|
Name |
Accession |
Description |
Interval |
E-value |
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-259 |
0e+00 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 512.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 1 MHDPRPVTLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHARG 80
Cdd:COG4598 1 MTDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 81 HRLAANPKQIERLRSRLGMVFQSFNLWSHMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQ 160
Cdd:COG4598 81 ELVPADRRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 161 QRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEA 240
Cdd:COG4598 161 QRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAE 240
|
250
....*....|....*....
gi 490999375 241 LFGAHGSPRFQQFISSHHQ 259
Cdd:COG4598 241 VFGNPKSERLRQFLSSSLK 259
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
9-255 |
6.32e-156 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 433.27 E-value: 6.32e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlAANPK 88
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-----------TDSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRSRLGMVFQSFNLWSHMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARA 168
Cdd:COG1126 71 DINKLRRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 169 LAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGAHGSP 248
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
....*..
gi 490999375 249 RFQQFIS 255
Cdd:COG1126 231 RTRAFLS 237
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
9-232 |
1.37e-129 |
|
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: 365.70 E-value: 1.37e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlaANPK 88
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-----------DDKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRSRLGMVFQSFNLWSHMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARA 168
Cdd:cd03262 70 NINELRQKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999375 169 LAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-255 |
1.77e-116 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 334.24 E-value: 1.77e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHARGHRLAANPK 88
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRSRLGMVFQSFNLWSHMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVGMLNR-KDFYPAQLSGGQQQRVAIAR 167
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 168 ALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGAHGS 247
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
....*...
gi 490999375 248 PRFQQFIS 255
Cdd:PRK10619 246 PRLQQFLK 253
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-254 |
4.79e-103 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 299.32 E-value: 4.79e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 13 DIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlaaNPKQIER 92
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN------------DPKVDER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 93 L-RSRLGMVFQSFNLWSHMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAM 171
Cdd:PRK09493 74 LiRQEAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 172 DPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGAHGSPRFQ 251
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQ 233
|
...
gi 490999375 252 QFI 254
Cdd:PRK09493 234 EFL 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
8-255 |
2.40e-102 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 298.20 E-value: 2.40e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 8 TLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHarghrLAANP 87
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARS-----LSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 KQIERLRSRLGMVFQSFNLWSHMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIAR 167
Cdd:PRK11264 78 GLIRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 168 ALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGAHGS 247
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
....*...
gi 490999375 248 PRFQQFIS 255
Cdd:PRK11264 238 PRTRQFLE 245
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
8-255 |
2.05e-91 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 269.96 E-value: 2.05e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 8 TLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHArghrlaaNP 87
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKP-------SE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 KQIERLRSRLGMVFQSFNLWSHMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIAR 167
Cdd:COG4161 75 KAIRLLRQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 168 ALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEaLFGAHGS 247
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQPQT 233
|
....*...
gi 490999375 248 PRFQQFIS 255
Cdd:COG4161 234 EAFAHYLS 241
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-232 |
1.53e-90 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 267.65 E-value: 1.53e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 8 TLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHharghrlAANP 87
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSK-------TPSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 KQIERLRSRLGMVFQSFNLWSHMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIAR 167
Cdd:PRK11124 75 KAIRELRRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999375 168 ALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
9-256 |
9.79e-86 |
|
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: 255.91 E-value: 9.79e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHARGHRLAANPK 88
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNGPLVPADEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRSRLGMVFQSFNLWSHMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARA 168
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 169 LAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGR-TMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGAHGS 247
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDlTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
....*....
gi 490999375 248 PRFQQFISS 256
Cdd:TIGR03005 241 ERTREFLSK 249
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
9-232 |
8.02e-84 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 249.96 E-value: 8.02e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGS----LDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlA 84
Cdd:COG1136 5 LELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIS----------S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 85 ANPKQIERLRSR-LGMVFQSFNLWSHMTVLQNViEGPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRV 163
Cdd:COG1136 75 LSERELARLRRRhIGFVFQFFNLLPELTALENV-ALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 164 AIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHvSNRVVFMHQGTI 232
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-256 |
8.60e-82 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 248.84 E-value: 8.60e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSF----GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrLA 84
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL----------TA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 85 ANPKQIERLRSRLGMVFQSFNLWSHMTVLQNvIEGPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVA 164
Cdd:COG1135 72 LSERELRAARRKIGMIFQHFNLLSSRTVAEN-VALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFG 243
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230
|
250
....*....|...
gi 490999375 244 AHGSPRFQQFISS 256
Cdd:COG1135 231 NPQSELTRRFLPT 243
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-254 |
7.42e-81 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 242.96 E-value: 7.42e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrLAANPK 88
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDI----------TGLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRSRLGMVFQSFNLWSHMTVLQNV----IEgpHYVLkrSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVA 164
Cdd:COG1127 76 ELYELRRRIGMLFQGGALFDSLTVFENVafplRE--HTDL--SEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFg 243
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL- 230
|
250
....*....|.
gi 490999375 244 AHGSPRFQQFI 254
Cdd:COG1127 231 ASDDPWVRQFL 241
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
9-232 |
3.97e-80 |
|
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: 240.47 E-value: 3.97e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLD----VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrLA 84
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDI----------SK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 85 ANPKQIERLRSR-LGMVFQSFNLWSHMTVLQNViEGPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRV 163
Cdd:cd03255 71 LSEKELAAFRRRhIGFVFQSFNLLPDLTALENV-ELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 164 AIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSnRVVFMHQGTI 232
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYAD-RIIELRDGKI 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
9-244 |
4.85e-76 |
|
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: 230.55 E-value: 4.85e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGS----LDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrLA 84
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDL----------TL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 85 ANPKQIERLRSRLGMVFQSFNLWSHMTVLQNViEGPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVA 164
Cdd:cd03258 72 LSGKELRKARRRIGMIFQHFNLLSSRTVFENV-ALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFG 243
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
.
gi 490999375 244 A 244
Cdd:cd03258 231 N 231
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
9-241 |
9.22e-76 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 230.33 E-value: 9.22e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSF-GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrLAANP 87
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDV----------TALRG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 KQIERLRSRLGMVFQSFNLWSHMTVLQNVIEG-------PHYVLKRSKQECIEQAEQLLDRVGMLNrKDFYPA-QLSGGQ 159
Cdd:COG3638 73 RALRRLRRRIGMIFQQFNLVPRLSVLTNVLAGrlgrtstWRSLLGLFPPEDRERALEALERVGLAD-KAYQRAdQLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 160 QQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAP 238
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPP 231
|
...
gi 490999375 239 EAL 241
Cdd:COG3638 232 AEL 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-253 |
1.55e-74 |
|
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: 227.00 E-value: 1.55e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrLAANPK 88
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDI----------SGLSEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRSRLGMVFQSFNLWSHMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARA 168
Cdd:cd03261 71 ELYRLRRRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 169 LAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFgAHGS 247
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR-ASDD 229
|
....*.
gi 490999375 248 PRFQQF 253
Cdd:cd03261 230 PLVRQF 235
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-242 |
2.03e-73 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 228.06 E-value: 2.03e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhhargHRLAANpk 88
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV--------TGLPPE-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qiERlrsRLGMVFQSFNLWSHMTVLQNVIEGPHyVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARA 168
Cdd:COG3842 76 --KR---NVGMVFQDYALFPHLTVAENVAFGLR-MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 169 LAMDPEVMLFDEPTSALDPELVGEVLKVMRSL-AEEGRTMLVVTHELG--FArhVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEeaLA--LADRIAVMNDGRIEQVGTPEEIY 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-244 |
1.23e-72 |
|
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: 230.56 E-value: 1.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 3 DPRPVtLSVSDIHKSF-----GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhh 77
Cdd:COG1123 256 AAEPL-LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLT---- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 78 arghrlAANPKQIERLRSRLGMVFQ----SFNlwSHMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVG----MLNRkd 149
Cdd:COG1123 331 ------KLSRRSLRELRRRVQMVFQdpysSLN--PRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGlppdLADR-- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 150 fYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMH 228
Cdd:COG1123 401 -YPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMY 479
|
250
....*....|....*.
gi 490999375 229 QGTIDCDGAPEALFGA 244
Cdd:COG1123 480 DGRIVEDGPTEEVFAN 495
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
8-242 |
1.14e-71 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 223.48 E-value: 1.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 8 TLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHARghrlaanp 87
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPR-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 kqiERlrsRLGMVFQSFNLWSHMTVLQNVIEGPHyVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIAR 167
Cdd:COG1118 74 ---ER---RVGFVFQHYALFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490999375 168 ALAMDPEVMLFDEPTSALDPELVGEVLKVMRSL-AEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
23-245 |
1.38e-71 |
|
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: 219.13 E-value: 1.38e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaaNPKQIERLRSRLGMVFQ 102
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI-------------TKKNLRELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 S-----FNlwshMTVLQNVIEGPHYvLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVML 177
Cdd:COG1122 83 NpddqlFA----PTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 178 FDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGAH 245
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-231 |
1.67e-71 |
|
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: 217.05 E-value: 1.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlAANPK 88
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL-----------TDLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRSRLGMVFQSFNLWSHMTVLQNVIEGphyvlkrskqecieqaeqlldrvgmlnrkdfypaqLSGGQQQRVAIARA 168
Cdd:cd03229 70 ELPPLRRRIGMVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARA 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999375 169 LAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGT 231
Cdd:cd03229 115 LAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-232 |
5.35e-70 |
|
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: 214.31 E-value: 5.35e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlAANPK 88
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-----------TGVPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QierlRSRLGMVFQSFNLWSHMTVLQNVIEGPhYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARA 168
Cdd:cd03259 70 E----RRNIGMVFQDYALFPHLTVAENIAFGL-KLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999375 169 LAMDPEVMLFDEPTSALDPELVGEVLKVMRSL-AEEGRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-252 |
1.29e-69 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 214.95 E-value: 1.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 1 MHDPRPVtLSVSDIHKSF----GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetiemkh 76
Cdd:COG1116 1 MSAAAPA-LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 77 harghrlaanpKQIERLRSRLGMVFQSFNL--WshMTVLQNVIEGPHyVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQ 154
Cdd:COG1116 73 -----------KPVTGPGPDRGVVFQEPALlpW--LTVLDNVALGLE-LRGVPKAERRERARELLELVGLAGFEDAYPHQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 155 LSGGQQQRVAIARALAMDPEVMLFDEPTSALDP----ELVGEVLKVmrsLAEEGRTMLVVTHELGFARHVSNRVVFMHQG 230
Cdd:COG1116 139 LSGGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
250 260
....*....|....*....|....*...
gi 490999375 231 ------TIDCDGAPEALFGAHGSPRFQQ 252
Cdd:COG1116 216 pgriveEIDVDLPRPRDRELRTSPEFAA 243
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-241 |
2.54e-67 |
|
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: 208.58 E-value: 2.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLD-VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlAANP 87
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDIN----------KLKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 KQIERLRSRLGMVFQSFNLWSHMTVLQNVIEG--PHYVLKRS-----KQECIEQAEQLLDRVGML----NRKDfypaQLS 156
Cdd:cd03256 71 KALRQLRRQIGMIFQQFNLIERLSVLENVLSGrlGRRSTWRSlfglfPKEEKQRALAALERVGLLdkayQRAD----QLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 157 GGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLA-EEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCD 235
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFD 226
|
....*.
gi 490999375 236 GAPEAL 241
Cdd:cd03256 227 GPPAEL 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-241 |
7.31e-67 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 207.22 E-value: 7.31e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetiemkhhargHRLAANPK 88
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLG-----------EDVARDPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIerlRSRLGMVFQSFNLWSHMTVLQNViegpHYVLK---RSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAI 165
Cdd:COG1131 70 EV---RRRIGYVPQEPALYPDLTVRENL----RFFARlygLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490999375 166 ARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEAL 241
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-232 |
3.50e-66 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 204.90 E-value: 3.50e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 13 DIHKSF-GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhhargHRLaaNPKQIE 91
Cdd:COG2884 6 NVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL--------SRL--KRREIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 92 RLRSRLGMVFQSFNLWSHMTVLQNVIegphYVLK---RSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARA 168
Cdd:COG2884 76 YLRRRIGVVFQDFRLLPDRTVYENVA----LPLRvtgKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999375 169 LAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-256 |
1.12e-65 |
|
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: 204.65 E-value: 1.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLD----VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrla 84
Cdd:COG1124 2 LEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 85 aNPKQIERLRSRLGMVFQ----SFNlwSHMTVLQnVIEGPHYVLKRSKQEciEQAEQLLDRVGM----LNRkdfYPAQLS 156
Cdd:COG1124 70 -TRRRRKAFRRRVQMVFQdpyaSLH--PRHTVDR-ILAEPLRIHGLPDRE--ERIAELLEQVGLppsfLDR---YPHQLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 157 GGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSL-AEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCD 235
Cdd:COG1124 141 GGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEE 220
|
250 260
....*....|....*....|.
gi 490999375 236 GAPEALFGAHGSPRFQQFISS 256
Cdd:COG1124 221 LTVADLLAGPKHPYTRELLAA 241
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
9-255 |
5.50e-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: 202.91 E-value: 5.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLEtpDAgvvsVGGETIEMKHHARGHRLAANPK 88
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMN--DL----VPGVRIEGKVLFDGQDIYDKKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRSRLGMVFQSFNLWShMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVGMLN----RKDFYPAQLSGGQQQRVA 164
Cdd:TIGR00972 76 DVVELRRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDevkdRLHDSALGLSGGQQQRLC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEgRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGA 244
Cdd:TIGR00972 155 IARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTN 233
|
250
....*....|.
gi 490999375 245 HGSPRFQQFIS 255
Cdd:TIGR00972 234 PKEKRTEDYIS 244
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
12-256 |
4.04e-64 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 203.88 E-value: 4.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 12 SDIHKSF----GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrLAANP 87
Cdd:PRK11153 5 KNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDL----------TALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 KQIERLRSRLGMVFQSFNLWSHMTVLQNV-----IEGphyvlkRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQR 162
Cdd:PRK11153 75 KELRKARRQIGMIFQHFNLLSSRTVFDNValpleLAG------TPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 163 VAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEAL 241
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
250
....*....|....*
gi 490999375 242 FGAHGSPRFQQFISS 256
Cdd:PRK11153 229 FSHPKHPLTREFIQS 243
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
9-232 |
4.41e-63 |
|
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: 197.34 E-value: 4.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSF----GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrLA 84
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDL----------LK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 85 ANPKQIERLRSRLGMVFQ----SFNlwSHMTVLQNVIEGPHYVLKRSKQEcIEQAEQLLDRVGMLNRKDF---YPAQLSG 157
Cdd:cd03257 72 LSRRLRKIRRKEIQMVFQdpmsSLN--PRMTIGEQIAEPLRIHGKLSKKE-ARKEAVLLLLVGVGLPEEVlnrYPHELSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490999375 158 GQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-232 |
7.96e-63 |
|
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: 196.63 E-value: 7.96e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLL-----ETPDAGVVSVGGETIemkhharghrl 83
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDI----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 84 AANPKQIERLRSRLGMVFQSFNLWsHMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVGMLNR-KD-FYPAQLSGGQQQ 161
Cdd:cd03260 70 YDLDVDVLELRRRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEvKDrLHALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490999375 162 RVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEgRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
9-241 |
1.56e-62 |
|
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: 196.37 E-value: 1.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLD-VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlAANP 87
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDIT----------KLRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 KQIERLRSRLGMVFQSFNLWSHMTVLQNVIEGP-------HYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQ 160
Cdd:TIGR02315 72 KKLRKLRRRIGMIFQHYNLIERLTVLENVLHGRlgykptwRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 161 QRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPE 239
Cdd:TIGR02315 152 QRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPS 231
|
..
gi 490999375 240 AL 241
Cdd:TIGR02315 232 EL 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-232 |
6.90e-62 |
|
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: 194.23 E-value: 6.90e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLD----VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGEtiemkhharghrla 84
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 85 anpkQIERLRSRLGMVFQSFNLWSHMTVLQNVIEGPHyVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVA 164
Cdd:cd03293 67 ----PVTGPGPDRGYVFQQDALLPWLTVLDNVALGLE-LQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490999375 165 IARALAMDPEVMLFDEPTSALDP---ELVGEVLkvMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQ--GTI 232
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDAltrEQLQEEL--LDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRI 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
10-242 |
2.15e-61 |
|
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: 194.40 E-value: 2.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 10 SVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrLAANPKQ 89
Cdd:cd03294 26 SKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDI----------AAMSRKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 90 IERLRS-RLGMVFQSFNLWSHMTVLQNVIEGPHyVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARA 168
Cdd:cd03294 96 LRELRRkKISMVFQSFALLPHRTVLENVAFGLE-VQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 169 LAMDPEVMLFDEPTSALDP----ELVGEVLKVMrslAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:cd03294 175 LAVDPDILLMDEAFSALDPlirrEMQDELLRLQ---AELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-240 |
5.19e-61 |
|
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: 192.27 E-value: 5.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIE-MKHHARghrlaanp 87
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITgLPPHEI-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 kqierlrSRLGMV--FQSFNLWSHMTVLQNVIEGPHYVLK---------RSKQECIEQAEQLLDRVGMLNRKDFYPAQLS 156
Cdd:cd03219 73 -------ARLGIGrtFQIPRLFPELTVLENVMVAAQARTGsglllararREEREARERAEELLERVGLADLADRPAGELS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 157 GGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDG 236
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEG 225
|
....
gi 490999375 237 APEA 240
Cdd:cd03219 226 TPDE 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
8-242 |
6.09e-60 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 193.37 E-value: 6.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 8 TLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGEtiEMKHHARGHRlaanp 87
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR--DVTDLPPKDR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 kqierlrsRLGMVFQSFNLWSHMTVLQNvIEGPHYVLKRSKQECIEQAEQLLDRVGM---LNRKdfyPAQLSGGQQQRVA 164
Cdd:COG3839 76 --------NIAMVFQSYALYPHMTVYEN-IAFPLKLRKVPKAEIDRRVREAAELLGLedlLDRK---PKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEvlkvMRS-----LAEEGRTMLVVTHE----LGFArhvsNRVVFMHQGTIDCD 235
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKLRVE----MRAeikrlHRRLGTTTIYVTHDqveaMTLA----DRIAVMNDGRIQQV 215
|
....*..
gi 490999375 236 GAPEALF 242
Cdd:COG3839 216 GTPEELY 222
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
9-242 |
1.37e-59 |
|
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: 189.48 E-value: 1.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhhargHRLaaNPK 88
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL--------ASL--SRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERlrsRLGMVFQSFNLWSHMTVLQNVIEG--PHY-VLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAI 165
Cdd:COG1120 72 ELAR---RIAYVPQEPPAPFGLTVRELVALGryPHLgLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 166 ARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLA-EEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-231 |
1.00e-58 |
|
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: 185.75 E-value: 1.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 10 SVSDIHKSFGSLD--VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaaNP 87
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL-------------TK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 KQIERLRSRLGMVFQS-----FNLwshmTVLQNVIEGPHYvLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQR 162
Cdd:cd03225 68 LSLKELRRKVGLVFQNpddqfFGP----TVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 163 VAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGT 231
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
27-254 |
1.11e-58 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 186.11 E-value: 1.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 27 ISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrLAANPKQieRLRSrlgMVFQSFNL 106
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL----------TALPPAE--RPVS---MLFQENNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 107 WSHMTVLQNVIEGPHYVLKRSKQEcIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALD 186
Cdd:COG3840 83 FPHLTVAQNIGLGLRPGLKLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 187 PELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGAHGSPRFQQFI 254
Cdd:COG3840 162 PALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-240 |
1.54e-58 |
|
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: 186.10 E-value: 1.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 1 MHDPRPVTLSVSDIHKSF----GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkh 76
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 77 hargHRLaaNPKQIERLRSR-LGMVFQSFNLWSHMTVLQNV---IEgphyvlKRSKQECIEQAEQLLDRVGMLNRKDFYP 152
Cdd:COG4181 77 ----FAL--DEDARARLRARhVGFVFQSFQLLPTLTALENVmlpLE------LAGRRDARARARALLERVGLGHRLDHYP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 153 AQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHvSNRVVFMHQGT 231
Cdd:COG4181 145 AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAGR 223
|
....*....
gi 490999375 232 IDCDGAPEA 240
Cdd:COG4181 224 LVEDTAATA 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-242 |
2.27e-58 |
|
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: 185.52 E-value: 2.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhhargHRLAANPK 88
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--------TNLPPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIerlrsrlGMVFQSFNLWSHMTVLQNVIEGPHyVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARA 168
Cdd:cd03300 73 PV-------NTVFQNYALFPHLTVFENIAFGLR-LKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999375 169 LAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-240 |
9.28e-58 |
|
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: 184.86 E-value: 9.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkHHARGHRLAanpk 88
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI---TGLPPHRIA---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qierlrsRLGMV--FQSFNLWSHMTVLQNVIEGPHYVLK--------------RSKQECIEQAEQLLDRVGMLNRKDFYP 152
Cdd:COG0411 78 -------RLGIArtFQNPRLFPELTVLENVLVAAHARLGrgllaallrlprarREEREARERAEELLERVGLADRADEPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 153 AQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSL-AEEGRTMLVVTHELGFARHVSNRVVFMHQGT 231
Cdd:COG0411 151 GNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
....*....
gi 490999375 232 IDCDGAPEA 240
Cdd:COG0411 231 VIAEGTPAE 239
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
9-239 |
4.30e-57 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 186.85 E-value: 4.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrLAANPK 88
Cdd:COG4175 28 KSKDEILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDI----------TKLSKK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLR-SRLGMVFQSFNLWSHMTVLQNV-----IEGphyvlkRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQR 162
Cdd:COG4175 98 ELRELRrKKMSMVFQHFALLPHRTVLENVafgleIQG------VPKAERRERAREALELVGLAGWEDSYPDELSGGMQQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 163 VAIARALAMDPEVMLFDEPTSALDP----ELVGEVLKVMRSLaeeGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAP 238
Cdd:COG4175 172 VGLARALATDPDILLMDEAFSALDPlirrEMQDELLELQAKL---KKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTP 248
|
.
gi 490999375 239 E 239
Cdd:COG4175 249 E 249
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-254 |
8.94e-57 |
|
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: 181.77 E-value: 8.94e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 8 TLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmKHHARghrlaanp 87
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT-DVPVQ-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 kqiERlrsRLGMVFQSFNLWSHMTVLQNVIEG---PHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVA 164
Cdd:cd03296 73 ---ER---NVGFVFQHYALFRHMTVFDNVAFGlrvKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFG 243
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
250
....*....|.
gi 490999375 244 AHGSPRFQQFI 254
Cdd:cd03296 227 HPASPFVYSFL 237
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
9-241 |
1.28e-56 |
|
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: 181.21 E-value: 1.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlaanpK 88
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR--------------K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRSRLGMVFQSFNLWSHMTVLQNV-IEGPHYvlKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIAR 167
Cdd:COG4555 68 EPREARRQIGVLPDERGLYDRLTVRENIrYFAELY--GLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999375 168 ALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEAL 241
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
9-232 |
6.20e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 178.47 E-value: 6.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaaNPK 88
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-------------SAM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRSRLGMVFQSFNLWsHMTVLQNVIEGPHYvlkRSKQECIEQAEQLLDRVG----MLNRKdfyPAQLSGGQQQRVA 164
Cdd:COG4619 68 PPPEWRRQVAYVPQEPALW-GGTVRDNLPFPFQL---RERKFDRERALELLERLGlppdILDKP---VERLSGGERQRLA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSL-AEEGRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:COG4619 141 LIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-232 |
6.97e-56 |
|
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: 181.79 E-value: 6.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSF----GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCI-NLLETP--DAGVVSVGGETIemkhhargh 81
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlGLLPPPgiTSGEILFDGEDL--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 82 rLAANPKQIERLR-SRLGMVFQ----SFNlwSHMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVGMLN---RKDFYPA 153
Cdd:COG0444 73 -LKLSEKELRKIRgREIQMIFQdpmtSLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDperRLDRYPH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 154 QLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
9-256 |
9.73e-56 |
|
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: 182.54 E-value: 9.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlAANPK 88
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDI-----------TRLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QierlRSRLGMVFQSFNLWSHMTVLQNVIEGPHYVlKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARA 168
Cdd:TIGR03265 74 Q----KRDYGIVFQSYALFPNLTVADNIAYGLKNR-GMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 169 LAMDPEVMLFDEPTSALDPE----LVGEVLKVMRSLaeeGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGA 244
Cdd:TIGR03265 149 LATSPGLLLLDEPLSALDARvrehLRTEIRQLQRRL---GVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRH 225
|
250
....*....|..
gi 490999375 245 HGSPRFQQFISS 256
Cdd:TIGR03265 226 PATPFVADFVGE 237
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-259 |
1.03e-55 |
|
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: 179.03 E-value: 1.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLD-VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrLAANP 87
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI----------REQDP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 kqiERLRSRLGMVFQSFNLWSHMTVLQNVIEGPHyVLKRSKQECIEQAEQLLDRVGM--LNRKDFYPAQLSGGQQQRVAI 165
Cdd:cd03295 71 ---VELRRKIGYVIQQIGLFPHMTVEENIALVPK-LLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 166 ARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGA 244
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
250
....*....|....*
gi 490999375 245 HGSPRFQQFISSHHQ 259
Cdd:cd03295 227 PANDFVAEFVGADRL 241
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-232 |
1.20e-54 |
|
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: 173.74 E-value: 1.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaanPK 88
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI--------------KK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRSRLGMVFQSFNLWSHMTVLQNViegphyvlkrskqecieqaeqlldrvgmlnrkdfypaQLSGGQQQRVAIARA 168
Cdd:cd03230 67 EPEEVKRRIGYLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQA 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999375 169 LAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:cd03230 110 LLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-245 |
4.24e-54 |
|
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: 182.41 E-value: 4.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSF--GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDA---GVVSVGGETI-EMKHHARGhr 82
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLlELSEALRG-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 83 laanpkqierlrSRLGMVFQ----SFNLwshMTVLQNVIEGPhYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGG 158
Cdd:COG1123 83 ------------RRIGMVFQdpmtQLNP---VTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 159 QQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSL-AEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGA 237
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
....*...
gi 490999375 238 PEALFGAH 245
Cdd:COG1123 227 PEEILAAP 234
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
11-227 |
1.49e-53 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 172.41 E-value: 1.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 11 VSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrLAANPKQI 90
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQET----------PPLNSKKA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 91 ERL-RSRLGMVFQSFNLWSHMTVLQNVIEGPHYVlKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARAL 169
Cdd:TIGR03608 71 SKFrREKLGYLFQNFALIENETVEENLDLGLKYK-KLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 170 AMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARhVSNRVVFM 227
Cdd:TIGR03608 150 LKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAK-QADRVIEL 206
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
13-241 |
3.19e-53 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 174.51 E-value: 3.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 13 DIHKSFGSLDV-LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrLAANPkqiE 91
Cdd:COG1125 6 NVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDI----------RDLDP---V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 92 RLRSRLGMVFQSFNLWSHMTVLQNVIEGPHyVLKRSKQECIEQAEQLLDRVGmLNRKDF---YPAQLSGGQQQRVAIARA 168
Cdd:COG1125 73 ELRRRIGYVIQQIGLFPHMTVAENIATVPR-LLGWDKERIRARVDELLELVG-LDPEEYrdrYPHELSGGQQQRVGVARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 169 LAMDPEVMLFDEPTSALDP----ELVGEVLKVMRSLaeeGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEAL 241
Cdd:COG1125 151 LAADPPILLMDEPFGALDPitreQLQDELLRLQREL---GKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEI 224
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
14-230 |
3.43e-53 |
|
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: 171.66 E-value: 3.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 14 IHKSF-GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkHHARGHRLAAnpkqier 92
Cdd:TIGR02673 7 VSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDV---NRLRGRQLPL------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 93 LRSRLGMVFQSFNLWSHMTVLQNVIEgPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMD 172
Cdd:TIGR02673 77 LRRRIGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 173 PEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQG 230
Cdd:TIGR02673 156 PPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-242 |
4.37e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 172.20 E-value: 4.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlaanpk 88
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR--------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qieRLRSRLGMVFQSFNL-WS-HMTVLQnVIEGPHY----VLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQR 162
Cdd:COG1121 72 ---RARRRIGYVPQRAEVdWDfPITVRD-VVLMGRYgrrgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 163 VAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIdCDGAPEALF 242
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEEVL 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
23-243 |
1.60e-52 |
|
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: 171.46 E-value: 1.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetieMKhharghrlAANPKQIERLRSRLGMVFQ 102
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG----LD--------TLDEENLWEIRKKVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 S-FNLWSHMTVLQNVIEGPHYvLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEP 181
Cdd:TIGR04520 85 NpDNQFVGATVEDDVAFGLEN-LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490999375 182 TSALDPELVGEVLKVMRSL-AEEGRTMLVVTHELGFARHvSNRVVFMHQGTIDCDGAPEALFG 243
Cdd:TIGR04520 164 TSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFS 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-230 |
3.75e-52 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 170.22 E-value: 3.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 3 DPRPVTLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLL--ETPDA---GVVSVGGETIemkhH 77
Cdd:COG1117 6 STLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGEDI----Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 78 ARGhrlaANPkqiERLRSRLGMVFQSFNLWShMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVGM-------LNRkdf 150
Cdd:COG1117 82 DPD----VDV---VELRRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwdevkdrLKK--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 151 yPAQ-LSGGQQQRVAIARALAMDPEVMLFDEPTSALDP-------ELvgevlkvMRSLAEEgRTMLVVTHELGFARHVSN 222
Cdd:COG1117 151 -SALgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPistakieEL-------ILELKKD-YTIVIVTHNMQQAARVSD 221
|
....*...
gi 490999375 223 RVVFMHQG 230
Cdd:COG1117 222 YTAFFYLG 229
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
24-242 |
5.35e-52 |
|
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: 170.71 E-value: 5.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKhharghrlaaNPKQIERLRSRLGMVFQS 103
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAK----------KKKKLKDLRKKVGLVFQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 -----FNLwshmTVLQNVIEGPHYvLKRSKQECIEQAEQLLDRVGMlnRKDFY---PAQLSGGQQQRVAIARALAMDPEV 175
Cdd:TIGR04521 91 pehqlFEE----TVYKDIAFGPKN-LGLSEEEAEERVKEALELVGL--DEEYLersPFELSGGQMRRVAIAGVLAMEPEV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 176 MLFDEPTSALDPELVGEVLKVMRSLA-EEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:TIGR04521 164 LILDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
23-230 |
2.13e-51 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 167.20 E-value: 2.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghRLAANPKQIERlRSRLGMVFQ 102
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVT--------NLSYSQKIILR-RELIGYIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 SFNLWSHMTVLQNvIEGPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEPT 182
Cdd:NF038007 91 SFNLIPHLSIFDN-VALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490999375 183 SALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHvSNRVVFMHQG 230
Cdd:NF038007 170 GNLDSKNARAVLQQLKYINQKGTTIIMVTHSDEASTY-GNRIINMKDG 216
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-239 |
2.87e-51 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 171.03 E-value: 2.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 8 TLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmKHHARghrlaanp 87
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS-RLHAR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 kqiERlrsRLGMVFQSFNLWSHMTVLQNVIEGPHyVLKRSKQ---ECIEQ-AEQLLDRVGMLNRKDFYPAQLSGGQQQRV 163
Cdd:PRK10851 73 ---DR---KVGFVFQHYALFRHMTVFDNIAFGLT-VLPRRERpnaAAIKAkVTQLLEMVQLAHLADRYPAQLSGGQKQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 164 AIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGR-TMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPE 239
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
9-241 |
4.97e-51 |
|
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: 166.46 E-value: 4.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhHARGHrlaanpk 88
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT---GLPPH------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qiERLRSRLGMVFQSFNLWSHMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVG-MLNRKDfypAQLSGGQQQRVAIAR 167
Cdd:cd03224 71 --ERARAGIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKeRRKQLA---GTLSGGEQQMLAIAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999375 168 ALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEAL 241
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-232 |
1.03e-50 |
|
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: 165.12 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMkhharghrlaANPK 88
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD----------LPPK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qiERlrsRLGMVFQSFNLWSHMTVLQNvIEGPHYVLKRSKQEC---IEQAEQLLDRVGMLNRKdfyPAQLSGGQQQRVAI 165
Cdd:cd03301 71 --DR---DIAMVFQNYALYPHMTVYDN-IAFGLKLRKVPKDEIderVREVAELLQIEHLLDRK---PKQLSGGQRQRVAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 166 ARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
8-242 |
3.62e-49 |
|
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: 165.66 E-value: 3.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 8 TLSVsDIHKSFGS--LDVlkgiSIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkHHARGHRLAA 85
Cdd:COG4148 2 MLEV-DFRLRRGGftLDV----DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQ--DSARGIFLPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 86 NpkqierlRSRLGMVFQSFNLWSHMTVLQNViegpHYVLKRS-KQECIEQAEQLLDRVG---MLNRkdfYPAQLSGGQQQ 161
Cdd:COG4148 75 H-------RRRIGYVFQEARLFPHLSVRGNL----LYGRKRApRAERRISFDEVVELLGighLLDR---RPATLSGGERQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 162 RVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRT-MLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEA 240
Cdd:COG4148 141 RVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAE 220
|
..
gi 490999375 241 LF 242
Cdd:COG4148 221 VL 222
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
16-239 |
6.80e-49 |
|
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: 165.03 E-value: 6.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 16 KSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrLAANPKQI-ERLR 94
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENI----------MKQSPVELrEVRR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 95 SRLGMVFQSFNLWSHMTVLQNVIEGPHyVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPE 174
Cdd:TIGR01186 71 KKIGMVFQQFALFPHMTILQNTSLGPE-LLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 175 VMLFDEPTSALDP----ELVGEVLKVMRSLaeeGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPE 239
Cdd:TIGR01186 150 ILLMDEAFSALDPlirdSMQDELKKLQATL---QKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPD 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-236 |
1.16e-48 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 158.75 E-value: 1.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 10 SVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlAANPKQ 89
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA----------SLSPKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 90 IERLRSrlgmvfqsfnlwshmtvlqnviegphYVLkrskqecieqaeQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARAL 169
Cdd:cd03214 71 LARKIA--------------------------YVP------------QALELLGLAHLADRPFNELSGGERQRVLLARAL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 170 AMDPEVMLFDEPTSALDPELVGEVLKVMRSLA-EEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDG 236
Cdd:cd03214 113 AQEPPILLLDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-231 |
9.40e-48 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 155.87 E-value: 9.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 10 SVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaaNPKQ 89
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI-------------AKLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 90 IERLRSRLGMVFQsfnlwshmtvlqnviegphyvlkrskqecieqaeqlldrvgmlnrkdfypaqLSGGQQQRVAIARAL 169
Cdd:cd00267 68 LEELRRRIGYVPQ----------------------------------------------------LSGGQRQRVALARAL 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490999375 170 AMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGT 231
Cdd:cd00267 96 LLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
9-259 |
1.93e-47 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 166.82 E-value: 1.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSF----GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlA 84
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVA----------T 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 85 ANPKQIERLR-SRLGMVFQSFNLWSHMTVLQNViEGPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRV 163
Cdd:PRK10535 75 LDADALAQLRrEHFGFIFQRYHLLSHLTAAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 164 AIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHvSNRVVFMHQGTIDCD-------- 235
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNppaqekvn 232
|
250 260
....*....|....*....|....*.
gi 490999375 236 --GAPEALfgAHGSPRFQQFISSHHQ 259
Cdd:PRK10535 233 vaGGTEPV--VNTASGWRQFVSGFRE 256
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-232 |
1.85e-46 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 157.97 E-value: 1.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 1 MHDPRPVtLSVSDIHKSF-----------GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGG 69
Cdd:COG4608 1 AAMAEPL-LEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 70 ETIemkHHARGHRLAanpkqieRLRSRLGMVFQ----SFNlwSHMTVLQNVIEGP--HYVLkrSKQECIEQAEQLLDRVG 143
Cdd:COG4608 80 QDI---TGLSGRELR-------PLRRRMQMVFQdpyaSLN--PRMTVGDIIAEPLriHGLA--SKAERRERVAELLELVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 144 M----LNRkdfYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFAR 218
Cdd:COG4608 146 LrpehADR---YPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVR 222
|
250
....*....|....
gi 490999375 219 HVSNRVVFMHQGTI 232
Cdd:COG4608 223 HISDRVAVMYLGKI 236
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-236 |
2.12e-46 |
|
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: 154.23 E-value: 2.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 10 SVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetiemkhharghrlaanpKQ 89
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG------------------KP 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 90 IERLRSRLGMVFQSFNL-WSH-MTVLQNVIEG--PHYVL-KRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVA 164
Cdd:cd03235 63 LEKERKRIGYVPQRRSIdRDFpISVRDVVLMGlyGHKGLfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMhQGTIDCDG 236
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
13-230 |
8.03e-45 |
|
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: 150.14 E-value: 8.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 13 DIHKSFGSLDvLKgISIQAqKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGET-------IEMKHHARghrlaa 85
Cdd:cd03297 5 DIEKRLPDFT-LK-IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkINLPPQQR------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 86 npkqierlrsRLGMVFQSFNLWSHMTVLQNVIegphYVLKRSKQ-ECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVA 164
Cdd:cd03297 76 ----------KIGLVFQQYALFPHLNVRENLA----FGLKRKRNrEDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQG 230
Cdd:cd03297 142 LARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
9-238 |
1.03e-44 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 154.33 E-value: 1.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghRLAANPK 88
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--------HVPAENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIErlrsrlgMVFQSFNLWSHMTVLQNVIEGphyvL---KRSKQECIEQAEQLLDRV---GMLNRKdfyPAQLSGGQQQR 162
Cdd:PRK09452 87 HVN-------TVFQSYALFPHMTVFENVAFG----LrmqKTPAAEITPRVMEALRMVqleEFAQRK---PHQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 163 VAIARALAMDPEVMLFDEPTSALDPELVGEV---LKVM-RSLaeeGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAP 238
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDYKLRKQMqneLKALqRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-225 |
1.30e-44 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 156.72 E-value: 1.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKhharghrlaaNPK 88
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFR----------SPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRsrLGMVFQSFNLWSHMTVLQNVIEGpHYVLKR---SKQECIEQAEQLLDRVGMlnrkDFYPAQ----LSGGQQQ 161
Cdd:COG1129 75 DAQAAG--IAIIHQELNLVPNLSVAENIFLG-REPRRGgliDWRAMRRRARELLARLGL----DIDPDTpvgdLSVAQQQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999375 162 RVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVV 225
Cdd:COG1129 148 LVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVT 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-183 |
2.56e-44 |
|
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: 146.64 E-value: 2.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaaNPKQIERLRSRLGMVFQS 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL-------------TDDERKSLRKEIGYVFQD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 FNLWSHMTVLQNVIEGPhYVLKRSKQECIEQAEQLLDRVGMLNRKD----FYPAQLSGGQQQRVAIARALAMDPEVMLFD 179
Cdd:pfam00005 68 PQLFPRLTVRENLRLGL-LLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLD 146
|
....
gi 490999375 180 EPTS 183
Cdd:pfam00005 147 EPTA 150
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
9-242 |
3.43e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 150.61 E-value: 3.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSF--GSLdVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMkhharghrlaaN 86
Cdd:PRK13639 2 LETRDLKYSYpdGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY-----------D 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 87 PKQIERLRSRLGMVFQSFN--LWSHmTVLQNVIEGPhYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVA 164
Cdd:PRK13639 70 KKSLLEVRKTVGIVFQNPDdqLFAP-TVEEDVAFGP-LNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-244 |
5.71e-44 |
|
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: 155.61 E-value: 5.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 3 DPRPVTLSVSDIHKSF-----------GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCI-NLLETpdAGVVSVGGE 70
Cdd:COG4172 270 PDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALlRLIPS--EGEIRFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 71 TIemkhharghrLAANPKQIERLRSRLGMVFQ----SFNlwSHMTVLQNVIEG--PHYVlKRSKQECIEQAEQLLDRVG- 143
Cdd:COG4172 348 DL----------DGLSRRALRPLRRRMQVVFQdpfgSLS--PRMTVGQIIAEGlrVHGP-GLSAAERRARVAEALEEVGl 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 144 ---MLNRkdfYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSL-AEEGRTMLVVTHELGFARH 219
Cdd:COG4172 415 dpaARHR---YPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRA 491
|
250 260
....*....|....*....|....*
gi 490999375 220 VSNRVVFMHQGTIDCDGAPEALFGA 244
Cdd:COG4172 492 LAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-247 |
7.32e-44 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 149.78 E-value: 7.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaaNPKQIERLRSRLGMVFQS 103
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL-------------SEETVWDVRRQVGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 -FNLWSHMTVLQNVIEG------PHyvlkrskQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVM 176
Cdd:PRK13635 90 pDNQFVGATVQDDVAFGlenigvPR-------EEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490999375 177 LFDEPTSALDPELVGEVLKVMRSLAEEGR-TMLVVTHELGFARHvSNRVVFMHQGTIDCDGAPEALFgAHGS 247
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF-KSGH 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
9-242 |
9.50e-44 |
|
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: 148.25 E-value: 9.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLdVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaANPK 88
Cdd:cd03299 1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI------------TNLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERlrsRLGMVFQSFNLWSHMTVLQNvIEgphYVLKRSKQECIEQAEQLLDRVGM------LNRKdfyPAQLSGGQQQR 162
Cdd:cd03299 68 PEKR---DISYVPQNYALFPHMTVYKN-IA---YGLKKRKVDKKEIERKVLEIAEMlgidhlLNRK---PETLSGGEQQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 163 VAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEAL 241
Cdd:cd03299 138 VAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
.
gi 490999375 242 F 242
Cdd:cd03299 218 F 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
9-241 |
1.05e-43 |
|
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: 147.82 E-value: 1.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkHHARGHRLAanpk 88
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI---TGLPPHRIA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qierlrsRLGMVF--QSFNLWSHMTVLQNVIEGPHyvLKRSKQEcieqAEQLLDRV--------GMLNRkdfyPA-QLSG 157
Cdd:COG0410 77 -------RLGIGYvpEGRRIFPSLTVEENLLLGAY--ARRDRAE----VRADLERVyelfprlkERRRQ----RAgTLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 158 GQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGA 237
Cdd:COG0410 140 GEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGT 219
|
....
gi 490999375 238 PEAL 241
Cdd:COG0410 220 AAEL 223
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
11-236 |
4.15e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 148.31 E-value: 4.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 11 VSDIHKSFGS-----LDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHARGHRLAA 85
Cdd:PRK13651 5 VKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 86 NP-----------KQIERLRSRLGMVFQ--SFNLWSHmTVLQNVIEGPhYVLKRSKQECIEQAEQLLDRVGM----LNRK 148
Cdd:PRK13651 85 EKlviqktrfkkiKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGP-VSMGVSKEEAKKRAAKYIELVGLdesyLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 149 DFypaQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMH 228
Cdd:PRK13651 163 PF---ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
....*...
gi 490999375 229 QGTIDCDG 236
Cdd:PRK13651 240 DGKIIKDG 247
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
24-232 |
4.64e-43 |
|
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: 145.63 E-value: 4.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhhARGHRlaanpKQIERLRSRLGMVFQS 103
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV-----SDLRG-----RAIPYLRRKIGVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 FNLWSHMTVLQNVIEgPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTS 183
Cdd:cd03292 87 FRLLPDRNVYENVAF-ALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490999375 184 ALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-232 |
1.07e-42 |
|
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: 142.95 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMkhharghrlaANPK 88
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF----------ASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qiERLRSRLGMVFQsfnlwshmtvlqnviegphyvlkrskqecieqaeqlldrvgmlnrkdfypaqLSGGQQQRVAIARA 168
Cdd:cd03216 71 --DARRAGIAMVYQ----------------------------------------------------LSVGERQMVEIARA 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999375 169 LAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:cd03216 97 LARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-236 |
1.51e-42 |
|
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: 144.17 E-value: 1.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 28 SIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetIEMKHharghrlaANPKqierlRSRLGMVFQSFNLW 107
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--VDVTA--------APPA-----DRPVSMLFQENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 108 SHMTVLQNVIEG--PHYVLKRSKQECIEQAeqlLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSAL 185
Cdd:cd03298 83 AHLTVEQNVGLGlsPGLKLTAEDRQAIEVA---LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490999375 186 DPELVGEVLK-VMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDG 236
Cdd:cd03298 160 DPALRAEMLDlVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-232 |
1.70e-42 |
|
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: 143.94 E-value: 1.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 10 SVSDIHKSFG-SLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKhharghrlaanpk 88
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qieRLRSRLGMVFQS--FNLWSHmTVLQNVIEGphyvlKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIA 166
Cdd:cd03226 68 ---ERRKSIGYVMQDvdYQLFTD-SVREELLLG-----LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490999375 167 RALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-242 |
3.95e-42 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 147.17 E-value: 3.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGEtiEMKHHARGHRlaanpk 88
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE--DVTHRSIQQR------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qierlrsRLGMVFQSFNLWSHMTVLQNVIEGPHyVLKRSKQEC---IEQAEQLLDRVGMLNRkdfYPAQLSGGQQQRVAI 165
Cdd:PRK11432 79 -------DICMVFQSYALFPHMSLGENVGYGLK-MLGVPKEERkqrVKEALELVDLAGFEDR---YVDQISGGQQQRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 166 ARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK11432 148 ARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-230 |
4.11e-42 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 150.18 E-value: 4.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKhharghrlaaNPK 88
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIR----------SPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qiERLRSRLGMVFQSFNLWSHMTVLQNVIEG--PHYVLKRSKQECIEQAEQLLDRVGM---LNRKdfyPAQLSGGQQQRV 163
Cdd:COG3845 76 --DAIALGIGMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLdvdPDAK---VEDLSVGEQQRV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 164 AIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQG 230
Cdd:COG3845 151 EILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-239 |
5.94e-42 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 144.14 E-value: 5.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 7 VTLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkHHARGHRLAAn 86
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPL---ADWSPAELAR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 87 pkqierlrsRLGMVFQSFNLWSHMTVLQnVIE---GPHYVLKRSKQECIEQAEQLLDRVGMLNRkdFYPaQLSGGQQQRV 163
Cdd:PRK13548 77 ---------RRAVLPQHSSLSFPFTVEE-VVAmgrAPHGLSRAEDDALVAAALAQVDLAHLAGR--DYP-QLSGGEQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 164 AIARALA------MDPEVMLFDEPTSALDPELVGEVLKVMRSLA-EEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDG 236
Cdd:PRK13548 144 QLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
...
gi 490999375 237 APE 239
Cdd:PRK13548 224 TPA 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
9-230 |
9.09e-42 |
|
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: 140.98 E-value: 9.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLD--VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETI-EMKHHArghrlaa 85
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLrDLDLES------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 86 npkqierLRSRLGMVFQSFNLWShMTVLQNViegphyvlkrskqecieqaeqlldrvgmlnrkdfypaqLSGGQQQRVAI 165
Cdd:cd03228 74 -------LRKNIAYVPQDPFLFS-GTIRENI--------------------------------------LSGGQRQRIAI 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999375 166 ARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAeEGRTMLVVTHELGFARHVsNRVVFMHQG 230
Cdd:cd03228 108 ARALLRDPPILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRDA-DRIIVLDDG 170
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
22-246 |
1.28e-41 |
|
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: 151.14 E-value: 1.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 22 DVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaanpKQIER--LRSRLGM 99
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL---------------RQIDPasLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 100 VFQSFNLWShMTVLQNVIEG-PHYvlkrskqeCIEQAEQLLDRVGMLnrkDF---YP-----------AQLSGGQQQRVA 164
Cdd:COG2274 554 VLQDVFLFS-GTIRENITLGdPDA--------TDEEIIEAARLAGLH---DFieaLPmgydtvvgeggSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAeEGRTMLVVTHELGFARHVsNRVVFMHQGTIDCDGAPEALFGA 244
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDGTHEELLAR 699
|
..
gi 490999375 245 HG 246
Cdd:COG2274 700 KG 701
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-256 |
1.79e-41 |
|
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: 144.94 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 39 ILGASGSGKSTLLRCINLLETPDAGVVSVGGETI-EMKHHARGhrlaanpkqierlrsrLGMVFQSFNLWSHMTVLQNVI 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVtNVPPHLRH----------------INMVFQSYALFPHMTVEENVA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 118 egphYVLKRSKQECIEQAEQLLDRVGMLNRKDF---YPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVL 194
Cdd:TIGR01187 65 ----FGLKMRKVPRAEIKPRVLEALRLVQLEEFadrKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQ 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999375 195 KVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFgAHGSPRF-QQFISS 256
Cdd:TIGR01187 141 LELKTIQEQlGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIY-EEPANLFvARFIGE 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-244 |
3.05e-41 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 148.29 E-value: 3.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLD----VLKGISIQAQKGDVISILGASGSGKS-TLLRCINLLETPDA---GVVSVGGETIemkhharg 80
Cdd:COG4172 7 LSVEDLSVAFGQGGgtveAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAAhpsGSILFDGQDL-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 81 hrLAANPKQIERLR-SRLGMVFQ----SFNlwSHMTVLQNVIEgphyVLKR----SKQECIEQAEQLLDRVGMLN---RK 148
Cdd:COG4172 79 --LGLSERELRRIRgNRIAMIFQepmtSLN--PLHTIGKQIAE----VLRLhrglSGAAARARALELLERVGIPDperRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 149 DFYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSL-AEEGRTMLVVTHELGFARHVSNRVVFM 227
Cdd:COG4172 151 DAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVM 230
|
250
....*....|....*..
gi 490999375 228 HQGTIDCDGAPEALFGA 244
Cdd:COG4172 231 RQGEIVEQGPTAELFAA 247
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-239 |
8.87e-41 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 141.02 E-value: 8.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIE-MKHHARGHRLAANP 87
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAaWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 KQierlrSRLgmvfqSFNLwshmTVLQNVIEG--PHYVLKRSKQECIEQAeqlLDRVGMLNRKD-FYPaQLSGGQQQRVA 164
Cdd:COG4559 82 QH-----SSL-----AFPF----TVEEVVALGraPHGSSAAQDRQIVREA---LALVGLAHLAGrSYQ-TLSGGEQQRVQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 165 IARALA-------MDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGA 237
Cdd:COG4559 144 LARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGT 223
|
..
gi 490999375 238 PE 239
Cdd:COG4559 224 PE 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-242 |
3.73e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 141.14 E-value: 3.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 4 PRPVT----LSVSDIHKSFGS-----LDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEM 74
Cdd:PRK13631 13 PNPLSddiiLRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 75 KHHARGHRLAANPKQIE---RLRSRLGMVFQ--SFNLWSHmTVLQNVIEGPhYVLKRSKQECIEQAEQLLDRVGM----L 145
Cdd:PRK13631 93 KKNNHELITNPYSKKIKnfkELRRRVSMVFQfpEYQLFKD-TIEKDIMFGP-VALGVKKSEAKKLAKFYLNKMGLddsyL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 146 NRKDFypaQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVV 225
Cdd:PRK13631 171 ERSPF---GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVI 247
|
250
....*....|....*..
gi 490999375 226 FMHQGTIDCDGAPEALF 242
Cdd:PRK13631 248 VMDKGKILKTGTPYEIF 264
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-242 |
3.74e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 139.28 E-value: 3.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLL-----ETPDAGVVSVGGETI-EMkhharghr 82
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIfKM-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 83 laanpkQIERLRSRLGMVFQSFNLWSHMTVLQNVIEGPHY-VLKRSKQECIEQAEQLLDRVGML----NRKDFYPAQLSG 157
Cdd:PRK14247 76 ------DVIELRRRVQMVFQIPNPIPNLSIFENVALGLKLnRLVKSKKELQERVRWALEKAQLWdevkDRLDAPAGKLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 158 GQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEgRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGA 237
Cdd:PRK14247 150 GQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGP 228
|
....*
gi 490999375 238 PEALF 242
Cdd:PRK14247 229 TREVF 233
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
24-242 |
4.05e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 140.16 E-value: 4.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKhharghrlaANPKQIERLRSRLGMVFQ- 102
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAG---------KKNKKLKPLRKKVGIVFQf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 -SFNLWSHmTVLQNVIEGPHYvLKRSKQECIEQAEQLLDRVGM----LNRKDFypaQLSGGQQQRVAIARALAMDPEVML 177
Cdd:PRK13634 94 pEHQLFEE-TVEKDICFGPMN-FGVSEEDAKQKAREMIELVGLpeelLARSPF---ELSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490999375 178 FDEPTSALDPELVGEVLKVMRSL-AEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIF 234
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
9-221 |
5.15e-40 |
|
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: 137.61 E-value: 5.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlaanpK 88
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR--------------D 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRSRLGMVFQSFNLWSHMTVLQNViegpHYVLKRSKQEC-IEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIAR 167
Cdd:COG4133 69 AREDYRRRLAYLGHADGLKPELTVRENL----RFWAALYGLRAdREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 168 ALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTH---ELGFARHVS 221
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqplELAAARVLD 201
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
9-241 |
1.28e-39 |
|
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: 137.27 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghRLAANpk 88
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDIT--------KLPPH-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qiERLRSRLGMVFQSFNLWSHMTVLQNVIEGPHyVLKRSKQECIEQAEQL---LDRvgMLNRKDfypAQLSGGQQQRVAI 165
Cdd:TIGR03410 71 --ERARAGIAYVPQGREIFPRLTVEENLLTGLA-ALPRRSRKIPDEIYELfpvLKE--MLGRRG---GDLSGGQQQQLAI 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 166 ARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGR-TMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEAL 241
Cdd:TIGR03410 143 ARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-247 |
1.29e-39 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 137.41 E-value: 1.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 28 SIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETiemkhhargHRlAANPKQieRLRSrlgMVFQSFNLW 107
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD---------HT-TTPPSR--RPVS---MLFQENNLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 108 SHMTVLQNVIEGPHYVLKRSKQEcIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDP 187
Cdd:PRK10771 84 SHLTVAQNIGLGLNPGLKLNAAQ-REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490999375 188 ELVGEVLKVMRSLAEEGR-TMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGAHGS 247
Cdd:PRK10771 163 ALRQEMLTLVSQVCQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKAS 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
9-241 |
3.05e-39 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 137.45 E-value: 3.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGV---VSVGGETIEmkhhaRGHRLAa 85
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQ-----REGRLA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 86 npKQIERLRSRLGMVFQSFNLWSHMTVLQNVIEG-----PHY--VLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGG 158
Cdd:PRK09984 79 --RDIRKSRANTGYIFQQFNLVNRLSVLENVLIGalgstPFWrtCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 159 QQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAE-EGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGA 237
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
....
gi 490999375 238 PEAL 241
Cdd:PRK09984 237 SQQF 240
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-242 |
4.05e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 136.51 E-value: 4.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 13 DIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCIN-LLE-TPDA---GVVSVGGETIemkhhargHRLAANP 87
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrLLElNEEArveGEVRLFGRNI--------YSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 KQIerlRSRLGMVFQSFNLWSHMTVLQNVIEGPHY-VLKRSKQECIEQAEQLLDRVGML----NRKDFYPAQLSGGQQQR 162
Cdd:PRK14267 81 IEV---RREVGMVFQYPNPFPHLTIYDNVAIGVKLnGLVKSKKELDERVEWALKKAALWdevkDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 163 VAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEgRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
9-236 |
8.86e-39 |
|
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: 134.80 E-value: 8.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLD----VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetiemkhhargHRLA 84
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-----------FDVV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 85 ANPKQIerlRSRLGMVFQSFNLWSHMTVLQNVIE-GPHYVLKRskQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRV 163
Cdd:cd03266 71 KEPAEA---RRRLGFVSDSTGLYDRLTARENLEYfAGLYGLKG--DELTARLEELADRLGMEELLDRRVGGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490999375 164 AIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDG 236
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
10-239 |
9.62e-39 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 135.60 E-value: 9.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 10 SVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkHHARGHRLAanpKQ 89
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDV---ATTPSRELA---KR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 90 IERLRsrlgmvfQSFNLWSHMTVLQNVIEG--PHY--VLKRSKQECIEQAeqlLDRVGMLNRKDFYPAQLSGGQQQRVAI 165
Cdd:COG4604 77 LAILR-------QENHINSRLTVRELVAFGrfPYSkgRLTAEDREIIDEA---IAYLDLEDLADRYLDELSGGQRQRAFI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999375 166 ARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPE 239
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPE 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-242 |
1.02e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 136.37 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGG-ETIEMKHharghrlaanpkqIERLRSRLGMVF 101
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDTSDEEN-------------LWDIRNKAGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 102 QS-FNLWSHMTVLQNVIEGPHYvLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDE 180
Cdd:PRK13633 92 QNpDNQIVATIVEEDVAFGPEN-LGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490999375 181 PTSALDPELVGEVLKVMRSL-AEEGRTMLVVTHELGFARHvSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
9-230 |
1.07e-38 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 135.67 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGgeTIEMKhharGHRLAANPK 88
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITG--SIVYN----GHNIYSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRSRLGMVFQSFNLWShMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVGMLNR-KDFYPAQ---LSGGQQQRVA 164
Cdd:PRK14239 80 DTVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEvKDRLHDSalgLSGGQQQRVC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEgRTMLVVTHELGFARHVSNRVVFMHQG 230
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-253 |
1.43e-38 |
|
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: 141.44 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 4 PRPVTLSVSDIHKSF--GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhhargH 81
Cdd:COG4987 329 PGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL--------R 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 82 RLAAnpkqiERLRSRLGMVFQSFNLWsHMTVLQNviegphyvLKRSKQECI-EQAEQLLDRVGMLNRKDFYP-------- 152
Cdd:COG4987 401 DLDE-----DDLRRRIAVVPQRPHLF-DTTLREN--------LRLARPDATdEELWAALERVGLGDWLAALPdgldtwlg 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 153 ---AQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAeEGRTMLVVTHELGFARHVsNRVVFMHQ 229
Cdd:COG4987 467 eggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGLERM-DRILVLED 544
|
250 260
....*....|....*....|....
gi 490999375 230 GTIDCDGAPEALfgAHGSPRFQQF 253
Cdd:COG4987 545 GRIVEQGTHEEL--LAQNGRYRQL 566
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-238 |
1.55e-38 |
|
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: 134.17 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLD--VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVggetiemkhhaRGHRLAAN 86
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYI-----------NGYSIRTD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 87 PKQIerlRSRLGMVFQSFNLWSHMTVLQNV-----IEGphyvlkRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQ 161
Cdd:cd03263 70 RKAA---RQSLGYCPQFDALFDELTVREHLrfyarLKG------LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 162 RVAIARALAMDPEVMLFDEPTSALDPE---LVGEVLKVMRSlaeeGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAP 238
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPAsrrAIWDLILEVRK----GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
24-241 |
1.63e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 135.63 E-value: 1.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaaNPKQIERLRSRLGMVFQS 103
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV-------------NAENEKWVRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 FN--LWShMTVLQNVIEGPHYvLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEP 181
Cdd:PRK13647 88 PDdqVFS-STVWDDVAFGPVN-MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 182 TSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEAL 241
Cdd:PRK13647 166 MAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-236 |
2.74e-38 |
|
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: 133.09 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGdVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaanPK 88
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV--------------LK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRSRLGMVFQSFNLWSHMTVLQNViegpHY--VLKR-SKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAI 165
Cdd:cd03264 66 QPQKLRRRIGYLPQEFGVYPNFTVREFL----DYiaWLKGiPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490999375 166 ARALAMDPEVMLFDEPTSALDPElvgEVLKVMRSLAE--EGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDG 236
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPE---ERIRFRNLLSElgEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
16-241 |
4.51e-38 |
|
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: 135.21 E-value: 4.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 16 KSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlaanpKQIERLRS 95
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV--------------REPRKVRR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 96 RLGMVFQSFNLWSHMTVLQN-VIEGPHYVLKRSKQEciEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPE 174
Cdd:TIGR01188 67 SIGIVPQYASVDEDLTGRENlEMMGRLYGLPKDEAE--ERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPD 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 175 VMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEAL 241
Cdd:TIGR01188 145 VLFLDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-227 |
4.62e-38 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 134.22 E-value: 4.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 8 TLSVSDIHKSFGSLD----VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrl 83
Cdd:COG4525 3 MLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 84 aaNPKQiERlrsrlGMVFQSFNLWSHMTVLQNVIEGphyvLK---RSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQ 160
Cdd:COG4525 73 --GPGA-DR-----GVVFQKDALLPWLNVLDNVAFG----LRlrgVPKAERRARAEELLALVGLADFARRRIWQLSGGMR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 161 QRVAIARALAMDPEVMLFDEPTSALDP---ELVGEVLkvMRSLAEEGRTMLVVTHELGFARHVSNRVVFM 227
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALDAltrEQMQELL--LDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-246 |
4.67e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 140.30 E-value: 4.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 22 DVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhhaRGHRLAAnpkqierLRSRLGMVF 101
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI------RDLTLES-------LRRQIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 102 QSFNLWsHMTVLQNVIEG-PHYvlkrSKQECIEQAE--QLLDRVGMLnrkdfyP-----------AQLSGGQQQRVAIAR 167
Cdd:COG1132 421 QDTFLF-SGTIRENIRYGrPDA----TDEEVEEAAKaaQAHEFIEAL------PdgydtvvgergVNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 168 ALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAeEGRTMLVVTHELGFARHVsNRVVFMHQGTIDCDGAPEALFGAHG 246
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRNA-DRILVLDDGRIVEQGTHEELLARGG 566
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
24-243 |
5.40e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 134.47 E-value: 5.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaaNPKQIERLRSRLGMVFQS 103
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL-------------TEENVWDIRHKIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 -FNLWSHMTVLQNVIEG------PHyvlkrskQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVM 176
Cdd:PRK13650 90 pDNQFVGATVEDDVAFGlenkgiPH-------EEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 177 LFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARhVSNRVVFMHQGTIDCDGAPEALFG 243
Cdd:PRK13650 163 ILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFS 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-246 |
6.19e-38 |
|
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: 139.89 E-value: 6.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 3 DPRPVTLSVSDIHKSF-GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetiemkhhargH 81
Cdd:COG4988 331 AAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING-----------V 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 82 RLAANPkqIERLRSRLGMVFQS---FnlwsHMTVLQNVIEG-PHYvlkrSKQEcIEQAeqlLDRVGMLnrkDFYPAQ--- 154
Cdd:COG4988 400 DLSDLD--PASWRRQIAWVPQNpylF----AGTIRENLRLGrPDA----SDEE-LEAA---LEAAGLD---EFVAALpdg 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 155 -----------LSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAeEGRTMLVVTHELGFARHvSNR 223
Cdd:COG4988 463 ldtplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADR 540
|
250 260
....*....|....*....|...
gi 490999375 224 VVFMHQGTIDCDGAPEALFGAHG 246
Cdd:COG4988 541 ILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-232 |
1.31e-37 |
|
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: 131.19 E-value: 1.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGEtiemkhharghrlaaNPK 88
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK---------------SYQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRSRLGMVFQSFNLWSHMTVLQNVIEGPHYVLKRSKQecieqAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARA 168
Cdd:cd03268 66 KNIEALRRIGALIEAPGFYPNLTARENLRLLARLLGIRKKR-----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999375 169 LAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
22-217 |
1.49e-37 |
|
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: 130.62 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 22 DVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGEtiEMKHHARGhrlaanpkqIERLRSRLGMVF 101
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGE--PLDYSRKG---------LLERRQRVGLVF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 102 QSFN--LWShMTVLQNVIEGPHYvLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFD 179
Cdd:TIGR01166 75 QDPDdqLFA-ADVDQDVAFGPLN-LGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLD 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 490999375 180 EPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFA 217
Cdd:TIGR01166 153 EPTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
9-256 |
2.75e-37 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 134.96 E-value: 2.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlaanpk 88
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRSRLGMVFQSFNLWSHMTVLQNVIEGphyvLKR---SKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAI 165
Cdd:PRK11607 85 HVPPYQRPINMMFQSYALFPHMTVEQNIAFG----LKQdklPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 166 ARALAMDPEVMLFDEPTSALDPELVGEV-LKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFgA 244
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY-E 239
|
250
....*....|...
gi 490999375 245 HGSPRFQ-QFISS 256
Cdd:PRK11607 240 HPTTRYSaEFIGS 252
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-241 |
3.20e-37 |
|
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: 130.95 E-value: 3.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 11 VSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGvvsvggetiemKHHARGHRLAANPKQI 90
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG-----------RATVAGHDVVREPREV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 91 erlRSRLGMVFQSFNLWSHMTVLQNV-IEGPHYVLKRSKQEciEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARAL 169
Cdd:cd03265 72 ---RRRIGIVFQDLSVDDELTGWENLyIHARLYGVPGAERR--ERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490999375 170 AMDPEVMLFDEPTSALDPELVGEVLKVMRSL-AEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEAL 241
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-243 |
7.56e-37 |
|
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: 130.28 E-value: 7.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetiemkhharghrlaanpKQIERLRSRLGMVFQS 103
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG------------------KQITEPGPDRMVVFQN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 FNLWSHMTVLQNVIEGPHYVLK-RSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEPT 182
Cdd:TIGR01184 63 YSLLPWLTVRENIALAVDRVLPdLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490999375 183 SALDPELVGEVL-KVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGtidcdgaPEALFG 243
Cdd:TIGR01184 143 GALDALTRGNLQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG-------PAANIG 197
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
9-227 |
7.85e-37 |
|
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: 129.86 E-value: 7.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSF-----GS--LDVLKGISIQAQKGDVISILGASGSGKSTLLRCI--NLLetPDAGVVSV--GGETIEMkhh 77
Cdd:COG4778 5 LEVENLSKTFtlhlqGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYL--PDSGSILVrhDGGWVDL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 78 arghrLAANPKQIERLRSR-LGMVFQSFNLWSHMTVLQNVIEgPHYVLKRSKQECIEQAEQLLDRvgmLNRK----DFYP 152
Cdd:COG4778 80 -----AQASPREILALRRRtIGYVSQFLRVIPRVSALDVVAE-PLLERGVDREEARARARELLAR---LNLPerlwDLPP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999375 153 AQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFM 227
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
28-232 |
1.44e-36 |
|
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: 128.83 E-value: 1.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 28 SIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetiemKHHARghrlaanpkqIERLRSRLGMVFQSFNLW 107
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVND-----QSHTG----------LAPYQRPVSMLFQENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 108 SHMTVLQNVIEGPHYVLKRSKQEcIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDP 187
Cdd:TIGR01277 83 AHLTVRQNIGLGLHPGLKLNAEQ-QEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490999375 188 ELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:TIGR01277 162 LLREEMLALVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-251 |
1.65e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 131.00 E-value: 1.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 8 TLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHARghrlaanp 87
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 kqI-----ERlrsrlGmvfqsfnLWSHMTVLQNVIegphYV--LK-RSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQ 159
Cdd:COG4152 73 --IgylpeER-----G-------LYPKMKVGEQLV----YLarLKgLSKAEAKRRADEWLERLGLGDRANKKVEELSKGN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 160 QQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPE 239
Cdd:COG4152 135 QQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD 214
|
250
....*....|..
gi 490999375 240 ALFGAHGSPRFQ 251
Cdd:COG4152 215 EIRRQFGRNTLR 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
8-238 |
3.43e-36 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 131.50 E-value: 3.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 8 TLSVSDIHKSF-GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETI-EMKHHARGhrlaa 85
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnELEPADRD----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 86 npkqierlrsrLGMVFQSFNLWSHMTVLQNViegpHYVLK-R--SKQEC---IEQAEQLLDRVGMLNRKdfyPAQLSGGQ 159
Cdd:PRK11650 78 -----------IAMVFQNYALYPHMSVRENM----AYGLKiRgmPKAEIeerVAEAARILELEPLLDRK---PRELSGGQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 160 QQRVAIARALAMDPEVMLFDEPTSALDPELVG----EVLKVMRSLaeeGRTMLVVTHELGFARHVSNRVVFMHQGTIDCD 235
Cdd:PRK11650 140 RQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVqmrlEIQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNGGVAEQI 216
|
...
gi 490999375 236 GAP 238
Cdd:PRK11650 217 GTP 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
24-242 |
3.66e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 129.97 E-value: 3.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHharghrlaanpKQIERLRSRLGMVFQS 103
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSR-----------KGLMKLRESVGMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 --FNLWShMTVLQNVIEGPhYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEP 181
Cdd:PRK13636 91 pdNQLFS-ASVYQDVSFGA-VNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490999375 182 TSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK13636 169 TAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-230 |
4.61e-36 |
|
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: 127.40 E-value: 4.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGEtiemkhharghrlaanPK 88
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK----------------PL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERlRSRLGMVFQSFNLWSHMTVLQNVIegphYV--LK-RSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAI 165
Cdd:cd03269 65 DIAA-RNRIGYLPEERGLYPKMKVIDQLV----YLaqLKgLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999375 166 ARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQG 230
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
9-258 |
5.94e-36 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 128.80 E-value: 5.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSF---------GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHAR 79
Cdd:COG4167 5 LEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 80 ghrlaanpkqierlRSRL-GMVFQ----SFNlwSHMTVLQnVIEGPhyvLKR----SKQECIEQAEQLLDRVGML-NRKD 149
Cdd:COG4167 85 --------------RCKHiRMIFQdpntSLN--PRLNIGQ-ILEEP---LRLntdlTAEEREERIFATLRLVGLLpEHAN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 150 FYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMH 228
Cdd:COG4167 145 FYPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMH 224
|
250 260 270
....*....|....*....|....*....|
gi 490999375 229 QGTIDCDGAPEALFGAHGSPRFQQFISSHH 258
Cdd:COG4167 225 QGEVVEYGKTAEVFANPQHEVTKRLIESHF 254
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
36-243 |
9.63e-36 |
|
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: 130.23 E-value: 9.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 36 VISILGASGSGKSTLLRCINLLETPDAGVVSVGGETieMKHHARGHRLAANpkqierlRSRLGMVFQSFNLWSHMTVLQN 115
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRT--LFDSRKGIFLPPE-------KRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 116 VIEGPHYVLKRSKQECIEQAEQLLDRVGMLNRkdfYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLK 195
Cdd:TIGR02142 96 LRYGMKRARPSERRISFERVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490999375 196 VMRSLAEEGRT-MLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFG 243
Cdd:TIGR02142 173 YLERLHAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
8-241 |
1.68e-35 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 126.68 E-value: 1.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 8 TLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkHHARGHRlaanp 87
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI---THLPMHK----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 kqierlRSRLGM--------VFQsfnlwsHMTVLQN---VIEgphyVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLS 156
Cdd:COG1137 75 ------RARLGIgylpqeasIFR------KLTVEDNilaVLE----LRKLSKKEREERLEELLEEFGITHLRKSKAYSLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 157 GGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEG----------RTMLVVThelgfarhvsNRVVF 226
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGigvlitdhnvRETLGIC----------DRAYI 208
|
250
....*....|....*
gi 490999375 227 MHQGTIDCDGAPEAL 241
Cdd:COG1137 209 ISEGKVLAEGTPEEI 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
8-244 |
1.80e-35 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 130.73 E-value: 1.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 8 TLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlAANP 87
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVE----------ALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 KQIERlrsRLGMVFQSFNLWSHMTVLQNVIEG--PHYVLKRSKQECIEQA-EQLLDRVGMLNRKDFYPAQLSGGQQQRVA 164
Cdd:PRK09536 73 RAASR---RVASVPQDTSLSFEFDVRQVVEMGrtPHRSRFDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGA 244
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTA 229
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
9-241 |
2.96e-35 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 126.64 E-value: 2.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKhhaRGHRLAanpk 88
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL---PGHQIA---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qierlrsRLGMV--FQSFNLWSHMTVLQNVIEGPHYVLK--------------RSKQECIEQAEQLLDRVGML---NRKd 149
Cdd:PRK11300 79 -------RMGVVrtFQHVRLFREMTVIENLLVAQHQQLKtglfsgllktpafrRAESEALDRAATWLERVGLLehaNRQ- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 150 fyPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMH 228
Cdd:PRK11300 151 --AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVN 228
|
250
....*....|...
gi 490999375 229 QGTIDCDGAPEAL 241
Cdd:PRK11300 229 QGTPLANGTPEEI 241
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
24-256 |
4.45e-35 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 128.16 E-value: 4.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrLAANPKQIERLRSRLGMVFQ- 102
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL----------LKADPEAQKLLRQKIQIVFQn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 ---SFNlwSHMTVLQnVIEGPHYV-LKRSKQECIEQAEQLLDRVGMlnRKDF---YPAQLSGGQQQRVAIARALAMDPEV 175
Cdd:PRK11308 101 pygSLN--PRKKVGQ-ILEEPLLInTSLSAAERREKALAMMAKVGL--RPEHydrYPHMFSGGQRQRIAIARALMLDPDV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 176 MLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGAHGSPRFQQFI 254
Cdd:PRK11308 176 VVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALL 255
|
..
gi 490999375 255 SS 256
Cdd:PRK11308 256 SA 257
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-241 |
5.68e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 127.23 E-value: 5.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 3 DPRPVT-LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhhargh 81
Cdd:PRK13537 1 GPMSVApIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 82 rlaanPKQIERLRSRLGMVFQSFNLWSHMTVLQNV-IEGPHYVLkrSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQ 160
Cdd:PRK13537 72 -----PSRARHARQRVGVVPQFDNLDPDFTVRENLlVFGRYFGL--SAAAARALVPPLLEFAKLENKADAKVGELSGGMK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 161 QRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEA 240
Cdd:PRK13537 145 RRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHA 224
|
.
gi 490999375 241 L 241
Cdd:PRK13537 225 L 225
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-249 |
1.19e-34 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 127.84 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 7 VTLSvsDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETI-EMKHHARGhrlaa 85
Cdd:PRK11000 4 VTLR--NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMnDVPPAERG----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 86 npkqierlrsrLGMVFQSFNLWSHMTVLQNVIEGphyvLKRSK------QECIEQAEQLLDRVGMLNRKdfyPAQLSGGQ 159
Cdd:PRK11000 77 -----------VGMVFQSYALYPHLSVAENMSFG----LKLAGakkeeiNQRVNQVAEVLQLAHLLDRK---PKALSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 160 QQRVAIARALAMDPEVMLFDEPTSALDPEL-VG---EVLKVMRSLaeeGRTMLVVTHELGFARHVSNRVVFMHQGTIDCD 235
Cdd:PRK11000 139 RQRVAIGRTLVAEPSVFLLDEPLSNLDAALrVQmriEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQV 215
|
250 260
....*....|....*....|...
gi 490999375 236 GAPEALF---------GAHGSPR 249
Cdd:PRK11000 216 GKPLELYhypanrfvaGFIGSPK 238
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
18-230 |
1.20e-34 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 124.22 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 18 FGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghRLAAnpKQIERLRSRL 97
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDIT--------RLKN--REVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 98 GMVFQSFNLWSHMTVLQNVIEgPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVML 177
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490999375 178 FDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQG 230
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-230 |
1.67e-34 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 126.74 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 1 MHDPRPVTLSVSDIHKSFG-------------SLDVLKGISIQAQKGDVISILGASGSGKSTLLRC-INLLETPDAGVVS 66
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAiIGLVKATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 67 VGGETIEMKHharghrlaanpKQIERLRSRLGMVFQ----SFNlwSHMTVlQNVIEGP--HYVLKRSKQECIEQAEQLLD 140
Cdd:PRK15079 81 LGKDLLGMKD-----------DEWRAVRSDIQMIFQdplaSLN--PRMTI-GEIIAEPlrTYHPKLSRQEVKDRVKAMML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 141 RVGML----NRkdfYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELG 215
Cdd:PRK15079 147 KVGLLpnliNR---YPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLA 223
|
250
....*....|....*
gi 490999375 216 FARHVSNRVVFMHQG 230
Cdd:PRK15079 224 VVKHISDRVLVMYLG 238
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-261 |
2.00e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 125.62 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 27 ISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMkhharghrlAANPKQIERLRSRLGMVFQ--SF 104
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSS---------TSKQKEIKPVRKKVGVVFQfpES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 105 NLWSHmTVLQNVIEGPHYvLKRSKQECIEQAEQLLDRVGMlnRKDFY---PAQLSGGQQQRVAIARALAMDPEVMLFDEP 181
Cdd:PRK13643 96 QLFEE-TVLKDVAFGPQN-FGIPKEKAEKIAAEKLEMVGL--ADEFWeksPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 182 TSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF------GAH--GSPRFQQF 253
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFqevdflKAHelGVPKATHF 251
|
....*...
gi 490999375 254 ISSHHQPG 261
Cdd:PRK13643 252 ADQLQKTG 259
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
24-243 |
2.02e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 125.28 E-value: 2.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKhharghrlaANPKQIERLRSRLGMVFQ- 102
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHK---------TKDKYIRPVRKRIGMVFQf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 -SFNLWSHmTVLQNVIEGPHYvLKRSKQECIEQAEQLLDRVGM-LNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDE 180
Cdd:PRK13646 94 pESQLFED-TVEREIIFGPKN-FKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999375 181 PTSALDPELVGEVLKVMRSLA-EEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFG 243
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-235 |
2.84e-34 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 124.02 E-value: 2.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkHHARghrlaanpk 88
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL---AEAR--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qiERLRsrlgMVFQSFNLWSHMTVLQNVIEGphyvLKRSKQEcieQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARA 168
Cdd:PRK11247 81 --EDTR----LMFQDARLLPWKKVIDNVGLG----LKGQWRD---AALQALAAVGLADRANEWPAALSGGQKQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 169 LAMDPEVMLFDEPTSALDPELVGEVLKVMRSL-AEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCD 235
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
23-242 |
5.18e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 123.95 E-value: 5.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaaNPKQIERLRSRLGMVFQ 102
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI-------------SKENLKEIRKKIGIIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 S-FNLWSHMTV-------LQNViegphyVLKRSKQECIeqAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPE 174
Cdd:PRK13632 91 NpDNQFIGATVeddiafgLENK------KVPPKKMKDI--IDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 175 VMLFDEPTSALDPELVGEVLKVMRSLAEEG-RTMLVVTHELGFARhVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEIL 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-242 |
1.06e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 123.62 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHharghrlaANPKQIerlRSRLGMVFQ- 102
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKK--------VKLSDI---RKKVGLVFQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 -SFNLWSHmTVLQNVIEGPHYvLKRSKQECIEQAEQLLDRVGM--LNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFD 179
Cdd:PRK13637 92 pEYQLFEE-TIEKDIAFGPIN-LGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999375 180 EPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
24-242 |
1.83e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 123.02 E-value: 1.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKhharghrlaANPKQIERLRSRLGMVFQ- 102
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPE---------TGNKNLKKLRKKVSLVFQf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 SFNLWSHMTVLQNVIEGPHYvLKRSKQECIEQAEQLLDRVG----MLNRKDFypaQLSGGQQQRVAIARALAMDPEVMLF 178
Cdd:PRK13641 94 PEAQLFENTVLKDVEFGPKN-FGFSEDEAKEKALKWLKKVGlsedLISKSPF---ELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999375 179 DEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
9-242 |
2.31e-33 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 121.34 E-value: 2.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAG-VVSVGGETiemkhhaRGHRlaanp 87
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGER-------RGGE----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 kQIERLRSRLGMVFQSFNLW--SHMTVLQNVIEGPHYVLKRSKQ---ECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQR 162
Cdd:COG1119 72 -DVWELRKRIGLVSPALQLRfpRDETVLDVVLSGFFDSIGLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 163 VAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEG-RTMLVVTHelgfarHVS------NRVVFMHQGTIDCD 235
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTH------HVEeippgiTHVLLLKDGRVVAA 224
|
....*..
gi 490999375 236 GAPEALF 242
Cdd:COG1119 225 GPKEEVL 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
15-242 |
2.34e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 122.60 E-value: 2.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 15 HKSFGSLD----VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDA---GVVSVGGETIemkhharghrlaaNP 87
Cdd:PRK13640 10 HVSFTYPDskkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITL-------------TA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 KQIERLRSRLGMVFQS-FNLWSHMTVLQNVIEGphyVLKR--SKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVA 164
Cdd:PRK13640 77 KTVWDIREKVGIVFQNpDNQFVGATVGDDVAFG---LENRavPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHvSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIF 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-230 |
3.43e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 120.69 E-value: 3.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 20 SLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhhargHRLAANPKQIERLRsRLGM 99
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPM--------SKLSSAAKAELRNQ-KLGF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 100 VFQSFNLWSHMTVLQNVIEgPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFD 179
Cdd:PRK11629 92 IYQFHHLLPDFTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490999375 180 EPTSALDPELVGEVLKVMRSL-AEEGRTMLVVTHELGFARHVSnRVVFMHQG 230
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMS-RQLEMRDG 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
9-232 |
8.02e-33 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 120.56 E-value: 8.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSF---------GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhhar 79
Cdd:PRK10419 4 LNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLA------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 80 ghrlAANPKQIERLRSRLGMVFQ----SFNlwSHMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVGM-LNRKDFYPAQ 154
Cdd:PRK10419 78 ----KLNRAQRKAFRRDIQMVFQdsisAVN--PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 155 LSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRT-MLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-245 |
8.49e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 122.25 E-value: 8.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 6 PVTLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaa 85
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV------------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 86 nPKQIERLRSRLGMVFQSFNLWSHMTVLQN-VIEGPHYVLKRSKQECIeqAEQLLDRVGMLNRKDFYPAQLSGGQQQRVA 164
Cdd:PRK13536 106 -PARARLARARIGVVPQFDNLDLEFTVRENlLVFGRYFGMSTREIEAV--IPSLLEFARLESKADARVSDLSGGMKRRLT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGA 244
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE 262
|
.
gi 490999375 245 H 245
Cdd:PRK13536 263 H 263
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-244 |
1.07e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 120.59 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 18 FGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharGHRLAANPKQIERLRSRL 97
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLL-------GGRSIFNYRDVLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 98 GMVFQSFNLWShMTVLQNVIEG--PHYVLKRSKQECIEQAEqlLDRVGMLN----RKDFYPAQLSGGQQQRVAIARALAM 171
Cdd:PRK14271 104 GMLFQRPNPFP-MSIMDNVLAGvrAHKLVPRKEFRGVAQAR--LTEVGLWDavkdRLSDSPFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490999375 172 DPEVMLFDEPTSALDPELVGEVLKVMRSLAEEgRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGA 244
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-246 |
1.08e-32 |
|
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: 119.26 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 15 HKSFG---SLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlaanPKQIE 91
Cdd:cd03253 5 NVTFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIR-------------EVTLD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 92 RLRSRLGMVFQSFNLWsHMTVLQNVIEGPhyvLKRSKQECIEQAE--QLLDRVgmLNRKDFYPAQ-------LSGGQQQR 162
Cdd:cd03253 72 SLRRAIGVVPQDTVLF-NDTIGYNIRYGR---PDATDEEVIEAAKaaQIHDKI--MRFPDGYDTIvgerglkLSGGEKQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 163 VAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAeEGRTMLVVTHELgfaRHVSN--RVVFMHQGTIDCDGAPEA 240
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRL---STIVNadKIIVLKDGRIVERGTHEE 221
|
....*.
gi 490999375 241 LFGAHG 246
Cdd:cd03253 222 LLAKGG 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-242 |
1.29e-32 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 123.22 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMkhharghrlAANPKQIERLRSRLGMVFQS 103
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAK---------ISDAELREVRRKKIAMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 FNLWSHMTVLQNVIEGPHyVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTS 183
Cdd:PRK10070 115 FALMPHMTVLDNTAFGME-LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490999375 184 ALDP----ELVGEVLKVMrslAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK10070 194 ALDPlirtEMQDELVKLQ---AKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
15-242 |
1.94e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 119.91 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 15 HKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaaNPKQIERLR 94
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI-------------TKENIREVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 95 SRLGMVFQSFN--LWShMTVLQNVIEGPhYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMD 172
Cdd:PRK13652 78 KFVGLVFQNPDdqIFS-PTVEQDIAFGP-INLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490999375 173 PEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIF 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-242 |
2.35e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 119.71 E-value: 2.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETiemkhharghrlAANPKQIERLRSRLGMVFQS 103
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID------------TGDFSKLQGIRKLVGIVFQN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 FNL-WSHMTVLQNVIEGPHYvLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEPT 182
Cdd:PRK13644 86 PETqFVGRTVEEDLAFGPEN-LCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 183 SALDPELVGEVLKVMRSLAEEGRTMLVVTHELGfARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
24-243 |
6.23e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 118.66 E-value: 6.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGEtiemkhharghRLAAnpKQIERLRSRLGMVFQS 103
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-----------LLTA--ENVWNLRRKIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 -FNLWSHMTVLQNVIEGPHYvLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEPT 182
Cdd:PRK13642 90 pDNQFVGATVEDDVAFGMEN-QGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDEST 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490999375 183 SALDPELVGEVLKVMRSLAEEGR-TMLVVTHELGFARHvSNRVVFMHQGTIDCDGAPEALFG 243
Cdd:PRK13642 169 SMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
9-224 |
8.89e-32 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 116.80 E-value: 8.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGS----LDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhhargHRLa 84
Cdd:PRK10584 7 VEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL--------HQM- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 85 aNPKQIERLRSR-LGMVFQSFNLWSHMTVLQNViEGPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRV 163
Cdd:PRK10584 78 -DEEARAKLRAKhVGFVFQSFMLIPTLNALENV-ELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490999375 164 AIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRV 224
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRL 217
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
9-232 |
9.49e-32 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 117.72 E-value: 9.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGEtiemkhHARGHRLAANPK 88
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR------DGQLRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIER--LRSRLGMVFQSFNLWSHMTVLQ--NVIEGPHYVLKRSKQECIEQAEQLLDRVGM-LNRKDFYPAQLSGGQQQRV 163
Cdd:PRK11701 81 AERRrlLRTEWGFVHQHPRDGLRMQVSAggNIGERLMAVGARHYGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 164 AIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSL-AEEGRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-233 |
2.52e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 120.94 E-value: 2.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 11 VSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVggetiemkhharghrlaanPKQI 90
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-------------------PKGL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 91 erlrsRLGMVFQSFNLWSHMTVLQNVIEG--PHYVLKRSKQECIE-----------------------------QAEQLL 139
Cdd:COG0488 62 -----RIGYLPQEPPLDDDLTVLDTVLDGdaELRALEAELEELEAklaepdedlerlaelqeefealggweaeaRAEEIL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 140 DRVGmLNRKDFY--PAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVG---EVLKvmrslAEEGrTMLVVTHEL 214
Cdd:COG0488 137 SGLG-FPEEDLDrpVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEwleEFLK-----NYPG-TVLVVSHDR 209
|
250
....*....|....*....
gi 490999375 215 GFARHVSNRVVFMHQGTID 233
Cdd:COG0488 210 YFLDRVATRILELDRGKLT 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-242 |
5.72e-31 |
|
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: 114.95 E-value: 5.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhHARGHRlaanpk 88
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT---KLPMHK------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qierlRSRLGMVF--QSFNLWSHMTVLQN---VIEgphyVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRV 163
Cdd:cd03218 72 -----RARLGIGYlpQEASIFRKLTVEENilaVLE----IRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 164 AIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:cd03218 143 EIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
9-256 |
6.28e-31 |
|
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: 115.31 E-value: 6.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVV---SVGGETIEMkhhargHRLAa 85
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyiMRSGAELEL------YQLS- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 86 NPKQIERLRSRLGMVFQSFNLWSHMTVLQ--NVIEGPHYVLKRSKQECIEQAEQLLDRVGM-LNRKDFYPAQLSGGQQQR 162
Cdd:TIGR02323 77 EAERRRLMRTEWGFVHQNPRDGLRMRVSAgaNIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 163 VAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEAL 241
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQV 236
|
250
....*....|....*
gi 490999375 242 FGAHGSPRFQQFISS 256
Cdd:TIGR02323 237 LDDPQHPYTQLLVSS 251
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
24-242 |
6.44e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 115.62 E-value: 6.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGvvsvggeTIEMKHHArghrlaANPKQIERLRSRLGMVFQS 103
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG-------EIFYNNQA------ITDDNFEKLRKHIGIVFQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 -FNLWSHMTVLQNVIEG--PHYVlkrSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDE 180
Cdd:PRK13648 92 pDNQFVGSIVKYDVAFGleNHAV---PYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490999375 181 PTSALDPELVGEVLKVMRSLAEEGR-TMLVVTHELGFARHvSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-212 |
8.37e-31 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 113.73 E-value: 8.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 8 TLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCInlLETPDAGVvSVGGETIemkhhARGHRLAANP 87
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAI--AGTLSPAF-SASGEVL-----LNGRRLTALP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 KQierlRSRLGMVFQSFNLWSHMTVLQNVIEG-PHYVLKRSKQECIEQAeqlLDRVGMLNRKDFYPAQLSGGQQQRVAIA 166
Cdd:COG4136 73 AE----QRRIGILFQDDLLFPHLSVGENLAFAlPPTIGRAQRRARVEQA---LEEAGLAGFADRDPATLSGGQRARVALL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490999375 167 RALAMDPEVMLFDEPTSALDPELVGEVLK-VMRSLAEEGRTMLVVTH 212
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTH 192
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
24-242 |
1.51e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 114.84 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghRLAANPKQIERLRSRLGMVFQ- 102
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLI---------TSTSKNKDIKQIRKKVGLVFQf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 -SFNLWSHmTVLQNVIEGPHYvLKRSKQECIEQAEQLLDRVGML-NRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDE 180
Cdd:PRK13649 94 pESQLFEE-TVLKDVAFGPQN-FGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490999375 181 PTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
23-246 |
2.21e-30 |
|
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: 113.40 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTllrCINLLE---TPDAGVVSVGGETIemkhhargHRLAanpkqIERLRSRLGM 99
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLErfyDPTSGEILLDGVDI--------RDLN-----LRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 100 VFQSFNLWShMTVLQNVIEGPHYVLKRSKQECIEQA----------EQLLDRVGmlnrkdFYPAQLSGGQQQRVAIARAL 169
Cdd:cd03249 82 VSQEPVLFD-GTIAENIRYGKPDATDEEVEEAAKKAnihdfimslpDGYDTLVG------ERGSQLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 170 AMDPEVMLFDEPTSALDPE---LVGEVL-KVMRslaeeGRTMLVVTHELGFARHvSNRVVFMHQGTIDCDGAPEALFGAH 245
Cdd:cd03249 155 LRNPKILLLDEATSALDAEsekLVQEALdRAMK-----GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQK 228
|
.
gi 490999375 246 G 246
Cdd:cd03249 229 G 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
23-246 |
2.51e-30 |
|
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: 113.09 E-value: 2.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetiemkHHARGHRLAAnpkqierLRSRLGMVFQ 102
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG------HDVRDYTLAS-------LRRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 SFNLWSHmTVLQNVIegphYVLKRSKQECIEQAEQlldrvgMLNRKDF-------YPA-------QLSGGQQQRVAIARA 168
Cdd:cd03251 84 DVFLFND-TVAENIA----YGRPGATREEVEEAAR------AANAHEFimelpegYDTvigergvKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 169 LAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAeEGRTMLVVTHELGFARHvSNRVVFMHQGTIDCDGAPEALFGAHG 246
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQGG 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
13-232 |
2.52e-30 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 115.74 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 13 DIHKSFGSLDVLKGISIQAQkgDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETieMKHHARGHRLAANpkqier 92
Cdd:PRK11144 5 NFKQQLGDLCLTVNLTLPAQ--GITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRV--LFDAEKGICLPPE------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 93 lRSRLGMVFQSFNLWSHMTVLQNViegpHYVLKRSKQECIEQAEQLLDRVGMLNRkdfYPAQLSGGQQQRVAIARALAMD 172
Cdd:PRK11144 75 -KRRIGYVFQDARLFPHYKVRGNL----RYGMAKSMVAQFDKIVALLGIEPLLDR---YPGSLSGGEKQRVAIGRALLTA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490999375 173 PEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRT-MLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:PRK11144 147 PELLLMDEPLASLDLPRKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-218 |
3.18e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 111.56 E-value: 3.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 17 SFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVsvggetiemkHHARGHRLAANPKQIERLRSR 96
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV----------RRAGGARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 97 LGMVFQ--SFNLWSHmtvlqnviEGPHYVLKRSKQECIEQAeqlLDRVGMLnrkDFYPAQ---LSGGQQQRVAIARALAM 171
Cdd:NF040873 71 PLTVRDlvAMGRWAR--------RGLWRRLTRDDRAAVDDA---LERVGLA---DLAGRQlgeLSGGQRQRALLAQGLAQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490999375 172 DPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFAR 218
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVR 183
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-232 |
7.33e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.87 E-value: 7.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSF--GSLD---VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETI-EMKHHARGhr 82
Cdd:COG1101 2 LELKNLSKTFnpGTVNekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtKLPEYKRA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 83 laanpKQIERlrsrlgmVFQ--SFNLWSHMTVLQNVI----EGPHYVLKRS-KQECIEQAEQLLDRVGM-L-NRKDFYPA 153
Cdd:COG1101 80 -----KYIGR-------VFQdpMMGTAPSMTIEENLAlayrRGKRRGLRRGlTKKRRELFRELLATLGLgLeNRLDTKVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 154 QLSGGQQQrvaiARALAM----DPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGR-TMLVVTHELGFARHVSNRVVFMH 228
Cdd:COG1101 148 LLSGGQRQ----ALSLLMatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNRLIMMH 223
|
....
gi 490999375 229 QGTI 232
Cdd:COG1101 224 EGRI 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-232 |
7.51e-30 |
|
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: 110.21 E-value: 7.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 6 PVTLSVSDIHKSfgslDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMK--HHARGHRL 83
Cdd:cd03215 2 EPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRspRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 84 AANPKqiERLRSrlGMVFQsfnlwshMTVLQNVIegphyvlkrskqecieqaeqlldrvgmlnrkdfYPAQLSGGQQQRV 163
Cdd:cd03215 78 AYVPE--DRKRE--GLVLD-------LSVAENIA---------------------------------LSSLLSGGNQQKV 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 164 AIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:cd03215 114 VLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-226 |
1.18e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 112.18 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 7 VTLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETpdagvvSVGGETIEMKHHARGHRLAAN 86
Cdd:PRK14243 9 TVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLND------LIPGFRVEGKVTFHGKNLYAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 87 PKQIERLRSRLGMVFQSFNLWSHmTVLQNVIEGPHYV-LKRSKQECIEQAEQ---LLDRVgmlnrKDFYPAQ---LSGGQ 159
Cdd:PRK14243 83 DVDPVEVRRRIGMVFQKPNPFPK-SIYDNIAYGARINgYKGDMDELVERSLRqaaLWDEV-----KDKLKQSglsLSGGQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 160 QQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEgRTMLVVTHELGFARHVSNRVVF 226
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAF 222
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
23-249 |
1.71e-29 |
|
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: 116.50 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaanpKQIER--LRSRLGMV 100
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDI---------------RQIDPadLRRNIGYV 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 101 FQSFNLWsHMTVLQNVIEGPHYVlkrSKQECIEQAEqlldRVGMLNRKDFYP-----------AQLSGGQQQRVAIARAL 169
Cdd:TIGR03375 545 PQDPRLF-YGTLRDNIALGAPYA---DDEEILRAAE----LAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARAL 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 170 AMDPEVMLFDEPTSALDPELVGEVLKVMRSLAeEGRTMLVVTHELGFARHVsNRVVFMHQGTIDCDGAPEALFGAHGSPR 249
Cdd:TIGR03375 617 LRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLLDLV-DRIIVMDNGRIVADGPKDQVLEALRKGR 694
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
19-218 |
2.83e-29 |
|
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: 115.46 E-value: 2.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 19 GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlAANPKQierLRSRLG 98
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA----------DADADS---WRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 99 MVFQSFNLWSHmTVLQNVIEGPHYVLKRSKQECIEQA---EQLLDRVGMLNRK-DFYPAQLSGGQQQRVAIARALAMDPE 174
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLARPDASDAEIREALERAgldEFVAALPQGLDTPiGEGGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490999375 175 VMLFDEPTSALDPELVGEVLKVMRSLAeEGRTMLVVTHELGFAR 218
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAA 521
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
23-246 |
3.07e-29 |
|
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: 110.01 E-value: 3.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaanpKQIER--LRSRLGMV 100
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI---------------RDISRksLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 101 FQSFNLWSHmTVLQNVIEGPHYVlkrSKQECIEQAEQL-LDRVGMlNRKDFYPAQ-------LSGGQQQRVAIARALAMD 172
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGRPNA---TDEEVIEAAKEAgAHDFIM-KLPNGYDTVlgenggnLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999375 173 PEVMLFDEPTSALDPELVGEVLKVMRSLaEEGRTMLVVTHELGFARHvSNRVVFMHQGTIDCDGAPEALFGAHG 246
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
23-255 |
3.81e-29 |
|
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: 115.82 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghRLaanpkQIERLRSRLGMVFQ 102
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLA--------GL-----DVQAVRRQLGVVLQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 SFNLWSHmTVLQNVIEGPHYVLKRSkQECIEQA--EQLLDRV--GMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLF 178
Cdd:TIGR03797 535 NGRLMSG-SIFENIAGGAPLTLDEA-WEAARMAglAEDIRAMpmGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLF 612
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 179 DEPTSALDPELVGevlKVMRSLAEEGRTMLVVTHELGFARHvSNRVVFMHQGTIDCDGAPEALFGAHGspRFQQFIS 255
Cdd:TIGR03797 613 DEATSALDNRTQA---IVSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMAREG--LFAQLAR 683
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-242 |
5.02e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 110.52 E-value: 5.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCIN-LLETPDAGVvSVGGETIemkhharghRLAANPKQIE--RLRSRLGM 99
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrLIEIYDSKI-KVDGKVL---------YFGKDIFQIDaiKLRKEVGM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 100 VFQSFNLWSHMTVLQNVIegphYVLK----RSKQECIEQAEQLLDRVGML----NRKDFYPAQLSGGQQQRVAIARALAM 171
Cdd:PRK14246 95 VFQQPNPFPHLSIYDNIA----YPLKshgiKEKREIKKIVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490999375 172 DPEVMLFDEPTSALDPELVGEVLKVMRSLAEEgRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
24-242 |
5.25e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 111.25 E-value: 5.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLetpdagVVSVGGETIemkhhARGHRLAANPKQIE---RLRSRLGMV 100
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGL------IISETGQTI-----VGDYAIPANLKKIKevkRLRKEIGLV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 101 FQ--SFNLWSHmTVLQNVIEGPHYvLKRSKQECIEQAEQLLDRVGMlnRKDFY---PAQLSGGQQQRVAIARALAMDPEV 175
Cdd:PRK13645 96 FQfpEYQLFQE-TIEKDIAFGPVN-LGENKQEAYKKVPELLKLVQL--PEDYVkrsPFELSGGQKRRVALAGIIAMDGNT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 176 MLFDEPTSALDPELVGEVLKVMRSL-AEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK13645 172 LVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-232 |
7.42e-29 |
|
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: 108.02 E-value: 7.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 6 PVTLSVSDIHK------SFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCIN--LLETPDAGVVSVGGEtiemkhh 77
Cdd:cd03213 1 GVTLSFRNLTVtvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 78 arghrlaanPKQIERLRSRLGMVFQSFNLWSHMTVlqnviegphyvlkrskQECIEQAEQLldrvgmlnrkdfypAQLSG 157
Cdd:cd03213 74 ---------PLDKRSFRKIIGYVPQDDILHPTLTV----------------RETLMFAAKL--------------RGLSG 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490999375 158 GQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHEL-GFARHVSNRVVFMHQGTI 232
Cdd:cd03213 115 GERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-228 |
7.97e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 110.13 E-value: 7.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVvsvggeTIEMKHHARGHRLAANPK 88
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEV------RVEGRVEFFNQNIYERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRSRLGMVFQSFNLWShMTVLQNVIEGPHYVLKRSKQEC---IEQA---EQLLDRVGmlNRKDFYPAQLSGGQQQR 162
Cdd:PRK14258 82 NLNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIddiVESAlkdADLWDEIK--HKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 163 VAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGR-TMLVVTHELGFARHVSNRVVFMH 228
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFFK 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-243 |
8.11e-29 |
|
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: 114.13 E-value: 8.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLD--VLK---GISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAG--VVSVGGETIEMkhhargh 81
Cdd:TIGR03269 280 IKVRNVSKRYISVDrgVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVGDEWVDM------- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 82 rlaANPKQIERLRSR--LGMVFQSFNLWSHMTVLQNV-----IEGPH--------YVLKRSKQEcIEQAEQLLDRvgmln 146
Cdd:TIGR03269 353 ---TKPGPDGRGRAKryIGILHQEYDLYPHRTVLDNLteaigLELPDelarmkavITLKMVGFD-EEKAEEILDK----- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 147 rkdfYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLK-VMRSLAEEGRTMLVVTHELGFARHVSNRVV 225
Cdd:TIGR03269 424 ----YPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAA 499
|
250
....*....|....*...
gi 490999375 226 FMHQGTIDCDGAPEALFG 243
Cdd:TIGR03269 500 LMRDGKIVKIGDPEEIVE 517
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
11-254 |
1.39e-28 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 109.47 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 11 VSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlAANPKQI 90
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIP----------AMSRSRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 91 ERLRSRLGMVFQSFNLWSHMTVLQNVIegphYVLKRSKQ--ECIEQAEQL--LDRVGMLNRKDFYPAQLSGGQQQRVAIA 166
Cdd:PRK11831 80 YTVRKRMSMLFQSGALFTDMNVFDNVA----YPLREHTQlpAPLLHSTVMmkLEAVGLRGAAKLMPSELSGGMARRAALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 167 RALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALfGAH 245
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL-QAN 234
|
....*....
gi 490999375 246 GSPRFQQFI 254
Cdd:PRK11831 235 PDPRVRQFL 243
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
17-245 |
1.67e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 108.95 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 17 SFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEM---KHHARghRLAANPKQ---- 89
Cdd:PRK11231 11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlssRQLAR--RLALLPQHhltp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 90 --------IERLRSrlgmvfQSFNLWSHMTvlqnviegphyvlkRSKQECIEQAEQLLDRVGMLNRKdfyPAQLSGGQQQ 161
Cdd:PRK11231 89 egitvrelVAYGRS------PWLSLWGRLS--------------AEDNARVNQAMEQTRINHLADRR---LTDLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 162 RVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEAL 241
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
....
gi 490999375 242 FGAH 245
Cdd:PRK11231 226 MTPG 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
23-239 |
2.06e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 108.25 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetiemkhharghRLAAnpkQIErlrsrLGMVFQ 102
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------------RVSA---LLE-----LGAGFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 SfnlwsHMTVLQNViegphY----VLKRSKQEcieqAEQLLDRVgmlnrKDFypAQL-----------SGGQQQRVAIAR 167
Cdd:COG1134 101 P-----ELTGRENI-----YlngrLLGLSRKE----IDEKFDEI-----VEF--AELgdfidqpvktySSGMRARLAFAV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490999375 168 ALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPE 239
Cdd:COG1134 160 ATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-232 |
3.21e-28 |
|
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: 107.36 E-value: 3.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 20 SLDVLKGISIQAQKGDVISILGASGSGKSTLLRCInlletpdAGVVSVGGETiemkhhaRGHRLAAN-PKQIERLRSRLG 98
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAI-------SGRVEGGGTT-------SGQILFNGqPRKPDQFQKCVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 99 MVFQSFNLWSHMTVLQNVIEGPHYVLKRSKQECIEQAE---QLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEV 175
Cdd:cd03234 85 YVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRvedVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 176 MLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELG---FarHVSNRVVFMHQGTI 232
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEI 222
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-246 |
3.71e-28 |
|
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: 107.57 E-value: 3.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 22 DVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetiemkhhargHRLAANPKqiERLRSRLGMVF 101
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG-----------HDLALADP--AWLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 102 QSfNLWSHMTVLQNVI---EGP--HYVLKRSK--------QECIEQAEQLLDRVGmlnrkdfypAQLSGGQQQRVAIARA 168
Cdd:cd03252 83 QE-NVLFNRSIRDNIAladPGMsmERVIEAAKlagahdfiSELPEGYDTIVGEQG---------AGLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 169 LAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAeEGRTMLVVTHELGFARHvSNRVVFMHQGTIDCDGAPEALFGAHG 246
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-239 |
4.74e-28 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 111.82 E-value: 4.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLET--PDAGVV--------------------- 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 66 --SVGGETIEMKhhaRGHRLAANPKQIERLRSRLGMVFQ-SFNLWSHMTVLQNVIEGPHYvLKRSKQECIEQAEQLLDRV 142
Cdd:TIGR03269 81 pcPVCGGTLEPE---EVDFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEE-IGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 143 GMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLA-EEGRTMLVVTHELGFARHVS 221
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLS 236
|
250
....*....|....*...
gi 490999375 222 NRVVFMHQGTIDCDGAPE 239
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPD 254
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-236 |
7.18e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 111.41 E-value: 7.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHARGHRLAanpk 88
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qierlrsrLGMVFQSFNLWSHMTVLQNVIEGPHYVLKR------SKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQR 162
Cdd:PRK09700 82 --------IGIIYQELSVIDELTVLENLYIGRHLTKKVcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999375 163 VAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDG 236
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-232 |
9.85e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.88 E-value: 9.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 2 HDPRPVTLSVSDIHKSfgslDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKhhargh 81
Cdd:COG1129 250 AAPGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR------ 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 82 rlaaNPKQieRLRSRLGMV-----FQSFNLwsHMTVLQNVI------EGPHYVLKRSKQEciEQAEQLLDRVGM-LNRKD 149
Cdd:COG1129 320 ----SPRD--AIRAGIAYVpedrkGEGLVL--DLSIRENITlasldrLSRGGLLDRRRER--ALAEEYIKRLRIkTPSPE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 150 FYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDpelVG---EVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVF 226
Cdd:COG1129 390 QPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILV 466
|
....*.
gi 490999375 227 MHQGTI 232
Cdd:COG1129 467 MREGRI 472
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-255 |
2.05e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 110.18 E-value: 2.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKST----LLRCINlletpDAGVVSVGGETIemkhhargHRLaaNPKQIERLRSRLG 98
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPL--------HNL--NRRQLLPVRHRIQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 99 MVFQSFN--LWSHMTVLQNVIEG---PHYVLKRSKQEciEQAEQLLDRVGM-LNRKDFYPAQLSGGQQQRVAIARALAMD 172
Cdd:PRK15134 366 VVFQDPNssLNPRLNVLQIIEEGlrvHQPTLSAAQRE--QQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILK 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 173 PEVMLFDEPTSALDPELVGEVLKVMRSLAEEGR-TMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGAHGSPRFQ 251
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTR 523
|
....
gi 490999375 252 QFIS 255
Cdd:PRK15134 524 QLLA 527
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
23-232 |
3.53e-27 |
|
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: 103.06 E-value: 3.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlAANPKQierLRSRLGMVFQ 102
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS----------QWDPNE---LGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 SFNLWSHmTVLQNViegphyvlkrskqecieqaeqlldrvgmlnrkdfypaqLSGGQQQRVAIARALAMDPEVMLFDEPT 182
Cdd:cd03246 84 DDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490999375 183 SALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVsNRVVFMHQGTI 232
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
9-214 |
4.10e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 105.17 E-value: 4.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHARGhrlaanpk 88
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERG-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qierlrsrlgMVFQSFNLWSHMTVLQNVIEGPHyVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARA 168
Cdd:PRK11248 74 ----------VVFQNEGLLPWRNVQDNVAFGLQ-LAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490999375 169 LAMDPEVMLFDEPTSALDP---ELVGEVLkvMRSLAEEGRTMLVVTHEL 214
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAftrEQMQTLL--LKLWQETGKQVLLITHDI 189
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-236 |
9.03e-27 |
|
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: 103.44 E-value: 9.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 22 DVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHARghrlaanpkqierLRSRLGMVF 101
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-------------LRRNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 102 QSFNLWSHmTVLQNVIEGPHYVlkrSKQECIEQAEqlLDRVGMLNRKDfyP-----------AQLSGGQQQRVAIARALA 170
Cdd:cd03245 85 QDVTLFYG-TLRDNITLGAPLA---DDERILRAAE--LAGVTDFVNKH--PngldlqigergRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490999375 171 MDPEVMLFDEPTSALDPELVGEVLKVMRSLAeEGRTMLVVTHELGFARHVsNRVVFMHQGTIDCDG 236
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLLDLV-DRIIVMDSGRIVADG 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-214 |
2.12e-26 |
|
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: 107.45 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 7 VTLSVSDIHKSF-GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHarghrlaa 85
Cdd:TIGR02868 333 PTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ-------- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 86 npkqiERLRSRLGMVFQSFNLWsHMTVLQNVIEGphyvlkrsKQECI-EQAEQLLDRVGMLNRKDFYP-----------A 153
Cdd:TIGR02868 405 -----DEVRRRVSVCAQDAHLF-DTTVRENLRLA--------RPDATdEELWAALERVGLADWLRALPdgldtvlgeggA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490999375 154 QLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSlAEEGRTMLVVTHEL 214
Cdd:TIGR02868 471 RLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-244 |
3.60e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 106.67 E-value: 3.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 5 RPVTLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGEtiemkhhargHRLA 84
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN----------PCAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 85 ANPKQIERLrsRLGMVFQSFNLWSHMTVLQNVIEGphyvLKRSkQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVA 164
Cdd:PRK15439 78 LTPAKAHQL--GIYLVPQEPLLFPNLSVKENILFG----LPKR-QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIdcdgapeALFGA 244
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI-------ALSGK 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-248 |
4.43e-26 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 106.67 E-value: 4.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPD---AGVVSVGGETIEMKhharghrlaanpkqieRLRSRLGMV 100
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAK----------------EMRAISAYV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 101 FQSFNLWSHMTVLQNVIEGPHYVLKR--SKQECIEQAEQLLDRVGMLNRKDF---YPAQ---LSGGQQQRVAIARALAMD 172
Cdd:TIGR00955 105 QQDDLFIPTLTVREHLMFQAHLRMPRrvTKKEKRERVDEVLQALGLRKCANTrigVPGRvkgLSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 173 PEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTH-------ELgFarhvsNRVVFMHQGTIDCDGAPEAL---F 242
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHqpsselfEL-F-----DKIILMAEGRVAYLGSPDQAvpfF 258
|
....*.
gi 490999375 243 GAHGSP 248
Cdd:TIGR00955 259 SDLGHP 264
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
9-236 |
1.94e-25 |
|
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: 98.92 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLD--VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhhargHRLAAN 86
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV--------SDLEKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 87 pkqierLRSRLGMVFQSFNLWShMTVLQNViegphyvlkrskqecieqaeqlldrvgmlnrkdfyPAQLSGGQQQRVAIA 166
Cdd:cd03247 73 ------LSSLISVLNQRPYLFD-TTLRNNL-----------------------------------GRRFSGGERQRLALA 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 167 RALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEgRTMLVVTHELGFARHVsNRVVFMHQGTIDCDG 236
Cdd:cd03247 111 RILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-256 |
3.23e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 104.02 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKS-TLLRCINLLETPDA----GVVSVGGETIemkhharghrLAANPKQIERLR-SR 96
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESL----------LHASEQTLRGVRgNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 97 LGMVFQ----SFNlwshmtVLQNvIEGPHY---VLKRSKQECIEQAEQL--LDRVGMLN---RKDFYPAQLSGGQQQRVA 164
Cdd:PRK15134 94 IAMIFQepmvSLN------PLHT-LEKQLYevlSLHRGMRREAARGEILncLDRVGIRQaakRLTDYPHQLSGGERQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFG 243
Cdd:PRK15134 167 IAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFS 246
|
250
....*....|...
gi 490999375 244 AHGSPRFQQFISS 256
Cdd:PRK15134 247 APTHPYTQKLLNS 259
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-254 |
4.31e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 103.75 E-value: 4.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 4 PRPVTLSVSDIHKSF--GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetiemkhhargH 81
Cdd:PRK11160 334 ADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG-----------Q 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 82 RLAANPKQieRLRSRLGMVFQSFNLWSHmTVLQNVI--------EGPHYVLKRSKQECIEQAEQLLDR-VGMLNRkdfyp 152
Cdd:PRK11160 403 PIADYSEA--ALRQAISVVSQRVHLFSA-TLRDNLLlaapnasdEALIEVLQQVGLEKLLEDDKGLNAwLGEGGR----- 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 153 aQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAeEGRTMLVVTHEL-GFARHvsNRVVFMHQGT 231
Cdd:PRK11160 475 -QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLtGLEQF--DRICVMDNGQ 550
|
250 260
....*....|....*....|...
gi 490999375 232 IDCDGAPEALFGAHGspRFQQFI 254
Cdd:PRK11160 551 IIEQGTHQELLAQQG--RYYQLK 571
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-233 |
1.12e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.45 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 4 PRPVtLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVgGETIEM----KHHAr 79
Cdd:COG0488 312 GKKV-LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIgyfdQHQE- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 80 ghrlaanpkqierlrsrlgmvfqsfNLWSHMTVLQNVIEGphyvlkrSKQECIEQAEQLLDRvgMLnrkdFYPAQ----- 154
Cdd:COG0488 389 -------------------------ELDPDKTVLDELRDG-------APGGTEQEVRGYLGR--FL----FSGDDafkpv 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 155 --LSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVgEVLKvmRSLAE-EGrTMLVVTHELGFARHVSNRVVFMHQGT 231
Cdd:COG0488 431 gvLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETL-EALE--EALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGG 506
|
..
gi 490999375 232 ID 233
Cdd:COG0488 507 VR 508
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
9-261 |
1.31e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 102.63 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSF----GSLDVLKGISIQAQKGDVISILGASGSGKS-TLLRCINLLETPdAGVVSVGGETIEMKHHARGHRL 83
Cdd:PRK10261 13 LAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQA-GGLVQCDKMLLRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 84 AANPKQIERLR-SRLGMVFQS--FNLWSHMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRV------GMLNRkdfYPAQ 154
Cdd:PRK10261 92 EQSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVripeaqTILSR---YPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 155 LSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTID 233
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260
....*....|....*....|....*...
gi 490999375 234 CDGAPEALFGAHGSPRFQQFISSHHQPG 261
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLAAVPQLG 276
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-214 |
3.35e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 100.76 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHArghrlaanpk 88
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTT---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qiERLRSRLGMVFQSFNLWSHMTVLQNVIEG--PHY--VLKRSkqECIEQAEQLLDRVGMlnrkDFYPAQ----LSGGQQ 160
Cdd:PRK11288 75 --AALAAGVAIIYQELHLVPEMTVAENLYLGqlPHKggIVNRR--LLNYEAREQLEHLGV----DIDPDTplkyLSIGQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490999375 161 QRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHEL 214
Cdd:PRK11288 147 QMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRM 200
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-244 |
3.74e-24 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 97.75 E-value: 3.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 18 FGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkHHARghrlaanpKQIERlrsRL 97
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ--HYAS--------KEVAR---RI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 98 GMVFQSFNLWSHMTVLQNVIEG--PHYVL-KRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPE 174
Cdd:PRK10253 84 GLLAQNATTPGDITVQELVARGryPHQPLfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490999375 175 VMLFDEPTSALDPELVGEVLKVMRSL-AEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGA 244
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
23-246 |
4.99e-24 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 100.97 E-value: 4.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetiemkhhargHRLA-ANPKQierLRSRLGMVF 101
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDG-----------VDLAiADPAW---LRRQMGVVL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 102 QSFNLWSHmTVLQNV-----------------IEGPHYVLKRSKQecieQAEQLLDRVGmlnrkdfypAQLSGGQQQRVA 164
Cdd:TIGR01846 538 QENVLFSR-SIRDNIalcnpgapfehvihaakLAGAHDFISELPQ----GYNTEVGEKG---------ANLSGGQRQRIA 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAeEGRTMLVVTHELGFARHvSNRVVFMHQGTIDCDGAPEALFGA 244
Cdd:TIGR01846 604 IARALVGNPRILIFDEATSALDYESEALIMRNMREIC-RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELLAL 681
|
..
gi 490999375 245 HG 246
Cdd:TIGR01846 682 QG 683
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-232 |
7.13e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.57 E-value: 7.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 1 MHDPRPVTLSVSDIHKSFG-----SLDVLKGISIQAQKGDVISILGASGSGKSTllrCINLLET---PDAGVVSVGGETI 72
Cdd:TIGR00958 469 TLAPLNLEGLIEFQDVSFSypnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNlyqPTGGQVLLDGVPL 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 73 -EMKHHArghrlaanpkqierLRSRLGMVFQSFNLWSHmTVLQNVIegphYVLKRSKQECIEQAEQlldrvgMLNRKDFY 151
Cdd:TIGR00958 546 vQYDHHY--------------LHRQVALVGQEPVLFSG-SVRENIA----YGLTDTPDEEIMAAAK------AANAHDFI 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 152 P--------------AQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPElVGEVLKVMRSLAeeGRTMLVVTHELGFA 217
Cdd:TIGR00958 601 MefpngydtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE-CEQLLQESRSRA--SRTVLLIAHRLSTV 677
|
250
....*....|....*
gi 490999375 218 RHvSNRVVFMHQGTI 232
Cdd:TIGR00958 678 ER-ADQILVLKKGSV 691
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
7-242 |
8.49e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.10 E-value: 8.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 7 VTLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHARghrlaan 86
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAK------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 87 pkqieRLRSRLGMVFQSFNLWSHMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRvgMLNRKDFYPAQLSGGQQQRVAIA 166
Cdd:PRK11614 77 -----IMREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490999375 167 RALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-247 |
1.19e-23 |
|
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: 100.09 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 27 ISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMkhharghrlaanpkQIERLRSRLGMVFQSFNL 106
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET--------------NLDAVRQSLGMCPQHNIL 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 107 WSHMTVLQNVIEgpHYVLK-RSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSAL 185
Cdd:TIGR01257 1015 FHHLTVAEHILF--YAQLKgRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999375 186 DP---ELVGEVLKVMRSlaeeGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGAHGS 247
Cdd:TIGR01257 1093 DPysrRSIWDLLLKYRS----GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGT 1153
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
20-246 |
1.86e-23 |
|
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: 99.02 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 20 SLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetiemkHHARGHRLAAnpkqierLRSRLGM 99
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG------HDLADYTLAS-------LRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 100 VFQSFNLWSHmTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYP-----AQLSGGQQQRVAIARALAMDPE 174
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPigengVLLSGGQRQRLAIARALLKDAP 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490999375 175 VMLFDEPTSALDPE---LVGEVL-KVMRslaeeGRTMLVVTHELGFARHvSNRVVFMHQGTIDCDGAPEALFGAHG 246
Cdd:TIGR02203 490 ILILDEATSALDNEserLVQAALeRLMQ-----GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLARNG 559
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
15-232 |
2.08e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 98.88 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 15 HKSF---GSLDVLKGISIQAQKGDVISILGASGSGKSTLlrcINLLE---TPDAGVVSVGGETIemkhhaRGHRLAAnpk 88
Cdd:PRK13657 339 DVSFsydNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQrvfDPQSGRILIDGTDI------RTVTRAS--- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qierLRSRLGMVFQSFNLWSHmTVLQNVIEGP--------HYVLKRSK-QECIEQAEQLLD-RVGMLNRkdfypaQLSGG 158
Cdd:PRK13657 407 ----LRRNIAVVFQDAGLFNR-SIEDNIRVGRpdatdeemRAAAERAQaHDFIERKPDGYDtVVGERGR------QLSGG 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490999375 159 QQQRVAIARALAMDPEVMLFDEPTSALDPELvgEVlKVMRSLAE--EGRTMLVVTHELGFARHvSNRVVFMHQGTI 232
Cdd:PRK13657 476 ERQRLAIARALLKDPPILILDEATSALDVET--EA-KVKAALDElmKGRTTFIIAHRLSTVRN-ADRILVFDNGRV 547
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-244 |
2.24e-23 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 95.72 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkHHARGHRLAANPKQIERLRsrlgmvfqs 103
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT---RQALQKNLVAYVPQSEEVD--------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 fnlWSHMTVLQNVIEGPHY----VLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFD 179
Cdd:PRK15056 91 ---WSFPVLVEDVVMMGRYghmgWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999375 180 EPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVfMHQGTIDCDGAPEALFGA 244
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTFTA 231
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
5-230 |
2.57e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 96.72 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 5 RPVTLSVSDIHKSFGSLD----VLKGISIQAQKGDVISILGASGSGKS-TLLRCINLLetpdAGVVSVGGETIemkhhAR 79
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPDgdvtAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLL----AANGRIGGSAT-----FN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 80 GHRLAANP-KQIERLRS-RLGMVFQ----SFNlwSHMTVLQNVIEgphyVL----KRSKQECIEQAEQLLDRVGM---LN 146
Cdd:PRK09473 80 GREILNLPeKELNKLRAeQISMIFQdpmtSLN--PYMRVGEQLME----VLmlhkGMSKAEAFEESVRMLDAVKMpeaRK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 147 RKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRT-MLVVTHELGFARHVSNRVV 225
Cdd:PRK09473 154 RMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVL 233
|
....*
gi 490999375 226 FMHQG 230
Cdd:PRK09473 234 VMYAG 238
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
9-232 |
2.88e-23 |
|
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: 94.39 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetiemkHHARGHRLaanpk 88
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDG------HPWTRKDL----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qierlrSRLGMVFQSFNLWSHMTVLQNVIegPHYVLKRSKQECIEQaeqLLDRVGMLNRKDFYPAQLSGGQQQRVAIARA 168
Cdd:TIGR03740 70 ------HKIGSLIESPPLYENLTARENLK--VHTTLLGLPDSRIDE---VLNIVDLTNTGKKKAKQFSLGMKQRLGIAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999375 169 LAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:TIGR03740 139 LLNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
9-231 |
4.08e-23 |
|
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: 91.74 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETiemkhharghrlaanpk 88
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qierlrsrlgmvfqsfnlwshmtvlqnviegphyvlkrskqecieqaeqlldRVGmlnrkdfYPAQLSGGQQQRVAIARA 168
Cdd:cd03221 64 ----------------------------------------------------KIG-------YFEQLSGGEKMRLALAKL 84
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490999375 169 LAMDPEVMLFDEPTSALDPELVgEVLKVMrsLAEEGRTMLVVTHELGFARHVSNRVVFMHQGT 231
Cdd:cd03221 85 LLENPNLLLLDEPTNHLDLESI-EALEEA--LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
23-249 |
7.19e-23 |
|
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: 97.13 E-value: 7.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetIEMKHHARghrlaanpkqiERLRSRLGMVFQ 102
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG--ADLSQWDR-----------EELGRHIGYLPQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 SFNLWSHmTVLQN-----------VIE-----GPHyvlkrskqECIEQAEQLLD-RVGMLnrkdfyPAQLSGGQQQRVAI 165
Cdd:COG4618 414 DVELFDG-TIAENiarfgdadpekVVAaaklaGVH--------EMILRLPDGYDtRIGEG------GARLSGGQRQRIGL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 166 ARALAMDPEVMLFDEPTSALDPElvGE--VLKVMRSLAEEGRTMLVVTHELGFARHVsNRVVFMHQGTIDCDGAPEALFG 243
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDE--GEaaLAAAIRALKARGATVVVITHRPSLLAAV-DKLLVLRDGRVQAFGPRDEVLA 555
|
....*.
gi 490999375 244 AHGSPR 249
Cdd:COG4618 556 RLARPA 561
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
8-242 |
1.15e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 93.03 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 8 TLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIE-MKHHARGHRlaan 86
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISlLPLHARARR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 87 pkqierlrsRLGMVFQSFNLWSHMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIA 166
Cdd:PRK10895 79 ---------GIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490999375 167 RALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
23-232 |
3.28e-22 |
|
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: 91.38 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTllrCINLLET---PDAGVVSVGGETIEMKHHarghrlaanpkqiERLRSRLGM 99
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKST---VVALLENfyqPQGGQVLLDGKPISQYEH-------------KYLHSKVSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 100 VFQSFNLWSHmTVLQNViegpHYVLKRSKQECIEQAEQlldrvgMLNRKDFYP--------------AQLSGGQQQRVAI 165
Cdd:cd03248 93 VGQEPVLFAR-SLQDNI----AYGLQSCSFECVKEAAQ------KAHAHSFISelasgydtevgekgSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 166 ARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSlAEEGRTMLVVTHELGFARHvSNRVVFMHQGTI 232
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
9-242 |
4.51e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 92.38 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkHHARGhrLAAnpk 88
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD--YSKRG--LLA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qierLRSRLGMVFQSFNLWSHMTVLQNVIEgphYVLKRSKQECIEQAEQLLDRVGMLNRKDF--YPAQ-LSGGQQQRVAI 165
Cdd:PRK13638 75 ----LRQQVATVFQDPEQQIFYTDIDSDIA---FSLRNLGVPEAEITRRVDEALTLVDAQHFrhQPIQcLSHGQKKRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 166 ARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
27-251 |
4.92e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 92.88 E-value: 4.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 27 ISIQAQKGDVISILGASGSGKS-TLLRCINLLETPdaGVVSvgGETIEMKHHargHRLAANPKQIERL-RSRLGMVFQ-- 102
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVM--AEKLEFNGQ---DLQRISEKERRNLvGAEVAMIFQdp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 --SFNlwSHMTVLQNVIEGPHYVLKRSKQECIEQAEQLLDRVGM---LNRKDFYPAQLSGGQQQRVAIARALAMDPEVML 177
Cdd:PRK11022 99 mtSLN--PCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999375 178 FDEPTSALDPELVGEVLKVMRSLAE-EGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGAHGSPRFQ 251
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQ 251
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
25-257 |
7.65e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 91.30 E-value: 7.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 25 KGISIQAQKGDVISILGASGSGKStlLRCINLLETPDAGVVSVGGETiemkhHARGHRLAANpkqieRLRSRL-GMVFQ- 102
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRV-----LLDGKPVAPC-----ALRGRKiATIMQn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 ---SFNLWSHMTvlQNVIEGphyVLKRSKQECIEQAEQLLDRVGMLNRK---DFYPAQLSGGQQQRVAIARALAMDPEVM 176
Cdd:PRK10418 88 prsAFNPLHTMH--THARET---CLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 177 LFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGAHGSPRFQQFIS 255
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVS 242
|
..
gi 490999375 256 SH 257
Cdd:PRK10418 243 AH 244
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
23-231 |
8.97e-22 |
|
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: 89.84 E-value: 8.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCInLLETP-DAGVVSVGGetiemkhharghrlaanpkqierlrsRLGMVF 101
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-LGELEkLSGSVSVPG--------------------------SIAYVS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 102 QS---FNlwshMTVLQNVIEGPHY-------VLKrskqecieqAEQLLDRVGMLNRKDFYP-----AQLSGGQQQRVAIA 166
Cdd:cd03250 73 QEpwiQN----GTIRENILFGKPFdeeryekVIK---------ACALEPDLEILPDGDLTEigekgINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 167 RALAMDPEVMLFDEPTSALDPElVGEVL--KVMRSLAEEGRTMLVVTHELGFARHVsNRVVFMHQGT 231
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAH-VGRHIfeNCILGLLLNNKTRILVTHQLQLLPHA-DQIVVLDNGR 204
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-236 |
9.11e-22 |
|
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: 90.47 E-value: 9.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 15 HKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETiemkhharghrlaanP-KQIERL 93
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV---------------PwKRRKKF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 94 RSRLGMVF-QSFNLWSHMTvlqnVIEGpHYVLKRSKQECIEQAEQLLDR-VGMLNRKDFY--PA-QLSGGQQQRVAIARA 168
Cdd:cd03267 93 LRRIGVVFgQKTQLWWDLP----VIDS-FYLLAAIYDLPPARFKKRLDElSELLDLEELLdtPVrQLSLGQRMRAEIAAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 169 LAMDPEVMLFDEPTSALDPELVGEVLKVMRSL-AEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDG 236
Cdd:cd03267 168 LLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-246 |
1.04e-21 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 94.10 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 3 DPRPVTLSVSDIHKSFG--SLDVLKGisiQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGgETIEMKhharg 80
Cdd:PRK13409 335 SERETLVEYPDLTKKLGdfSLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYK----- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 81 hrlaanPKQIERLrsrlgmvfqsfnlwSHMTV---LQNV---IEGPHYvlkrsKQECIE--QAEQLLDRvgmlNRKDfyp 152
Cdd:PRK13409 406 ------PQYIKPD--------------YDGTVedlLRSItddLGSSYY-----KSEIIKplQLERLLDK----NVKD--- 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 153 aqLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRV-VFmhqg 230
Cdd:PRK13409 454 --LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLmVF---- 527
|
250
....*....|....*.
gi 490999375 231 tidcDGAPealfGAHG 246
Cdd:PRK13409 528 ----EGEP----GKHG 535
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-232 |
1.52e-21 |
|
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: 93.35 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETI-EMKHHArghrlaanpkqierLRSRLGMVF 101
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIrDVTQAS--------------LRAAIGIVP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 102 QS---FNlwshMTVLQNVIEGphyvlkR---SKQECIEQAE--QLLDRVGMLnrKDFYPAQ-------LSGGQQQRVAIA 166
Cdd:COG5265 439 QDtvlFN----DTIAYNIAYG------RpdaSEEEVEAAARaaQIHDFIESL--PDGYDTRvgerglkLSGGEKQRVAIA 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490999375 167 RALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAeEGRTMLVVTHELGFARHvSNRVVFMHQGTI 232
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAHRLSTIVD-ADEILVLEAGRI 570
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
9-239 |
1.91e-21 |
|
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: 88.74 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCI--NLLETPDAGVVSVGGETIemkhharghrLAAN 86
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDI----------TDLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 87 PKqiERLRSRLGMVFQS---FNLWSHMTVLQNVIEGphyvlkrskqecieqaeqlldrvgmlnrkdfypaqLSGGQQQRV 163
Cdd:cd03217 71 PE--ERARLGIFLAFQYppeIPGVKNADFLRYVNEG-----------------------------------FSGGEKKRN 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 164 AIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHV-SNRVVFMHQGTIDCDGAPE 239
Cdd:cd03217 114 EILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKE 190
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-236 |
4.05e-21 |
|
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: 88.36 E-value: 4.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetiemkhharghRLAAnpkQIErlrsrLGMVFQ 102
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------------RVSS---LLG-----LGGGFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 sfnlwSHMTVLQNVIEGpHYVLKRSKQEcieqAEQLLDRVGMLNR-KDFYPAQL---SGGQQQRVAIARALAMDPEVMLF 178
Cdd:cd03220 97 -----PELTGRENIYLN-GRLLGLSRKE----IDEKIDEIIEFSElGDFIDLPVktySSGMKARLAFAIATALEPDILLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 179 DEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDG 236
Cdd:cd03220 167 DEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-232 |
5.27e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 89.08 E-value: 5.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 21 LDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHarghrlaanpkqieRLRS-RLGM 99
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDY--------------SYRSqRIRM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 100 VFQ----SFNLWSHMTVLQNVIEGPHYVLKRSKQEciEQAEQLLDRVGML-NRKDFYPAQLSGGQQQRVAIARALAMDPE 174
Cdd:PRK15112 92 IFQdpstSLNPRQRISQILDFPLRLNTDLEPEQRE--KQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 175 VMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:PRK15112 170 VIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
20-238 |
6.28e-21 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 88.62 E-value: 6.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 20 SLDVLKGisiQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKhharghrlaanPKQIE-----RLR 94
Cdd:cd03237 14 TLEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYK-----------PQYIKadyegTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 95 SRLgmvfqsfnlwshMTVLQNVIEGPHYvlkrsKQECIE--QAEQLLDRvgMLNrkdfypaQLSGGQQQRVAIARALAMD 172
Cdd:cd03237 80 DLL------------SSITKDFYTHPYF-----KTEIAKplQIEQILDR--EVP-------ELSGGELQRVAIAACLSKD 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 173 PEVMLFDEPTSALDPELVGEVLKVMRSLAEEG-RTMLVVTHELGFARHVSNRV-VFMHQGTIDCDGAP 238
Cdd:cd03237 134 ADIYLLDEPSAYLDVEQRLMASKVIRRFAENNeKTAFVVEHDIIMIDYLADRLiVFEGEPSVNGVANP 201
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-242 |
7.00e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.46 E-value: 7.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 27 ISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlAANPKQIERLRSRLGMVFQS--F 104
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRID----------TLSPGKLQALRRDIQFIFQDpyA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 105 NLWSHMTVLQNVIEgP---HYVLKrsKQECIEQAEQLLDRVGMLNRKDF-YPAQLSGGQQQRVAIARALAMDPEVMLFDE 180
Cdd:PRK10261 413 SLDPRQTVGDSIME-PlrvHGLLP--GKAAAARVAWLLERVGLLPEHAWrYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490999375 181 PTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALF 242
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVF 552
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-232 |
9.47e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.00 E-value: 9.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 25 KGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHharghRLAANPKQIERL---RSRLGMvF 101
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRS-----PLDAVKKGMAYItesRRDNGF-F 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 102 QSFNLWSHMTVLQNVIEGPH-----YVLKRSKQECIEQAEQLLD-RVGMLNRKdfyPAQLSGGQQQRVAIARALAMDPEV 175
Cdd:PRK09700 354 PNFSIAQNMAISRSLKDGGYkgamgLFHEVDEQRTAENQRELLAlKCHSVNQN---ITELSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 176 MLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-232 |
9.64e-21 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 91.26 E-value: 9.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 19 GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetiemkhharghrlaANPKQIER--LRSR 96
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG---------------ADLKQWDRetFGKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 97 LGMVFQSFNLWSHmTVLQNVIE-----GPHYVLKRSKqecIEQAEQLLDRVGMLNRKDFYP--AQLSGGQQQRVAIARAL 169
Cdd:TIGR01842 394 IGYLPQDVELFPG-TVAENIARfgenaDPEKIIEAAK---LAGVHELILRLPDGYDTVIGPggATLSGGQRQRIALARAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999375 170 AMDPEVMLFDEPTSALDPElvGE--VLKVMRSLAEEGRTMLVVTHELGfARHVSNRVVFMHQGTI 232
Cdd:TIGR01842 470 YGDPKLVVLDEPNSNLDEE--GEqaLANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
10-213 |
1.25e-20 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 91.09 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 10 SVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCInlletpdAGVVSVGGETiemkhharGHRLAANPKQ 89
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQGNNFT--------GTILANNRKP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 90 IERLRSRLGMVFQSFNLWSHMTVLQNVIEGPHYVLKRS--KQECIEQAEQLLDRVGMLNRKDF-----YPAQLSGGQQQR 162
Cdd:PLN03211 135 TKQILKRTGFVTQDDILYPHLTVRETLVFCSLLRLPKSltKQEKILVAESVISELGLTKCENTiignsFIRGISGGERKR 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490999375 163 VAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHE 213
Cdd:PLN03211 215 VSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
9-214 |
5.03e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 88.91 E-value: 5.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKhharghrlaaNPK 88
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFN----------GPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERlrSRLGMVFQSFNLWSHMTVLQNVIEGPHYVLKRSK---QECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAI 165
Cdd:PRK10762 75 SSQE--AGIGIIHQELNLIPQLTIAENIFLGREFVNRFGRidwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490999375 166 ARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHEL 214
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRL 201
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-232 |
7.88e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.16 E-value: 7.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 4 PRPVTLSVSDIH-KSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghr 82
Cdd:COG3845 253 PGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDIT--------- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 83 lAANPKQIERL--------RSRLGMVfQSFNLWSHMtVLQNVIEGP---HYVLKRSKQEciEQAEQLLDRVGMLNRKDFY 151
Cdd:COG3845 324 -GLSPRERRRLgvayipedRLGRGLV-PDMSVAENL-ILGRYRRPPfsrGGFLDRKAIR--AFAEELIEEFDVRTPGPDT 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 152 PA-QLSGGQQQRVAIARALAMDPEVMLFDEPTSALDpelVG---EVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFM 227
Cdd:COG3845 399 PArSLSGGNQQKVILARELSRDPKLLIAAQPTRGLD---VGaieFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVM 475
|
....*
gi 490999375 228 HQGTI 232
Cdd:COG3845 476 YEGRI 480
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
5-246 |
1.60e-19 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 87.53 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 5 RPVTLSVSDIHKSFG--SLDVLKGisiQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSvGGETIEMKhharghr 82
Cdd:COG1245 338 EETLVEYPDLTKSYGgfSLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKISYK------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 83 laanPKQIERLrsrlgmvfqsfnlwSHMTV---LQNVIEGP---HYVlkrsKQECIE--QAEQLLDRvgmlNRKDfypaq 154
Cdd:COG1245 407 ----PQYISPD--------------YDGTVeefLRSANTDDfgsSYY----KTEIIKplGLEKLLDK----NVKD----- 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 155 LSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRV-VFmhqgti 232
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLmVF------ 529
|
250
....*....|....
gi 490999375 233 dcDGAPealfGAHG 246
Cdd:COG1245 530 --EGEP----GVHG 537
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
9-212 |
2.95e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 82.79 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkHHARGHRlaanPK 88
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL---AEQRDEP----HE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRSRLGMVfqsfnlwSHMTVLQNViegpHYV--LKRSKQECIEQAeqlLDRVGMLNRKDFYPAQLSGGQQQRVAIA 166
Cdd:TIGR01189 74 NILYLGHLPGLK-------PELSALENL----HFWaaIHGGAQRTIEDA---LAAVGLTGFEDLPAAQLSAGQQRRLALA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490999375 167 RALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTH 212
Cdd:TIGR01189 140 RLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
9-246 |
3.82e-19 |
|
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: 86.72 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLD-VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaanp 87
Cdd:TIGR01193 474 IVINDVSYSYGYGSnILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL--------------- 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 KQIER--LRSRLGMVFQSFNLWSHmTVLQNVIEGPHyvlKRSKQECIEQAEQLLD--------RVGMLNRKDFYPAQLSG 157
Cdd:TIGR01193 539 KDIDRhtLRQFINYLPQEPYIFSG-SILENLLLGAK---ENVSQDEIWAACEIAEikddienmPLGYQTELSEEGSSISG 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 158 GQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEegRTMLVVTHELGFARHvSNRVVFMHQGTIDCDGA 237
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGS 691
|
....*....
gi 490999375 238 PEALFGAHG 246
Cdd:TIGR01193 692 HDELLDRNG 700
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
22-252 |
4.18e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 86.30 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 22 DVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVsvggetiemkhhaRGHRLAANPKQIERLRSRLGMVF 101
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI-------------RFHDIPLTKLQLDSWRSRLAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 102 QSFNLWSHmTVLQNVIEG-PHyvlkrSKQECIEQAEQLLD-RVGMLNRKDFYPAQ-------LSGGQQQRVAIARALAMD 172
Cdd:PRK10789 396 QTPFLFSD-TVANNIALGrPD-----ATQQEIEHVARLASvHDDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 173 PEVMLFDEPTSALDPELVGEVLKVMRSLAeEGRTMLVVTHELGFARHVSNRVVfMHQGTIDCDGAPEALFGAHG----SP 248
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLSALTEASEILV-MQHGHIAQRGNHDQLAQQSGwyrdMY 547
|
....
gi 490999375 249 RFQQ 252
Cdd:PRK10789 548 RYQQ 551
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-212 |
6.25e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 82.70 E-value: 6.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 6 PVTLSVSDIHKSFG-SLD-----VLKGISIQAQKGDVISILGASGSGKSTLLRCI--NLLETPDAGVVSVggetiemkhh 77
Cdd:COG2401 22 DLSERVAIVLEAFGvELRvveryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDV---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 78 arghrlaanpkqierlrsrlgmvfQSFNLWSHMTVLQNViegphyvlkrSKQECIEQAEQLLDRVGmLNRKDFY---PAQ 154
Cdd:COG2401 92 ------------------------PDNQFGREASLIDAI----------GRKGDFKDAVELLNAVG-LSDAVLWlrrFKE 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 155 LSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTH 212
Cdd:COG2401 137 LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATH 195
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
8-212 |
9.44e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.84 E-value: 9.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 8 TLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHAR-----GHR 82
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEachylGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 83 LAANPkqierlrsrlgmvfqsfnlwsHMTVLQNV-----IEGPHyvlkrskQECIEQAeqlLDRVGM---LNRKDFYpaq 154
Cdd:PRK13539 82 NAMKP---------------------ALTVAENLefwaaFLGGE-------ELDIAAA---LEAVGLaplAHLPFGY--- 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 155 LSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTH 212
Cdd:PRK13539 128 LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
9-239 |
1.05e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.42 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCI--NLLETPDAGVVSVGGETIemkhharghrLAAN 86
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDI----------LELS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 87 PKQierlRSRLGMvFQSFnlwshmtvlQNVIEGP----HYVLKRSK----------QECIEQAEQLLDRVGM----LNR- 147
Cdd:COG0396 71 PDE----RARAGI-FLAF---------QYPVEIPgvsvSNFLRTALnarrgeelsaREFLKLLKEKMKELGLdedfLDRy 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 148 --KDFypaqlSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVS-NRV 224
Cdd:COG0396 137 vnEGF-----SGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIKpDFV 211
|
250
....*....|....*
gi 490999375 225 VFMHQGTIDCDGAPE 239
Cdd:COG0396 212 HVLVDGRIVKSGGKE 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
23-241 |
1.06e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.91 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEM---KHHARghRLAANPKQIERLRSrlgm 99
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwssKAFAR--KVAYLPQQLPAAEG---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 100 vfqsfnlwshMTVLQNVIEGP---HYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVM 176
Cdd:PRK10575 100 ----------MTVRELVAIGRypwHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490999375 177 LFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEAL 241
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-214 |
2.28e-18 |
|
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: 84.07 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 32 QKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHARG-------HRLAAN-------PKQIERLRSRL 97
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWDEVLKRFRGtelqdyfKKLANGeikvahkPQYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 98 -GMVfqsfnlwshMTVLQNVIEgphyvlkRSKqecieqAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVM 176
Cdd:COG1245 177 kGTV---------RELLEKVDE-------RGK------LDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490999375 177 LFDEPTSALDpelVGE---VLKVMRSLAEEGRTMLVVTHEL 214
Cdd:COG1245 235 FFDEPSSYLD---IYQrlnVARLIRELAEEGKYVLVVEHDL 272
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
23-232 |
3.18e-18 |
|
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: 80.62 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaanpKQI--ERLRSRLGMV 100
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI---------------SKIglHDLRSRISII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 101 FQSFNLWSHmTVLQNV-IEGPHY------VLKRS--KQECIEQAEQLLDRV--GMLNrkdfypaqLSGGQQQRVAIARAL 169
Cdd:cd03244 84 PQDPVLFSG-TIRSNLdPFGEYSdeelwqALERVglKEFVESLPGGLDTVVeeGGEN--------LSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999375 170 AMDPEVMLFDEPTSALDPELVGEVLKVMRSlAEEGRTMLVVTHELgfaRHV--SNRVVFMHQGTI 232
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRL---DTIidSDRILVLDKGRV 215
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-230 |
3.72e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.04 E-value: 3.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLeTPDAGVVSVGGETIEmkhHARGHRLAanpkqieRLRSRLGmvfQS 103
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLS---DWSAAELA-------RHRAYLS---QQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 FNLWSHMTVLQnviegphYV-LKRSKQECIEQAEQLLDRV-GMLNRKDFYP---AQLSGGQQQRVAIARAL-----AMDP 173
Cdd:COG4138 78 QSPPFAMPVFQ-------YLaLHQPAGASSEAVEQLLAQLaEALGLEDKLSrplTQLSGGEWQRVRLAAVLlqvwpTINP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 174 E--VMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQG 230
Cdd:COG4138 151 EgqLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQG 209
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-213 |
4.88e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.14 E-value: 4.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 1 MHDPRPVtLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharg 80
Cdd:PRK10247 1 MQENSPL-LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 81 hrLAANPkqiERLRSRLGMVFQSFNLWSHmTVLQNVIEgPHYVLKRSKQECIEQAEqlLDRVG----MLNRKdfyPAQLS 156
Cdd:PRK10247 72 --STLKP---EIYRQQVSYCAQTPTLFGD-TVYDNLIF-PWQIRNQQPDPAIFLDD--LERFAlpdtILTKN---IAELS 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 157 GGQQQRVAIARALAMDPEVMLFDEPTSALDP---ELVGEVlkVMRSLAEEGRTMLVVTHE 213
Cdd:PRK10247 140 GGEKQRISLIRNLQFMPKVLLLDEITSALDEsnkHNVNEI--IHRYVREQNIAVLWVTHD 197
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-214 |
6.71e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.67 E-value: 6.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCInlletpdAGVVSVGgeTIEMKHHARGHRL-AANP 87
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL-------SGVYPHG--TYEGEIIFEGEELqASNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 KQIERlrSRLGMVFQSFNLWSHMTVLQNVIEG----PHYVLKRSKQecIEQAEQLLDRVGMlnrkDFYPA----QLSGGQ 159
Cdd:PRK13549 77 RDTER--AGIAIIHQELALVKELSVLENIFLGneitPGGIMDYDAM--YLRAQKLLAQLKL----DINPAtpvgNLGLGQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490999375 160 QQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHEL 214
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKL 203
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
9-230 |
1.41e-17 |
|
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: 81.79 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCInlletpdAGVVSVGgeTIEMKHHARGHRL-AANP 87
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKIL-------SGVYPHG--TWDGEIYWSGSPLkASNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 KQIERlrSRLGMVFQSFNLWSHMTVLQNVIEGPHYVLKRSKQ---ECIEQAEQLLDRVGMLNRKDFYP-AQLSGGQQQRV 163
Cdd:TIGR02633 73 RDTER--AGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMaynAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 164 AIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQG 230
Cdd:TIGR02633 151 EIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-212 |
1.98e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 78.30 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 19 GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGvvsvggetiemkhharghRLAANPKQIERLRSRLg 98
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAG------------------RVLLNGGPLDFQRDSI- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 99 mvfQSFNLW-SH---MTVLQNVIEGPHYVLKRSKQECIEQAeqlLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPE 174
Cdd:cd03231 72 ---ARGLLYlGHapgIKTTLSVLENLRFWHADHSDEQVEEA---LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRP 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 490999375 175 VMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTH 212
Cdd:cd03231 146 LWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
27-235 |
3.18e-17 |
|
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: 80.64 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 27 ISIQAQKGDVISILGASGSGKSTLLRCI-NLLETPDAGVVSVGGETIEMKHHARG--HRLAANPKQierlRSRLGMVfqs 103
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNPAQAirAGIAMVPED----RKRHGIV--- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 fnlwSHMTVLQNVIEGphyVLKR--SKQECIEQAEQLLDRVGM--LNRKDFYP----AQLSGGQQQRVAIARALAMDPEV 175
Cdd:TIGR02633 352 ----PILGVGKNITLS---VLKSfcFKMRIDAAAELQIIGSAIqrLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 176 MLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCD 235
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
11-231 |
4.56e-17 |
|
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: 77.37 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 11 VSDIHKSFGS-LDVLKGISIQAQKGDVISILGASGSGKSTLLRCInLLETpdagvvsvggETIEMKHHARGHRLAANPKQ 89
Cdd:cd03290 3 VTNGYFSWGSgLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAI-LGEM----------QTLEGKVHWSNKNESEPSFE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 90 IERLRSRLGMVFQSFNLWS-HMTVLQNVIEGPHYVLKRSK---QECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAI 165
Cdd:cd03290 72 ATRSRNRYSVAYAAQKPWLlNATVEENITFGSPFNKQRYKavtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 166 ARALAMDPEVMLFDEPTSALDPELVGEVLK--VMRSLAEEGRTMLVVTHELGFARHvSNRVVFMHQGT 231
Cdd:cd03290 152 ARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDGS 218
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
24-214 |
4.90e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 80.45 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetiemkHHARGHRLAAnpkqierLRSRLGMVFQS 103
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG------HDLRDYTLAS-------LRNQVALVSQN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 FNLWSHmTVLQNVI--EGPHY----VLKRSKQ----ECIEQAEQLLDRVGMLNrkdfyPAQLSGGQQQRVAIARALAMDP 173
Cdd:PRK11176 426 VHLFND-TIANNIAyaRTEQYsreqIEEAARMayamDFINKMDNGLDTVIGEN-----GVLLSGGQRQRIAIARALLRDS 499
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490999375 174 EVMLFDEPTSALDPELVGEVLKVMRSLaEEGRTMLVVTHEL 214
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRL 539
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-212 |
7.98e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 76.38 E-value: 7.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 26 GISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlaanpKQIERLRSRLgmvfqsfn 105
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR--------------RQRDEYHQDL-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 106 LW--------SHMTVLQNViegpHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVML 177
Cdd:PRK13538 77 LYlghqpgikTELTALENL----RFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*
gi 490999375 178 FDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTH 212
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-249 |
8.96e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 78.21 E-value: 8.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGEtiemkhharghrlaaNP-KQIERLRSRLGMVF- 101
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY---------------VPfKRRKEFARRIGVVFg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 102 QSFNLWSHMTVLQNViegphYVLKR----SKQEcieqAEQLLDR-VGMLNRKDFY--PA-QLSGGQQQRVAIARALAMDP 173
Cdd:COG4586 103 QRSQLWWDLPAIDSF-----RLLKAiyriPDAE----YKKRLDElVELLDLGELLdtPVrQLSLGQRMRCELAAALLHRP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 174 EVMLFDEPTSALDP---ELVGEVLKVMRslAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFGAHGSPR 249
Cdd:COG4586 174 KILFLDEPTIGLDVvskEAIREFLKEYN--RERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYK 250
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
27-246 |
1.19e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.12 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 27 ISIQAQKGDVISILGASGSGKSTLLrciNLLE--TPDAGVVSVGGetIEMKhharghrlAANPKQierLRSRLGMVFQSF 104
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLL---NALLgfLPYQGSLKING--IELR--------ELDPES---WRKHLSWVGQNP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 105 NLWsHMTVLQNVIEGPHyvlkrskQECIEQAEQLLDRVGMlnrKDFYPAQ--------------LSGGQQQRVAIARALA 170
Cdd:PRK11174 433 QLP-HGTLRDNVLLGNP-------DASDEQLQQALENAWV---SEFLPLLpqgldtpigdqaagLSVGQAQRLALARALL 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 171 MDPEVMLFDEPTSALDpeLVGEVLkVMRSL--AEEGRTMLVVTHELGFARHVSNRVVfMHQGTIDCDGAPEALFGAHG 246
Cdd:PRK11174 502 QPCQLLLLDEPTASLD--AHSEQL-VMQALnaASRRQTTLMVTHQLEDLAQWDQIWV-MQDGQIVQQGDYAELSQAGG 575
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-212 |
1.47e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.70 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCInlletpdAGVVSVGGETIEMKHHARghrlaanpkqierlrsrlgMVF- 101
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAI-------AGLWPYGSGRIARPAGAR-------------------VLFl 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 102 -QSfnlwSHMTV--LQNVIEGPHYVLKRSKqeciEQAEQLLDRVG------MLNRKDFYPAQLSGGQQQRVAIARALAMD 172
Cdd:COG4178 432 pQR----PYLPLgtLREALLYPATAEAFSD----AELREALEAVGlghlaeRLDEEADWDQVLSLGEQQRLAFARLLLHK 503
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490999375 173 PEVMLFDEPTSALDPELVGEVLKVMRSlAEEGRTMLVVTH 212
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-214 |
1.99e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 78.31 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 32 QKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHARG-------HRLAAN-------PKQIERLRsrl 97
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVLKRFRGtelqnyfKKLYNGeikvvhkPQYVDLIP--- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 98 gMVFQSfnlwshmtvlqNVIEgphyVLKRSKQECIeqAEQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVML 177
Cdd:PRK13409 174 -KVFKG-----------KVRE----LLKKVDERGK--LDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490999375 178 FDEPTSALDpelVGE---VLKVMRSLAeEGRTMLVVTHEL 214
Cdd:PRK13409 236 FDEPTSYLD---IRQrlnVARLIRELA-EGKYVLVVEHDL 271
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-214 |
2.92e-16 |
|
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: 75.87 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 34 GDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHARGHRLAanpKQIERLRSrlGMVfqsfnlwshmtvl 113
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSELQ---NYFTKLLE--GDV------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 114 qNVIEGPHYVLKRSKQ------ECIEQA------EQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEP 181
Cdd:cd03236 88 -KVIVKPQYVDLIPKAvkgkvgELLKKKdergklDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190
....*....|....*....|....*....|...
gi 490999375 182 TSALDPELVGEVLKVMRSLAEEGRTMLVVTHEL 214
Cdd:cd03236 167 SSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-238 |
3.04e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 76.40 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCI--NLLETPDAGVVSVGGE-TIEmkhharGHRLAA-NPKQIERLRSRLG 98
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGGGAPRGARVTGDvTLN------GEPLAAiDAPRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 99 MVFQSFNLWShmtVLQNVIEG--PHyvLKRSKQECIEQ---AEQLLDRVGM--LNRKDFypAQLSGGQQQRVAIARALAM 171
Cdd:PRK13547 90 QAAQPAFAFS---AREIVLLGryPH--ARRAGALTHRDgeiAWQALALAGAtaLVGRDV--TTLSGGELARVQFARVLAQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 172 ---------DPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRT-MLVVTHELGFARHVSNRVVFMHQGTIDCDGAP 238
Cdd:PRK13547 163 lwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
9-258 |
6.34e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.15 E-value: 6.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSvggetiemkhHARGHRLAANPK 88
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----------RNGKLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIErLRSRLGMVFQSFnlwshMTVLQNVIEG---PhyVLKRSkqecieQAEQLLDrvgmlnrkdfYPAQ-LSGGQQQRVA 164
Cdd:PRK09544 75 KLY-LDTTLPLTVNRF-----LRLRPGTKKEdilP--ALKRV------QAGHLID----------APMQkLSGGETQRVL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEE-GRTMLVVTHELGFARHVSNRVVFMHQgTIDCDGAPE---- 239
Cdd:PRK09544 131 LARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEvvsl 209
|
250 260
....*....|....*....|....
gi 490999375 240 -----ALFGAHGSPrfQQFISSHH 258
Cdd:PRK09544 210 hpefiSMFGPRGAE--QLGIYRHH 231
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
23-215 |
8.61e-16 |
|
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: 73.60 E-value: 8.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKhharghrlaanpkQIERLRSRLGMVFQ 102
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI-------------PLEDLRSSLTIIPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 SFNLWSHmTVLQNviegphyvlkrskqecieqaeqlLDRVGMLNRKDFYPA--------QLSGGQQQRVAIARALAMDPE 174
Cdd:cd03369 90 DPTLFSG-TIRSN-----------------------LDPFDEYSDEEIYGAlrvsegglNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490999375 175 VMLFDEPTSALDPELVGEVLKVMRSLAeEGRTMLVVTHELG 215
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEF-TNSTILTIAHRLR 185
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-252 |
3.35e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.16 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCInLLETP---DAGVVsvggetiemkhharghrlaanpkqierLRSRLGMV 100
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAM-LGELPprsDASVV---------------------------IRGTVAYV 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 101 FQS---FNlwshMTVLQNVIEGPHYVLKRSkqecieqaEQLLDRVGMLNRKDFYPA-----------QLSGGQQQRVAIA 166
Cdd:PLN03130 685 PQVswiFN----ATVRDNILFGSPFDPERY--------ERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMA 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 167 RALAMDPEVMLFDEPTSALDPELVGEVLKvmRSLAEE--GRTMLVVTHELGFARHVsNRVVFMHQGTIDCDGAPEALfgA 244
Cdd:PLN03130 753 RAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDElrGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEEL--S 827
|
....*...
gi 490999375 245 HGSPRFQQ 252
Cdd:PLN03130 828 NNGPLFQK 835
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-230 |
1.04e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 72.63 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 19 GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCInlletpdagvvsVGgeTIEMKHHARGHR--------LAANPKQI 90
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAI------------CG--ITKDNWHVTADRfrwngidlLKLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 91 ERLRSR-LGMVFQ--SFNLWSHMTVLQNVIEG-PHYVLKRS----KQECIEQAEQLLDRVGMLNRKDF---YPAQLSGGQ 159
Cdd:COG4170 84 RKIIGReIAMIFQepSSCLDPSAKIGDQLIEAiPSWTFKGKwwqrFKWRKKRAIELLHRVGIKDHKDImnsYPHELTEGE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490999375 160 QQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAE-EGRTMLVVTHELGFARHVSNRVVFMHQG 230
Cdd:COG4170 164 CQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCG 235
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
12-214 |
1.81e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.45 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 12 SDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKhharghrlaaNPKqiE 91
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFK----------SSK--E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 92 RLRSRLGMVFQSFNLWSHMTVLQNVIEGpHYVLKR---SKQECIEQAEQLLDRVGMlnrkDFYP----AQLSGGQQQRVA 164
Cdd:PRK10982 70 ALENGISMVHQELNLVLQRSVMDNMWLG-RYPTKGmfvDQDKMYRDTKAIFDELDI----DIDPrakvATLSVSQMQMIE 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHEL 214
Cdd:PRK10982 145 IAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKM 194
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-232 |
1.98e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.64 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 27 ISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMK--HHARGHRLAANPKQierlRSRLGMVfqsf 104
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRspRDAIRAGIMLCPED----RKAEGII---- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 105 nlwSHMTVLQNV-IEG-PHYV----LKRSKQEcIEQAEQLLDRvgmLNRKDFYPAQ----LSGGQQQRVAIARALAMDPE 174
Cdd:PRK11288 344 ---PVHSVADNInISArRHHLragcLINNRWE-AENADRFIRS---LNIKTPSREQlimnLSGGNQQKAILGRWLSEDMK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490999375 175 VMLFDEPTSALDpelVG---EVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:PRK11288 417 VILLDEPTRGID---VGakhEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-232 |
3.81e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.57 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHARGhrLAANPKQIERLRSRLGMVFQs 103
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDG--LANGIVYISEDRKRDGLVLG- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 fnlwshMTVLQNV-IEGPHYVLKRSKQeCIEQAEQLL--DRVGMLNRKDFYPAQ----LSGGQQQRVAIARALAMDPEVM 176
Cdd:PRK10762 345 ------MSVKENMsLTALRYFSRAGGS-LKHADEQQAvsDFIRLFNIKTPSMEQaiglLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 177 LFDEPTSALDpelVG---EVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:PRK10762 418 ILDEPTRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
153-235 |
6.69e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.73 E-value: 6.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 153 AQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDpelVG---EVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQ 229
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHE 480
|
....*.
gi 490999375 230 GTIDCD 235
Cdd:PRK13549 481 GKLKGD 486
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
19-256 |
1.24e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 69.45 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 19 GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCI------NLLETPDAGVVsvggETIEMkhharghrLAANPKQIER 92
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdNWRVTADRMRF----DDIDL--------LRLSPRERRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 93 L-RSRLGMVFQ--------SFNLWSHMtvLQNvIEGPHY------VLKRSKQECIEqaeqLLDRVGMLNRKDF---YPAQ 154
Cdd:PRK15093 86 LvGHNVSMIFQepqscldpSERVGRQL--MQN-IPGWTYkgrwwqRFGWRKRRAIE----LLHRVGIKDHKDAmrsFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 155 LSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAE-EGRTMLVVTHELGFARHVSNRVVFMHQGTID 233
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250 260
....*....|....*....|...
gi 490999375 234 CDGAPEALFGAHGSPRFQQFISS 256
Cdd:PRK15093 239 ETAPSKELVTTPHHPYTQALIRA 261
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
9-241 |
1.33e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 69.76 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLeTPDAGvvsvggetiemKHHARGHRLAANPK 88
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*-GPDAG-----------RRPWRF*TWCANRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERL----RSRLGMVFQSFNLWSHMTVLQNViegphyvLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQRVA 164
Cdd:NF000106 82 ALRRTig*hRPVR*GRRESFSGRENLYMIGR*-------LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 165 IARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEAL 241
Cdd:NF000106 155 LAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
32-232 |
2.17e-13 |
|
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: 69.44 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 32 QKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlaanPKQIERLRSRLGMVFQSFNLWSHMT 111
Cdd:COG4615 356 RRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT-------------ADNREAYRQLFSAVFSDFHLFDRLL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 112 VLQNVIEGphyvlkrskqeciEQAEQLLDRVGM-----LNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALD 186
Cdd:COG4615 423 GLDGEADP-------------ARARELLERLELdhkvsVEDGRFSTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQD 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490999375 187 P--------ELVGEvlkvmrsLAEEGRTMLVVTHELGFArHVSNRVVFMHQGTI 232
Cdd:COG4615 490 PefrrvfytELLPE-------LKARGKTVIAISHDDRYF-DLADRVLKMDYGKL 535
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-257 |
2.83e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 69.59 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCInLLETpdagvvsvggETIEMKHHARGhRLAANPKQIerlrsrlgmvfqs 103
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL-LAEM----------DKVEGHVHMKG-SVAYVPQQA------------- 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 fnlWSHMTVLQ-NVIEGPHYVLKRSKQecIEQAEQLLDRVGMLNRKDFYP-----AQLSGGQQQRVAIARALAMDPEVML 177
Cdd:TIGR00957 709 ---WIQNDSLReNILFGKALNEKYYQQ--VLEACALLPDLEILPSGDRTEigekgVNLSGGQKQRVSLARAVYSNADIYL 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 178 FDEPTSALDPElVGE-----VLKVMRSLAeeGRTMLVVTHELGFARHVsNRVVFMHQGTIDCDGAPEALFGAHGSprFQQ 252
Cdd:TIGR00957 784 FDDPLSAVDAH-VGKhifehVIGPEGVLK--NKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDGA--FAE 857
|
....*
gi 490999375 253 FISSH 257
Cdd:TIGR00957 858 FLRTY 862
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-202 |
5.89e-13 |
|
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: 68.04 E-value: 5.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVgGETIemkhharghrlaanpk 88
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV---------------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 qierlrsRLGMVFQSF-NLWSHMTVLQnVIEGPHYVLKRSKQECIEQAeqlldRVGMLNRK----DFYPAQLSGGQQQRV 163
Cdd:TIGR03719 386 -------KLAYVDQSRdALDPNKTVWE-EISGGLDIIKLGKREIPSRA-----YVGRFNFKgsdqQKKVGQLSGGERNRV 452
|
170 180 190
....*....|....*....|....*....|....*....
gi 490999375 164 AIARALAMDPEVMLFDEPTSALDPElvgevlkVMRSLAE 202
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLDVE-------TLRALEE 484
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
9-212 |
6.94e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.59 E-value: 6.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCI------NLLEtpdaGVVSVGGETIemkhharghr 82
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpayKILE----GDILFKGESI---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 83 LAANPKQierlRSRLGmVFQSFnlwshmtvlQNVIEGP----------HYVLKRSKQ--------ECIEQAEQLLDRVGM 144
Cdd:CHL00131 74 LDLEPEE----RAHLG-IFLAF---------QYPIEIPgvsnadflrlAYNSKRKFQglpeldplEFLEIINEKLKLVGM 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999375 145 ----LNR---KDFypaqlSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTH 212
Cdd:CHL00131 140 dpsfLSRnvnEGF-----SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
40-255 |
7.60e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.84 E-value: 7.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 40 LGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaaNPKQIErLRSRLGMVFQSFNLWSHMTVLQNVIEg 119
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-------------DAGDIA-TRRRVGYMSQAFSLYGELTVRQNLEL- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 120 pHYVLKRSKQECIEQA-EQLLDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDP-------ELVG 191
Cdd:NF033858 363 -HARLFHLPAAEIAARvAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPvardmfwRLLI 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490999375 192 EvlkvmrsLA-EEGRTMLVVTHelgF----ARhvSNRVVFMHQGTI-DCDgAPEALFGAHGSPRFQQ-FIS 255
Cdd:NF033858 442 E-------LSrEDGVTIFISTH---FmneaER--CDRISLMHAGRVlASD-TPAALVAARGAATLEEaFIA 499
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-238 |
1.52e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 66.74 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLrciNLLetpdAGVVSVGgeTIEMKHHARGhrlaaNPK 88
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLM---KVL----SGVYPHG--SYEGEILFDG-----EVC 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIERLRS--RLGMVF--QSFNLWSHMTVLQNVIEGpHYVLKR---SKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQ 161
Cdd:NF040905 68 RFKDIRDseALGIVIihQELALIPYLSIAENIFLG-NERAKRgviDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 162 RVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQG----TIDCDGA 237
Cdd:NF040905 147 LVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGrtieTLDCRAD 226
|
.
gi 490999375 238 P 238
Cdd:NF040905 227 E 227
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-211 |
2.25e-12 |
|
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: 64.21 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 16 KSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGV---VSVGGETI-EMKHHARGHrlaanpkqie 91
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVegdIHYNGIPYkEFAEKYPGE---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 92 rlrsrLGMVFQSFNLWSHMTVlqnviegphyvlkrskqecieqaEQLLDRVGMLNRKDFYPAqLSGGQQQRVAIARALAM 171
Cdd:cd03233 85 -----IIYVSEEDVHFPTLTV-----------------------RETLDFALRCKGNEFVRG-ISGGERKRVSIAEALVS 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490999375 172 DPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVT 211
Cdd:cd03233 136 RASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS 175
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-242 |
2.59e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.54 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCInLLETPDAGVVSVggetiemkhHARGhRLAANPKqierlrsrlgmVFQS 103
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAM-LGELSHAETSSV---------VIRG-SVAYVPQ-----------VSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 FNlwshMTVLQNVIEGPHYVLKRSKQEcieqaeqlLDRVGMLNRKDFYPAQ-----------LSGGQQQRVAIARALAMD 172
Cdd:PLN03232 691 FN----ATVRENILFGSDFESERYWRA--------IDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 173 PEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVsNRVVFMHQGTIDCDGAPEALF 242
Cdd:PLN03232 759 SDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS 827
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
155-232 |
3.21e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 3.21e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 155 LSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
155-225 |
6.39e-12 |
|
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: 62.59 E-value: 6.39e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490999375 155 LSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEG-RTMLVVTHELGFARHVSNRVV 225
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHDLAVLDYLSDRIH 143
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-222 |
6.42e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.96 E-value: 6.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCInlletpdAGV-VSVGGETIEMKHHARGHrLAANPK------------- 88
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AGVdKDFNGEARPQPGIKVGY-LPQEPQldptktvrenvee 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 ---QIERLRSRLGMVFQSFN--------LWSHMTVLQNVIE--GPHYVLKRskqecIEQAEQLLdrvgMLNRKDFYPAQL 155
Cdd:TIGR03719 92 gvaEIKDALDRFNEISAKYAepdadfdkLAAEQAELQEIIDaaDAWDLDSQ-----LEIAMDAL----RCPPWDADVTKL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 156 SGGQQQRVAIARALAMDPEVMLFDEPTSALDPElvgEVLKVMRSLAEEGRTMLVVTHELGFARHVSN 222
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQEYPGTVVAVTHDRYFLDNVAG 226
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-232 |
6.72e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.99 E-value: 6.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghrlAANPkqiERLRSRLGMVFQS 103
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT----------AEQP---EDYRKLFSAVFTD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 FNLWSHMTvlqnvieGPhyvlkRSKQECIEQAEQLLDRVGM---LNRKD--FYPAQLSGGQQQRVAIARALAMDPEVMLF 178
Cdd:PRK10522 406 FHLFDQLL-------GP-----EGKPANPALVEKWLERLKMahkLELEDgrISNLKLSKGQKKRLALLLALAEERDILLL 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 179 DEPTSALDP----ELVGEVLKVMRslaEEGRTMLVVTHELGFARHvSNRVVFMHQGTI 232
Cdd:PRK10522 474 DEWAADQDPhfrrEFYQVLLPLLQ---EMGKTIFAISHDDHYFIH-ADRLLEMRNGQL 527
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-239 |
9.23e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.41 E-value: 9.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 27 ISIQAQKGDVISILGASGSGKSTLLRCINLLeTPDAGVVSVGGETIEmkhHARGHRLAanpkqieRLRSRLGmvfQSFNL 106
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLE---AWSAAELA-------RHRAYLS---QQQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 107 WSHMTVLqnviegpHYV-LKRSKQECIEQAEQLLDRV-GMLNRKDFYP---AQLSGGQQQRVAIARA-LAMDPEV----- 175
Cdd:PRK03695 81 PFAMPVF-------QYLtLHQPDKTRTEAVASALNEVaEALGLDDKLGrsvNQLSGGEWQRVRLAAVvLQVWPDInpagq 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999375 176 -MLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPE 239
Cdd:PRK03695 154 lLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRD 218
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-231 |
1.07e-11 |
|
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: 63.34 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVsvggetiemKHHARghrlaanpkqierlrsrlgMVFQ 102
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---------KHSGR-------------------ISFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 SFNLW-SHMTVLQNVIEGPHYVLKRSKQecIEQAEQLLDRVGMLNRKDFYP-----AQLSGGQQQRVAIARALAMDPEVM 176
Cdd:cd03291 104 SQFSWiMPGTIKENIIFGVSYDEYRYKS--VVKACQLEEDITKFPEKDNTVlgeggITLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 177 LFDEPTSALDPELVGEVL-----KVMRSlaeegRTMLVVTHELGFARhVSNRVVFMHQGT 231
Cdd:cd03291 182 LLDSPFGYLDVFTEKEIFescvcKLMAN-----KTRILVTSKMEHLK-KADKILILHEGS 235
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-213 |
2.41e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCinLLETPDAGVVSvggetiemkhhaRGHRLAANPKQIERLRSRLGMVFQ 102
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNV--LAERVTTGVIT------------GGDRLVNGRPLDSSFQRSIGYVQQ 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 SFNLWSHMTVLQNVI-----EGPHYVlkrSKQECIEQAEQLLDRVGMLNRKDFY---PAQ-LSGGQQQRVAIARALAMDP 173
Cdd:TIGR00956 844 QDLHLPTSTVRESLRfsaylRQPKSV---SKSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKP 920
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490999375 174 EVMLF-DEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHE 213
Cdd:TIGR00956 921 KLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-230 |
5.47e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.62 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGvvsvggetiEMKHHARghrlaanpkqierlrsrlgMVFQ 102
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG---------KIKHSGR-------------------ISFS 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 SFNLW-SHMTVLQNVIEGPHYVLKRSKQecIEQAEQLLDRVGMLNRKDFYP-----AQLSGGQQQRVAIARALAMDPEVM 176
Cdd:TIGR01271 493 PQTSWiMPGTIKDNIIFGLSYDEYRYTS--VIKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLY 570
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 177 LFDEPTSALDPELVGEVL-----KVMRSlaeegRTMLVVTHELGFARHvSNRVVFMHQG 230
Cdd:TIGR01271 571 LLDSPFTHLDVVTEKEIFesclcKLMSN-----KTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-241 |
5.67e-11 |
|
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: 62.72 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 27 ISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIemkhharghrlaanpkqierlRSRLGMVFQSFNL 106
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI---------------------LTNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 107 WSHMTVLQNVIEGPH--YVLKRSKQECIEQAEQL----LDRVGMLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDE 180
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREhlYLYARLRGVPAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490999375 181 PTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEAL 241
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-223 |
9.49e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 9.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 21 LDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVsvggeTIEMKHHARGHRLaanpkqiERLRSRLGMV 100
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-----IINDSHNLKDINL-------KWWRSKIGVV 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 101 FQSFNLWSHMtvLQNVIEGPHYVLK--------------------RSKQECIEQAE-------QLLDRVGMLNRK----- 148
Cdd:PTZ00265 466 SQDPLLFSNS--IKNNIKYSLYSLKdlealsnyynedgndsqenkNKRNSCRAKCAgdlndmsNTTDSNELIEMRknyqt 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 149 ----------------DFYPA--------------QLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMR 198
Cdd:PTZ00265 544 ikdsevvdvskkvlihDFVSAlpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN 623
|
250 260 270
....*....|....*....|....*....|..
gi 490999375 199 SL-AEEGRTMLVVTHELGFARH------VSNR 223
Cdd:PTZ00265 624 NLkGNENRITIIIAHRLSTIRYantifvLSNR 655
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-213 |
2.02e-10 |
|
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: 58.41 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 19 GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETpdAGVVSvggetiemkhharGHRLAANPKQIERLRSRLG 98
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKT--AGVIT-------------GEILINGRPLDKNFQRSTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 99 MVFQSFNLWSHMTVlqnviegphyvlkrskQECIEQAEQLLDrvgmlnrkdfypaqLSGGQQQRVAIARALAMDPEVMLF 178
Cdd:cd03232 83 YVEQQDVHSPNLTV----------------REALRFSALLRG--------------LSVEQRKRLTIGVELAAKPSILFL 132
|
170 180 190
....*....|....*....|....*....|....*
gi 490999375 179 DEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHE 213
Cdd:cd03232 133 DEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQ 167
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-213 |
2.62e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEMKHHAR-------GHRLAANPKQIERLRS 95
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYqkqlcfvGHRSGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 96 RLGMVFQSFNLwsHMTVLQNVIEGPHYVlkrskqecieqaeqlldrvgmlnrkDFYPAQLSGGQQQRVAIARALAMDPEV 175
Cdd:PRK13540 96 LYDIHFSPGAV--GITELCRLFSLEHLI-------------------------DYPCGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 490999375 176 MLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHE 213
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-212 |
3.82e-10 |
|
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: 57.16 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCInlletpdAGVVSVGGETIEMkhHARGHRLaanpkqierlrsrlgMVFQ 102
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-------AGLWPWGSGRIGM--PEGEDLL---------------FLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 SfnlwSHMTVLqnviegphyVLKrskqecieqaEQLLdrvgmlnrkdfYP--AQLSGGQQQRVAIARALAMDPEVMLFDE 180
Cdd:cd03223 72 R----PYLPLG---------TLR----------EQLI-----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|..
gi 490999375 181 PTSALDPELVGEVLKVMRslaEEGRTMLVVTH 212
Cdd:cd03223 118 ATSALDEESEDRLYQLLK---ELGITVISVGH 146
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-204 |
3.88e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.75 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 11 VSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVgGETIemkhharghrlaanpkqi 90
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV------------------ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 91 erlrsRLGMVFQSF-NLWSHMTVLQNVIEGpHYVLKRSKQECIEQAeqlldRVGMLNRKDfyPAQ------LSGGQQQRV 163
Cdd:PRK11819 388 -----KLAYVDQSRdALDPNKTVWEEISGG-LDIIKVGNREIPSRA-----YVGRFNFKG--GDQqkkvgvLSGGERNRL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490999375 164 AIARALAMDPEVMLFDEPTSALDPElvgevlkVMRSLaEEG 204
Cdd:PRK11819 455 HLAKTLKQGGNVLLLDEPTNDLDVE-------TLRAL-EEA 487
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
151-226 |
5.55e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 5.55e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 151 YPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEG-RTMLVVTHELGFARHVSNRVVF 226
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKRSDKIVVF 1431
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
24-232 |
6.98e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.13 E-value: 6.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETiemkhharghrlaanpkqierlrsrlGMVFQS 103
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA--------------------------ALIAIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 FNLWSHMTVLQNV-IEGPHYVLKRSK-QECIEQAEQLLDRVGMLNRkdfyPAQ-LSGGQQQRVAIARALAMDPEVMLFDE 180
Cdd:PRK13545 94 SGLNGQLTGIENIeLKGLMMGLTKEKiKEIIPEIIEFADIGKFIYQ----PVKtYSSGMKSRLGFAISVHINPDILVIDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490999375 181 PTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTI 232
Cdd:PRK13545 170 ALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-224 |
7.28e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 7.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 11 VSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCinLLE--TPDAGVVSVGGEtIEMKHHARgHRLAANPK 88
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKL--MLGqlQADSGRIHCGTK-LEVAYFDQ-HRAELDPE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QierlrsrlgmvfqsfnlwshmTVLQNVIEGphyvlkrsKQECieqaeqlldrvgMLNRKD-----------FYPAQ--- 154
Cdd:PRK11147 398 K---------------------TVMDNLAEG--------KQEV------------MVNGRPrhvlgylqdflFHPKRamt 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999375 155 ----LSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVgEVLKVMrsLAEEGRTMLVVTHELGFarhVSNRV 224
Cdd:PRK11147 437 pvkaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETL-ELLEEL--LDSYQGTVLLVSHDRQF---VDNTV 504
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
24-231 |
9.29e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 56.56 E-value: 9.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLLRcinlletpdagvvsvggETIEMKHHARGHRLAANPKqierlRSRLGMVFQs 103
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------------EGLYASGKARLISFLPKFS-----RNKLIFIDQ- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 fnlwshmtvLQNVIE-GPHYVlkrskqecieqaeqlldrvgMLNRKdfyPAQLSGGQQQRVAIARALAMDPE--VMLFDE 180
Cdd:cd03238 68 ---------LQFLIDvGLGYL--------------------TLGQK---LSTLSGGELQRVKLASELFSEPPgtLFILDE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490999375 181 PTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHvSNRVVFMHQGT 231
Cdd:cd03238 116 PSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPGS 165
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-246 |
1.53e-09 |
|
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: 58.42 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCI-NLLETPDAGVVSVGGETIEMKHHARGHRLAANPKQIERLRSRLGMVF 101
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLfRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 102 QSFNLWSHMTVLQnVIEGPHYVLKRSKQ------ECIEQAEqlldrvgmlnrkdfypaQLSGGQQQRVAIARALAMDPEV 175
Cdd:TIGR00957 1381 DPFSQYSDEEVWW-ALELAHLKTFVSALpdkldhECAEGGE-----------------NLSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490999375 176 MLFDEPTSALDPELVGEVLKVMRSLAEEGrTMLVVTHELGFARHVSnRVVFMHQGTIDCDGAPEALFGAHG 246
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLIQSTIRTQFEDC-TVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQRG 1511
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
155-232 |
2.17e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.49 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 155 LSGGQQQRVAIARALAMDPEVMLFDEPTSALDpelVG---EVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGT 231
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGR 481
|
.
gi 490999375 232 I 232
Cdd:NF040905 482 I 482
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-231 |
2.31e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.69 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 33 KGDVISILGASGSGKSTLLRCI-NLLETPDAGVVSVGGETIEMKHHARGHRLAANPKqierlrsrlgmvfqsfnlwshmt 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGK----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 112 vlqnviegphyvlkrskqecieqaeqlldrvgmlnrkdfyPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVG 191
Cdd:smart00382 58 ----------------------------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEA 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490999375 192 EVLK------VMRSLAEEGRTMLVVTHELGF-----ARHVSNRVVFMHQGT 231
Cdd:smart00382 98 LLLLleelrlLLLLKSEKNLTVILTTNDEKDlgpalLRRRFDRRIVLLLIL 148
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
21-213 |
3.23e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.16 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 21 LDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETpdagvvsvgGETIEmkhharGH-RLAANPKQIERLRSRLGM 99
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKT---------GGYIE------GDiRISGFPKKQETFARISGY 957
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 100 VFQSFNLWSHMTVLQNVIEGPHYVLKR--SKQECIEQAEQLLDRVGMLNRKDF---YPA--QLSGGQQQRVAIARALAMD 172
Cdd:PLN03140 958 CEQNDIHSPQVTVRESLIYSAFLRLPKevSKEEKMMFVDEVMELVELDNLKDAivgLPGvtGLSTEQRKRLTIAVELVAN 1037
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490999375 173 PEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHE 213
Cdd:PLN03140 1038 PSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-212 |
3.60e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPdagvvsVGGETiemkhharghRLAANPKqierlrsrLGMVFQ 102
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE------FEGEA----------RPAPGIK--------VGYLPQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 SFNLWSHMTVLQNVIEGPHYV---LKRSKQ------ECIEQAEQLLDRVGMLNRK------------------------- 148
Cdd:PRK11819 78 EPQLDPEKTVRENVEEGVAEVkaaLDRFNEiyaayaEPDADFDALAAEQGELQEIidaadawdldsqleiamdalrcppw 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999375 149 DFYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPElvgEVLKVMRSLAEEGRTMLVVTH 212
Cdd:PRK11819 158 DAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLEQFLHDYPGTVVAVTH 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
9-225 |
3.67e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCIN--------------------LLETPDAGV---- 64
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevllddgriiyeqdlivarLQQDPPRNVegtv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 65 ---VSVG----GETIEMKHHArGHRLAANP--KQIERLrSRLGMVFQSFNLWShmtvLQNVIegphyvlkrskQECIEQA 135
Cdd:PRK11147 84 ydfVAEGieeqAEYLKRYHDI-SHLVETDPseKNLNEL-AKLQEQLDHHNLWQ----LENRI-----------NEVLAQL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 136 EqlLDRVGMLnrkdfypAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVG---EVLKVMRSlaeegrTMLVVTH 212
Cdd:PRK11147 147 G--LDPDAAL-------SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEwleGFLKTFQG------SIIFISH 211
|
250
....*....|...
gi 490999375 213 ELGFARHVSNRVV 225
Cdd:PRK11147 212 DRSFIRNMATRIV 224
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
6-212 |
5.79e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 5.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 6 PVTLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGetiemKHHARGHRlaa 85
Cdd:PRK13543 9 PPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG-----KTATRGDR--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 86 npkqiERLRSRLGmvfqsfnlwsHMTVLQ---NVIEGPHYVLKRSKQECIEQAEQLLDRVGMLNRKDFYPAQLSGGQQQR 162
Cdd:PRK13543 81 -----SRFMAYLG----------HLPGLKadlSTLENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490999375 163 VAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTH 212
Cdd:PRK13543 146 LALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-236 |
5.96e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.05 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSvGGETIEMKHHARGHRlaanpK 88
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK-WSENANIGYYAQDHA-----Y 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 89 QIErlrsrlgmvfQSFNLWSHMTvlqnviegphyvlkRSKQEciEQAEQLLdRvGMLNRKDF------YPAQ-LSGGQQQ 161
Cdd:PRK15064 394 DFE----------NDLTLFDWMS--------------QWRQE--GDDEQAV-R-GTLGRLLFsqddikKSVKvLSGGEKG 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 162 RVAIARALAMDPEVMLFDEPTSALDPELVgEVLkvmrSLAEE---GrTMLVVTHELGFARHVSNRVV-FMHQGTIDCDG 236
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMDMESI-ESL----NMALEkyeG-TLIFVSHDREFVSSLATRIIeITPDGVVDFSG 518
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
9-212 |
6.20e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.18 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLE--TPDAGVVSVGGETIemkhharghrLAAN 86
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDL----------LELS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 87 PKqiERLRSRLGMVFQ---SFNLWSHMTVLQNVIEGphyVLKRSKQECIEQ---AEQLLDRVGMLNrkdfYPAQL----- 155
Cdd:PRK09580 72 PE--DRAGEGIFMAFQypvEIPGVSNQFFLQTALNA---VRSYRGQEPLDRfdfQDLMEEKIALLK----MPEDLltrsv 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490999375 156 ----SGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTH 212
Cdd:PRK09580 143 nvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
17-212 |
1.13e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 17 SFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCInlleTPD------AGVVSVG-----GETI-EMKHHarghrla 84
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI----TGDhpqgysNDLTLFGrrrgsGETIwDIKKH------- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 85 anpkqierlrsrLGMVFQSFnlwsHM-----TVLQNVIEGPHY--------VLKRSKQecieQAEQLLDRVGMLNRKDFY 151
Cdd:PRK10938 338 ------------IGYVSSSL----HLdyrvsTSVRNVILSGFFdsigiyqaVSDRQQK----LAQQWLDILGIDKRTADA 397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490999375 152 PAQ-LSGGQQQRVAIARALAMDPEVMLFDEPTSALDP---ELVGEVLKVMRSlaeEGRT-MLVVTH 212
Cdd:PRK10938 398 PFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVLIS---EGETqLLFVSH 460
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
155-230 |
2.57e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 2.57e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490999375 155 LSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQG 230
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-240 |
5.82e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 5.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRciNLLETPDAGVVSVGGE-TIE--------MKHHARGHRLAANPKQIERL 93
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQ--SLLSQFEISEGRVWAErSIAyvpqqawiMNATVRGNILFFDEEDAARL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 94 rsrlgmvfqsfnlwshmtvlQNVIegphyvlkRSKQecIEQAEQLLDRvGMLNRKDFYPAQLSGGQQQRVAIARALAMDP 173
Cdd:PTZ00243 753 --------------------ADAV--------RVSQ--LEADLAQLGG-GLETEIGEKGVNLSGGQKARVSLARAVYANR 801
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490999375 174 EVMLFDEPTSALDPElVGEvlKVMRSL---AEEGRTMLVVTHELgfarHVSNR---VVFMHQGTIDCDGAPEA 240
Cdd:PTZ00243 802 DVYLLDDPLSALDAH-VGE--RVVEECflgALAGKTRVLATHQV----HVVPRadyVVALGDGRVEFSGSSAD 867
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-252 |
9.95e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 52.41 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 2 HDPRPVTLSVSDI-HKSFGSLD---VLKGISIQAQKGDVISILGASGSGKSTLlrcINLLE---TPDAGVVSVGGETIEM 74
Cdd:PRK10790 331 NDDRPLQSGRIDIdNVSFAYRDdnlVLQNINLSVPSRGFVALVGHTGSGKSTL---ASLLMgyyPLTEGEIRLDGRPLSS 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 75 KHHARghrlaanpkqierLRSRLGMVFQSFNLWSHmTVLQNViegphyVLKRSKQEciEQAEQLLDRV-----------G 143
Cdd:PRK10790 408 LSHSV-------------LRQGVAMVQQDPVVLAD-TFLANV------TLGRDISE--EQVWQALETVqlaelarslpdG 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 144 MLNRKDFYPAQLSGGQQQRVAIARALAMDPEVMLFDEPTSALDP---ELVGEVLKVMRslaeEGRTMLVVTHELGFARHV 220
Cdd:PRK10790 466 LYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSgteQAIQQALAAVR----EHTTLVVIAHRLSTIVEA 541
|
250 260 270
....*....|....*....|....*....|..
gi 490999375 221 SNRVVfMHQGTIDCDGAPEALFGAHGspRFQQ 252
Cdd:PRK10790 542 DTILV-LHRGQAVEQGTHQQLLAAQG--RYWQ 570
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
155-214 |
1.29e-07 |
|
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: 51.46 E-value: 1.29e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490999375 155 LSGGQQQRVAIARALAM---DPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHEL 214
Cdd:cd03271 170 LSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL 232
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
36-212 |
2.61e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 50.01 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 36 VISILGASGSGKSTLLRCINLL--------ETPDAGVVSVGGE----TIEMKHHARGHR-----------LAANPKQIER 92
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAIRYAlygkarsrSKLRSDLINVGSEeasvELEFEHGGKRYRierrqgefaefLEAKPSERKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 93 LRSRLGMVFQSFNLWSHMTVLQNVIEGphyvLKRSKQECIEQAEQLLDRVGMLNRkdfyPAQLSGGQQQRVAIARALAmd 172
Cdd:COG0419 105 ALKRLLGLEIYEELKERLKELEEALES----ALEELAELQKLKQEILAQLSGLDP----IETLSGGERLRLALADLLS-- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490999375 173 pevMLFDepTSALDPELVGEVLKVMRSLAeegrtmlVVTH 212
Cdd:COG0419 175 ---LILD--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
154-225 |
3.09e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 3.09e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490999375 154 QLSGGQQQRVAIARALAMDPEVMLFDEPTSALDpelVGEVLKVMRSLAEEGRTMLVVTHelgfARHVSNRVV 225
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSH----AREFLNTVV 408
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
23-214 |
4.59e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 49.85 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRC-INLLETpdAGVVSVGGetiemkhharghrLAANPKQIERLRSRLGMVF 101
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAfLRLLNT--EGDIQIDG-------------VSWNSVPLQKWRKAFGVIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 102 QSFNLWSHmTVLQNVieGPHYvlKRSKQECIEQAEQlldrVGMLNRKDFYPAQ-----------LSGGQQQRVAIARALA 170
Cdd:cd03289 84 QKVFIFSG-TFRKNL--DPYG--KWSDEEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490999375 171 MDPEVMLFDEPTSALDPELVGEVLKVMRSlAEEGRTMLVVTHEL 214
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRI 197
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
16-254 |
5.13e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.43 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 16 KSFGSLDvlkGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGvvsvggetiEMKHHARGHRLAANPkqierlrs 95
Cdd:PRK13546 35 KTFFALD---DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG---------KVDRNGEVSVIAISA-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 96 rlgmvfqsfNLWSHMTVLQNvIEGPHYVLKRSKQECIEQAEQLLDrVGMLNRKDFYPAQ-LSGGQQQRVAIARALAMDPE 174
Cdd:PRK13546 95 ---------GLSGQLTGIEN-IEFKMLCMGFKRKEIKAMTPKIIE-FSELGEFIYQPVKkYSSGMRAKLGFSINITVNPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 175 VMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALFgahgsPRFQQFI 254
Cdd:PRK13546 164 ILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL-----PKYEAFL 238
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-187 |
5.15e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.68 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDaGVVSVGGetiemkhharghrLAANPKQIERLRSRLGMVFQ 102
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDG-------------VSWNSVTLQTWRKAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 SFNLWSHmTVLQNVieGPHYvlKRSKQECIEQAEQlldrVGMLNRKDFYPAQL-----------SGGQQQRVAIARALAM 171
Cdd:TIGR01271 1300 KVFIFSG-TFRKNL--DPYE--QWSDEEIWKVAEE----VGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILS 1370
|
170
....*....|....*.
gi 490999375 172 DPEVMLFDEPTSALDP 187
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDP 1386
|
|
| Rad50_Sulf |
NF041034 |
DNA double-strand break repair ATPase Rad50; |
154-213 |
6.47e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 468963 [Multi-domain] Cd Length: 872 Bit Score: 50.10 E-value: 6.47e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490999375 154 QLSGGQQ------QRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHE 213
Cdd:NF041034 779 ALSGGERisialaLRLAIAKSLMDEIGFMILDEPTVHLDEERKKELIDIIRSSMEIVPQIIVVTHD 844
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
39-219 |
6.89e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 48.76 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 39 ILGASGSGKSTLLRCINLLETPDAGVVSVGGetiemKHHARGHRLAANPKQIE-RLRSRLG---MVFQSFNlwshmtVLQ 114
Cdd:cd03240 27 IVGQNGAGKTTIIEALKYALTGELPPNSKGG-----AHDPKLIREGEVRAQVKlAFENANGkkyTITRSLA------ILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 115 NVIegphYVlkrsKQEciEQAEQLLDRVGmlnrkdfypaQLSGGQQQ------RVAIARALAMDPEVMLFDEPTSALDPE 188
Cdd:cd03240 96 NVI----FC----HQG--ESNWPLLDMRG----------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEE 155
|
170 180 190
....*....|....*....|....*....|...
gi 490999375 189 LVGEVL-KVMRS-LAEEGRTMLVVTHELGFARH 219
Cdd:cd03240 156 NIEESLaEIIEErKSQKNFQLIVITHDEELVDA 188
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
146-212 |
7.99e-07 |
|
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: 49.31 E-value: 7.99e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 146 NRKDFYPAQLSGGQQQ---RVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTH 212
Cdd:pfam13304 228 GGGELPAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-224 |
9.82e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 9.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 9 LSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVG-GEtiemkhharghrlaanp 87
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNE----------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 88 kqierlrsRLGMVFQSFNLWSHMTVLQNVIEGpHYVLKRSKQE--CI----EQAEQLLDRVGMLNRK----DFYPA---- 153
Cdd:PRK15064 65 --------RLGKLRQDQFAFEEFTVLDTVIMG-HTELWEVKQErdRIyalpEMSEEDGMKVADLEVKfaemDGYTAeara 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 154 -------------------QLSGGQQQRVAIARALAMDPEVMLFDEPTSALDpelvgevLKVMRSLAEE--GR--TMLVV 210
Cdd:PRK15064 136 gelllgvgipeeqhyglmsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------INTIRWLEDVlnERnsTMIII 208
|
250
....*....|....
gi 490999375 211 THElgfaRHVSNRV 224
Cdd:PRK15064 209 SHD----RHFLNSV 218
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
154-217 |
1.01e-06 |
|
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: 47.35 E-value: 1.01e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 154 QLSGGQQQRVAIARALAM-----DPEVmLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFA 217
Cdd:cd03227 77 QLSGGEKELSALALILALaslkpRPLY-ILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELA 144
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
155-214 |
1.61e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.86 E-value: 1.61e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490999375 155 LSGGQQQRVAIARAL---AMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHEL 214
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
24-246 |
2.08e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.25 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVISILGASGSGKSTLL---------------------RCINLLETPDAGVVSVGGETIEMKHHarghR 82
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSIEGLSPAIAIDQK----T 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 83 LAANPkqierlRSRLGMVFQSFN----LWSHMTVLQNViegphyvlkrskqecieqaeQLLDRVGM----LNRKdfyPAQ 154
Cdd:cd03270 87 TSRNP------RSTVGTVTEIYDylrlLFARVGIRERL--------------------GFLVDVGLgyltLSRS---APT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 155 LSGGQQQRVAIARALAMDPEVML--FDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARHvSNRVVfmhqgti 232
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVI------- 209
|
250
....*....|....
gi 490999375 233 dcDGAPEAlfGAHG 246
Cdd:cd03270 210 --DIGPGA--GVHG 219
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
153-213 |
9.10e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 9.10e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999375 153 AQLSGGQQQRVAIARALAmdPEVM----LFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHE 213
Cdd:PRK00635 475 ATLSGGEQERTALAKHLG--AELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD 537
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-235 |
1.05e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhharghRLAanpkqIERLRSRLGMVFQ 102
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS--------KFG-----LMDLRKVLGIIPQ 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 103 S---------FNL---WSHMTV-LQNVIEGPHY--VLKRSKQ----ECIEQAEQLldrvgmlnrkdfypaqlSGGQQQRV 163
Cdd:PLN03130 1321 ApvlfsgtvrFNLdpfNEHNDAdLWESLERAHLkdVIRRNSLgldaEVSEAGENF-----------------SVGQRQLL 1383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999375 164 AIARALAMDPEVMLFDEPTSALDpelVGEVLKVMRSLAEEGR--TMLVVTHELgfarhvsNRVvfmhqgtIDCD 235
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVD---VRTDALIQKTIREEFKscTMLIIAHRL-------NTI-------IDCD 1440
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
37-190 |
2.50e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 37 ISILGASGSGKSTLLRCINLLETPDAGVVSVGGET---IEMKHHARGHRLAANPKQI----------ERLRSRLGMVFQS 103
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVrmaVFSQHHVDGLDLSSNPLLYmmrcfpgvpeQKLRAHLGSFGVT 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 104 FNLwshmtVLQnviegPHYVLkrskqecieqaeqlldrvgmlnrkdfypaqlSGGQQQRVAIARALAMDPEVMLFDEPTS 183
Cdd:PLN03073 618 GNL-----ALQ-----PMYTL-------------------------------SGGQKSRVAFAKITFKKPHILLLDEPSN 656
|
....*..
gi 490999375 184 ALDPELV 190
Cdd:PLN03073 657 HLDLDAV 663
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
155-214 |
2.52e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.40 E-value: 2.52e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490999375 155 LSGGQQQRVAIARALAM---DPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHEL 214
Cdd:COG0178 827 LSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNL 889
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
155-212 |
2.84e-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: 45.12 E-value: 2.84e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 490999375 155 LSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGevlKVMRSLAEEGRTMLVVTH 212
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG---YMYRLCREFGITLFSVSH 637
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
24-212 |
4.07e-05 |
|
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: 44.22 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 24 LKGISIQAQKGDVIsILGASGSGKSTLLRCINLLETPDAGV------------VSVGGETIE----------MKHHARGH 81
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSSRkfdeedfylgddPDLPEIEIEltfgsllsrlLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 82 RLAANPKQIERLRSRLGMVFQSFNlwSHMT-VLQNVIEGPHYVLKRSKQECIEQAEQLldRVGMLNRKDFYPAQLSGGQQ 160
Cdd:COG3593 93 DKEELEEALEELNEELKEALKALN--ELLSeYLKELLDGLDLELELSLDELEDLLKSL--SLRIEDGKELPLDRLGSGFQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490999375 161 QRVAIA--RALAM-----DPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTH 212
Cdd:COG3593 169 RLILLAllSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-187 |
4.62e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.35 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 10 SVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCInlletpdAGV-------VSVGGETIEMKHHAR--G 80
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AGArkiqqgrVEVLGGDMADARHRRavC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 81 HRLAANPKQIERlrsrlgmvfqsfNLWSHMTVLQNV-----IEGphyvlkRSKQECIEQAEQLLDRVGM---LNRkdfyP 152
Cdd:NF033858 76 PRIAYMPQGLGK------------NLYPTLSVFENLdffgrLFG------QDAAERRRRIDELLRATGLapfADR----P 133
|
170 180 190
....*....|....*....|....*....|....*.
gi 490999375 153 A-QLSGGQQQRVAIARALAMDPEVMLFDEPTSALDP 187
Cdd:NF033858 134 AgKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 169
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-233 |
5.29e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 4 PRPVtLSVSDIHKSFGSLDVLKGISIQAQKGDVISILGASGSGKSTLlrcINLLetpdAGVVSVGGETIEMkhhARGHRL 83
Cdd:PRK10636 309 PNPL-LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTL---IKLL----AGELAPVSGEIGL---AKGIKL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 84 AANPK-QIERLRSRlgmvfqsfnlwshmtvlqnviEGPHYVLKRSKQECIEQaeQLLDRVGML----NRKDFYPAQLSGG 158
Cdd:PRK10636 378 GYFAQhQLEFLRAD---------------------ESPLQHLARLAPQELEQ--KLRDYLGGFgfqgDKVTEETRRFSGG 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 159 QQQRVAIARALAMDPEVMLFDEPTSALDpelvgevLKVMRSLAE-----EGrTMLVVTHELGFARHVSNRVVFMHQGTID 233
Cdd:PRK10636 435 EKARLVLALIVWQRPNLLLLDEPTNHLD-------LDMRQALTEalidfEG-ALVVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-210 |
9.46e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 32 QKGDVISILGASGSGKSTLLRcinlletpdagvvSVGGETIEMK-----HHARGHRLAanpkqIERLRSRLGMVFQSFN- 105
Cdd:PRK10938 27 NAGDSWAFVGANGSGKSALAR-------------ALAGELPLLSgerqsQFSHITRLS-----FEQLQKLVSDEWQRNNt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 106 -LWSH------MTVLQNVIEGPHyvlkrSKQECIEQAEQ-----LLDRVGMlnrkdfypaQLSGGQQQRVAIARALAMDP 173
Cdd:PRK10938 89 dMLSPgeddtgRTTAEIIQDEVK-----DPARCEQLAQQfgitaLLDRRFK---------YLSTGETRKTLLCQALMSEP 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 490999375 174 EVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVV 210
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
23-257 |
1.08e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 42.59 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 23 VLKGISIQAQKGDVISILGASGSGKSTL-LRCINLLETPDAGVVSVGGETIEMKHHArghrlaanpkqierLRSRLGMVF 101
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFDGKIVIDGIDISKLPLHT--------------LRSRLSIIL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 102 QSFNLWSHmTVLQNVieGPHYVLKRSK-QECIEQAeQL----------LDRVGMLNRKDFypaqlSGGQQQRVAIARALA 170
Cdd:cd03288 102 QDPILFSG-SIRFNL--DPECKCTDDRlWEALEIA-QLknmvkslpggLDAVVTEGGENF-----SVGQRQLFCLARAFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 171 MDPEVMLFDEPTSALDPELVGEVLK-VMRSLAEegRTMLVVTHELGFARHVSNRVVFMHQGTIDCDGAPEALfgAHGSPR 249
Cdd:cd03288 173 RKSSILIMDEATASIDMATENILQKvVMTAFAD--RTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL--AQEDGV 248
|
....*...
gi 490999375 250 FQQFISSH 257
Cdd:cd03288 249 FASLVRTD 256
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-262 |
1.61e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.04 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 4 PRPVTLSVSDIHKSF--GSLDVLKGISIQAQKGDVISILGASGSGKSTLLRCINLLETPDAGVVSVGGETIEmkhhargh 81
Cdd:PLN03232 1230 PSRGSIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA-------- 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 82 rlaanPKQIERLRSRLGMVFQSFNLWSHmTVLQNVIEGPHY-------VLKRSK-QECIEQAEQLLDRVGMLNRKDFypa 153
Cdd:PLN03232 1302 -----KFGLTDLRRVLSIIPQSPVLFSG-TVRFNIDPFSEHndadlweALERAHiKDVIDRNPFGLDAEVSEGGENF--- 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 154 qlSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRslaEEGR--TMLVVTHELGFARHVsNRVVFMHQGT 231
Cdd:PLN03232 1373 --SVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR---EEFKscTMLVIAHRLNTIIDC-DKILVLSSGQ 1446
|
250 260 270
....*....|....*....|....*....|.
gi 490999375 232 IDCDGAPEALFGAHGSPRFQQFISSHHQPGQ 262
Cdd:PLN03232 1447 VLEYDSPQELLSRDTSAFFRMVHSTGPANAQ 1477
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
39-181 |
1.94e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 41.91 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 39 ILGASGSGKSTLLRCINL-LETPDAGVVSVGGETIEMKHHARG-----------HRL--AANPKQIERLRSRLGMVFQSF 104
Cdd:COG3950 30 LVGENGSGKTTLLEAIALaLSGLLSRLDDVKFRKLLIRNGEFGdsaklilyygtSRLllDGPLKKLERLKEEYFSRLDGY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 105 --------NLWSHMTVLQNVIEGPHYVLKRSKQECIEQAEQLL---------------DRVGMLNRKD---FYPAQLSGG 158
Cdd:COG3950 110 dslldedsNLREFLEWLREYLEDLENKLSDELDEKLEAVREALnkllpdfkdiridrdPGRLVILDKNgeeLPLNQLSDG 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 490999375 159 QQQRVAIARALAMD--------------PEVMLFDEP 181
Cdd:COG3950 190 ERSLLALVGDLARRlaelnpalenplegEGIVLIDEI 226
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
152-220 |
2.68e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 152 PAQLSGGQQQ------RVAIARALA--------MDPevMLFDEPTSALDPELVGEVLKV---MRSLAEEgrTMLVVTH-- 212
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAegiegdapLPP--LILDEPTVFLDSGHVSQLVDLvesMRRLGVE--QIVVVSHdd 854
|
....*....
gi 490999375 213 EL-GFARHV 220
Cdd:PRK02224 855 ELvGAADDL 863
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
155-214 |
4.14e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 4.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490999375 155 LSGGQQQRVAIARAL---AMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHEL 214
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM 872
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
152-214 |
1.52e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 1.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999375 152 PA-QLSGGQQQRVAIARALAMDPE---VMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHEL 214
Cdd:PRK00349 827 PAtTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNL 893
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
154-203 |
1.57e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.78 E-value: 1.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 490999375 154 QLSGGQQQRVAIARALAM---DPEVM-LFDEPTSALDPELVGEVLKVMRSLAEE 203
Cdd:cd03272 158 QLSGGQKSLVALALIFAIqkcDPAPFyLFDEIDAALDAQYRTAVANMIKELSDG 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
134-232 |
3.15e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 38.61 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 134 QAEQLLDRVGMLNRKDFYPAQ-LSGGQQQRVAIARALAMDPEVMLFDEPTSALDPELVGEVLKVMRSLAEegrTMLVVTH 212
Cdd:PRK10636 128 RAASLLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISH 204
|
90 100
....*....|....*....|
gi 490999375 213 ELGFARHVSNRVVFMHQGTI 232
Cdd:PRK10636 205 DRDFLDPIVDKIIHIEQQSL 224
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
129-241 |
5.37e-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: 38.07 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 129 QECIEQAEQLLDrVGM----LNRKdfyPAQLSGGQQQRVAIARALAMDPEVMLF--DEPTSALDPELVGEVLKVMRSLAE 202
Cdd:TIGR00630 463 KEIRERLGFLID-VGLdylsLSRA---AGTLSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRD 538
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 490999375 203 EGRTMLVVTHELGFARHvSNRVVFM------HQGTIDCDGAPEAL 241
Cdd:TIGR00630 539 LGNTLIVVEHDEDTIRA-ADYVIDIgpgageHGGEVVASGTPEEI 582
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
153-219 |
5.98e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 5.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 153 AQLSGGQQQRVAIARALAMDPE---VMLFDEPTSALDPELVGEVLKVMRSLAEEGRTMLVVTHELGFARH 219
Cdd:PRK00635 1698 SSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQ 1767
|
|
| DUF87 |
pfam01935 |
Helicase HerA, central domain; This entry represents the central domain found in archaeal ... |
37-140 |
6.43e-03 |
|
Helicase HerA, central domain; This entry represents the central domain found in archaeal proteins such as DNA double-strand break repair helicase HerA (EC:3.6.4.12). HerA is a helicase which is able to utilize either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding. It forms a complex with NurA nuclease, this complex has the 5'-3' DNA end resection activity and is essential for cell viability in the crenarchaeon Sulfolobus islandicus. This domain includes the the central RecA-like catalytic core and a flanking four-helix bundle. The function of this prokaryotic domain is unknown. It contains several conserved aspartates and histidines that could be metal ligands.
Pssm-ID: 376671 [Multi-domain] Cd Length: 220 Bit Score: 36.96 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999375 37 ISILGASGSGKSTLLRCI--NLLETPDAGVV--SVGGEtiemkHHARGHRLAANPKQIERLRSRLGMVFQSFNLWSHMTV 112
Cdd:pfam01935 26 FAILGSTGSGKSNTVAVLleELLEKKGATVLifDPHGE-----YGTLFRDLGAENVNVITPDPELKINPWLLSPEDLADL 100
|
90 100
....*....|....*....|....*....
gi 490999375 113 LqNVIEGPHY-VLKRSKQECIEQAEQLLD 140
Cdd:pfam01935 101 L-EELNLPNAeVQRSILEEALDQLKSEEL 128
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
22-52 |
8.37e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 37.48 E-value: 8.37e-03
10 20 30
....*....|....*....|....*....|.
gi 490999375 22 DVLKGISIQAQKGDVISILGASGSGKSTLLR 52
Cdd:COG5635 168 ESLKRLELLEAKKKRLLILGEPGSGKTTLLR 198
|
|
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