGQNIGLvrdkdgqlkvadknqlRL 89
Cdd:TIGR00955 33 RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDA----------------KE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 90 LRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLG--LSKQEARERAVKYLAKVGI----DERQQVKYPVH-LSGGQQQRVS 162
Cdd:TIGR00955 97 MRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPrrVTKKEKRERVDEVLQALGLrkcaNTRIGVPGRVKgLSGGERKRLA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEmgfarhVSS-------HVIFLHQGKIEEEGH 235
Cdd:TIGR00955 177 FASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQ------PSSelfelfdKIILMAEGRVAYLGS 250
|
..
gi 1709668069 236 PD 237
Cdd:TIGR00955 251 PD 252
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-242 |
5.18e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.93 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdGQLKVADKN 85
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC-------ARLTPAKAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLrtrltMVFQHFNLWSHMTVLENVMeapiqvLGLSKQEARERAVKYLAKvgideRQQVKYPVHLSGG-----QQQR 160
Cdd:PRK15439 85 QLGIY-----LVPQEPLLFPNLSVKENIL------FGLPKRQASMQKMKQLLA-----ALGCQLDLDSSAGslevaDRQI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIeeeghpdALF 240
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI-------ALS 221
|
..
gi 1709668069 241 GA 242
Cdd:PRK15439 222 GK 223
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
152-229 |
8.21e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 69.40 E-value: 8.21e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709668069 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLRimQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
Cdd:cd03221 70 QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI-EALE--EALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
129-253 |
8.69e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 72.53 E-value: 8.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 129 RERAVKYLAKVGIDERQQV--KYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTM 205
Cdd:PRK15093 133 KRRAIELLHRVGIKDHKDAmrSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTI 212
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1709668069 206 VVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFGAPKSPRLQQFLK 253
Cdd:PRK15093 213 LLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQALIR 260
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-239 |
9.44e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.46 E-value: 9.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 21 LKGVSLQAKAGDVISIIGSSGSGKSTFlrcINFLEK---PSEGTIVVSGQNIGLVrdkdgqlkvadknQLRLLRTRLTMV 97
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRvfdPQSGRILIDGTDIRTV-------------TRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 98 FQHFNLWSHmTVLENvmeapiqvLGLSKQEARE----RAVKYLAKVGIDERQQVKYPVH-------LSGGQQQRVSIARA 166
Cdd:PRK13657 415 FQDAGLFNR-SIEDN--------IRVGRPDATDeemrAAAERAQAHDFIERKPDGYDTVvgergrqLSGGERQRLAIARA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709668069 167 LAMEPEVLLFDEPTSALDPELvgEVlRIMQQLAE--EGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGHPDAL 239
Cdd:PRK13657 486 LLKDPPILILDEATSALDVET--EA-KVKAALDElmKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDEL 556
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-236 |
1.02e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 70.52 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 3 DNKLNVIDLHKRYGEH--EVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCI-NFLEkPSEGTIVVSGQNIGLVrdkdgql 79
Cdd:cd03369 4 HGEIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALfRFLE-AEEGKIEIDGIDISTI------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 80 kvadknQLRLLRTRLTMVFQHFNLWSHmTVLENV----MEAPIQVLG-LSKQEAREravkylakvgiderqqvkypvHLS 154
Cdd:cd03369 76 ------PLEDLRSSLTIIPQDPTLFSG-TIRSNLdpfdEYSDEEIYGaLRVSEGGL---------------------NLS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRimqqlaEE--GKTMVVVTHEMG----FARhvsshVIFL 225
Cdd:cd03369 128 QGQRQLLCLARALLKRPRVLVLDEATASIDYAtdaLIQKTIR------EEftNSTILTIAHRLRtiidYDK-----ILVM 196
|
250
....*....|.
gi 1709668069 226 HQGKIEEEGHP 236
Cdd:cd03369 197 DAGEVKEYDHP 207
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
79-253 |
1.54e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.86 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 79 LKVADKNQLRLLRTRLTMVFQHFNlwSHMTVLENVMEAPIQVLGLS---------KQEARERAVKYLAKVGIDERQQV-- 147
Cdd:COG4170 76 LKLSPRERRKIIGREIAMIFQEPS--SCLDPSAKIGDQLIEAIPSWtfkgkwwqrFKWRKKRAIELLHRVGIKDHKDImn 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 148 KYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLH 226
Cdd:COG4170 154 SYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILlISHDLESISQWADTITVLY 233
|
170 180
....*....|....*....|....*..
gi 1709668069 227 QGKIEEEGHPDALFGAPKSPRLQQFLK 253
Cdd:COG4170 234 CGQTVESGPTEQILKSPHHPYTKALLR 260
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-210 |
3.86e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 68.92 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDGQlKVADKN 85
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE-NILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 QLRLLRTRLTmvfqhfnlwshmtVLENvmeapIQVLGLSKQEARERAVKYLAKVGIDERQQVkyPVH-LSGGQQQRVSIA 164
Cdd:TIGR01189 80 HLPGLKPELS-------------ALEN-----LHFWAAIHGGAQRTIEDALAAVGLTGFEDL--PAAqLSAGQQRRLALA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1709668069 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTH 210
Cdd:TIGR01189 140 RLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-238 |
5.16e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.97 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNK--LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDgq 78
Cdd:PRK10247 1 MQENSplLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 79 lkvadknqlrlLRTRLTMVFQHFNLWSHmTVLENVMeAPIQVLGlsKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQ 158
Cdd:PRK10247 79 -----------YRQQVSYCAQTPTLFGD-TVYDNLI-FPWQIRN--QQPDPAIFLDDLERFALPDTILTKNIAELSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHvSSHVIFL--HQGKIEEEGH 235
Cdd:PRK10247 144 QRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwVTHDKDEINH-ADKVITLqpHAGEMQEARY 222
|
...
gi 1709668069 236 PDA 238
Cdd:PRK10247 223 ELA 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
153-233 |
6.47e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.97 E-value: 6.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
.
gi 1709668069 233 E 233
Cdd:PRK09700 490 I 490
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
144-210 |
9.27e-14 |
|
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: 67.18 E-value: 9.27e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 144 RQQVKYPVH--LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGevlRIMQQLAEEGKTMVVVTH 210
Cdd:cd03223 81 REQLIYPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED---RLYQLLKELGITVISVGH 146
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
152-257 |
1.32e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.81 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGE---VLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHqg 228
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLD---IYQrlnVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILY-- 286
|
90 100 110
....*....|....*....|....*....|....
gi 1709668069 229 kieeeGHPDAlFG---APKSPR--LQQFLKGSLK 257
Cdd:COG1245 287 -----GEPGV-YGvvsKPKSVRvgINQYLDGYLP 314
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
6-239 |
1.57e-13 |
|
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: 69.77 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYG-EHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRC-INFLEkPSEGTIVVSGQNIglvrdkdgqlKVAD 83
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLlVGFFQ-ARSGEILLNGFSL----------KDID 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 84 KNQLRLLrtrLTMVFQHFNLWSHmTVLENVMeapIQVLGLSKQEARERAVKyLAKVGID-ERQQVKYPVHL-------SG 155
Cdd:TIGR01193 543 RHTLRQF---INYLPQEPYIFSG-SILENLL---LGAKENVSQDEIWAACE-IAEIKDDiENMPLGYQTELseegssiSG 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGH 235
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGS 691
|
....
gi 1709668069 236 PDAL 239
Cdd:TIGR01193 692 HDEL 695
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
153-247 |
1.64e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.45 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGevlRIMQQLAEE--GKTMVVVTHEMGFARHvsshviflHQGKI 230
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEA---ALYQLLREElpGTTVISVGHRSTLAAF--------HDRVL 554
|
90
....*....|....*..
gi 1709668069 231 EEEGHPDALFGAPKSPR 247
Cdd:COG4178 555 ELTGDGSWQLLPAEAPA 571
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-243 |
1.82e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 69.36 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 17 EHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvadkNQLRL--LRTRL 94
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL---------------TKLQLdsWRSRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 95 TMVFQHFNLWSHmTVLENVmeapiqVLGL--SKQEARERAVK--------------YLAKVGidERQqvkypVHLSGGQQ 158
Cdd:PRK10789 392 AVVSQTPFLFSD-TVANNI------ALGRpdATQQEIEHVARlasvhddilrlpqgYDTEVG--ERG-----VMLSGGQK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGfARHVSSHVIFLHQGKIEEEGHPDA 238
Cdd:PRK10789 458 QRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQ 535
|
....*
gi 1709668069 239 LFGAP 243
Cdd:PRK10789 536 LAQQS 540
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-213 |
2.24e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.99 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 18 HEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCInflekpsegtivvsgqnIGLVRDKDGQLKVADKNQLRLLRTRL-TM 96
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKAL-----------------MGFVRLASGKISILGQPTRQALQKNLvAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 97 VFQHFNL-WSHMTVLENVME----APIQVLGLSKQEARERAVKYLAKVGIDERQQVKYPvHLSGGQQQRVSIARALAMEP 171
Cdd:PRK15056 83 VPQSEEVdWSFPVLVEDVVMmgryGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIG-ELSGGQKKRVFLARAIAQQG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1709668069 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMG 213
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLG 203
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
151-240 |
3.00e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.23 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSShVIFLHQGKI 230
Cdd:PLN03232 739 VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDR-IILVSEGMI 817
|
90
....*....|
gi 1709668069 231 EEEGHPDALF 240
Cdd:PLN03232 818 KEEGTFAELS 827
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
120-233 |
3.12e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 120 VLGLS-KQEARERAVKYLAKVGI-----DERQQV---------KYPVH------LSGGQQQRVSIARALAMEPEVLLFDE 178
Cdd:PRK10762 342 VLGMSvKENMSLTALRYFSRAGGslkhaDEQQAVsdfirlfniKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDE 421
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1709668069 179 PTSALDpelVG---EVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
Cdd:PRK10762 422 PTRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGE 476
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-210 |
3.73e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.52 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 14 RYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCInflekpsegtivvsgqnIGLVRDKDGQLKVadknqlrllrtr 93
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL-----------------AGALKGTPVAGCV------------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 94 ltmVFQHFNLWSHMTVLENVmeapiqvlgLSKQEARErAVKYLAKVGIDERQQVKYPV-HLSGGQQQRVSIARALAMEPE 172
Cdd:COG2401 90 ---DVPDNQFGREASLIDAI---------GRKGDFKD-AVELLNAVGLSDAVLWLRRFkELSTGQKFRFRLALLLAERPK 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1709668069 173 VLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTH 210
Cdd:COG2401 157 LLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATH 195
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-236 |
5.32e-13 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 65.98 E-value: 5.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 14 RYGEHE--VLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRdkdgqlkvadknqLRLLR 91
Cdd:cd03244 11 RYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG-------------LHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 92 TRLTMVFQHFNLWSHmTVLENVmeAPiqvLGLSKQEARERAvkyLAKVGIDERQQVK-----YPV-----HLSGGQQQRV 161
Cdd:cd03244 78 SRISIIPQDPVLFSG-TIRSNL--DP---FGEYSDEELWQA---LERVGLKEFVESLpggldTVVeeggeNLSVGQRQLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 162 SIARALAMEPEVLLFDEPTSALDPELVgevlRIMQQLAEE---GKTMVVVTHE----MGFARhvsshVIFLHQGKIEEEG 234
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETD----ALIQKTIREafkDCTVLTIAHRldtiIDSDR-----ILVLDKGRVVEFD 219
|
..
gi 1709668069 235 HP 236
Cdd:cd03244 220 SP 221
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
119-239 |
7.60e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 67.07 E-value: 7.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 119 QVLGLSKQEARERAVKYLAKVGIDE---RQQVKYpvhlSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIM 195
Cdd:NF000106 112 R*LDLSRKDARARADELLERFSLTEaagRAAAKY----SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV 187
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1709668069 196 QQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDAL 239
Cdd:NF000106 188 RSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
152-230 |
1.79e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.49 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVG---EVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
..
gi 1709668069 229 KI 230
Cdd:PRK13549 482 KL 483
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
153-239 |
1.83e-12 |
|
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: 66.38 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEE 232
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAHRLSTIVD-ADEILVLEAGRIVE 572
|
....*..
gi 1709668069 233 EGHPDAL 239
Cdd:COG5265 573 RGTHAEL 579
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
153-231 |
2.11e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.39 E-value: 2.11e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
152-257 |
3.16e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 64.70 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHqgkie 231
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLY----- 213
|
90 100 110
....*....|....*....|....*....|
gi 1709668069 232 eeGHPDA--LFGAPKSPR--LQQFLKGSLK 257
Cdd:cd03236 214 --GEPGAygVVTLPKSVRegINEFLDGYLP 241
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-210 |
3.78e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.74 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 4 NKLNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRdkdgqlkvad 83
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 84 knqlrlLRTRLTMVfQHFN-LWSHMTVLENVmEAPIQVLGlskqEARERAVKYLAKVGIDERQQVKYPvHLSGGQQQRVS 162
Cdd:PRK13539 71 ------VAEACHYL-GHRNaMKPALTVAENL-EFWAAFLG----GEELDIAAALEAVGLAPLAHLPFG-YLSAGQKRRVA 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1709668069 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTH 210
Cdd:PRK13539 138 LARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
121-233 |
4.91e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 121 LGLSKQEARERAV--KYLAKVGI---DERQQVKypvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIM 195
Cdd:PRK15439 370 RGFWIKPARENAVleRYRRALNIkfnHAEQAAR---TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLI 446
|
90 100 110
....*....|....*....|....*....|....*...
gi 1709668069 196 QQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
Cdd:PRK15439 447 RSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGA 484
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-229 |
6.36e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNKLNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLR--CINFLEKPSEGTIVVSGQNI--GLVRDKD 76
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKvlSGVYPHGTYEGEIIFEGEELqaSNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 77 gqlkvadknqlrllRTRLTMVFQHFNLWSHMTVLENV-MEAPIQVLGLSKQEA-RERAVKYLAKVGIDerQQVKYPV-HL 153
Cdd:PRK13549 81 --------------RAGIAIIHQELALVKELSVLENIfLGNEITPGGIMDYDAmYLRAQKLLAQLKLD--INPATPVgNL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709668069 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
Cdd:PRK13549 145 GLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
151-234 |
7.74e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.19 E-value: 7.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElVGEvlRIMQQL---AEEGKTMVVVTHEMgfarHV---SSHVIF 224
Cdd:PTZ00243 781 VNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH-VGE--RVVEECflgALAGKTRVLATHQV----HVvprADYVVA 853
|
90
....*....|
gi 1709668069 225 LHQGKIEEEG 234
Cdd:PTZ00243 854 LGDGRVEFSG 863
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-210 |
7.88e-12 |
|
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: 62.51 E-value: 7.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 16 GEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDGQ--LKVADKNQLRllrTR 93
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARglLYLGHAPGIK---TT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 94 LTmVFQHFNLWSHMTVLENVMEApiqvlglskqeareravkyLAKVGIDERQQVkyPVH-LSGGQQQRVSIARALAMEPE 172
Cdd:cd03231 88 LS-VLENLRFWHADHSDEQVEEA-------------------LARVGLNGFEDR--PVAqLSAGQQRRVALARLLLSGRP 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 1709668069 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTH 210
Cdd:cd03231 146 LWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
128-230 |
8.96e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.50 E-value: 8.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 128 ARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVV 207
Cdd:PLN03073 320 AEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIV 396
|
90 100
....*....|....*....|...
gi 1709668069 208 VTHEMGFARHVSSHVIFLHQGKI 230
Cdd:PLN03073 397 VSHAREFLNTVVTDILHLHGQKL 419
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
106-239 |
9.25e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 64.48 E-value: 9.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 106 HMTVLENVMeapiqvlgLSKQEARERAVKY-LAKVGIDE-----RQQVKYPVH-----LSGGQQQRVSIARALAMEPEVL 174
Cdd:PRK11174 436 HGTLRDNVL--------LGNPDASDEQLQQaLENAWVSEflpllPQGLDTPIGdqaagLSVGQAQRLALARALLQPCQLL 507
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709668069 175 LFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGHPDAL 239
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAEL 570
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
6-215 |
9.73e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.51 E-value: 9.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKdgqlkvadkn 85
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 qlrllrtrltmvFQHFNLW--------SHMTVLENVMEApiqvLGLSKQEARERAVKYLAKVGIDERQQVkyPVH-LSGG 156
Cdd:PRK13538 72 ------------YHQDLLYlghqpgikTELTALENLRFY----QRLHGPGDDEALWEALAQVGLAGFEDV--PVRqLSAG 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709668069 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKtMVVVT--HEMGFA 215
Cdd:PRK13538 134 QQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGG-MVILTthQDLPVA 193
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
151-240 |
1.43e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.20 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElVGE-----VLRIMQQLAeeGKTMVVVTHEMGFARHVSShVIFL 225
Cdd:TIGR00957 759 VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH-VGKhifehVIGPEGVLK--NKTRILVTHGISYLPQVDV-IIVM 834
|
90
....*....|....*
gi 1709668069 226 HQGKIEEEGHPDALF 240
Cdd:TIGR00957 835 SGGKISEMGSYQELL 849
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
152-257 |
1.53e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGE---VLRIMQQLAeEGKTMVVVTHEMGFARHVSS--HVIFlh 226
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD---IRQrlnVARLIRELA-EGKYVLVVEHDLAVLDYLADnvHIAY-- 285
|
90 100 110
....*....|....*....|....*....|....*
gi 1709668069 227 qgkieeeGHPDA--LFGAPKSPR--LQQFLKGSLK 257
Cdd:PRK13409 286 -------GEPGAygVVSKPKGVRvgINEYLKGYLP 313
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
10-211 |
1.60e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.75 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 10 DLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCI-------NFlekpsEGTIVVSGQNIGlvrdkdgqlkva 82
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALagriqgnNF-----TGTILANNRKPT------------ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 83 dKNQLRllrtRLTMVFQHFNLWSHMTVLENVMEAPIQVL--GLSKQEARERAVKYLAKVGIDERQQV----KYPVHLSGG 156
Cdd:PLN03211 136 -KQILK----RTGFVTQDDILYPHLTVRETLVFCSLLRLpkSLTKQEKILVAESVISELGLTKCENTiignSFIRGISGG 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1709668069 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
Cdd:PLN03211 211 ERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
44-224 |
2.00e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.89 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCINFLEKPSEGTivvSGQNIGLVRDK-----DGqLKVADKNqLRLLRTRLTMVFQHFNLWShMTVLENVMeapi 118
Cdd:PTZ00265 1248 QNVGMKNVNEFSLTKEGG---SGEDSTVFKNSgkillDG-VDICDYN-LKDLRNLFSIVSQEPMLFN-MSIYENIK---- 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 119 qvlgLSKQEARERAVKYLAK-VGIDERQQV----------KYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP-- 185
Cdd:PTZ00265 1318 ----FGKEDATREDVKRACKfAAIDEFIESlpnkydtnvgPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSns 1393
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1709668069 186 -ELVGEVLRIMQQLAEegKTMVVVTHEMGFARHVSSHVIF 224
Cdd:PTZ00265 1394 eKLIEKTIVDIKDKAD--KTIITIAHRIASIKRSDKIVVF 1431
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
151-217 |
2.40e-11 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 61.58 E-value: 2.40e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMGFARH 217
Cdd:cd03290 139 INLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH 207
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-234 |
2.75e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 61.62 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVisiigssgsgKSTFLRCI--NFLEKPSEGTIVVSGQNIGlvrdkdgQLKVAD 83
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVhaimgpngsgKSTLAKVLmgHPKYEVTSGSILLDGEDIL-------ELSPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 84 knqlrllRTR--LTMVFQH---------FNLWshMTVLENVMEAPIqvlglSKQEARERAVKYLAKVGIDE----Rqqvk 148
Cdd:COG0396 74 -------RARagIFLAFQYpveipgvsvSNFL--RTALNARRGEEL-----SAREFLKLLKEKMKELGLDEdfldR---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 149 yPVH--LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVS-SHVIFL 225
Cdd:COG0396 136 -YVNegFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIKpDFVHVL 214
|
....*....
gi 1709668069 226 HQGKIEEEG 234
Cdd:COG0396 215 VDGRIVKSG 223
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
127-212 |
2.76e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.88 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 127 EARERAV--KYLAKVGI---DERQQVkypVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVG---EVLRIMQQL 198
Cdd:NF040905 377 ENEEIKVaeEYRKKMNIktpSVFQKV---GNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID---VGakyEIYTIINEL 450
|
90
....*....|....
gi 1709668069 199 AEEGKTMVVVTHEM 212
Cdd:NF040905 451 AAEGKGVIVISSEL 464
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-229 |
2.78e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.82 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 21 LKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDGqlkvadknqlrlLRTRLTMVFQH 100
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA------------LENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 101 FNLWSHMTVLENVMEAPIQVLGL----SKQEARERAVKYLAKVGIDERQQVkypVHLSGGQQQRVSIARALAMEPEVLLF 176
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRYPTKGMfvdqDKMYRDTKAIFDELDIDIDPRAKV---ATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1709668069 177 DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
44-223 |
4.10e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 61.27 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCINFLEKPSEGTIVVSGQNIGLvrdKDGQLKVADKNQLRLLRTRLTMVFQHFNLWShmtvlENVMEaPIQVLGL 123
Cdd:cd03237 38 KTTFIKMLAGVLKPDEGDIEIELDTVSY---KPQYIKADYEGTVRDLLSSITKDFYTHPYFK-----TEIAK-PLQIEQI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 124 SKQEAREravkylakvgiderqqvkypvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEG- 202
Cdd:cd03237 109 LDREVPE----------------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNe 166
|
170 180
....*....|....*....|.
gi 1709668069 203 KTMVVVTHEMGFARHVSSHVI 223
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRLI 187
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
132-257 |
6.16e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 59.51 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 132 AVKYLAKVGIDERQQVKYP----------VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE 201
Cdd:cd03222 41 AVKILAGQLIPNGDNDEWDgitpvykpqyIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709668069 202 G-KTMVVVTHEMGFARHVSSHVIFLhqgkieeEGHP--DALFGAPKSPR--LQQFLKGSLK 257
Cdd:cd03222 121 GkKTALVVEHDLAVLDYLSDRIHVF-------EGEPgvYGIASQPKGTRegINRFLRGYLI 174
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
153-251 |
6.62e-11 |
|
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: 61.98 E-value: 6.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvGE--VLRIMQQLAEEGKTMVVVTHEMGfARHVSSHVIFLHQGKI 230
Cdd:TIGR01842 455 LSGGQRQRIALARALYGDPKLVVLDEPNSNLDEE--GEqaLANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
90 100
....*....|....*....|.
gi 1709668069 231 eeeghpdALFGaPKSPRLQQF 251
Cdd:TIGR01842 532 -------ARFG-ERDEVLAKL 544
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
147-212 |
9.90e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 9.90e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709668069 147 VKYPVH------LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM 212
Cdd:PRK10982 380 VKTPGHrtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEM 451
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
125-238 |
1.37e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.70 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 125 KQEArERAVKYLAKVGI---DERQQVkypVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVG---EVLRIMQQL 198
Cdd:PRK11288 370 RWEA-ENADRFIRSLNIktpSREQLI---MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID---VGakhEIYNVIYEL 442
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1709668069 199 AEEGKTMVVVTHE----MGfarhVSSHVIFLHQGKIEEE-GHPDA 238
Cdd:PRK11288 443 AAQGVAVLFVSSDlpevLG----VADRIVVMREGRIAGElAREQA 483
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
126-231 |
1.65e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.57 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 126 QEARERAVKYLAKVGIDERQQVKYpVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTM 205
Cdd:NF040905 114 NETNRRARELLAKVGLDESPDTLV-TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITS 192
|
90 100
....*....|....*....|....*..
gi 1709668069 206 VVVTHEMGFARHVSSHVIFLHQGK-IE 231
Cdd:NF040905 193 IIISHKLNEIRRVADSITVLRDGRtIE 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-229 |
2.32e-10 |
|
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: 60.22 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 13 KRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLR--CINFLEKPSEGTIVVSGQNIGL--VRDKDgqlkvadknqlr 88
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKilSGVYPHGTWDGEIYWSGSPLKAsnIRDTE------------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 89 llRTRLTMVFQHFNLWSHMTVLENV-MEAPIQVLG--LSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIAR 165
Cdd:TIGR02633 77 --RAGIVIIHQELTLVPELSVAENIfLGNEITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709668069 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-230 |
2.74e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 59.33 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 11 LHKRYGEHEVLKGVSLQAK------------AGdvisiigssgsgKSTFLRCINFLEKPSEGTIVVSGqniglvrdkdgq 78
Cdd:COG4586 28 FRREYREVEAVDDISFTIEpgeivgfigpngAG------------KSTTIKMLTGILVPTSGEVRVLG------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 79 lKVADKNQLRLLRtRLTMVF-QHFNLWSHMTVLE--NVMEApiqVLGLSKQEARERaVKYLAKV-GIDE--RQQVKypvH 152
Cdd:COG4586 84 -YVPFKRRKEFAR-RIGVVFgQRSQLWWDLPAIDsfRLLKA---IYRIPDAEYKKR-LDELVELlDLGEllDTPVR---Q 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDP---ELVGEVLRIMQQlaEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
Cdd:COG4586 155 LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVvskEAIREFLKEYNR--ERGTTILLTSHDMDDIEALCDRVIVIDHGR 232
|
.
gi 1709668069 230 I 230
Cdd:COG4586 233 I 233
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
44-237 |
4.66e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 58.31 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCINFLEkPSEGTIVVSGQNIGlvrdkdgQLKVAdknQLRLLRTRLTmvfQHFNLWSHMTVLenvmeapiQVLGL 123
Cdd:COG4138 35 KSTLLARMAGLL-PGQGEILLNGRPLS-------DWSAA---ELARHRAYLS---QQQSPPFAMPVF--------QYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 124 SKQ-----EARERAVKYLA-KVGIDErqqvKYP---VHLSGGQQQRVSIARAL-----AMEPE--VLLFDEPTSALDPEL 187
Cdd:COG4138 93 HQPagassEAVEQLLAQLAeALGLED----KLSrplTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1709668069 188 VGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPD 237
Cdd:COG4138 169 QAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
151-239 |
8.39e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.49 E-value: 8.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvGEvlRIMQQLAEE---GKTMVVVTHEMGFARHvSSHVIFLHQ 227
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALDTE--SE--RAIQAALDElqkNRTSLVIAHRLSTIEK-ADEILVVED 553
|
90
....*....|...
gi 1709668069 228 GKIEEEG-HPDAL 239
Cdd:PRK11176 554 GEIVERGtHAELL 566
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
153-253 |
1.40e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVI-FlhQGKI 230
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLMvF--EGEP 531
|
90 100
....*....|....*....|....*
gi 1709668069 231 EEEGHPDalfgAPKSPR--LQQFLK 253
Cdd:PRK13409 532 GKHGHAS----GPMDMRegMNRFLK 552
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
44-253 |
1.62e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.87 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCINFLEKPSEGTIvvsgqniglvrdkDGQLKVADKNQLrlLRTRltmvfqhfnlwSHMTVLENVMEAPIQVLGL 123
Cdd:COG1245 379 KTTFAKILAGVLKPDEGEV-------------DEDLKISYKPQY--ISPD-----------YDGTVEEFLRSANTDDFGS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 124 SKqeARERAVKYLakvGIDE--RQQVKypvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE 201
Cdd:COG1245 433 SY--YKTEIIKPL---GLEKllDKNVK---DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEN 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1709668069 202 -GKTMVVVTHEMGFARHVSSHVI-FLhqGKIEEEGHPDalfgAPKSPR--LQQFLK 253
Cdd:COG1245 505 rGKTAMVVDHDIYLIDYISDRLMvFE--GEPGVHGHAS----GPMDMRegMNRFLK 554
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
99-239 |
2.24e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.44 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 99 QHFNLWSHMTVLEN-VMEApiQVLGLSKQEARERAVKYLAKVGIDERQQVKyPVHLSGGQQQRVSIARALAMEPEVLLFD 177
Cdd:NF033858 346 QAFSLYGELTVRQNlELHA--RLFHLPAAEIAARVAEMLERFDLADVADAL-PDSLPLGIRQRLSLAVAVIHKPELLILD 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709668069 178 EPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFA----RhVSshviFLHQGKIEEEGHPDAL 239
Cdd:NF033858 423 EPTSGVDPVARDMFWRLLIELSrEDGVTIFISTHFMNEAercdR-IS----LMHAGRVLASDTPAAL 484
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
152-236 |
2.34e-09 |
|
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: 57.25 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGkie 231
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRG--- 234
|
....*
gi 1709668069 232 eEGHP 236
Cdd:TIGR03719 235 -RGIP 238
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-230 |
5.25e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.19 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLH-KRYGEHEVLKGVSLQAKAGDVisiigssgsgkSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdGQLKVADK 84
Cdd:COG3845 258 LEVENLSvRDDRGVPALKDVSLEVRAGEIlgiagvagngqSELAEALAGLRPPASGSIRLDGEDI-------TGLSPRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 85 NQLRLLRT---RLTM-VFQHFNLWSHMtVLENVMEAPIQVLG-LSKQEARERAVKYLAKVGI---DERQQVKypvHLSGG 156
Cdd:COG3845 331 RRLGVAYIpedRLGRgLVPDMSVAENL-ILGRYRRPPFSRGGfLDRKAIRAFAEELIEEFDVrtpGPDTPAR---SLSGG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709668069 157 QQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQL---AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLD---VGAIEFIHQRLlelRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
129-230 |
7.21e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.79 E-value: 7.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 129 RERAVKYLAKVGIDERQqVKYPVH-LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKT-MV 206
Cdd:PRK10938 378 QKLAQQWLDILGIDKRT-ADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLL 456
|
90 100
....*....|....*....|....*
gi 1709668069 207 VVTHEMGFARHVSSH-VIFLHQGKI 230
Cdd:PRK10938 457 FVSHHAEDAPACITHrLEFVPDGDI 481
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-212 |
7.41e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 7.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 21 LKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGLVRDKDGQlkvadknqlrllRTRLTMVFQH 100
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQ------------EAGIGIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 101 FNLWSHMTVLENVM--EAPIQVLGLSK-QEARERAVKYLAKVGiderqqVKYPVH-----LSGGQQQRVSIARALAMEPE 172
Cdd:PRK10762 88 LNLIPQLTIAENIFlgREFVNRFGRIDwKKMYAEADKLLARLN------LRFSSDklvgeLSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1709668069 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM 212
Cdd:PRK10762 162 VIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRL 201
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
153-225 |
1.63e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 1.63e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSShvIFL 225
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLSTIRYANT--IFV 651
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
153-211 |
1.69e-08 |
|
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: 53.02 E-value: 1.69e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
Cdd:cd03232 109 LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQ 167
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-234 |
2.90e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.13 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 18 HEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQN--IGLVRDKDGQLkvadknqlrllrtrlt 95
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAalIAISSGLNGQL---------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 96 mvfqhfnlwshmTVLENVmEAPIQVLGLSKQEARERAVKYL--AKVGIDERQQVKYpvhLSGGQQQRVSIARALAMEPEV 173
Cdd:PRK13545 101 ------------TGIENI-ELKGLMMGLTKEKIKEIIPEIIefADIGKFIYQPVKT---YSSGMKSRLGFAISVHINPDI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709668069 174 LLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
Cdd:PRK13545 165 LVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYG 225
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
83-230 |
4.47e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.42 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 83 DKNQLRLlrTRLTMVFQHFNLWShmtvLENVMEAPIQVLGLSkqearerAVKYLAKvgiderqqvkypvhLSGGQQQRVS 162
Cdd:PRK11147 114 EKNLNEL--AKLQEQLDHHNLWQ----LENRINEVLAQLGLD-------PDAALSS--------------LSGGWLRKAA 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709668069 163 IARALAMEPEVLLFDEPTSALDPELVgEVLRimQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDIETI-EWLE--GFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
119-239 |
6.48e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 53.09 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 119 QVLGLSKQEARE---------RAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARAL---AMEPEVLLFDEPTSALDPE 186
Cdd:TIGR00630 787 DVLDMTVEEAYEffeavpsisRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFD 866
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 187 LVGEVLRIMQQLAEEGKTMVVVTHEMGFARhVSSHVIFL------HQGKIEEEGHPDAL 239
Cdd:TIGR00630 867 DIKKLLEVLQRLVDKGNTVVVIEHNLDVIK-TADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
119-212 |
7.47e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 51.85 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 119 QVLGLSKQEARE---------RAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARALAME---PEVLLFDEPTSALDPE 186
Cdd:cd03271 127 DVLDMTVEEALEffenipkiaRKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFH 206
|
90 100
....*....|....*....|....*.
gi 1709668069 187 LVGEVLRIMQQLAEEGKTMVVVTHEM 212
Cdd:cd03271 207 DVKKLLEVLQRLVDKGNTVVVIEHNL 232
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
153-209 |
1.04e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 50.72 E-value: 1.04e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVT 209
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS 175
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
152-210 |
1.99e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.27 E-value: 1.99e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQQLAEEGKTMVVVTH 210
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLEQFLHDYPGTVVAVTH 218
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
153-234 |
2.53e-07 |
|
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: 49.24 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPE--VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFL----- 225
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFgpgsg 166
|
90
....*....|
gi 1709668069 226 -HQGKIEEEG 234
Cdd:cd03238 167 kSGGKVVFSG 176
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
70-210 |
3.53e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.46 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 70 GLVRDKDGQLKVADKNQLRLLRTRLTMVFQHF-NLWSHMTVLENVMeapiQVLGLSKQEARERAVKYLAKVGIDERQQVK 148
Cdd:PRK13543 59 GLLHVESGQIQIDGKTATRGDRSRFMAYLGHLpGLKADLSTLENLH----FLCGLHGRRAKQMPGSALAIVGLAGYEDTL 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709668069 149 YPvHLSGGQQQRVSIARaLAMEPEVL-LFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTH 210
Cdd:PRK13543 135 VR-QLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-223 |
3.79e-07 |
|
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: 50.70 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 3 DNKLNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVsGQNIglvrdkdgqlKVA 82
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 83 DKNQLRLlrtrltmvfqhfNLWSHMTVLENVMEApIQVLGLSKQEARERAvkYLAKVGIDERQQVKYPVHLSGGQQQRVS 162
Cdd:TIGR03719 389 YVDQSRD------------ALDPNKTVWEEISGG-LDIIKLGKREIPSRA--YVGRFNFKGSDQQKKVGQLSGGERNRVH 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709668069 163 IARALAMEPEVLLFDEPTSALDPelvgEVLRIMQQ-LAEEGKTMVVVTHEMGFARHVSSHVI 223
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDV----ETLRALEEaLLNFAGCAVVISHDRWFLDRIATHIL 511
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-253 |
3.85e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.81 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 21 LKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIvvsgqniglvrDKDGQLKVADKNQlrllrtrltmvfqh 100
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------DRNGEVSVIAISA-------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 101 fNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYL--AKVGIDERQQVKypvHLSGGQQQRVSIARALAMEPEVLLFDE 178
Cdd:PRK13546 95 -GLSGQLTGIENI-EFKMLCMGFKRKEIKAMTPKIIefSELGEFIYQPVK---KYSSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709668069 179 PTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGHPDALFgapksPRLQQFLK 253
Cdd:PRK13546 170 ALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL-----PKYEAFLN 239
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
42-239 |
5.13e-07 |
|
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: 50.18 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 42 SGKSTFLRCINFLEKPSEGTIVVsgqniglvrdkDGQLkVADKNQLRlLRTRLTMVFQHFNLWSHmtvlenvmeapiqVL 121
Cdd:COG4615 369 SGKSTLAKLLTGLYRPESGEILL-----------DGQP-VTADNREA-YRQLFSAVFSDFHLFDR-------------LL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 122 GLSKQEARERAVKYLAKVGIDERQQVK----YPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP--------ELVG 189
Cdd:COG4615 423 GLDGEADPARARELLERLELDHKVSVEdgrfSTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPefrrvfytELLP 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1709668069 190 EvlrimqqLAEEGKTMVVVTH-EMGFarHVSSHVIFLHQGKIEEEGHPDAL 239
Cdd:COG4615 503 E-------LKARGKTVIAISHdDRYF--DLADRVLKMDYGKLVELTGPAAL 544
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
6-211 |
9.00e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.02 E-value: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIglvrDKDgqlkvadkn 85
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKD--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 86 qLRLLRTRLTMVFQHFNLWSHMTVLENVMEApiqvLGLSKqeareravkylAKVGIDE-------RQQVKYPVH-LSGGQ 157
Cdd:PRK13540 69 -LCTYQKQLCFVGHRSGINPYLTLRENCLYD----IHFSP-----------GAVGITElcrlfslEHLIDYPCGlLSSGQ 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1709668069 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
Cdd:PRK13540 133 KRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
115-231 |
1.66e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 115 EAPIQVLG-LSKQEARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelvgevLR 193
Cdd:PRK10636 392 ESPLQHLArLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD-------LD 464
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1709668069 194 IMQQLAE-----EGkTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
Cdd:PRK10636 465 MRQALTEalidfEG-ALVVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
15-184 |
1.98e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.80 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 15 YGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIvvsgqniglvrDKDGQLKVADKNQLRLLRTRL 94
Cdd:PRK09544 14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQKLYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 95 TMVFQHFnlwshMTVLENVMEAPIqvlglskQEARERavkylakvgIDERQQVKYPVH-LSGGQQQRVSIARALAMEPEV 173
Cdd:PRK09544 83 PLTVNRF-----LRLRPGTKKEDI-------LPALKR---------VQAGHLIDAPMQkLSGGETQRVLLARALLNRPQL 141
|
170
....*....|.
gi 1709668069 174 LLFDEPTSALD 184
Cdd:PRK09544 142 LVLDEPTQGVD 152
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
153-211 |
2.22e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 2.22e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLF-DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
Cdd:TIGR00956 902 LNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
43-211 |
2.76e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.04 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 43 GKSTFLRCINFLEKPSEGTIVVSGQNIglvrdkdgqlkvaDKNQLRLLRTRLTMVFQHFNLWSHMtvlenvmeapiqvLG 122
Cdd:PRK10522 361 GKSTLAMLLTGLYQPQSGEILLDGKPV-------------TAEQPEDYRKLFSAVFTDFHLFDQL-------------LG 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 123 LSKQEARERAV-KYLAKVGIDERQQVK----YPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR-IMQ 196
Cdd:PRK10522 415 PEGKPANPALVeKWLERLKMAHKLELEdgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQvLLP 494
|
170
....*....|....*
gi 1709668069 197 QLAEEGKTMVVVTHE 211
Cdd:PRK10522 495 LLQEMGKTIFAISHD 509
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
153-211 |
5.44e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 5.44e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
154-212 |
5.55e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 47.32 E-value: 5.55e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM 212
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSM 2130
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
153-228 |
7.23e-06 |
|
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: 44.67 E-value: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRI------MQQLAEEGKTMVVVTHEMGF-----ARHVSSH 221
Cdd:smart00382 61 GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrllLLLKSEKNLTVILTTNDEKDlgpalLRRRFDR 140
|
....*..
gi 1709668069 222 VIFLHQG 228
Cdd:smart00382 141 RIVLLLI 147
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
152-237 |
7.82e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 45.69 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 152 HLSGGQQQRVSIA-------RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIF 224
Cdd:PRK03695 126 QLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWL 205
|
90
....*....|...
gi 1709668069 225 LHQGKIEEEGHPD 237
Cdd:PRK03695 206 LKQGKLLASGRRD 218
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
153-225 |
8.20e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 8.20e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709668069 153 LSGGQQQRVSIARAL---AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARhVSSHVIFL 225
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYVLEL 884
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
153-242 |
9.03e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 46.25 E-value: 9.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPelvGEVLRIMQQLAE--EGKTMVVVTHEMGFARHVSShVIFLHQGKI 230
Cdd:PRK10790 477 LSVGQKQLLALARVLVQTPQILILDEATANIDS---GTEQAIQQALAAvrEHTTLVVIAHRLSTIVEADT-ILVLHRGQA 552
|
90
....*....|..
gi 1709668069 231 EEEGHPDALFGA 242
Cdd:PRK10790 553 VEQGTHQQLLAA 564
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
150-210 |
1.24e-05 |
|
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: 45.46 E-value: 1.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709668069 150 PVHLSGGQQQ---RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTH 210
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
100-209 |
1.59e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 100 HFnlwSHMTVLENV-----MEAP-IQVLGLSKQEARERAVKYLA-----------KVGIDERQQVkypvhlSGGQQQRVS 162
Cdd:TIGR00956 149 HF---PHLTVGETLdfaarCKTPqNRPDGVSREEYAKHIADVYMatyglshtrntKVGNDFVRGV------SGGERKRVS 219
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1709668069 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVT 209
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVA 266
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
153-212 |
1.99e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.40 E-value: 1.99e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709668069 153 LSGGQQQRVSIARALAMEPE---VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM 212
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNL 889
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-234 |
1.99e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.78 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 6 LNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLE--KPSEGTIVVSGQNIGLV--RDKDGQlkv 81
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELspEDRAGE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 82 adknqlrllrtRLTMVFQHfnlwshmtvlenvmeaPIQVLGLSKQEARERAV----KYLAKVGID----------ERQQV 147
Cdd:PRK09580 79 -----------GIFMAFQY----------------PVEIPGVSNQFFLQTALnavrSYRGQEPLDrfdfqdlmeeKIALL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 148 KYP---------VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHV 218
Cdd:PRK09580 132 KMPedlltrsvnVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYI 211
|
250
....*....|....*..
gi 1709668069 219 S-SHVIFLHQGKIEEEG 234
Cdd:PRK09580 212 KpDYVHVLYQGRIVKSG 228
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
130-208 |
2.11e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 130 ERAVKYLAKVGID---ERQqVKYpvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMV 206
Cdd:PRK10938 114 ARCEQLAQQFGITallDRR-FKY---LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLV 189
|
..
gi 1709668069 207 VV 208
Cdd:PRK10938 190 LV 191
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
128-230 |
2.12e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 128 ARERAVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPelvgEVLRIMQQ-LAEEGKTMV 206
Cdd:PRK15064 131 AEARAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI----NTIRWLEDvLNERNSTMI 206
|
90 100
....*....|....*....|....
gi 1709668069 207 VVTHEMGFARHVSSHVIFLHQGKI 230
Cdd:PRK15064 207 IISHDRHFLNSVCTHMADLDYGEL 230
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
153-236 |
2.21e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.82 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAM---------EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSSHV 222
Cdd:PRK13547 146 LSGGELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLaIVHDPNLAARHADRI 225
|
90
....*....|....
gi 1709668069 223 IFLHQGKIEEEGHP 236
Cdd:PRK13547 226 AMLADGAIVAHGAP 239
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-210 |
3.84e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.86 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 1 MSDNKLNVIDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCInfLEKPS----EGTIVVSGQNIglvrdkd 76
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--AGHPAykilEGDILFKGESI------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 77 GQLKVADKNQLRLLrtrltMVFQHfnlwshmtvlenvmeaPIQVLGLSKQEARERAV----KYLAKVGIDERQQVKY--- 149
Cdd:CHL00131 74 LDLEPEERAHLGIF-----LAFQY----------------PIEIPGVSNADFLRLAYnskrKFQGLPELDPLEFLEIine 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709668069 150 --------PVHL--------SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTH 210
Cdd:CHL00131 133 klklvgmdPSFLsrnvnegfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
152-242 |
3.90e-05 |
|
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: 44.55 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRimQQLaeEGKTMVVVTHE----MGFARhvsshVIF 224
Cdd:TIGR00957 1421 NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLEtdnLIQSTIR--TQF--EDCTVLTIAHRlntiMDYTR-----VIV 1491
|
90
....*....|....*...
gi 1709668069 225 LHQGKIEEEGHPDALFGA 242
Cdd:TIGR00957 1492 LDKGEVAEFGAPSNLLQQ 1509
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
153-223 |
4.16e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.40 E-value: 4.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLL--FDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVI 223
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVI 209
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
153-210 |
6.88e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 43.58 E-value: 6.88e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGevlRIMQQLAEEGKTMVVVTH 210
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG---YMYRLCREFGITLFSVSH 637
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
153-211 |
7.97e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 7.97e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709668069 153 LSGGQQQRVSIARALAMEPE--VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD 537
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-228 |
1.16e-04 |
|
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: 43.36 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 20 VLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGqniglvrdkdgqlkvadknqlrllrtRLTMVFQ 99
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--------------------------RISFSPQ 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 100 hFNLWSHMTVLENVmeapiqVLGLSKQEARERAVKYLAKVgidERQQVKYP-----------VHLSGGQQQRVSIARALA 168
Cdd:TIGR01271 495 -TSWIMPGTIKDNI------IFGLSYDEYRYTSVIKACQL---EEDIALFPekdktvlgeggITLSGGQRARISLARAVY 564
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709668069 169 MEPEVLLFDEPTSALDPELVGEVL-RIMQQLAEEgKTMVVVTHEMGFARHvSSHVIFLHQG 228
Cdd:TIGR01271 565 KDADLYLLDSPFTHLDVVTEKEIFeSCLCKLMSN-KTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
44-186 |
1.37e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 44 KSTFLRCINFLEKPSEGTIVVsGQNIglvrdkdgqlKVADKNQLRLlrtrltmvfqhfNLWSHMTVLENVMEApIQVLGL 123
Cdd:PRK11819 363 KSTLFKMITGQEQPDSGTIKI-GETV----------KLAYVDQSRD------------ALDPNKTVWEEISGG-LDIIKV 418
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709668069 124 SKQEARERAvkYLAKV---GIDERQQVKypvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE 186
Cdd:PRK11819 419 GNREIPSRA--YVGRFnfkGGDQQKKVG---VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
129-232 |
1.55e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 129 RERAVKYLAKVGIDErQQVKYPVH-LSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVV 207
Cdd:PRK10636 126 RSRAASLLHGLGFSN-EQLERPVSdFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLIL 201
|
90 100
....*....|....*....|....*
gi 1709668069 208 VTHEMGFARHVSSHVIFLHQGKIEE 232
Cdd:PRK10636 202 ISHDRDFLDPIVDKIIHIEQQSLFE 226
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-228 |
1.78e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 41.77 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 20 VLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGqniglvrdkdgqlkvadknqlrllrtRLTMVFQ 99
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--------------------------RISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 100 hFNLWSHMTVLENVmeapiqVLGLSKQEARERAVKYLAKVgidERQQVKYP-----------VHLSGGQQQRVSIARALA 168
Cdd:cd03291 106 -FSWIMPGTIKENI------IFGVSYDEYRYKSVVKACQL---EEDITKFPekdntvlgeggITLSGGQRARISLARAVY 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARhVSSHVIFLHQG 228
Cdd:cd03291 176 KDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLK-KADKILILHEG 234
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
153-210 |
1.91e-04 |
|
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: 40.81 E-value: 1.91e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709668069 153 LSGGQQQRVSIARALAME---PEVL-LFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTH 210
Cdd:cd03227 78 LSGGEKELSALALILALAslkPRPLyILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
154-239 |
2.46e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.03 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGK--TMVVVTHEMGFARHvSSHVIFLHQGKIE 231
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVD---VRTDALIQKTIREEFKscTMLIIAHRLNTIID-CDRILVLDAGRVV 1451
|
....*...
gi 1709668069 232 EEGHPDAL 239
Cdd:PLN03130 1452 EFDTPENL 1459
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
102-239 |
8.31e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.49 E-value: 8.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 102 NLWSHMTVLENvmeapIQ----VLGLSKQEARERAVKYLAKVGID---ERQQVKypvhLSGGQQQRVSIARALAMEPEVL 174
Cdd:NF033858 88 NLYPTLSVFEN-----LDffgrLFGQDAAERRRRIDELLRATGLApfaDRPAGK----LSGGMKQKLGLCCALIHDPDLL 158
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709668069 175 LFDEPTSALDP-------ELVGevlRIMQQlaEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGHPDAL 239
Cdd:NF033858 159 ILDEPTTGVDPlsrrqfwELID---RIRAE--RPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAEL 224
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
153-223 |
1.14e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.13 E-value: 1.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 153 LSGGQQQRVSIARALAMEP------EVLLFDEPTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHVsSHVI 223
Cdd:cd03240 116 CSGGEKVLASLIIRLALAEtfgsncGILALDEPTTNLDEENIEESLAeiIEERKSQKNFQLIVITHDEELVDAA-DHIY 193
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
153-210 |
1.63e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 1.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709668069 153 LSGGQQQRVSIARALAMEPE---VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTH 210
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEH 891
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
153-240 |
1.88e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.57 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQqlaEEGK--TMVVVTHEMGFARHVSShVIFLHQGKI 230
Cdd:PLN03232 1372 FSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR---EEFKscTMLVIAHRLNTIIDCDK-ILVLSSGQV 1447
|
90
....*....|
gi 1709668069 231 EEEGHPDALF 240
Cdd:PLN03232 1448 LEYDSPQELL 1457
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
153-210 |
1.96e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.40 E-value: 1.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709668069 153 LSGGQQQRVSIARALAMEPEV---------LLF-DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTH 210
Cdd:cd03279 124 LSGGETFLASLSLALALSEVLqnrggarleALFiDEGFGTLDPEALEAVATALELIRTENRMVGVISH 191
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
153-211 |
3.72e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.30 E-value: 3.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1709668069 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLriMQQLAEEGKTMVVVTHE 211
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAV-EAL--IQGLVLFQGGVLMVSHD 683
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
150-238 |
5.09e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 38.01 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 150 PVH-LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLRIMqqLAEEGKTMVVVTHEMGFARH-VSSHVIFLHQ 227
Cdd:PRK11147 437 PVKaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETL-ELLEEL--LDSYQGTVLLVSHDRQFVDNtVTECWIFEGN 513
|
90
....*....|...
gi 1709668069 228 GKIEE--EGHPDA 238
Cdd:PRK11147 514 GKIGRyvGGYHDA 526
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
84-223 |
5.76e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 37.67 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 84 KNQLRLLRTRLTMVFQHFNlwshmTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERQQVKYPVHLSG-GQQQRVS 162
Cdd:COG3593 98 EEALEELNEELKEALKALN-----ELLSEYLKELLDGLDLELELSLDELEDLLKSLSLRIEDGKELPLDRLGsGFQRLIL 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709668069 163 IARALAM-------EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHemgfarhvSSHVI 223
Cdd:COG3593 173 LALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH--------SPHLL 232
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
153-246 |
5.90e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 153 LSGGQQQRVSIARALAM---EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGK 229
Cdd:PRK00635 1700 LSLSEKIAIKIAKFLYLppkHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQ-ADYLIEMGPGS 1778
|
90
....*....|....*...
gi 1709668069 230 IEEEGHpdALF-GAPKSP 246
Cdd:PRK00635 1779 GKTGGK--ILFsGPPKDI 1794
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
126-245 |
6.45e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.69 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 126 QEARERaVKYLAKVGIDERQQVKYPVHLSGGQQQRVSIARALAMEPEVLLF--DEPTSALDPELVGEVLRIMQQLAEEGK 203
Cdd:TIGR00630 463 KEIRER-LGFLIDVGLDYLSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRDLGN 541
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1709668069 204 TMVVVTHEMGFARHvSSHVIFL------HQGKIEEEGHPDALFGAPKS 245
Cdd:TIGR00630 542 TLIVVEHDEDTIRA-ADYVIDIgpgageHGGEVVASGTPEEILANPDS 588
|
|
| Rad50_Sulf |
NF041034 |
DNA double-strand break repair ATPase Rad50; |
153-211 |
6.59e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 468963 [Multi-domain] Cd Length: 872 Bit Score: 37.77 E-value: 6.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709668069 153 LSGGQQ------QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
Cdd:NF041034 780 LSGGERisialaLRLAIAKSLMDEIGFMILDEPTVHLDEERKKELIDIIRSSMEIVPQIIVVTHD 844
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
9-187 |
7.28e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 37.45 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 9 IDLHKRYGEHEVLKGVSLQAKAGDVISIIGSSGSGKSTFLRCINFLEKPSEGTIVVSGQNIGlvrdkdgqlkvadKNQLR 88
Cdd:PTZ00243 1314 VQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG-------------AYGLR 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709668069 89 LLRTRLTMVFQHFNLWSHmTVLENV---MEA-------PIQVLGLSKQEARERAvkylakvGIDERQQ---VKYPVhlsg 155
Cdd:PTZ00243 1381 ELRRQFSMIPQDPVLFDG-TVRQNVdpfLEAssaevwaALELVGLRERVASESE-------GIDSRVLeggSNYSV---- 1448
|
170 180 190
....*....|....*....|....*....|...
gi 1709668069 156 GQQQRVSIARALAMEPE-VLLFDEPTSALDPEL 187
Cdd:PTZ00243 1449 GQRQLMCMARALLKKGSgFILMDEATANIDPAL 1481
|
|
| |
