|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-254 |
2.46e-167 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 461.77 E-value: 2.46e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHghsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyrvdakgvvh 80
Cdd:COG1126 1 MIEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 rLHPKVVARQRRRIGMVFQRFHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRV 160
Cdd:COG1126 67 -DSKKDINKLRRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 161 AIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLD 240
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFE 225
|
250
....*....|....
gi 915259206 241 APREQRTRDFLAHV 254
Cdd:COG1126 226 NPQHERTRAFLSKV 239
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-255 |
7.61e-133 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 375.29 E-value: 7.61e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAKGVVH 80
Cdd:COG4598 8 ALEVRDLHKSFG----DLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARQRRRIGMVFQRFHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRV 160
Cdd:COG4598 84 PADRRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 161 AIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLD 240
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFG 243
|
250
....*....|....*
gi 915259206 241 APREQRTRDFLAHVL 255
Cdd:COG4598 244 NPKSERLRQFLSSSL 258
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-229 |
8.34e-128 |
|
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: 360.69 E-value: 8.34e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHghsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyrvdakgvvhr 81
Cdd:cd03262 1 IEIKNLHKSFGD----FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPKVVARQRRRIGMVFQRFHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVA 161
Cdd:cd03262 66 DDKKNINELRQKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVV 229
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-254 |
1.60e-126 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 358.64 E-value: 1.60e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHghsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrVDAKGvvh 80
Cdd:PRK09493 1 MIEFKNVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG------LKVND--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 rlhPKVVARQ-RRRIGMVFQRFHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQR 159
Cdd:PRK09493 68 ---PKVDERLiRQEAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 160 VAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVL 239
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
250
....*....|....*
gi 915259206 240 DAPREQRTRDFLAHV 254
Cdd:PRK09493 225 KNPPSQRLQEFLQHV 239
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-255 |
1.92e-101 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 298.53 E-value: 1.92e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyrvdakgVVH 80
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGV----------DLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARQRRRIGMVFQRFHLFPHLTATANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRV 160
Cdd:COG1135 71 ALSERELRAARRKIGMIFQHFNLLSSRTVAENV-ALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 161 AIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVL 239
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVF 229
|
250
....*....|....*.
gi 915259206 240 DAPREQRTRDFLAHVL 255
Cdd:COG1135 230 ANPQSELTRRFLPTVL 245
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-255 |
2.99e-95 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 279.71 E-value: 2.99e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFgHGHSavhVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVdGErmgYRVDA----- 75
Cdd:PRK11264 3 AIEVKNLVKKF-HGQT---VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GD---ITIDTarsls 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 76 --KGVVHRLhpkvvarqRRRIGMVFQRFHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLS 153
Cdd:PRK11264 75 qqKGLIRQL--------RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 154 GGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQG 233
Cdd:PRK11264 147 GGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
|
250 260
....*....|....*....|..
gi 915259206 234 PPSEVLDAPREQRTRDFLAHVL 255
Cdd:PRK11264 227 PAKALFADPQQPRTRQFLEKFL 248
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
2-255 |
3.28e-93 |
|
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: 274.78 E-value: 3.28e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHghsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAKGVVHR 81
Cdd:TIGR03005 1 VRFSDVTKRFGI----LTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNGPLVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPKVVARQRRRIGMVFQRFHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVA 161
Cdd:TIGR03005 77 ADEKHLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAA-SGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLD 240
Cdd:TIGR03005 157 IARALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASeHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFR 236
|
250
....*....|....*
gi 915259206 241 APREQRTRDFLAHVL 255
Cdd:TIGR03005 237 QPKEERTREFLSKVI 251
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-232 |
3.10e-92 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 271.15 E-value: 3.10e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVH 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQD----------IS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARQRRR-IGMVFQRFHLFPHLTATANVMeAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQR 159
Cdd:COG1136 74 SLSERELARLRRRhIGFVFQFFNLLPELTALENVA-LPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 160 VAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAA-SGMTMIVVTHEIGFArEVADEVVFMDQGVVVEQ 232
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNReLGTTIVMVTHDPELA-ARADRVIRLRDGRIVSD 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-243 |
4.15e-92 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 270.99 E-value: 4.15e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyrvdakgvvh 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLT---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARQRRRIGMVFQRFHLFPHLTATANVMeAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRV 160
Cdd:cd03258 71 LLSGKELRKARRRIGMIFQHFNLLSSRTVFENVA-LPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 161 AIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVL 239
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
....
gi 915259206 240 DAPR 243
Cdd:cd03258 230 ANPQ 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-255 |
1.12e-90 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 268.38 E-value: 1.12e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 4 LTGIHKEFGHGHsavhVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAKGVVHRLH 83
Cdd:PRK10619 8 VIDLHKRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 84 PKVVARQRRRIGMVFQRFHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGLADRA-DHYPAQLSGGQQQRVAI 162
Cdd:PRK10619 84 KNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 163 ARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAP 242
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
250
....*....|...
gi 915259206 243 REQRTRDFLAHVL 255
Cdd:PRK10619 244 QSPRLQQFLKGSL 256
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-253 |
1.12e-90 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 267.65 E-value: 1.12e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRvdakgvvHR 81
Cdd:COG4161 3 IQLKNINCFYG----SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFS-------QK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPKVVARQRRRIGMVFQRFHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVA 161
Cdd:COG4161 72 PSEKAIRLLRQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGpPSEVLDA 241
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQ 230
|
250
....*....|..
gi 915259206 242 PREQRTRDFLAH 253
Cdd:COG4161 231 PQTEAFAHYLSH 242
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-253 |
5.63e-90 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 266.11 E-value: 5.63e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAKgvvhr 81
Cdd:PRK11124 3 IQLNGINCFYG----AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPS----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 lhPKVVARQRRRIGMVFQRFHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVA 161
Cdd:PRK11124 74 --DKAIRELRRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEvLDA 241
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQ 230
|
250
....*....|..
gi 915259206 242 PREQRTRDFLAH 253
Cdd:PRK11124 231 PQTEAFKNYLSH 242
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-229 |
3.12e-87 |
|
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: 258.19 E-value: 3.12e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyrvdakgVVHR 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGT----------DISK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPKVVARQRRR-IGMVFQRFHLFPHLTATANVMeAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRV 160
Cdd:cd03255 71 LSEKELAAFRRRhIGFVFQSFNLLPDLTALENVE-LPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 161 AIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAA-SGMTMIVVTHEIGFAREvADEVVFMDQGVV 229
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-251 |
5.94e-85 |
|
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: 252.98 E-value: 5.94e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVH 80
Cdd:COG1127 5 MIEVRNLTKSFG----DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQD----------IT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARQRRRIGMVFQRFHLFPHLTATANVMeAPMRVRG-LSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQR 159
Cdd:COG1127 71 GLSEKELYELRRRIGMLFQGGALFDSLTVFENVA-FPLREHTdLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 160 VAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEV 238
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELrDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
250
....*....|...
gi 915259206 239 LDAPrEQRTRDFL 251
Cdd:COG1127 230 LASD-DPWVRQFL 241
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-251 |
5.31e-83 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 251.94 E-value: 5.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyrvdakgVVH 80
Cdd:COG3842 5 ALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR----------DVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPkvvarQRRRIGMVFQRFHLFPHLTATANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRV 160
Cdd:COG3842 71 GLPP-----EKRNVGMVFQDYALFPHLTVAENV-AFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 161 AIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVL 239
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIY 224
|
250
....*....|..
gi 915259206 240 DAPREQRTRDFL 251
Cdd:COG3842 225 ERPATRFVADFI 236
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-255 |
3.78e-82 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 249.72 E-value: 3.78e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyrvdakgvvh 80
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLT---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARQRRRIGMVFQRFHLFPHLTATANVmeA-PMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQR 159
Cdd:PRK11153 71 ALSEKELRKARRQIGMIFQHFNLLSSRTVFDNV--AlPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 160 VAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEV 238
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
250
....*....|....*..
gi 915259206 239 LDAPREQRTRDFLAHVL 255
Cdd:PRK11153 229 FSHPKHPLTREFIQSTL 245
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-254 |
1.11e-79 |
|
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: 248.66 E-value: 1.11e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFG-HGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvV 79
Cdd:COG1123 260 LLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKD----------L 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 80 HRLHPKVVARQRRRIGMVFQR-FH-LFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGL-ADRADHYPAQLSGGQ 156
Cdd:COG1123 330 TKLSRRSLRELRRRVQMVFQDpYSsLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 157 QQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPP 235
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
250
....*....|....*....
gi 915259206 236 SEVLDAPREQRTRDFLAHV 254
Cdd:COG1123 490 EEVFANPQHPYTRALLAAV 508
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-249 |
1.34e-79 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 240.38 E-value: 1.34e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvvh 80
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 rlhpkvVARQRRRIGMVFQRFHLFPHLTATANVMeAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRV 160
Cdd:COG1116 75 ------VTGPGPDRGVVFQEPALLPWLTVLDNVA-LGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 161 AIARALAMDPELMLFDEPTSALDP----ELVGEVLAVmkdLAASGMTMIVVTHEIgfarevaDEVVFMDQGVVVEQGPPS 236
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTHDV-------DEAVFLADRVVVLSARPG 217
|
250 260
....*....|....*....|
gi 915259206 237 EV-------LDAPREQRTRD 249
Cdd:COG1116 218 RIveeidvdLPRPRDRELRT 237
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-238 |
2.27e-78 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 236.49 E-value: 2.27e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGhsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyrvdakgvvh 80
Cdd:COG3638 2 MLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVT---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARQRRRIGMVFQRFHLFPHLTATANV-------MEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLS 153
Cdd:COG3638 69 ALRGRALRRLRRRIGMIFQQFNLVPRLSVLTNVlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 154 GGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQ 232
Cdd:COG3638 149 GGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFD 228
|
....*.
gi 915259206 233 GPPSEV 238
Cdd:COG3638 229 GPPAEL 234
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
19-252 |
1.07e-77 |
|
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: 234.88 E-value: 1.07e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 19 HVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDIT-----AGSVVVDGERM-GYRVDakgvvhrlhpkvVARQRR 92
Cdd:TIGR00972 15 EALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVpgvriEGKVLFDGQDIyDKKID------------VVELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 93 RIGMVFQRFHLFPhLTATANVMEAPmRVRGL-SKADARTQALDLLRRVGL----ADRADHYPAQLSGGQQQRVAIARALA 167
Cdd:TIGR00972 83 RVGMVFQKPNPFP-MSIYDNIAYGP-RLHGIkDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 168 MDPELMLFDEPTSALDPELVGEVLAVMKDLAASgMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPREQRT 247
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRT 239
|
....*
gi 915259206 248 RDFLA 252
Cdd:TIGR00972 240 EDYIS 244
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-237 |
1.33e-77 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 233.79 E-value: 1.33e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHsavHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVH 80
Cdd:COG2884 1 MIRFENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQD----------LS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARQRRRIGMVFQRFHLFPHLTATANVMeAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRV 160
Cdd:COG2884 68 RLKRREIPYLRRRIGVVFQDFRLLPDRTVYENVA-LPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 161 AIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSE 237
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-233 |
1.64e-76 |
|
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: 230.87 E-value: 1.64e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHR 81
Cdd:cd03259 1 LELKGLSKTYG----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRD----------VTG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPkvvarQRRRIGMVFQRFHLFPHLTATANVmeA-PMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRV 160
Cdd:cd03259 67 VPP-----ERRNIGMVFQDYALFPHLTVAENI--AfGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 161 AIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQG 233
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-243 |
1.32e-75 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 233.04 E-value: 1.32e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVH 80
Cdd:COG3839 3 SLELENVSKSYG----GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD----------VT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKvvarqRRRIGMVFQRFHLFPHLTATANvMEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRV 160
Cdd:COG3839 69 DLPPK-----DRNIAMVFQSYALYPHMTVYEN-IAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 161 AIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVL 239
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELY 222
|
....
gi 915259206 240 DAPR 243
Cdd:COG3839 223 DRPA 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-250 |
8.66e-75 |
|
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: 8.66e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHGHsavhVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHR 81
Cdd:cd03261 1 IELRGLTKSFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGED----------ISG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPKVVARQRRRIGMVFQRFHLFPHLTATANVMeAPMRVRG-LSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRV 160
Cdd:cd03261 67 LSEAELYRLRRRMGMLFQSGALFDSLTVFENVA-FPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 161 AIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVL 239
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
250
....*....|.
gi 915259206 240 DAPrEQRTRDF 250
Cdd:cd03261 226 ASD-DPLVRQF 235
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-251 |
1.08e-74 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 230.80 E-value: 1.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAkgvvhr 81
Cdd:COG1118 3 IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPP------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 lhpkvvarQRRRIGMVFQRFHLFPHLTATANVMEApMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVA 161
Cdd:COG1118 73 --------RERRVGFVFQHYALFPHMTVAENIAFG-LRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 162 IARALAMDPELMLFDEPTSALD----PELVGEVLAVMKDLaasGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSE 237
Cdd:COG1118 144 LARALAVEPEVLLLDEPFGALDakvrKELRRWLRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDE 220
|
250
....*....|....
gi 915259206 238 VLDAPREQRTRDFL 251
Cdd:COG1118 221 VYDRPATPFVARFL 234
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-240 |
2.97e-73 |
|
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: 222.73 E-value: 2.97e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvvhr 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 lhpkvVARQRRRIGMVFQRFHLFPHLTATANVMeAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVA 161
Cdd:cd03293 68 -----VTGPGPDRGYVFQQDALLPWLTVLDNVA-LGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 162 IARALAMDPELMLFDEPTSALDP---ELVGEVLavMKDLAASGMTMIVVTHEIgfarevaDEVVFMDQGVVVEQGPPSEV 238
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDAltrEQLQEEL--LDIWRETGKTVLLVTHDI-------DEAVFLADRVVVLSARPGRI 212
|
..
gi 915259206 239 LD 240
Cdd:cd03293 213 VA 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-241 |
9.91e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 221.86 E-value: 9.91e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHghsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHR 81
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGED----------VAR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPKVvarqRRRIGMVFQRFHLFPHLTATANVMEApMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVA 161
Cdd:COG1131 67 DPAEV----RRRIGYVPQEPALYPDLTVRENLRFF-ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDA 241
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-252 |
1.64e-72 |
|
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: 221.60 E-value: 1.64e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAkgvvh 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 rlhpkvvaRQRRRIGMVFQ----RFHlfPHLTATANVMEaPMRVRGLSKADARtqALDLLRRVGLADR-ADHYPAQLSGG 155
Cdd:COG1124 76 --------AFRRRVQMVFQdpyaSLH--PRHTVDRILAE-PLRIHGLPDREER--IAELLEQVGLPPSfLDRYPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 156 QQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGP 234
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELT 222
|
250
....*....|....*...
gi 915259206 235 PSEVLDAPREQRTRDFLA 252
Cdd:COG1124 223 VADLLAGPKHPYTRELLA 240
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-246 |
3.55e-72 |
|
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: 220.52 E-value: 3.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 3 ELTGIHKEFGHGhsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHRL 82
Cdd:cd03256 2 EVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTD----------INKL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 83 HPKVVARQRRRIGMVFQRFHLFPHLTATANVMEA------PMRV--RGLSKADaRTQALDLLRRVGLADRADHYPAQLSG 154
Cdd:cd03256 69 KGKALRQLRRQIGMIFQQFNLIERLSVLENVLSGrlgrrsTWRSlfGLFPKEE-KQRALAALERVGLLDKAYQRADQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 155 GQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQG 233
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDG 227
|
250
....*....|...
gi 915259206 234 PPSEvLDAPREQR 246
Cdd:cd03256 228 PPAE-LTDEVLDE 239
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
18-244 |
2.06e-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: 218.36 E-value: 2.06e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 18 VHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvvhrLHPKVVARQRRRIGMV 97
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKD-------------ITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 98 FQrfhlFP-----HLTATANVMEAPMRvRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPEL 172
Cdd:COG1122 81 FQ----NPddqlfAPTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 915259206 173 MLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPRE 244
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-233 |
8.33e-71 |
|
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: 216.60 E-value: 8.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyrvdakgVVH 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGK----------DLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARQRRRIGMVFQ--RFHLFPHLTATANVMEAPMRVRGLSKADAR-TQALDLLRRVGL-ADRADHYPAQLSGGQ 156
Cdd:cd03257 71 KLSRRLRKIRRKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARkEAVLLLLVGVGLpEEVLNRYPHELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 915259206 157 QQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQG 233
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-251 |
8.60e-70 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 216.88 E-value: 8.60e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAVhvlRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyrvDAKGV-V 79
Cdd:COG1125 1 MIEFENVTKRYPDGTVAV---DDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGE------DIRDLdP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 80 HRLhpkvvarqRRRIGMVFQRFHLFPHLTATANVMEAPmRVRGLSKADARTQALDLLRRVGL--ADRADHYPAQLSGGQQ 157
Cdd:COG1125 72 VEL--------RRRIGYVIQQIGLFPHMTVAENIATVP-RLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 158 QRVAIARALAMDPELMLFDEPTSALDP----ELVGEVLAVMKDLaasGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQG 233
Cdd:COG1125 143 QRVGVARALAADPPILLMDEPFGALDPitreQLQDELLRLQREL---GKTIVFVTHDIDEALKLGDRIAVMREGRIVQYD 219
|
250
....*....|....*...
gi 915259206 234 PPSEVLDAPREQRTRDFL 251
Cdd:COG1125 220 TPEEILANPANDFVADFV 237
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-227 |
1.51e-67 |
|
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: 206.65 E-value: 1.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHghsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvvHR 81
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGED-----------LT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPKVVARQRRRIGMVFQRFHLFPHLTATANVMEApmrvrglskadartqaldllrrvgladradhypaqLSGGQQQRVA 161
Cdd:cd03229 66 DLEDELPPLRRRIGMVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAA-SGMTMIVVTHEIGFAREVADEVVFMDQG 227
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-241 |
1.35e-66 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 206.38 E-value: 1.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHsavHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyrvDAKGvvh 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDIT---KLRG--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 rlhpKVVARQRRRIGMVFQRFHLFPHLTATANVMEA--------PMRVRGLSKADaRTQALDLLRRVGLADRADHYPAQL 152
Cdd:TIGR02315 72 ----KKLRKLRRRIGMIFQHYNLIERLTVLENVLHGrlgykptwRSLLGRFSEED-KERALSALERVGLADKAYQRADQL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 153 SGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVE 231
Cdd:TIGR02315 147 SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVF 226
|
250
....*....|
gi 915259206 232 QGPPSEVLDA 241
Cdd:TIGR02315 227 DGAPSELDDE 236
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-251 |
4.15e-66 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 205.66 E-value: 4.15e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 19 HVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCIN---ELEDI--TAGSVVVDGERMgyrvdakgvvhrLHPKV-VARQRR 92
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNrmnDLIPGarVEGEILLDGEDI------------YDPDVdVVELRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 93 RIGMVFQRFHLFPHlTATANVmEAPMRVRGL---SKADARTQalDLLRRVGL----ADRADHYPAQLSGGQQQRVAIARA 165
Cdd:COG1117 93 RVGMVFQKPNPFPK-SIYDNV-AYGLRLHGIkskSELDEIVE--ESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 166 LAMDPELMLFDEPTSALDP-------ELvgevlavMKDLAASgMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEV 238
Cdd:COG1117 169 LAVEPEVLLMDEPTSALDPistakieEL-------ILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
250
....*....|...
gi 915259206 239 LDAPREQRTRDFL 251
Cdd:COG1117 241 FTNPKDKRTEDYI 253
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-237 |
9.90e-66 |
|
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: 203.82 E-value: 9.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgyrvdakgvvH 80
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL----------F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARQRRR-IGMVFQRFHLFPHLTATANVMeAPMRVRGlsKADARTQALDLLRRVGLADRADHYPAQLSGGQQQR 159
Cdd:COG4181 78 ALDEDARARLRARhVGFVFQSFQLLPTLTALENVM-LPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 915259206 160 VAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREvADEVVFMDQGVVVEQGPPSE 237
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-227 |
2.67e-65 |
|
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: 201.93 E-value: 2.67e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 11 FGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvvhrLHPKVVARQ 90
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKD-------------LTKLSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 91 RRRIGMVFQR-FHLFPHLTATANVMEAPmRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMD 169
Cdd:cd03225 74 RRKVGLVFQNpDDQFFGPTVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 915259206 170 PELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQG 227
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-254 |
3.55e-65 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 203.64 E-value: 3.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyRVDAKgvvhrlhpKVVARQRRRIGMVFQR 100
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA-AMSRK--------ELRELRRKKISMVFQS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 101 FHLFPHLTATANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPTS 180
Cdd:cd03294 111 FALLPHRTVLENV-AFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 915259206 181 ALDP----ELVGEVLAVMKDLaasGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPREQRTRDFLAHV 254
Cdd:cd03294 190 ALDPlirrEMQDELLRLQAEL---QKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGV 264
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-254 |
3.84e-65 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 207.26 E-value: 3.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 7 IHKEFGHghsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyRVDAKgvvhRLhpkv 86
Cdd:COG4175 33 ILEKTGQ----TVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDIT-KLSKK----EL---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 87 vaRQ--RRRIGMVFQRFHLFPHLTATANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIAR 164
Cdd:COG4175 100 --RElrRKKMSMVFQHFALLPHRTVLENV-AFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLAR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 165 ALAMDPELMLFDEPTSALDP----ELVGEVLAVMKDLaasGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLD 240
Cdd:COG4175 177 ALATDPDILLMDEAFSALDPlirrEMQDELLELQAKL---KKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILT 253
|
250
....*....|....
gi 915259206 241 APREQRTRDFLAHV 254
Cdd:COG4175 254 NPANDYVADFVEDV 267
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-243 |
1.56e-64 |
|
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: 203.75 E-value: 1.56e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELED---ITAGSVVVDGERmgyrvdakg 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGED--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 78 vVHRLHPKVVARQR-RRIGMVFQ----RFHlfPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGL---ADRADHYP 149
Cdd:COG0444 72 -LLKLSEKELRKIRgREIQMIFQdpmtSLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 150 AQLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGV 228
Cdd:COG0444 149 HELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGR 228
|
250
....*....|....*
gi 915259206 229 VVEQGPPSEVLDAPR 243
Cdd:COG0444 229 IVEEGPVEELFENPR 243
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-238 |
4.18e-64 |
|
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: 199.71 E-value: 4.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGsVVVDGERmgyRVDAKGVVHR 81
Cdd:cd03260 1 IELRDLNVYYG----DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPG-APDEGEV---LLDGKDIYDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 lhPKVVARQRRRIGMVFQRFHLFPhLTATANVmEAPMRVRG-LSKADARTQALDLLRRVGL----ADRADhyPAQLSGGQ 156
Cdd:cd03260 73 --DVDVLELRRRVGMVFQKPNPFP-GSIYDNV-AYGLRLHGiKLKEELDERVEEALRKAALwdevKDRLH--ALGLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 157 QQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASgMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPS 236
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
|
..
gi 915259206 237 EV 238
Cdd:cd03260 226 QI 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-251 |
7.42e-64 |
|
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: 199.00 E-value: 7.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHGHsavhVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgyrvdakgvvHR 81
Cdd:cd03300 1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI----------TN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPkvvarQRRRIGMVFQRFHLFPHLTATANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVA 161
Cdd:cd03300 67 LPP-----HKRPVNTVFQNYALFPHLTVFENI-AFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLD 240
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
250
....*....|.
gi 915259206 241 APREQRTRDFL 251
Cdd:cd03300 221 EPANRFVADFI 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-244 |
2.56e-62 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 203.60 E-value: 2.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGhsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITA---GSVVVDGErmgyrvDAKG 77
Cdd:COG1123 4 LLEVRDLSVRYPGG--DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGR------DLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 78 VVHRLHpkvvarqRRRIGMVFQRF--HLFPhLTATANVMEAPmRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGG 155
Cdd:COG1123 76 LSEALR-------GRRIGMVFQDPmtQLNP-VTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 156 QQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAA-SGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGP 234
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
250
....*....|
gi 915259206 235 PSEVLDAPRE 244
Cdd:COG1123 227 PEEILAAPQA 236
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-251 |
2.65e-61 |
|
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: 192.90 E-value: 2.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHGHSAVhvlRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHR 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAV---NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGED----------IRE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPkvvARQRRRIGMVFQRFHLFPHLTATANVMEAPmRVRGLSKADARTQALDLLRRVGL--ADRADHYPAQLSGGQQQR 159
Cdd:cd03295 68 QDP---VELRRKIGYVIQQIGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 160 VAIARALAMDPELMLFDEPTSALDP----ELVGEVLAVMKDLaasGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPP 235
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALDPitrdQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
|
250
....*....|....*.
gi 915259206 236 SEVLDAPREQRTRDFL 251
Cdd:cd03295 221 DEILRSPANDFVAEFV 236
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-227 |
2.70e-61 |
|
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: 192.08 E-value: 2.70e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAvhvLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVH 80
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAA---LHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGED----------VN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARQRRRIGMVFQRFHLFPHLTATANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRV 160
Cdd:TIGR02673 68 RLRGRQLPLLRRRIGVVFQDFRLLPDRTVYENV-ALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 161 AIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQG 227
Cdd:TIGR02673 147 AIARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-243 |
5.84e-61 |
|
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: 192.57 E-value: 5.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHkeFGHGHsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVH 80
Cdd:COG1120 1 MLEAENLS--VGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRD----------LA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARqrrRIGMVFQRFHLFPHLTATANVMeapM-------RVRGLSKADaRTQALDLLRRVGLADRADHYPAQLS 153
Cdd:COG1120 67 SLSRRELAR---RIAYVPQEPPAPFGLTVRELVA---LgryphlgLFGRPSAED-REAVEEALERTGLEHLADRPVDELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 154 GGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQ 232
Cdd:COG1120 140 GGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
250
....*....|.
gi 915259206 233 GPPSEVLDAPR 243
Cdd:COG1120 220 GPPEEVLTPEL 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-243 |
1.44e-60 |
|
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: 190.73 E-value: 1.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 3 ELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHRL 82
Cdd:cd03219 2 EVRGLTKRFG----GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGED----------ITGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 83 HPKVVARqrRRIGMVFQRFHLFPHLTATANVMEAPMRVRGLS---------KADARTQALDLLRRVGLADRADHYPAQLS 153
Cdd:cd03219 68 PPHEIAR--LGIGRTFQIPRLFPELTVLENVMVAAQARTGSGlllararreEREARERAEELLERVGLADLADRPAGELS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 154 GGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQG 233
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEG 225
|
250
....*....|
gi 915259206 234 PPSEVLDAPR 243
Cdd:cd03219 226 TPDEVRNNPR 235
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-255 |
3.17e-60 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 190.30 E-value: 3.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHkeFGHGHsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvvh 80
Cdd:COG1121 6 AIELENLT--VSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 rlhpkvVARQRRRIGMVFQRFHLFPHLTATanVME-------APMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLS 153
Cdd:COG1121 70 ------PRRARRRIGYVPQRAEVDWDFPIT--VRDvvlmgryGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 154 GGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEqG 233
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-G 220
|
250 260
....*....|....*....|..
gi 915259206 234 PPSEVLDAPREQRTRDFLAHVL 255
Cdd:COG1121 221 PPEEVLTPENLSRAYGGPVALL 242
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-251 |
3.39e-60 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 189.97 E-value: 3.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHsavhvLRgVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyrvdakgvvh 80
Cdd:COG3840 1 MLRLDDLTYRYGDFP-----LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPkvvarQRRRIGMVFQRFHLFPHLTATANV---MEAPMRvrgLSKADaRTQALDLLRRVGLADRADHYPAQLSGGQQ 157
Cdd:COG3840 65 ALPP-----AERPVSMLFQENNLFPHLTVAQNIglgLRPGLK---LTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 158 QRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPS 236
Cdd:COG3840 136 QRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTA 215
|
250
....*....|....*
gi 915259206 237 EVLDAPREQRTRDFL 251
Cdd:COG3840 216 ALLDGEPPPALAAYL 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-243 |
2.42e-59 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 188.32 E-value: 2.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVH 80
Cdd:COG0411 4 LLEVRGLTKRFG----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRD----------IT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPkvvaRQRRRIGMV--FQRFHLFPHLTATANVMEAPMRVRGLS--------------KADARTQALDLLRRVGLADR 144
Cdd:COG0411 70 GLPP----HRIARLGIArtFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreEREARERAEELLERVGLADR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 145 ADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAA-SGMTMIVVTHEIGFAREVADEVVF 223
Cdd:COG0411 146 ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVV 225
|
250 260
....*....|....*....|
gi 915259206 224 MDQGVVVEQGPPSEVLDAPR 243
Cdd:COG0411 226 LDFGRVIAEGTPAEVRADPR 245
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-255 |
6.37e-59 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 186.99 E-value: 6.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHghsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyrvdakgVVH 80
Cdd:COG4555 1 MIEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE----------DVR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVvarqRRRIGMVFQRFHLFPHLTATANV-MEApmRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQR 159
Cdd:COG4555 67 KEPREA----RRQIGVLPDERGLYDRLTVRENIrYFA--ELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 160 VAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVL 239
Cdd:COG4555 141 VALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
250
....*....|....*.
gi 915259206 240 DAPREQRTRDFLAHVL 255
Cdd:COG4555 221 EEIGEENLEDAFVALI 236
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
3-250 |
1.63e-58 |
|
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: 189.48 E-value: 1.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 3 ELTGIHKEFGHgHSAvhvLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyrvdakgVVHRL 82
Cdd:TIGR03265 6 SIDNIRKRFGA-FTA---LKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGR----------DITRL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 83 HPkvvarQRRRIGMVFQRFHLFPHLTATANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAI 162
Cdd:TIGR03265 72 PP-----QKRDYGIVFQSYALFPNLTVADNI-AYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 163 ARALAMDPELMLFDEPTSALDPE----LVGEVLAVMKDLaasGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEV 238
Cdd:TIGR03265 146 ARALATSPGLLLLDEPLSALDARvrehLRTEIRQLQRRL---GVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEI 222
|
250
....*....|..
gi 915259206 239 LDAPREQRTRDF 250
Cdd:TIGR03265 223 YRHPATPFVADF 234
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-243 |
4.28e-58 |
|
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: 184.85 E-value: 4.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHR 81
Cdd:cd03296 3 IEVRNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGED----------ATD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPkvvarQRRRIGMVFQRFHLFPHLTATANV---MEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQ 158
Cdd:cd03296 69 VPV-----QERNVGFVFQHYALFRHMTVFDNVafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 159 RVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSE 237
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
....*.
gi 915259206 238 VLDAPR 243
Cdd:cd03296 224 VYDHPA 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-240 |
5.75e-56 |
|
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: 178.78 E-value: 5.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 14 GHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHRLHPkvVARQRRR 93
Cdd:cd03224 9 GYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRD----------ITGLPP--HERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 94 IGMVFQRFHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRvgLADRADHYPAQLSGGQQQRVAIARALAMDPELM 173
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 174 LFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLD 240
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-233 |
9.43e-56 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 177.83 E-value: 9.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYrvdakgvvhr 81
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPKvvarqRRRIGMVFQRFHLFPHLTATANvMEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVA 161
Cdd:cd03301 67 LPPK-----DRDIAMVFQNYALYPHMTVYDN-IAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQG 233
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-242 |
6.34e-55 |
|
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: 180.30 E-value: 6.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 24 VDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgyrVDAKGVVHrlhpkvVARQRRRIGMVFQRFHL 103
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL---QDSARGIF------LPPHRRRIGYVFQEARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 104 FPHLTATANVMEAPMRVRGLSKADARTQALDLLrrvGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPTSALD 183
Cdd:COG4148 89 FPHLSVRGNLLYGRKRAPRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 184 PELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAP 242
Cdd:COG4148 166 LARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-253 |
3.94e-54 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 177.99 E-value: 3.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGhghSAVhVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyrvdakGVVHR 81
Cdd:PRK11432 7 VVLKNITKRFG---SNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE---------DVTHR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 lhpkvvARQRRRIGMVFQRFHLFPHLTATANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVA 161
Cdd:PRK11432 74 ------SIQQRDICMVFQSYALFPHMSLGENV-GYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLD 240
Cdd:PRK11432 147 LARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
250
....*....|...
gi 915259206 241 APREQrtrdFLAH 253
Cdd:PRK11432 227 QPASR----FMAS 235
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
24-254 |
6.01e-54 |
|
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: 177.74 E-value: 6.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 24 VDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAKgvvhrlhpkVVARQRRRIGMVFQRFHL 103
Cdd:TIGR01186 12 ADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVE---------LREVRRKKIGMVFQQFAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 104 FPHLTATANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPTSALD 183
Cdd:TIGR01186 83 FPHMTILQNT-SLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 915259206 184 PELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPREQRTRDFLAHV 254
Cdd:TIGR01186 162 PLIRDSMQDELKKLQATlQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-252 |
8.92e-54 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 181.42 E-value: 8.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 11 FGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKS----TLLRCINELEDITAGSVVVDGERMGyrvdakgvvhRLHPKV 86
Cdd:COG4172 16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLL----------GLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 87 VARQR-RRIGMVFQR--FHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGLAD---RADHYPAQLSGGQQQRV 160
Cdd:COG4172 86 LRRIRgNRIAMIFQEpmTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 161 AIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVL 239
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELF 245
|
250
....*....|...
gi 915259206 240 DAPREQRTRDFLA 252
Cdd:COG4172 246 AAPQHPYTRKLLA 258
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-246 |
1.97e-53 |
|
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: 172.47 E-value: 1.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHkeFGHGHSavHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVH 80
Cdd:COG0410 3 MLEVENLH--AGYGGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED----------IT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARqrRRIGMVFQRFHLFPHLTATANvMEAPMRVRGLSKADART--QALDLLRRvgLADRADHYPAQLSGGQQQ 158
Cdd:COG0410 69 GLPPHRIAR--LGIGYVPEGRRIFPSLTVEEN-LLLGAYARRDRAEVRADleRVYELFPR--LKERRRQRAGTLSGGEQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 159 RVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEV 238
Cdd:COG0410 144 MLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
....*...
gi 915259206 239 LDAPREQR 246
Cdd:COG0410 224 LADPEVRE 231
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
20-227 |
2.70e-53 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 171.83 E-value: 2.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgVVHRLHPKVVARQRRRIGMVFQ 99
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKE---------VTNLSYSQKIILRRELIGYIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPHLTATANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPT 179
Cdd:NF038007 91 SFNLIPHLSIFDNV-ALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 915259206 180 SALDPELVGEVLAVMKDLAASGMTMIVVTHEIGfAREVADEVVFMDQG 227
Cdd:NF038007 170 GNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDG 216
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-244 |
4.43e-53 |
|
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: 173.02 E-value: 4.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 17 AVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgYRVDAKGvvhrlhPKVVARQRRRIGM 96
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDG----RDITAKK------KKKLKDLRKKVGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 97 VFQrfhlFPH-----LTATANVMEAPMRVrGLSKADARTQALDLLRRVGL-ADRADHYPAQLSGGQQQRVAIARALAMDP 170
Cdd:TIGR04521 87 VFQ----FPEhqlfeETVYKDIAFGPKNL-GLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 915259206 171 ELMLFDEPTSALDPELVGEVLAVMKDLA-ASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPRE 244
Cdd:TIGR04521 162 EVLILDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDE 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-252 |
8.95e-53 |
|
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: 178.72 E-value: 8.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 11 FGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDiTAGSVVVDGERmgyrvdakgvVHRLHPKVVARQ 90
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQD----------LDGLSRRALRPL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 91 RRRIGMVFQR-F-HLFPHLTATANVMEaPMRV--RGLSKADARTQALDLLRRVGL-ADRADHYPAQLSGGQQQRVAIARA 165
Cdd:COG4172 361 RRRMQVVFQDpFgSLSPRMTVGQIIAE-GLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 166 LAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPRE 244
Cdd:COG4172 440 LILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQH 519
|
....*...
gi 915259206 245 QRTRDFLA 252
Cdd:COG4172 520 PYTRALLA 527
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-209 |
1.26e-52 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 169.90 E-value: 1.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHGHSAVHvlrGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHR 81
Cdd:cd03292 1 IEFINVTKTYPNGTAALD---GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQD----------VSD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPKVVARQRRRIGMVFQRFHLFPHLTATANVMeAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVA 161
Cdd:cd03292 68 LRGRAIPYLRRKIGVVFQDFRLLPDRNVYENVA-FALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTH 209
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
6-231 |
3.02e-52 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 169.07 E-value: 3.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 6 GIHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgyrvdakgvvHRLHPK 85
Cdd:TIGR02211 6 NLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSL----------SKLSSN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 86 VVARQR-RRIGMVFQRFHLFPHLTATANVMeAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIAR 164
Cdd:TIGR02211 76 ERAKLRnKKLGFIYQFHHLLPDFTALENVA-MPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 915259206 165 ALAMDPELMLFDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREvADEVVFMDQGVVVE 231
Cdd:TIGR02211 155 ALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELnRELNTSFLVVTHDLELAKK-LDRVLEMKDGQLFN 221
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
11-243 |
4.27e-52 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 172.22 E-value: 4.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 11 FGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHRLHPKVVARQ 90
Cdd:COG4608 24 FGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD----------ITGLSGRELRPL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 91 RRRIGMVFQRFH--LFPHLTATANVMEaPMRVRGL-SKADARTQALDLLRRVGL-ADRADHYPAQLSGGQQQRVAIARAL 166
Cdd:COG4608 94 RRRMQMVFQDPYasLNPRMTVGDIIAE-PLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARAL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 915259206 167 AMDPELMLFDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPR 243
Cdd:COG4608 173 ALNPKLIVCDEPVSALDVSIQAQVLNLLEDLqDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-254 |
6.19e-52 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 172.58 E-value: 6.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHghsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHR 81
Cdd:PRK10851 3 IEIANIKKSFGR----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTD----------VSR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHpkvvARQRRrIGMVFQRFHLFPHLTATANVMEA----PMRVRgLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQ 157
Cdd:PRK10851 69 LH----ARDRK-VGFVFQHYALFRHMTVFDNIAFGltvlPRRER-PNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 158 QRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPS 236
Cdd:PRK10851 143 QRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
250
....*....|....*...
gi 915259206 237 EVLDAPREQRTRDFLAHV 254
Cdd:PRK10851 223 QVWREPATRFVLEFMGEV 240
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-239 |
1.21e-51 |
|
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: 169.15 E-value: 1.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 16 SAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrvdakgvVHRLHPKVVARQRRRIG 95
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG------------LDTLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 96 MVFQRfhlfP--HLTAT------ANVMEApmrvRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALA 167
Cdd:TIGR04520 81 MVFQN----PdnQFVGAtveddvAFGLEN----LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 915259206 168 MDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREvADEVVFMDQGVVVEQGPPSEVL 239
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIF 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-238 |
2.34e-51 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 174.44 E-value: 2.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVH 80
Cdd:COG1129 4 LLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEP----------VR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKvvARQRRRIGMVFQRFHLFPHLTATANVM--EAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQ 158
Cdd:COG1129 70 FRSPR--DAQAAGIAIIHQELNLVPNLSVAENIFlgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 159 RVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTH---EIgfaREVADEVVFMDQGVVVEQGPP 235
Cdd:COG1129 148 LVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHrldEV---FEIADRVTVLRDGRLVGTGPV 224
|
...
gi 915259206 236 SEV 238
Cdd:COG1129 225 AEL 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-242 |
8.08e-51 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 170.13 E-value: 8.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHGHsavhVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyRVDAkgvvhr 81
Cdd:PRK09452 15 VELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-HVPA------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 lhpkvvarQRRRIGMVFQRFHLFPHLTATANVMEApMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVA 161
Cdd:PRK09452 84 --------ENRHVNTVFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLD 240
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYE 234
|
..
gi 915259206 241 AP 242
Cdd:PRK09452 235 EP 236
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-235 |
9.65e-51 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 175.30 E-value: 9.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSvvvdgermgYRVDAKGVVh 80
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGT---------YRVAGQDVA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARQRRR-IGMVFQRFHLFPHLTATANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQR 159
Cdd:PRK10535 74 TLDADALAQLRREhFGFIFQRYHLLSHLTAAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 915259206 160 VAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREvADEVVFMDQGVVVEQGPP 235
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPA 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-229 |
1.26e-50 |
|
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: 163.34 E-value: 1.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHGHsavhVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyrvdakgvvhr 81
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 lhpKVVARQRRRIGMVFQRFHLFPHLTATANVmeapmrvrglskadartqaldllrrvgladradhypaQLSGGQQQRVA 161
Cdd:cd03230 66 ---KEPEEVKRRIGYLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVV 229
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-229 |
4.18e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 163.06 E-value: 4.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 3 ELTGIHKEFGHGHsavhVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgyrvdAKGVVHRL 82
Cdd:COG4619 2 ELEGLSFRVGGKP----ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-----SAMPPPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 83 hpkvvarqRRRIGMVFQRFHLFPHlTATANvMEAPMRVRGlsKADARTQALDLLRRVGLADRADHYPA-QLSGGQQQRVA 161
Cdd:COG4619 73 --------RRQVAYVPQEPALWGG-TVRDN-LPFPFQLRE--RKFDRERALELLERLGLPPDILDKPVeRLSGGERQRLA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVV 229
Cdd:COG4619 141 LIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-229 |
2.32e-49 |
|
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: 161.55 E-value: 2.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 19 HVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvvhrlhpkvVARQRRRIGMVF 98
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP------------------LEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 99 QRFHL---FPhLTATANVMEAPMR----VRGLSKADARtQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPE 171
Cdd:cd03235 75 QRRSIdrdFP-ISVRDVVLMGLYGhkglFRRLSKADKA-KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 915259206 172 LMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVV 229
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
6-233 |
3.19e-49 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 161.31 E-value: 3.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 6 GIHKEFGHghsavHVLRgVDLTVPrGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgyrVDAKGVVHrLHPk 85
Cdd:cd03297 5 DIEKRLPD-----FTLK-IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL---FDSRKKIN-LPP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 86 vvarQRRRIGMVFQRFHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGLADRadhYPAQLSGGQQQRVAIARA 165
Cdd:cd03297 73 ----QQRKIGLVFQQYALFPHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNR---YPAQLSGGEKQRVALARA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 915259206 166 LAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQG 233
Cdd:cd03297 146 LAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-251 |
8.08e-49 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 160.96 E-value: 8.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCIneleditAGSVVVDGERMgyRVDAKGVVHrLHPkvvarQRRRIGMVFQ 99
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETI-------AGFIKPDSGKI--LLNGKDITN-LPP-----EKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPHLTATANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPT 179
Cdd:cd03299 79 NYALFPHMTVYKNI-AYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 915259206 180 SALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPREQRTRDFL 251
Cdd:cd03299 158 SALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-180 |
1.31e-48 |
|
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: 157.42 E-value: 1.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrvdakgvvHRLHPKVVARQRRRIGMVFQR 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDG-------------QDLTDDERKSLRKEIGYVFQD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 101 FHLFPHLTATANVMEaPMRVRGLSKADARTQALDLLRRVGLAD----RADHYPAQLSGGQQQRVAIARALAMDPELMLFD 176
Cdd:pfam00005 68 PQLFPRLTVRENLRL-GLLLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLD 146
|
....
gi 915259206 177 EPTS 180
Cdd:pfam00005 147 EPTA 150
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-241 |
1.38e-48 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 162.20 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVdakgvvh 80
Cdd:COG4152 1 MLELKGLTKRFG----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 rlhpkvvarqRRRIG-MVFQRfHLFPHLTatanVMEAPM---RVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQ 156
Cdd:COG4152 70 ----------RRRIGyLPEER-GLYPKMK----VGEQLVylaRLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 157 QQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPS 236
Cdd:COG4152 135 QQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD 214
|
....*
gi 915259206 237 EVLDA 241
Cdd:COG4152 215 EIRRQ 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-251 |
2.56e-48 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 160.08 E-value: 2.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHghsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINEL-----EDITAGSVVVDGERMgYRVDak 76
Cdd:PRK14247 4 IEIRDLKVSFGQ----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDI-FKMD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 77 gvvhrlhpkvVARQRRRIGMVFQRFHLFPHLTATANVMEAPMRVRGL-SKADARTQALDLLRRVGL----ADRADHYPAQ 151
Cdd:PRK14247 77 ----------VIELRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLwdevKDRLDAPAGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 152 LSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASgMTMIVVTHEIGFAREVADEVVFMDQGVVVE 231
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVE 225
|
250 260
....*....|....*....|
gi 915259206 232 QGPPSEVLDAPREQRTRDFL 251
Cdd:PRK14247 226 WGPTREVFTNPRHELTEKYV 245
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-227 |
2.83e-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: 156.64 E-value: 2.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 3 ELTGIHKEFGHGHsavhVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrvdakgvvHRL 82
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG-------------KDI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 83 HPKVVARQRRRIGMVFQrfhlfphltatanvmeapmrvrglskadartqaldllrrvgladradhypaqLSGGQQQRVAI 162
Cdd:cd00267 64 AKLPLEELRRRIGYVPQ----------------------------------------------------LSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 915259206 163 ARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQG 227
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-246 |
3.54e-48 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 160.03 E-value: 3.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrVDAKGVvh 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP----VTGPGA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 rlhpkvvarqrRRiGMVFQRFHLFPHLTATANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRV 160
Cdd:COG4525 77 -----------DR-GVVFQKDALLPWLNVLDNV-AFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 161 AIARALAMDPELMLFDEPTSALDP---ELVGEVLavMKDLAASGMTMIVVTHEIgfarevaDEVVFMDQGVVVEQGPP-- 235
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDAltrEQMQELL--LDVWQRTGKGVFLITHSV-------EEALFLATRLVVMSPGPgr 214
|
250
....*....|..
gi 915259206 236 -SEVLDAPREQR 246
Cdd:COG4525 215 iVERLELDFSRR 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-241 |
2.00e-47 |
|
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: 166.93 E-value: 2.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHkeFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrVDakgvVHR 81
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDG------ID----LRQ 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPKVVarqRRRIGMVFQRFHLFpHLTATANVMeapmrvrgLSKADA-RTQALDLLRRVGLADRADHYP----------- 149
Cdd:COG2274 542 IDPASL---RRQIGVVLQDVFLF-SGTIRENIT--------LGDPDAtDEEIIEAARLAGLHDFIEALPmgydtvvgegg 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 150 AQLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAsGMTMIVVTHEIGFAREvADEVVFMDQGVV 229
Cdd:COG2274 610 SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRL-ADRIIVLDKGRI 687
|
250
....*....|..
gi 915259206 230 VEQGPPSEVLDA 241
Cdd:COG2274 688 VEDGTHEELLAR 699
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-238 |
2.17e-47 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 164.04 E-value: 2.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVH 80
Cdd:COG3845 5 ALELRGITKRFG----GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP----------VR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVvARqRRRIGMVFQRFHLFPHLTATANVM--EAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQ 158
Cdd:COG3845 71 IRSPRD-AI-ALGIGMVHQHFMLVPNLTVAENIVlgLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 159 RVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEV 238
Cdd:COG3845 149 RVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
20-233 |
2.25e-47 |
|
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: 155.29 E-value: 2.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHRLHPKVVARqrrRIGMVFQ 99
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKD----------LASLSPKELAR---KIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 rfhlfphltatanvmeapmrvrglskadartqaldLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPT 179
Cdd:cd03214 81 -----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 915259206 180 SALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQG 233
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-242 |
8.49e-47 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 158.43 E-value: 8.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 36 ILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgVVHrlhpkvVARQRRRIGMVFQRFHLFPHLTATANVmE 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGED---------VTN------VPPHLRHINMVFQSYALFPHMTVEENV-A 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 116 APMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMK 195
Cdd:TIGR01187 65 FGLKMRKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 915259206 196 DLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAP 242
Cdd:TIGR01187 145 TIQEQlGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-230 |
1.08e-46 |
|
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: 154.34 E-value: 1.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 3 ELTGIHKEFGHGHSavhVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRvdakgvvhrl 82
Cdd:cd03226 1 RIENISFSYKKGTE---ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 83 hpkvvaRQRRRIGMVFQ--RFHLFphltaTANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRV 160
Cdd:cd03226 68 ------ERRKSIGYVMQdvDYQLF-----TDSV-REELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 161 AIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVV 230
Cdd:cd03226 136 AIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-224 |
3.26e-46 |
|
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: 153.15 E-value: 3.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 4 LTGIHKEFGHghsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAKGVVHRlh 83
Cdd:TIGR03608 1 LKNISKKFGD----KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 84 pkvvarqRRRIGMVFQRFHLFPHLTATANvMEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIA 163
Cdd:TIGR03608 75 -------REKLGYLFQNFALIENETVEEN-LDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 915259206 164 RALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFArEVADEVVFM 224
Cdd:TIGR03608 147 RAILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-227 |
1.34e-45 |
|
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: 152.20 E-value: 1.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEF---GHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCI--NELedITAGSVVVDgeRMGYRVDa 75
Cdd:COG4778 4 LLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYL--PDSGSILVR--HDGGWVD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 76 kgvVHRLHPKVVARQRRR-IGMVFQRFHLFPHLTATANVMEaPMRVRGLSKADARTQALDLLRRVGLADR-ADHYPAQLS 153
Cdd:COG4778 79 ---LAQASPREILALRRRtIGYVSQFLRVIPRVSALDVVAE-PLLERGVDREEARARARELLARLNLPERlWDLPPATFS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 154 GGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQG 227
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-227 |
2.37e-45 |
|
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: 149.84 E-value: 2.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHkeFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrVDAKGV-VH 80
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG------VDLRDLdLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLhpkvvarqRRRIGMVFQRFHLFpHLTATANVmeapmrvrglskadartqaldllrrvgladradhypaqLSGGQQQRV 160
Cdd:cd03228 73 SL--------RKNIAYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRI 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 161 AIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAsGMTMIVVTHEIGFAREvADEVVFMDQG 227
Cdd:cd03228 106 AIARALLRDPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-242 |
5.58e-45 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 154.23 E-value: 5.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAVHvlrGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyrvdakgVVH 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIK---GIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR----------VVN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKvvarqRRRIGMVFQRFHLFPHLTATANvMEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRV 160
Cdd:PRK11650 70 ELEPA-----DRDIAMVFQNYALYPHMSVREN-MAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 161 AIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGvVVEQ-GPPSEV 238
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGG-VAEQiGTPVEV 222
|
....
gi 915259206 239 LDAP 242
Cdd:PRK11650 223 YEKP 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-233 |
6.11e-45 |
|
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: 149.95 E-value: 6.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIhkEFGHGHSAVHVlrgvDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAkgvvhr 81
Cdd:cd03298 1 VRLDKI--RFSYGEQPMHF----DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 lhpkvvarqRRRIGMVFQRFHLFPHLTATANVMEApmRVRGLSKADARTQALD-LLRRVGLADRADHYPAQLSGGQQQRV 160
Cdd:cd03298 69 ---------DRPVSMLFQENNLFAHLTVEQNVGLG--LSPGLKLTAEDRQAIEvALARVGLAGLEKRLPGELSGGERQRV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 161 AIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQG 233
Cdd:cd03298 138 ALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-255 |
6.64e-45 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 151.53 E-value: 6.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 19 HVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAgSVVVDGErmgYRVDAKGVvhrLHPKVVA-RQRRRIGMV 97
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNE-EARVEGE---VRLFGRNI---YSPDVDPiEVRREVGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 98 FQRFHLFPHLTATANVMEApMRVRGLSKA----DARTQALdlLRRVGL----ADRADHYPAQLSGGQQQRVAIARALAMD 169
Cdd:PRK14267 91 FQYPNPFPHLTIYDNVAIG-VKLNGLVKSkkelDERVEWA--LKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 170 PELMLFDEPTSALDP---ELVGEVLAVMKDlaasGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPREQR 246
Cdd:PRK14267 168 PKILLMDEPTANIDPvgtAKIEELLFELKK----EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHEL 243
|
....*....
gi 915259206 247 TRDFLAHVL 255
Cdd:PRK14267 244 TEKYVTGAL 252
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-243 |
1.30e-44 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 153.65 E-value: 1.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHghsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYrvdakgvvhr 81
Cdd:PRK11000 4 VTLRNVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 lhpkvVARQRRRIGMVFQRFHLFPHLTATANvMEAPMRVRGLSKADAR---TQALDLLRRVGLADRAdhyPAQLSGGQQQ 158
Cdd:PRK11000 70 -----VPPAERGVGMVFQSYALYPHLSVAEN-MSFGLKLAGAKKEEINqrvNQVAEVLQLAHLLDRK---PKALSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 159 RVAIARALAMDPELMLFDEPTSALDPEL----VGEVLAVMKDLaasGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGP 234
Cdd:PRK11000 141 RVAIGRTLVAEPSVFLLDEPLSNLDAALrvqmRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGK 217
|
....*....
gi 915259206 235 PSEVLDAPR 243
Cdd:PRK11000 218 PLELYHYPA 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-241 |
1.50e-44 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 157.63 E-value: 1.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrVDakgvVHRLHPKVVarqRRRIGMVFQ 99
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG------VD----IRDLTLESL---RRQIGVVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFpHLTATANVmeapmrvrGLSKADA-RTQALDLLRRVGLADRADHYP-----------AQLSGGQQQRVAIARALA 167
Cdd:COG1132 422 DTFLF-SGTIRENI--------RYGRPDAtDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 168 MDPELMLFDEPTSALDPELVGEVLAVMKDLAAsGMTMIVVTHEIGFAREvADEVVFMDQGVVVEQGPPSEVLDA 241
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELLAR 564
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-238 |
3.16e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 151.54 E-value: 3.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 18 VHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAKGVVHRLHPKVVA---RQRRRI 94
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSKKIKnfkELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 95 GMVFQ--RFHLFPHlTATANVMEAPMRVrGLSKADARTQALDLLRRVGLADR-ADHYPAQLSGGQQQRVAIARALAMDPE 171
Cdd:PRK13631 119 SMVFQfpEYQLFKD-TIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 172 LMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEV 238
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
7-252 |
3.45e-44 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 151.66 E-value: 3.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 7 IHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyrvDAKGvvhrlHPKV 86
Cdd:PRK11308 17 VKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQ------DLLK-----ADPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 87 VARQRRR-IGMVFQRFH--LFPHLTATAnVMEAPMRVR-GLSKADARTQALDLLRRVGL-ADRADHYPAQLSGGQQQRVA 161
Cdd:PRK11308 86 AQKLLRQkIQIVFQNPYgsLNPRKKVGQ-ILEEPLLINtSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLD 240
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFN 244
|
250
....*....|..
gi 915259206 241 APREQRTRDFLA 252
Cdd:PRK11308 245 NPRHPYTQALLS 256
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-238 |
4.95e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 149.84 E-value: 4.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAvhvLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYrvDAKGVVh 80
Cdd:PRK13639 1 ILETRDLKYSYPDGTEA---LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY--DKKSLL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 rlhpKVvarqRRRIGMVFQR--FHLFPHlTATANVMEAPMRVrGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQ 158
Cdd:PRK13639 75 ----EV----RKTVGIVFQNpdDQLFAP-TVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 159 RVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEV 238
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
12-238 |
1.00e-43 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 147.67 E-value: 1.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 12 GHGHSavHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHRLHPKvvARQR 91
Cdd:TIGR03410 9 YYGQS--HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGED----------ITKLPPH--ERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 92 RRIGMVFQRFHLFPHLTATANV-MEAPMRVRGLSKADARTQAL-----DLLRRVGladradhypAQLSGGQQQRVAIARA 165
Cdd:TIGR03410 75 AGIAYVPQGREIFPRLTVEENLlTGLAALPRRSRKIPDEIYELfpvlkEMLGRRG---------GDLSGGQQQQLAIARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 166 LAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEV 238
Cdd:TIGR03410 146 LVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-230 |
1.65e-43 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 144.88 E-value: 1.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHR 81
Cdd:cd03216 1 LELRGITKRFG----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE----------VSF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPKvvARQRRRIGMVFQrfhlfphltatanvmeapmrvrglskadartqaldllrrvgladradhypaqLSGGQQQRVA 161
Cdd:cd03216 67 ASPR--DARRAGIAMVYQ----------------------------------------------------LSVGERQMVE 92
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVV 230
Cdd:cd03216 93 IARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
20-251 |
5.54e-43 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 149.37 E-value: 5.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCIneleditAGSVVVDGERMGYRVDAKGVVHrLHPkvvarQRRRIGMVFQ 99
Cdd:TIGR03258 20 VLDDLSLEIEAGELLALIGKSGCGKTTLLRAI-------AGFVKAAGLTGRIAIADRDLTH-APP-----HKRGLALLFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPHLTATANVMEApMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPT 179
Cdd:TIGR03258 87 NYALFPHLKVEDNVAFG-LRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 180 SALDPELVGEVLAVMKDLAAS--GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPREQRTRDFL 251
Cdd:TIGR03258 166 SALDANIRANMREEIAALHEElpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFL 239
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
11-242 |
6.64e-43 |
|
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: 153.00 E-value: 6.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 11 FGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrVDakgvVHRLHPKVVarq 90
Cdd:COG4987 341 FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG------VD----LRDLDEDDL--- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 91 RRRIGMVFQRFHLFpHLTATANVMeapmrvrgLSKADA-RTQALDLLRRVGLADRADHYP-----------AQLSGGQQQ 158
Cdd:COG4987 408 RRRIAVVPQRPHLF-DTTLRENLR--------LARPDAtDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 159 RVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAsGMTMIVVTHEIGfAREVADEVVFMDQGVVVEQGPPSEV 238
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEEL 556
|
....
gi 915259206 239 LDAP 242
Cdd:COG4987 557 LAQN 560
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-242 |
1.65e-42 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 147.95 E-value: 1.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 24 VDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgyRVDAKGVVHRLHpkvvarqRRRIGMVFQRFHL 103
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL--FDSRKGIFLPPE-------KRRIGYVFQEARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 104 FPHLTATANVMEAPMRVRGLSKADARTQALDLLrrvGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPTSALD 183
Cdd:TIGR02142 87 FPHLSVRGNLRYGMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 184 PELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAP 242
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-217 |
1.96e-42 |
|
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: 143.39 E-value: 1.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHghsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAKgvvh 80
Cdd:COG4133 2 MLEAENLSCRRGE----RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 rlhpkvvarqRRRIGMVFQRFHLFPHLTATANVmEAPMRVRGLSKADARtqALDLLRRVGLADRADHYPAQLSGGQQQRV 160
Cdd:COG4133 74 ----------RRRLAYLGHADGLKPELTVRENL-RFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 161 AIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTH---EIGFAREV 217
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqplELAAARVL 200
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-233 |
2.91e-42 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 143.19 E-value: 2.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVdakgvvhr 81
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 lhpkvvarqRRRIGMVFQRFHLFPHLTatanVMEAPM---RVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQ 158
Cdd:cd03269 69 ---------RNRIGYLPEERGLYPKMK----VIDQLVylaQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 915259206 159 RVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQG 233
Cdd:cd03269 136 KVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
21-237 |
3.08e-42 |
|
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: 146.00 E-value: 3.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVdgerMGYRV--DAKGVvhrlhpkvvarqRRRIGMVF 98
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARV----AGYDVvrEPRKV------------RRSIGIVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 99 QRFHLFPHLTATANvMEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEP 178
Cdd:TIGR01188 73 QYASVDEDLTGREN-LEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 915259206 179 TSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSE 237
Cdd:TIGR01188 152 TTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-214 |
3.09e-42 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 143.77 E-value: 3.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgyrvdakgvvH 80
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL----------H 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARQR-RRIGMVFQRFHLFPHLTATANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQR 159
Cdd:PRK10584 76 QMDEEARAKLRaKHVGFVFQSFMLIPTLNALENV-ELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 160 VAIARALAMDPELMLFDEPTSALDPElVGEVLAvmkDLAAS-----GMTMIVVTHEIGFA 214
Cdd:PRK10584 155 VALARAFNGRPDVLFADEPTGNLDRQ-TGDKIA---DLLFSlnrehGTTLILVTHDLQLA 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
20-239 |
3.13e-42 |
|
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: 151.06 E-value: 3.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHRLHPkvvARQRRRIGMVFQ 99
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD----------LSDLDP---ASWRRQIAWVPQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFpHLTATANVMeapmrvrgLSKADA-RTQALDLLRRVGLADRADHYP-----------AQLSGGQQQRVAIARALA 167
Cdd:COG4988 419 NPYLF-AGTIRENLR--------LGRPDAsDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 915259206 168 MDPELMLFDEPTSALDPELVGEVLAVMKDLAAsGMTMIVVTHEIGFAREvADEVVFMDQGVVVEQGPPSEVL 239
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELL 559
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-251 |
6.65e-42 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 143.65 E-value: 6.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGY-----RVDAkgvvhrlhpkvvARQRRRI 94
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFgkdifQIDA------------IKLRKEV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 95 GMVFQRFHLFPHLTATANVmEAPMRVRGLS-KADARTQALDLLRRVGL----ADRADHYPAQLSGGQQQRVAIARALAMD 169
Cdd:PRK14246 93 GMVFQQPNPFPHLSIYDNI-AYPLKSHGIKeKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 170 PELMLFDEPTSALDPELVGEVLAVMKDLAASgMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPREQRTRD 249
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
..
gi 915259206 250 FL 251
Cdd:PRK14246 251 YV 252
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
21-252 |
7.74e-42 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 143.77 E-value: 7.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGsvvvdgermgYRVDAKGVVH-------RLHPKVVarqRRR 93
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG----------FRVEGKVTFHgknlyapDVDPVEV---RRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 94 IGMVFQRFHLFPHlTATANVMEAPmRVRG-------LSKADARTQAL-----DLLRRVGLAdradhypaqLSGGQQQRVA 161
Cdd:PRK14243 93 IGMVFQKPNPFPK-SIYDNIAYGA-RINGykgdmdeLVERSLRQAALwdevkDKLKQSGLS---------LSGGQQQRLC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASgMTMIVVTHEIGFAREVADEVVFMD---------QGVVVEQ 232
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEF 240
|
250 260
....*....|....*....|
gi 915259206 233 GPPSEVLDAPREQRTRDFLA 252
Cdd:PRK14243 241 DRTEKIFNSPQQQATRDYVS 260
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-254 |
9.54e-42 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 147.10 E-value: 9.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAKgvvhrlhpkVVARQRRRIGMVFQR 100
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAE---------LREVRRKKIAMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 101 FHLFPHLTATANVMEApMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPTS 180
Cdd:PRK10070 115 FALMPHMTVLDNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 915259206 181 ALDPELVGEVLAVMKDLAASGM-TMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPREQRTRDFLAHV 254
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-233 |
1.06e-41 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 141.59 E-value: 1.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHGHsavhVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAkgvvhr 81
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 lhpkvvarqRRRIGMVFQRFHLFPHLTATANvMEAPMRVRGLSKADARtqalDLLRRVGLADRADHYPAQLSGGQQQRVA 161
Cdd:cd03268 71 ---------LRRIGALIEAPGFYPNLTAREN-LRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQG 233
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-239 |
1.29e-41 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 142.53 E-value: 1.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 19 HVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAG-SVVVDGERMGyRVDakgvvhrlhpkvVARQRRRIGMV 97
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRG-GED------------VWELRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 98 FQRFHLFphLTATANVMEA--------PMRVRGLSKADaRTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMD 169
Cdd:COG1119 84 SPALQLR--FPRDETVLDVvlsgffdsIGLYREPTDEQ-RERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 915259206 170 PELMLFDEPTSALDPELVGEVLAVMKDLAASG-MTMIVVTH---EI--GFarevaDEVVFMDQGVVVEQGPPSEVL 239
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhveEIppGI-----THVLLLKDGRVVAAGPKEEVL 231
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
18-214 |
1.20e-40 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 138.32 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 18 VHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYrvDAKGVVHRlhpkvvarqRRRIGMV 97
Cdd:TIGR01166 5 PEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDY--SRKGLLER---------RQRVGLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 98 FQRF--HLFpHLTATANVMEAPMRVrGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLF 175
Cdd:TIGR01166 74 FQDPddQLF-AADVDQDVAFGPLNL-GLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLL 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 915259206 176 DEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFA 214
Cdd:TIGR01166 152 DEPTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
19-254 |
1.57e-40 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 143.44 E-value: 1.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 19 HVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYrvdakgvvhrlhpkvVARQRRRIGMVF 98
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH---------------VPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 99 QRFHLFPHLTATANVMEApMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEP 178
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 179 TSALDPELVGEV-LAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPREQRTRDFLAHV 254
Cdd:PRK11607 177 MGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSV 253
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-209 |
2.30e-40 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 138.38 E-value: 2.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRCI--NELEDITA-GSVVVDGERmgyrvdakgvVHRLHPkvvarQRRRIGMV 97
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagTLSPAFSAsGEVLLNGRR----------LTALPA-----EQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 98 FQRFHLFPHLTATANVMEA-PmrvRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFD 176
Cdd:COG4136 82 FQDDLLFPHLSVGENLAFAlP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190
....*....|....*....|....*....|....
gi 915259206 177 EPTSALDPELVGEVLA-VMKDLAASGMTMIVVTH 209
Cdd:COG4136 159 EPFSKLDAALRAQFREfVFEQIRQRGIPALLVTH 192
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-238 |
3.63e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 139.84 E-value: 3.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrVDAKGVVHrlhpkvVARQRRRIGMVFQ 99
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG------LDTSDEEN------LWDIRNKAGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RfhlfPHLTATANVME-----APMRVrGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELML 174
Cdd:PRK13633 93 N----PDNQIVATIVEedvafGPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 915259206 175 FDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREvADEVVFMDQGVVVEQGPPSEV 238
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-244 |
3.72e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 140.16 E-value: 3.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVdGERMgyrvdakgVVHRLHPKVVARQRRRIGMVFQr 100
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERV--------ITAGKKNKKLKPLRKKVGIVFQ- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 101 fhlFPHL-----TATANVMEAPMRVrGLSKADARTQALDLLRRVGL-ADRADHYPAQLSGGQQQRVAIARALAMDPELML 174
Cdd:PRK13634 93 ---FPEHqlfeeTVEKDICFGPMNF-GVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 915259206 175 FDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPRE 244
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-237 |
4.32e-40 |
|
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: 137.89 E-value: 4.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGhGHSAVhvlRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgyRVDAKGVvhr 81
Cdd:cd03265 1 IEVENLVKKYG-DFEAV---RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV--VREPREV--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 lhpkvvarqRRRIGMVFQRFHLFPHLTATANvMEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVA 161
Cdd:cd03265 72 ---------RRRIGIVFQDLSVDDELTGWEN-LYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSE 237
Cdd:cd03265 142 IARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-233 |
4.88e-40 |
|
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: 137.32 E-value: 4.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHGHsavhVLRGVDLTVPRGsVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrVDAKGVVHR 81
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG------QDVLKQPQK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LhpkvvarqRRRIGMVFQRFHLFPHLTATAnVMEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVA 161
Cdd:cd03264 70 L--------RRRIGYLPQEFGVYPNFTVRE-FLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAsGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQG 233
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE-DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-243 |
2.49e-39 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 137.17 E-value: 2.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCIN-ELEdITAGSVVVDGERmgyrvdakgvVHRLHPKVVARQRrriGMVF 98
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTgELT-PSSGEVRLNGRP----------LAAWSPWELARRR---AVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 99 QRFHL-FPhLTATANVMeapM--RVRGLSKADARTQALDLLRRVGLADRAD-HYPaQLSGGQQQRVAIARALA------- 167
Cdd:COG4559 82 QHSSLaFP-FTVEEVVA---LgrAPHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVLAqlwepvd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 915259206 168 MDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPR 243
Cdd:COG4559 157 GGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDEL 232
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
3-248 |
3.04e-39 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 136.89 E-value: 3.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 3 ELTGIHKEFGH-----GHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrvdakg 77
Cdd:COG4167 6 EVRNLSKTFKYrtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILING----------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 78 vvHRLHPKVVARQRRRIGMVFQ--RFHLFPHLTaTANVMEAPMRVR-GLSKADARTQALDLLRRVGL-ADRADHYPAQLS 153
Cdd:COG4167 75 --HKLEYGDYKYRCKHIRMIFQdpNTSLNPRLN-IGQILEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 154 GGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQ 232
Cdd:COG4167 152 SGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEVVEY 231
|
250
....*....|....*.
gi 915259206 233 GPPSEVLDAPREQRTR 248
Cdd:COG4167 232 GKTAEVFANPQHEVTK 247
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-225 |
5.66e-39 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 135.33 E-value: 5.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 9 KEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgyrvdakgvvHRLHPKVVA 88
Cdd:PRK11629 13 KRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPM----------SKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 89 RQR-RRIGMVFQRFHLFPHLTATANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALA 167
Cdd:PRK11629 83 ELRnQKLGFIYQFHHLLPDFTALENV-AMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 915259206 168 MDPELMLFDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREVADEVVFMD 225
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMRD 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-238 |
6.09e-39 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 136.68 E-value: 6.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvvhrLHPKVVARQRRRIGMVFQR 100
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-------------LSEETVWDVRRQVGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 101 -FHLFPHLTATANVMEApMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPT 179
Cdd:PRK13635 90 pDNQFVGATVQDDVAFG-LENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 180 SALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREvADEVVFMDQGVVVEQGPPSEV 238
Cdd:PRK13635 169 SMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-242 |
7.24e-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: 7.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHghsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVH 80
Cdd:COG4604 1 MIEIKNVSKRYGG----KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLD----------VA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARqrrRIGMVFQRFHL--------------FPHltatanvmeapmrVRG-LSKADAR--TQALDLLrrvGLAD 143
Cdd:COG4604 67 TTPSRELAK---RLAILRQENHInsrltvrelvafgrFPY-------------SKGrLTAEDREiiDEAIAYL---DLED 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 144 RADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLA-ASGMTMIVVTHEIGFAREVADEVV 222
Cdd:COG4604 128 LADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdELGKTVVIVLHDINFASCYADHIV 207
|
250 260
....*....|....*....|
gi 915259206 223 FMDQGVVVEQGPPSEVLDAP 242
Cdd:COG4604 208 AMKDGRVVAQGTPEEIITPE 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-252 |
8.82e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 136.38 E-value: 8.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 14 GHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRvdakgvvHRLHPKVVARQRRR 93
Cdd:PRK14271 30 GFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGR-------SIFNYRDVLEFRRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 94 IGMVFQRFHLFPhLTATANVMEAPMRVRGLSKADARTQALDLLRRVGL----ADRADHYPAQLSGGQQQRVAIARALAMD 169
Cdd:PRK14271 103 VGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 170 PELMLFDEPTSALDPELVGEVLAVMKDLAASgMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPREQRTRD 249
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETAR 260
|
...
gi 915259206 250 FLA 252
Cdd:PRK14271 261 YVA 263
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-233 |
8.95e-39 |
|
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: 134.22 E-value: 8.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 25 DLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHRLHPkvvarQRRRIGMVFQRFHLF 104
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS----------HTGLAP-----YQRPVSMLFQENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 105 PHLTATANV---MEAPMRVRGLSKadarTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPTSA 181
Cdd:TIGR01277 83 AHLTVRQNIglgLHPGLKLNAEQQ----EKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 915259206 182 LDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQG 233
Cdd:TIGR01277 159 LDPLLREEMLALVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
21-251 |
1.15e-38 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 135.29 E-value: 1.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDI-----TAGSVVVDGERM-GYRVDAkgvvhrlhpkvvARQRRRI 94
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIySPRTDT------------VDLRKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 95 GMVFQRFHLFPhLTATANVMEApMRVRGLSKADARTQALDL-LRRVGL----ADRADHYPAQLSGGQQQRVAIARALAMD 169
Cdd:PRK14239 89 GMVFQQPNPFP-MSIYENVVYG-LRLKGIKDKQVLDEAVEKsLKGASIwdevKDRLHDSALGLSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 170 PELMLFDEPTSALDPELVGEVLAVMKDLAASgMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPREQRTRD 249
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETED 245
|
..
gi 915259206 250 FL 251
Cdd:PRK14239 246 YI 247
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-233 |
1.97e-38 |
|
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: 133.65 E-value: 1.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVH 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD----------VV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RlHPKVVarqRRRIGMVFQRFHLFPHLTATANVmEAPMRVRGLsKADARTQALD-LLRRVGLADRADHYPAQLSGGQQQR 159
Cdd:cd03266 71 K-EPAEA---RRRLGFVSDSTGLYDRLTARENL-EYFAGLYGL-KGDELTARLEeLADRLGMEELLDRRVGGFSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 160 VAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQG 233
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-240 |
2.70e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 134.86 E-value: 2.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 19 HVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVdgerMGYRVdakgvvhrlHPKVVARQRRRIGMVF 98
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKV----MGREV---------NAENEKWVRSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 99 QR--FHLFPhLTATANVMEAPMRVrGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFD 176
Cdd:PRK13647 86 QDpdDQVFS-STVWDDVAFGPVNM-GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 177 EPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLD 240
Cdd:PRK13647 164 EPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-237 |
2.91e-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: 133.01 E-value: 2.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHGhsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAkgvvhr 81
Cdd:cd03263 1 LQIRNLTKTYKKG--TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 lhpkvvarQRRRIGMVFQRFHLFPHLTatanVMEAPM---RVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQ 158
Cdd:cd03263 73 --------ARQSLGYCPQFDALFDELT----VREHLRfyaRLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 915259206 159 RVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLaASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSE 237
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-239 |
2.94e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 135.60 E-value: 2.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHGHS-AVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVV----------VDGERMG 70
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 71 YRVD---AKGVVHRLhpKVVARQRRRIGMVFQ--RFHLFPHlTATANVMEAPMRVrGLSKADARTQALDLLRRVGL-ADR 144
Cdd:PRK13651 83 VLEKlviQKTRFKKI--KKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLdESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 145 ADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFM 224
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|....*
gi 915259206 225 DQGVVVEQGPPSEVL 239
Cdd:PRK13651 239 KDGKIIKDGDTYDIL 253
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-238 |
4.85e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 134.49 E-value: 4.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgyRVDAKGvvhrlhpKVVARQRRRIGMVFQr 100
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLI--TSTSKN-------KDIKQIRKKVGLVFQ- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 101 fhlFPHL-----TATANVMEAPMRVrGLSKADARTQALDLLRRVGLADRA-DHYPAQLSGGQQQRVAIARALAMDPELML 174
Cdd:PRK13649 93 ---FPESqlfeeTVLKDVAFGPQNF-GVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 175 FDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEV 238
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-238 |
5.94e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 134.19 E-value: 5.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAKGVvhrlhpkvvARQRRRIGMVFQ- 99
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNL---------KKLRKKVSLVFQf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 -RFHLFPHlTATANVMEAPMRVrGLSKADARTQALDLLRRVGLA-DRADHYPAQLSGGQQQRVAIARALAMDPELMLFDE 177
Cdd:PRK13641 94 pEAQLFEN-TVLKDVEFGPKNF-GFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 915259206 178 PTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEV 238
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-240 |
3.40e-37 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 130.86 E-value: 3.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 25 DLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyrvdakgvVHRLHPKvvarQRRRIGMVFQRFHLF 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----------DHTTTPP----SRRPVSMLFQENNLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 105 PHLTATANVmeapmrvrGLS-------KADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDE 177
Cdd:PRK10771 84 SHLTVAQNI--------GLGlnpglklNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 178 PTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLD 240
Cdd:PRK10771 156 PFSALDPALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-242 |
1.03e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 130.69 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 16 SAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgyrvdAKGVVHRLhpkvvarqRRRIG 95
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI-----TKENIREV--------RKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 96 MVFQRF--HLFPHlTATANVMEAPMRVrGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELM 173
Cdd:PRK13652 82 LVFQNPddQIFSP-TVEQDIAFGPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 174 LFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAP 242
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
20-240 |
1.40e-36 |
|
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: 129.27 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyrvDAKGV-VHRLhpkvvarqRRRIGMVF 98
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ------DIREVtLDSL--------RRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 99 QRFHLFpHLTATANVMEAPMRVrglSKADARTQAldllRRVGLADRADHYPAQ-----------LSGGQQQRVAIARALA 167
Cdd:cd03253 82 QDTVLF-NDTIGYNIRYGRPDA---TDEEVIEAA----KAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 915259206 168 MDPELMLFDEPTSALDPELVGEVLAVMKDLAAsGMTMIVVTHEIgfaREV--ADEVVFMDQGVVVEQGPPSEVLD 240
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRL---STIvnADKIIVLKDGRIVERGTHEELLA 224
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-255 |
2.03e-36 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 129.28 E-value: 2.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 6 GIHKEFGHGHSavhvLRGVDLTVPRGSVTVILGPSGSGKSTLLRCIneleditAGSVVVDGERMGYRvDAKGVVHRLHPK 85
Cdd:PRK11701 11 GLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNAL-------SARLAPDAGEVHYR-MRDGQLRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 86 VVARQRR----RIGMVFQ--RFHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGL-ADRADHYPAQLSGGQQQ 158
Cdd:PRK11701 79 SEAERRRllrtEWGFVHQhpRDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 159 RVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSE 237
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQ 238
|
250
....*....|....*...
gi 915259206 238 VLDAPREQRTRDFLAHVL 255
Cdd:PRK11701 239 VLDDPQHPYTQLLVSSVL 256
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
8-242 |
2.22e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 129.92 E-value: 2.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 8 HKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINEL---EDITAGSVVVDGERMGyrvdakgvvhrlhP 84
Cdd:PRK13640 10 HVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLT-------------A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 85 KVVARQRRRIGMVFQR-FHLFPHLTATANVMEApMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIA 163
Cdd:PRK13640 77 KTVWDIREKVGIVFQNpDNQFVGATVGDDVAFG-LENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 164 RALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAA-SGMTMIVVTHEIGFArEVADEVVFMDQGVVVEQGPPSEVLDAP 242
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-254 |
2.27e-36 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 128.74 E-value: 2.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrVDAKGvvhrlhPKVVarqrrrigMVFQR 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQ----ITEPG------PDRM--------VVFQN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 101 FHLFPHLTATANVMEAPMRV-RGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPT 179
Cdd:TIGR01184 63 YSLLPWLTVRENIALAVDRVlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 915259206 180 SALDPELVGEVL-AVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGppsEVLDAPREqRTRDFLAHV 254
Cdd:TIGR01184 143 GALDALTRGNLQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG---QILEVPFP-RPRDRLEVV 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-229 |
3.53e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 129.03 E-value: 3.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 4 LTGIHKEFGHGHsavhVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyrvdakgvvhrlh 83
Cdd:PRK11247 15 LNAVSKRYGERT----VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA---------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 84 PKVVARQRRRigMVFQRFHLFPHLTATANVmeapmrvrGLS-KADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAI 162
Cdd:PRK11247 75 PLAEAREDTR--LMFQDARLLPWKKVIDNV--------GLGlKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 915259206 163 ARALAMDPELMLFDEPTSALDPELVGEvlavMKDLAAS-----GMTMIVVTHEIGFAREVADEVVFMDQGVV 229
Cdd:PRK11247 145 ARALIHRPGLLLLDEPLGALDALTRIE----MQDLIESlwqqhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-239 |
6.04e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.57 E-value: 6.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIhkEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYrvdakgvvh 80
Cdd:PRK13632 7 MIKVENV--SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 rlhpKVVARQRRRIGMVFQR-FHLFPHLTATANV---MEApmrvRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQ 156
Cdd:PRK13632 76 ----ENLKEIRKKIGIIFQNpDNQFIGATVEDDIafgLEN----KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 157 QQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGM-TMIVVTHEIgfaREV--ADEVVFMDQGVVVEQG 233
Cdd:PRK13632 148 KQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDM---DEAilADKVIVFSEGKLIAQG 224
|
....*.
gi 915259206 234 PPSEVL 239
Cdd:PRK13632 225 KPKEIL 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-244 |
7.13e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 128.81 E-value: 7.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGhsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYrvDAKGVVh 80
Cdd:PRK13636 5 ILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDY--SRKGLM- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 rlhpkvvaRQRRRIGMVFQR--FHLFphltaTANVME----APMRVrGLSKADARTQALDLLRRVGLADRADHYPAQLSG 154
Cdd:PRK13636 79 --------KLRESVGMVFQDpdNQLF-----SASVYQdvsfGAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 155 GQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQG 233
Cdd:PRK13636 145 GQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQG 224
|
250
....*....|.
gi 915259206 234 PPSEVLdAPRE 244
Cdd:PRK13636 225 NPKEVF-AEKE 234
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-241 |
8.45e-36 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 127.35 E-value: 8.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 11 FGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrVDAKGVVhrlhpkvVARQ 90
Cdd:cd03251 8 FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG------HDVRDYT-------LASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 91 RRRIGMVFQRFHLFpHLTATANVMEApmrVRGLSKADAR-----TQALDLLRRV--GLADRADHYPAQLSGGQQQRVAIA 163
Cdd:cd03251 75 RRQIGLVSQDVFLF-NDTVAENIAYG---RPGATREEVEeaaraANAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 915259206 164 RALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAsGMTMIVVTHEIGFAREvADEVVFMDQGVVVEQGPPSEVLDA 241
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-238 |
1.24e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 128.24 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERM-GYRVDAKGVvhrlhpkvvarqRRRIGMVFQ 99
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItDKKVKLSDI------------RKKVGLVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 --RFHLFPHlTATANVMEAPMRvRGLSKADARTQALDLLRRVGLA--DRADHYPAQLSGGQQQRVAIARALAMDPELMLF 175
Cdd:PRK13637 91 ypEYQLFEE-TIEKDIAFGPIN-LGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 176 DEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEV 238
Cdd:PRK13637 169 DEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-238 |
1.36e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 127.97 E-value: 1.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgVVHRLHPKVVARQRRRIGMVFQr 100
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDIT---------ITHKTKDKYIRPVRKRIGMVFQ- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 101 fhlFPHLTATANVMEAPM----RVRGLSKADARTQALDLLRRVGLA-DRADHYPAQLSGGQQQRVAIARALAMDPELMLF 175
Cdd:PRK13646 93 ---FPESQLFEDTVEREIifgpKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 176 DEPTSALDPELVGEVLAVMKDLAA-SGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEV 238
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQTdENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-233 |
1.56e-35 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 127.44 E-value: 1.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHgHSAVHvlrGVDLTVPRGSVTVILGPSGSGKSTLLRCINEL--EDITAGSVVvdgERMGYRVDAKGV 78
Cdd:PRK09984 4 IIRVEKLAKTFNQ-HQALH---AVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGSHI---ELLGRTVQREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 79 VHRlhpkVVARQRRRIGMVFQRFHLFPHLTATANVMEAPMR--------VRGLSKADaRTQALDLLRRVGLADRADHYPA 150
Cdd:PRK09984 77 LAR----DIRKSRANTGYIFQQFNLVNRLSVLENVLIGALGstpfwrtcFSWFTREQ-KQRALQALTRVGMVHFAHQRVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 151 QLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVV 229
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
....
gi 915259206 230 VEQG 233
Cdd:PRK09984 232 FYDG 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-252 |
1.63e-35 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 132.52 E-value: 1.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 19 HVLRGVDLTVPRGSVTVILGPSGSGKST----LLRCINelediTAGSVVVDGERMgyrvdakgvvHRLHPKVVARQRRRI 94
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPL----------HNLNRRQLLPVRHRI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 95 GMVFQ--RFHLFPHLTAtANVMEAPMRV--RGLSKADARTQALDLLRRVGLADRADH-YPAQLSGGQQQRVAIARALAMD 169
Cdd:PRK15134 365 QVVFQdpNSSLNPRLNV-LQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILK 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 170 PELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPREQRTR 248
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTR 523
|
....
gi 915259206 249 DFLA 252
Cdd:PRK15134 524 QLLA 527
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-239 |
2.21e-35 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 127.11 E-value: 2.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 5 TGIHKEFGHG-----HSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyrvdakgvv 79
Cdd:PRK10419 7 SGLSHHYAHGglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLA--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 80 hRLHPKVVARQRRRIGMVFQRF--HLFPHLTATANVMEaPMR-VRGLSKADARTQALDLLRRVGLADR-ADHYPAQLSGG 155
Cdd:PRK10419 78 -KLNRAQRKAFRRDIQMVFQDSisAVNPRKTVREIIRE-PLRhLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 156 QQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGP 234
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
....*
gi 915259206 235 PSEVL 239
Cdd:PRK10419 236 VGDKL 240
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-227 |
3.69e-35 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 125.37 E-value: 3.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAvhvLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVH 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQA---LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHD----------IT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARQRRRIGMVFQRFHLFPHLTATANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRV 160
Cdd:PRK10908 68 RLKNREVPFLRRQIGMIFQDHHLLMDRTVYDNV-AIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 161 AIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQG 227
Cdd:PRK10908 147 GIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-239 |
1.62e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 125.23 E-value: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 17 AVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVvvdgermgyRVDAKGVVHRLHPKVVARQRRRIGM 96
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV---------TVGDIVVSSTSKQKEIKPVRKKVGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 97 VFQ--RFHLFPHlTATANVMEAPMRVrGLSKADARTQALDLLRRVGLADRA-DHYPAQLSGGQQQRVAIARALAMDPELM 173
Cdd:PRK13643 89 VFQfpESQLFEE-TVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 915259206 174 LFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVL 239
Cdd:PRK13643 167 VLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-239 |
2.08e-34 |
|
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: 123.80 E-value: 2.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 18 VHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgyrvdakgvvHRLHPKVVarqRRRIGMV 97
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI----------RDLNLRWL---RSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 98 FQRFHLFP-----HLTATANVMEAPMRVRGLSKADArtqaLDLLrrVGLADRAD----HYPAQLSGGQQQRVAIARALAM 168
Cdd:cd03249 83 SQEPVLFDgtiaeNIRYGKPDATDEEVEEAAKKANI----HDFI--MSLPDGYDtlvgERGSQLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 169 DPELMLFDEPTSALDPE---LVGEVLavmkDLAASGMTMIVVTHEIGFAREvADEVVFMDQGVVVEQGPPSEVL 239
Cdd:cd03249 157 NPKILLLDEATSALDAEsekLVQEAL----DRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELM 225
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-251 |
2.14e-34 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 124.49 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 24 VDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHRLHPKVVARQRRRIGMVFQRFHL 103
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEN----------IPAMSRSRLYTVRKRMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 104 FPHLTATANVmEAPMRVRG-LSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPTSAL 182
Cdd:PRK11831 96 FTDMNVFDNV-AYPLREHTqLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 183 DPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEvLDAPREQRTRDFL 251
Cdd:PRK11831 175 DPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA-LQANPDPRVRQFL 243
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-243 |
2.17e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 124.11 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHghsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCI-NELEdITAGSVVVDGErmgyrvdakgVV 79
Cdd:PRK13548 2 MLEARNLSVRLGG----RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGELS-PDSGEVRLNGR----------PL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 80 HRLHPKVVARQRrriGMVFQRFHL-FPhLTATANV-M-EAPmrvRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQ 156
Cdd:PRK13548 67 ADWSPAELARRR---AVLPQHSSLsFP-FTVEEVVaMgRAP---HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 157 QQRVAIARALA------MDPELMLFDEPTSALDPELVGEVLAVMKDLA-ASGMTMIVVTHEIGFAREVADEVVFMDQGVV 229
Cdd:PRK13548 140 QQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
250
....*....|....
gi 915259206 230 VEQGPPSEVLDAPR 243
Cdd:PRK13548 220 VADGTPAEVLTPET 233
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-255 |
4.01e-34 |
|
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: 123.40 E-value: 4.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAvhvlRGVDLTVPRGSVTVILGPSGSGKSTLLRCIneleditAGSVVVDGERMGYRvDAKGVVH 80
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGC----RDVSFDLYPGEVLGIVGESGSGKSTLLGCL-------AGRLAPDHGTATYI-MRSGAEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARQRRRI----GMVFQ--RFHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGL-ADRADHYPAQLS 153
Cdd:TIGR02323 71 ELYQLSEAERRRLMrtewGFVHQnpRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 154 GGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQ 232
Cdd:TIGR02323 151 GGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVES 230
|
250 260
....*....|....*....|...
gi 915259206 233 GPPSEVLDAPREQRTRDFLAHVL 255
Cdd:TIGR02323 231 GLTDQVLDDPQHPYTQLLVSSIL 253
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
11-246 |
8.33e-34 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 128.83 E-value: 8.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 11 FGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrVDakgvVHRLHPKVVarq 90
Cdd:TIGR03375 471 FAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDG------VD----IRQIDPADL--- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 91 RRRIGMVFQRFHLFpHLTATANVMeapMRVRGLSKADArtqaLDLLRRVGLADRADHYP-----------AQLSGGQQQR 159
Cdd:TIGR03375 538 RRNIGYVPQDPRLF-YGTLRDNIA---LGAPYADDEEI----LRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQA 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 160 VAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAsGMTMIVVTHEIGFArEVADEVVFMDQGVVVEQGPPSEVL 239
Cdd:TIGR03375 610 VALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA-GKTLVLVTHRTSLL-DLVDRIIVMDNGRIVADGPKDQVL 687
|
....*..
gi 915259206 240 DAPREQR 246
Cdd:TIGR03375 688 EALRKGR 694
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-235 |
1.06e-33 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 122.50 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrVDAKGVvh 80
Cdd:PRK11248 1 MLQISHLYADYG----GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP----VEGPGA-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 rlhpkvvarQRrriGMVFQRFHLFPHLTATANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRV 160
Cdd:PRK11248 71 ---------ER---GVVFQNEGLLPWRNVQDNV-AFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 161 AIARALAMDPELMLFDEPTSALDP---ELVGEVLavMKDLAASGMTMIVVTHEIGFAREVADEVVFM--DQGVVVEQGPP 235
Cdd:PRK11248 138 GIARALAANPQLLLLDEPFGALDAftrEQMQTLL--LKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVERLPL 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-240 |
3.32e-33 |
|
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: 120.41 E-value: 3.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHGHsavHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrVDAKGVVHr 81
Cdd:cd03254 3 IEFENVNFSYDEKK---PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDG------IDIRDISR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 lhpkvvARQRRRIGMVFQRFHLFP----------HLTATANVMEapmrvrglsKADARTQALDLLRRvgLADRADHYPAQ 151
Cdd:cd03254 73 ------KSLRSMIGVVLQDTFLFSgtimenirlgRPNATDEEVI---------EAAKEAGAHDFIMK--LPNGYDTVLGE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 152 ----LSGGQQQRVAIARALAMDPELMLFDEPTSALDPE---LVGEVLAVMKDlaasGMTMIVVTHEIGFAREvADEVVFM 224
Cdd:cd03254 136 nggnLSQGERQLLAIARAMLRDPKILILDEATSNIDTEtekLIQEALEKLMK----GRTSIIIAHRLSTIKN-ADKILVL 210
|
250
....*....|....*.
gi 915259206 225 DQGVVVEQGPPSEVLD 240
Cdd:cd03254 211 DDGKIIEEGTHDELLA 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-222 |
4.18e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 118.88 E-value: 4.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 14 GHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrvdakgvvhrlhpkvvarqRRR 93
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG------------------------GAR 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 94 IGMVFQRFHLFPHLTATAN--VMEAPMRVRGLSK---ADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAM 168
Cdd:NF040873 57 VAYVPQRSEVPDSLPLTVRdlVAMGRWARRGLWRrltRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 915259206 169 DPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREvADEVV 222
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCV 189
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-238 |
6.09e-33 |
|
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: 125.30 E-value: 6.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDI--TAGSVVVdgeRMGY-----RVD 74
Cdd:TIGR03269 1 IEVKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIY---HVALcekcgYVE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 75 AKGVVHRLHP------------------KVVARQRRRIGMVFQR-FHLFPHLTATANVMEApMRVRGLSKADARTQALDL 135
Cdd:TIGR03269 74 RPSKVGEPCPvcggtlepeevdfwnlsdKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEA-LEEIGYEGKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 136 LRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPTSALDPE---LVGEvlAVMKDLAASGMTMIVVTHEIG 212
Cdd:TIGR03269 153 IEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtakLVHN--ALEEAVKASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*.
gi 915259206 213 FAREVADEVVFMDQGVVVEQGPPSEV 238
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-251 |
8.26e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 120.14 E-value: 8.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 9 KEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITaGSVVVDG--ERMGYRVDAKGVVhrlhpkv 86
Cdd:PRK14258 11 NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrvEFFNQNIYERRVN------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 87 VARQRRRIGMVFQRFHLFPhLTATANVMEAPMRVRGLSKADARTQALDLLRRVGLADRADH----YPAQLSGGQQQRVAI 162
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHkihkSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 163 ARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLA-ASGMTMIVVTHEIGFAREVADEVVFMDQ-----GVVVEQGPPS 236
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTK 241
|
250
....*....|....*
gi 915259206 237 EVLDAPREQRTRDFL 251
Cdd:PRK14258 242 KIFNSPHDSRTREYV 256
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
14-239 |
9.53e-33 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 119.73 E-value: 9.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 14 GHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyrvdakgvvhRLHPKVVARQrrr 93
Cdd:PRK11231 11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIS----------MLSSRQLARR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 94 IGMVFQRfHLFPHLTATANVME---AP-MRVRG-LSKADAR--TQALDLLRRVGLADRAdhyPAQLSGGQQQRVAIARAL 166
Cdd:PRK11231 78 LALLPQH-HLTPEGITVRELVAygrSPwLSLWGrLSAEDNArvNQAMEQTRINHLADRR---LTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 915259206 167 AMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVL 239
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-238 |
2.21e-32 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 121.13 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTgIHKEFGHghsavHVLRgVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyRV---DAKG 77
Cdd:PRK11144 1 MLELN-FKQQLGD-----LCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG-----RVlfdAEKG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 78 VVhrlhpkvVARQRRRIGMVFQRFHLFPHLTATANVMeapmrvRGLSKADaRTQALDLLRRVGLADRADHYPAQLSGGQQ 157
Cdd:PRK11144 69 IC-------LPPEKRRIGYVFQDARLFPHYKVRGNLR------YGMAKSM-VAQFDKIVALLGIEPLLDRYPGSLSGGEK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 158 QRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIV-VTHEIGFAREVADEVVFMDQGVVVEQGPPS 236
Cdd:PRK11144 135 QRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILyVSHSLDEILRLADRVVVLEQGKVKAFGPLE 214
|
..
gi 915259206 237 EV 238
Cdd:PRK11144 215 EV 216
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-238 |
6.57e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 118.30 E-value: 6.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyrvdakgvvhRLHPKVVARQRRRIGMVFQR 100
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-------------LLTEENVWDIRHKIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 101 -FHLFPHLTATANVMEApMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPT 179
Cdd:PRK13650 90 pDNQFVGATVEDDVAFG-LENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 915259206 180 SALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGfarEVA--DEVVFMDQGVVVEQGPPSEV 238
Cdd:PRK13650 169 SMLDPEGRLELIKTIKGIRDDyQMTVISITHDLD---EVAlsDRVLVMKNGQVESTSTPREL 227
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-251 |
1.02e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 118.69 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 22 RGVD---LTVPRGSVTVILGPSGSGKSTLLRCINELED----ITAGSVVVDGERMgyrvdakgvvhrlhPKVVARQRRRI 94
Cdd:PRK11022 21 RAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDL--------------QRISEKERRNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 95 -----GMVFQ--RFHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGLAD---RADHYPAQLSGGQQQRVAIAR 164
Cdd:PRK11022 87 vgaevAMIFQdpMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 165 ALAMDPELMLFDEPTSALDPELVGEVLAVMKDLA-ASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPR 243
Cdd:PRK11022 167 AIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPR 246
|
....*...
gi 915259206 244 EQRTRDFL 251
Cdd:PRK11022 247 HPYTQALL 254
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-240 |
2.32e-31 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 121.69 E-value: 2.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 19 HVLRGVDLTVPRGSVTVILGPSGSGKSTLLrciNELEDITAGSVVVDGERM--GYRVDAKgvvhrlhpkvvaRQRRRIGM 96
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFRSPKGVKGSGSVLlnGMPIDAK------------EMRAISAY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 97 VFQRFHLFPHLTATANVM-EAPMRV-RGLSKADARTQALDLLRRVGLADRAD---HYPAQ---LSGGQQQRVAIARALAM 168
Cdd:TIGR00955 104 VQQDDLFIPTLTVREHLMfQAHLRMpRRVTKKEKRERVDEVLQALGLRKCANtriGVPGRvkgLSGGERKRLAFASELLT 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 915259206 169 DPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTH----EIgFarEVADEVVFMDQGVVVEQGPPSEVLD 240
Cdd:TIGR00955 184 DPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHqpssEL-F--ELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-233 |
2.95e-31 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 114.19 E-value: 2.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELED--ITAGSVVVDGermgyrvdakgvvHRLHPKVVarqRRRIGMV 97
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLING-------------RPLDKRSF---RKIIGYV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 98 FQRFHLFPHLTATANVMEApMRVRGLSkadartqaldllrrvgladradhypaqlsGGQQQRVAIARALAMDPELMLFDE 177
Cdd:cd03213 88 PQDDILHPTLTVRETLMFA-AKLRGLS-----------------------------GGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 915259206 178 PTSALDPELVGEVLAVMKDLAASGMTMIVVTHE---IGFarEVADEVVFMDQGVVVEQG 233
Cdd:cd03213 138 PTSGLDSSSALQVMSLLRRLADTGRTIICSIHQpssEIF--ELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-239 |
3.02e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 116.65 E-value: 3.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVdGErmgYRVDAKgvVHRLhpKVVARQRRRIGMVFQ- 99
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GD---YAIPAN--LKKI--KEVKRLRKEIGLVFQf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 -RFHLFPHlTATANVMEAPMRVrGLSKADARTQALDLLRRVGLA-DRADHYPAQLSGGQQQRVAIARALAMDPELMLFDE 177
Cdd:PRK13645 99 pEYQLFQE-TIEKDIAFGPVNL-GENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 915259206 178 PTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVL 239
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-252 |
4.78e-31 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 115.66 E-value: 4.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 18 VHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrvdakgvvHRLHPKVVARQRRRIGMV 97
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD-------------HPLHFGDYSYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 98 FQ--RFHLFPHlTATANVMEAPMRVRGLSKADARTQALDL-LRRVGL-ADRADHYPAQLSGGQQQRVAIARALAMDPELM 173
Cdd:PRK15112 93 FQdpSTSLNPR-QRISQILDFPLRLNTDLEPEQREKQIIEtLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 174 LFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPREQRTRDFLA 252
Cdd:PRK15112 172 IADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIA 251
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-243 |
5.55e-31 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 118.41 E-value: 5.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVH 80
Cdd:PRK09536 3 MIDVSDLSVEFG----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDD----------VE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARQrrrIGMVFQRFHLFPHLTATANVM--EAPMRVRGLSKADARTQALD-LLRRVGLADRADHYPAQLSGGQQ 157
Cdd:PRK09536 69 ALSARAASRR---VASVPQDTSLSFEFDVRQVVEmgRTPHRSRFDTWTETDRAAVErAMERTGVAQFADRPVTSLSGGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 158 QRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSE 237
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAD 225
|
....*.
gi 915259206 238 VLDAPR 243
Cdd:PRK09536 226 VLTADT 231
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-239 |
6.16e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 119.93 E-value: 6.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHkeFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrvdakgvvHR 81
Cdd:PRK11160 339 LTLNNVS--FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG-------------QP 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPKVVARQRRRIGMVFQRFHLFPHlTATANVMeapmrvrgLSKADARTQAL-DLLRRVGLADRADHYPA---------- 150
Cdd:PRK11160 404 IADYSEAALRQAISVVSQRVHLFSA-TLRDNLL--------LAAPNASDEALiEVLQQVGLEKLLEDDKGlnawlgeggr 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 151 QLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAsGMTMIVVTHEIgFAREVADEVVFMDQGVVV 230
Cdd:PRK11160 475 QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRL-TGLEQFDRICVMDNGQII 552
|
....*....
gi 915259206 231 EQGPPSEVL 239
Cdd:PRK11160 553 EQGTHQELL 561
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
20-241 |
6.86e-31 |
|
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: 119.82 E-value: 6.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrvdakgvvHRLHPKVVARQRRRIGMVFQ 99
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG-------------HDLADYTLASLRRQVALVSQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPHlTATANVMEAPMRVRGLSKADARTQALDLLRRVGLADRADHYP-----AQLSGGQQQRVAIARALAMDPELML 174
Cdd:TIGR02203 414 DVVLFND-TIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPigengVLLSGGQRQRLAIARALLKDAPILI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 175 FDEPTSALDPELVGEVLAVMKDLaASGMTMIVVTHEIGfAREVADEVVFMDQGVVVEQGPPSEVLDA 241
Cdd:TIGR02203 493 LDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-241 |
7.14e-31 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 114.41 E-value: 7.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSA------------------VHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSV 62
Cdd:COG1134 4 MIEVENVSKSYRLYHEPsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 63 VVDGermgyRVDAkgvvhrlhpkVVArqrrrIGMVFQrfhlfPHLTATANVMeAPMRVRGLSKADARtqalDLLRRV--- 139
Cdd:COG1134 84 EVNG-----RVSA----------LLE-----LGAGFH-----PELTGRENIY-LNGRLLGLSRKEID----EKFDEIvef 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 140 -GLADRAD----HYpaqlSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFA 214
Cdd:COG1134 134 aELGDFIDqpvkTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAV 209
|
250 260
....*....|....*....|....*..
gi 915259206 215 REVADEVVFMDQGVVVEQGPPSEVLDA 241
Cdd:COG1134 210 RRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-233 |
1.09e-30 |
|
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: 113.52 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCIN---ELEDITAGSVVVDGERMgyrvdakgvvhrlHPKVVarqRRRIGM 96
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPR-------------KPDQF---QKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 97 VFQRFHLFPHLTatanVME-----APMRVRGLSKADARTQ--ALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMD 169
Cdd:cd03234 86 VRQDDILLPGLT----VREtltytAILRLPRKSSDAIRKKrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 170 PELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIG---FarEVADEVVFMDQGVVVEQG 233
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIVYSG 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
8-241 |
3.55e-30 |
|
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: 112.58 E-value: 3.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 8 HKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYrVDAkgvvhrlhpkvv 87
Cdd:cd03252 5 HVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAL-ADP------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 88 ARQRRRIGMVFQRFHLFPH-------LTATANVMEAPMRVRGLSKADARTQALDLLRRVGLADRAdhypAQLSGGQQQRV 160
Cdd:cd03252 72 AWLRRQVGVVLQENVLFNRsirdniaLADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQG----AGLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 161 AIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAsGMTMIVVTHEIGFAREvADEVVFMDQGVVVEQGPPSEVLD 240
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
.
gi 915259206 241 A 241
Cdd:cd03252 226 E 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-224 |
5.45e-30 |
|
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: 117.00 E-value: 5.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvvhrLHPKVVARQRRRIGMVFQ 99
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP-------------LADADADSWRDQIAWVPQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPHlTATANVmeapmrvrGLSKADARTQAL-DLLRRVGLAD-----------RADHYPAQLSGGQQQRVAIARALA 167
Cdd:TIGR02857 404 HPFLFAG-TIAENI--------RLARPDASDAEIrEALERAGLDEfvaalpqgldtPIGEGGAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 168 MDPELMLFDEPTSALDPELVGEVLAVMKDLaASGMTMIVVTHEIGFAREvADEVVFM 224
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-252 |
1.23e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 115.96 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 11 FGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKStllrcineledITAGSVV-------VDGERMGYRVDAKGVVHRLH 83
Cdd:PRK15134 15 FRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKS-----------VTALSILrllpsppVVYPSGDIRFHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 84 PKVVARQRRRIGMVFQR--FHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGL---ADRADHYPAQLSGGQQQ 158
Cdd:PRK15134 84 QTLRGVRGNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 159 RVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSE 237
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAAT 243
|
250
....*....|....*
gi 915259206 238 VLDAPREQRTRDFLA 252
Cdd:PRK15134 244 LFSAPTHPYTQKLLN 258
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-233 |
1.29e-29 |
|
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: 110.76 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIhkEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrVDAKgvvhR 81
Cdd:cd03245 3 IEFRNV--SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG------TDIR----Q 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPKVVarqRRRIGMVFQRFHLF------------PHLTaTANVMEApMRVRGLSKAdARTQALDLLRRVGlaDRADhyp 149
Cdd:cd03245 71 LDPADL---RRNIGYVPQDVTLFygtlrdnitlgaPLAD-DERILRA-AELAGVTDF-VNKHPNGLDLQIG--ERGR--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 150 aQLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAsGMTMIVVTHEIGFArEVADEVVFMDQGVV 229
Cdd:cd03245 140 -GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLL-DLVDRIIVMDSGRI 216
|
....
gi 915259206 230 VEQG 233
Cdd:cd03245 217 VADG 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-239 |
1.36e-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: 116.06 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 18 VHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVdgeRMGYR-VDA--KGVVHRlhpkvvARQRRRI 94
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV---RVGDEwVDMtkPGPDGR------GRAKRYI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 95 GMVFQRFHLFPHLTATANVMEAPmrvrGLSKAD--ARTQALDLLRRVGLADRA-----DHYPAQLSGGQQQRVAIARALA 167
Cdd:TIGR03269 368 GILHQEYDLYPHRTVLDNLTEAI----GLELPDelARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVALAQVLI 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 915259206 168 MDPELMLFDEPTSALDPELVGEVL-AVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVL 239
Cdd:TIGR03269 444 KEPRIVILDEPTGTMDPITKVDVThSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
8-240 |
1.84e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.77 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 8 HKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrvdakgvvHRLHPKVV 87
Cdd:PRK13648 12 NVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN-------------QAITDDNF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 88 ARQRRRIGMVFQR---------------FHLFPHLTATANVmeapmrVRGLSKAdartqaldlLRRVGLADRADHYPAQL 152
Cdd:PRK13648 79 EKLRKHIGIVFQNpdnqfvgsivkydvaFGLENHAVPYDEM------HRRVSEA---------LKQVDMLERADYEPNAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 153 SGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREvADEVVFMDQGVVVE 231
Cdd:PRK13648 144 SGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYK 222
|
....*....
gi 915259206 232 QGPPSEVLD 240
Cdd:PRK13648 223 EGTPTEIFD 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-242 |
3.29e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 111.23 E-value: 3.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAvhvLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAKGVvh 80
Cdd:PRK13644 1 MIRLENVSYSYPDGTPA---LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 rlhpkvvarqRRRIGMVFQRFHL-FPHLTATANVMEAPMRVrGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQR 159
Cdd:PRK13644 76 ----------RKLVGIVFQNPETqFVGRTVEEDLAFGPENL-CLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQC 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 160 VAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGfAREVADEVVFMDQGVVVEQGPPSEVL 239
Cdd:PRK13644 145 VALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVL 223
|
...
gi 915259206 240 DAP 242
Cdd:PRK13644 224 SDV 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-243 |
3.29e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 110.12 E-value: 3.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHghsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyrvdakgVVH 80
Cdd:COG1137 3 TLEAENLVKSYGK----RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE----------DIT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RL--HpkvvarQRRRIGM--------VFQRfhlfphLTATANVMeAPMRVRGLSKADARTQALDLLRRVGLADRADHYPA 150
Cdd:COG1137 69 HLpmH------KRARLGIgylpqeasIFRK------LTVEDNIL-AVLELRKLSKKEREERLEELLEEFGITHLRKSKAY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 151 QLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIgfaRE---VADEVVFMDQG 227
Cdd:COG1137 136 SLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNV---REtlgICDRAYIISEG 212
|
250
....*....|....*.
gi 915259206 228 VVVEQGPPSEVLDAPR 243
Cdd:COG1137 213 KVLAEGTPEEILNNPL 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-254 |
3.85e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 115.34 E-value: 3.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 18 VHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAKgvvhrLHPkvvarQRRRIGMV 97
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGK-----LQA-----LRRDIQFI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 98 FQRFH--LFPHLTATANVMEaPMRVRGLSKAD-ARTQALDLLRRVGL-ADRADHYPAQLSGGQQQRVAIARALAMDPELM 173
Cdd:PRK10261 407 FQDPYasLDPRQTVGDSIME-PLRVHGLLPGKaAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 174 LFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPREQRTRDFLA 252
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMA 565
|
..
gi 915259206 253 HV 254
Cdd:PRK10261 566 AV 567
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-243 |
4.77e-29 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 110.08 E-value: 4.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGhGHSAVHvlrGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERM----GYRVDAK 76
Cdd:PRK11300 5 LLSVSGLMMRFG-GLLAVN---NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 77 GVVHrlhpkvvarqrrrigmVFQRFHLFPHLTATANVMEAPMR------VRGL--------SKADARTQALDLLRRVGLA 142
Cdd:PRK11300 81 GVVR----------------TFQHVRLFREMTVIENLLVAQHQqlktglFSGLlktpafrrAESEALDRAATWLERVGLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 143 DRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEV 221
Cdd:PRK11300 145 EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRI 224
|
250 260
....*....|....*....|..
gi 915259206 222 VFMDQGVVVEQGPPSEVLDAPR 243
Cdd:PRK11300 225 YVVNQGTPLANGTPEEIRNNPD 246
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
20-229 |
7.02e-29 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 107.30 E-value: 7.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrVDakgvVHRLHPkvvARQRRRIGMVFQ 99
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG------AD----ISQWDP---NELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPHlTATANVmeapmrvrglskadartqaldllrrvgladradhypaqLSGGQQQRVAIARALAMDPELMLFDEPT 179
Cdd:cd03246 84 DDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 915259206 180 SALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREvADEVVFMDQGVV 229
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
23-254 |
1.18e-28 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 110.95 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 23 GVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgyrvdakgvvHRLHPKVVARQRRRIGMVFQR-- 100
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL----------LGMKDDEWRAVRSDIQMIFQDpl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 101 FHLFPHLTaTANVMEAPMRVR--GLSKADARTQALDLLRRVGL-ADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDE 177
Cdd:PRK15079 109 ASLNPRMT-IGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 915259206 178 PTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPREQRTRDFLAHV 254
Cdd:PRK15079 188 PVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAV 265
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
3-233 |
2.07e-28 |
|
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: 107.48 E-value: 2.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 3 ELTGIHKEFGHGHsavhVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyRVDakgvvhrL 82
Cdd:TIGR03740 2 ETKNLSKRFGKQT----AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT-RKD-------L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 83 HpkvvarqrrRIGMVFQRFHLFPHLTATANvmeapMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAI 162
Cdd:TIGR03740 70 H---------KIGSLIESPPLYENLTAREN-----LKVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGI 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 915259206 163 ARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQG 233
Cdd:TIGR03740 136 AIALLNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQG 206
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
16-252 |
2.70e-28 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 108.25 E-value: 2.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 16 SAVHVLRGVDLTVPRGSVTVILGPSGSGKStlLRCINELEDITAGSVVVDGermgyRVDAKGVvhRLHPKVVarQRRRIG 95
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAG-----RVLLDGK--PVAPCAL--RGRKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 96 MVFQ--RFHLFPHLTATANVMEApMRVRGLSKADArtQALDLLRRVGLADRA---DHYPAQLSGGQQQRVAIARALAMDP 170
Cdd:PRK10418 83 TIMQnpRSAFNPLHTMHTHARET-CLALGKPADDA--TLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 171 ELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPREQRTRD 249
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRS 239
|
...
gi 915259206 250 FLA 252
Cdd:PRK10418 240 LVS 242
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-240 |
3.37e-28 |
|
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: 106.46 E-value: 3.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELED--ITAGSVVVDGERMgyrvdakgvvhrLHPKVVARQRRRIGMV 97
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDI------------TDLPPEERARLGIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 98 FQRfhlfphltatanvmeaPMRVRGLSKADartqaldLLRRVGladradhypAQLSGGQQQRVAIARALAMDPELMLFDE 177
Cdd:cd03217 83 FQY----------------PPEIPGVKNAD-------FLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 915259206 178 PTSALDPELVGEVLAVMKDLAASGMTMIVVTH--EIgFAREVADEVVFMDQGVVVEQGPPSEVLD 240
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREEGKSVLIITHyqRL-LDYIKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-239 |
3.89e-28 |
|
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: 107.24 E-value: 3.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHR 81
Cdd:cd03218 1 LRAENLSKRYG----KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQD----------ITK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPKvvarQRRRIGMVF--QRFHLFPHLTATANVMeAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQR 159
Cdd:cd03218 67 LPMH----KRARLGIGYlpQEASIFRKLTVEENIL-AVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 160 VAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEigfARE---VADEVVFMDQGVVVEQGPPS 236
Cdd:cd03218 142 VEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHN---VREtlsITDRAYIIYEGKVLAEGTPE 218
|
...
gi 915259206 237 EVL 239
Cdd:cd03218 219 EIA 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-233 |
8.11e-28 |
|
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: 104.70 E-value: 8.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 11 FGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyrvdakgvvhrlHPKVVARQ 90
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGV---------------PVSDLEKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 91 RRR-IGMVFQRFHLFphltatanvmeapmrvrglskadartqALDLLRRVGladradhypAQLSGGQQQRVAIARALAMD 169
Cdd:cd03247 73 LSSlISVLNQRPYLF---------------------------DTTLRNNLG---------RRFSGGERQRLALARILLQD 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 170 PELMLFDEPTSALDPELVGEVLAVMKDlAASGMTMIVVTHEIGfAREVADEVVFMDQGVVVEQG 233
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSLIFE-VLKDKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
20-242 |
8.94e-28 |
|
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: 111.59 E-value: 8.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrVDAKGVVhrlhpkvVARQRRRIGMVFQ 99
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDG------QDLAGLD-------VQAVRRQLGVVLQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPhltatANVME-----APMRVRglskadartQALDLLRRVGLADRADHYP-----------AQLSGGQQQRVAIA 163
Cdd:TIGR03797 535 NGRLMS-----GSIFEniaggAPLTLD---------EAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIA 600
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 915259206 164 RALAMDPELMLFDEPTSALDPELVGevlAVMKDLAASGMTMIVVTHEIGFAREvADEVVFMDQGVVVEQGPPSEVLDAP 242
Cdd:TIGR03797 601 RALVRKPRILLFDEATSALDNRTQA---IVSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
16-239 |
1.04e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.10 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 16 SAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvvhrLHPKVVARQRRRIG 95
Cdd:PRK13642 18 SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEL-------------LTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 96 MVFQR-FHLFPHLTATANVMEApMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELML 174
Cdd:PRK13642 85 MVFQNpDNQFVGATVEDDVAFG-MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 915259206 175 FDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREvADEVVFMDQGVVVEQGPPSEVL 239
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-248 |
1.07e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 106.71 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGH-SAVHVLRGVDLTVPRGS-VTVIlGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAKgv 78
Cdd:COG1101 1 MLELKNLSKTFNPGTvNEKRALDGLNLTIEEGDfVTVI-GSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 79 vhrlhpkvvarqR-RRIGMVFQRFHL--FPHLTATANVMEAPMR------VRGLSKADaRTQALDLLRRV--GLADRADH 147
Cdd:COG1101 78 ------------RaKYIGRVFQDPMMgtAPSMTIEENLALAYRRgkrrglRRGLTKKR-RELFRELLATLglGLENRLDT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 148 YPAQLSGGQQQrvaiARALAM----DPELMLFDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREVADEVV 222
Cdd:COG1101 145 KVGLLSGGQRQ----ALSLLMatltKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLI 220
|
250 260
....*....|....*....|....*.
gi 915259206 223 FMDQGVVveqgppseVLDAPREQRTR 248
Cdd:COG1101 221 MMHEGRI--------ILDVSGEEKKK 238
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-238 |
2.65e-27 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 109.49 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgyrvdakgvvH 80
Cdd:PRK09700 5 YISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINY----------N 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARQRrrIGMVFQRFHLFPHLTATAN--VMEAPMR-VRGLSKAD---ARTQALDLLRRVGLADRADHYPAQLSG 154
Cdd:PRK09700 71 KLDHKLAAQLG--IGIIYQELSVIDELTVLENlyIGRHLTKkVCGVNIIDwreMRVRAAMMLLRVGLKVDLDEKVANLSI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 155 GQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGP 234
Cdd:PRK09700 149 SHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGM 228
|
....
gi 915259206 235 PSEV 238
Cdd:PRK09700 229 VSDV 232
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-241 |
2.78e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 106.81 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgyrvdakgvvhr 81
Cdd:PRK13537 8 IDFRNVEKRYG----DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 lhPKVVARQRRRIGMVFQRFHLFPHLTATANVMeAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVA 161
Cdd:PRK13537 72 --PSRARHARQRVGVVPQFDNLDPDFTVRENLL-VFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDA 241
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-240 |
7.46e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 106.07 E-value: 7.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHGHsavhVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgyrvdakgvvhr 81
Cdd:PRK13536 42 IDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV------------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 lhPKVVARQRRRIGMVFQRFHLFPHLTATANVMeAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVA 161
Cdd:PRK13536 106 --PARARLARARIGVVPQFDNLDLEFTVRENLL-VFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLD 240
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-209 |
1.41e-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: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 11 FGHGHSAVhVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvvhrLHPKVVARQ 90
Cdd:TIGR02868 342 AGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVP-------------VSSLDQDEV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 91 RRRIGMVFQRFHLFpHLTATANVMeapmrvrgLSKADARTQAL-DLLRRVGLADRADHYP-----------AQLSGGQQQ 158
Cdd:TIGR02868 408 RRRVSVCAQDAHLF-DTTVRENLR--------LARPDATDEELwAALERVGLADWLRALPdgldtvlgeggARLSGGERQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 915259206 159 RVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDlAASGMTMIVVTH 209
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-242 |
2.21e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 107.50 E-value: 2.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHK--------EFGH------GHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGE 67
Cdd:TIGR00958 464 IPLTGTLAplnlegliEFQDvsfsypNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 68 RMgyrvdAKGVVHRLHPKVVArqrrrigmVFQRFHLFPHlTATANV--------MEAPMRVRGLSKADARTQALDllrrV 139
Cdd:TIGR00958 544 PL-----VQYDHHYLHRQVAL--------VGQEPVLFSG-SVRENIaygltdtpDEEIMAAAKAANAHDFIMEFP----N 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 140 GLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGevlAVMKDLAASGMTMIVVTHEIGFAREvAD 219
Cdd:TIGR00958 606 GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ---LLQESRSRASRTVLLIAHRLSTVER-AD 681
|
250 260
....*....|....*....|...
gi 915259206 220 EVVFMDQGVVVEQGPPSEVLDAP 242
Cdd:TIGR00958 682 QILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
14-241 |
3.00e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 103.14 E-value: 3.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 14 GHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHRLHPKVVARqrrR 93
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEH----------IQHYASKEVAR---R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 94 IGMVFQRFHL-----FPHLTATANVMEAPMRVRGLSK-ADARTQALdllRRVGLADRADHYPAQLSGGQQQRVAIARALA 167
Cdd:PRK10253 83 IGLLAQNATTpgditVQELVARGRYPHQPLFTRWRKEdEEAVTKAM---QATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 915259206 168 MDPELMLFDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDA 241
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-254 |
3.39e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 106.86 E-value: 3.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVvvDGERMGYRVDAKGVVH 80
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLV--QCDKMLLRRRSRQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVARQRRR---IGMVFQR--FHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGLADRA---DHYPAQL 152
Cdd:PRK10261 90 LSEQSAAQMRHVRgadMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 153 SGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVE 231
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVE 249
|
250 260
....*....|....*....|...
gi 915259206 232 QGPPSEVLDAPREQRTRDFLAHV 254
Cdd:PRK10261 250 TGSVEQIFHAPQHPYTRALLAAV 272
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-239 |
4.74e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 102.78 E-value: 4.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYrvDAKGVVhrlhpkvvaRQRRRIGMVFQ 99
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY--SKRGLL---------ALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGlADRADHYPAQ-LSGGQQQRVAIARALAMDPELMLFDEP 178
Cdd:PRK13638 85 DPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 915259206 179 TSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVL 239
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
11-241 |
6.42e-26 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 105.60 E-value: 6.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 11 FGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrVDakgvVHRLHPkvvARQ 90
Cdd:COG4618 338 VVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG------AD----LSQWDR---EEL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 91 RRRIGMVFQRFHLFPHlTATANVmeapmrVRgLSKADARtQALDLLRRVGLADRADHYP-----------AQLSGGQQQR 159
Cdd:COG4618 405 GRHIGYLPQDVELFDG-TIAENI------AR-FGDADPE-KVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 160 VAIARALAMDPELMLFDEPTSALDPElvGE--VLAVMKDLAASGMTMIVVTHEIGfAREVADEVVFMDQGVVVEQGPPSE 237
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDE--GEaaLAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDE 552
|
....
gi 915259206 238 VLDA 241
Cdd:COG4618 553 VLAR 556
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
20-239 |
1.71e-25 |
|
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: 104.82 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyrvdakgvvhRLHPkvvARQRRRIGMVFQ 99
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLA----------IADP---AWLRRQMGVVLQ 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPHLTATANVMEAP-MRVRGLSKADARTQALDLLRRV--GLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFD 176
Cdd:TIGR01846 539 ENVLFSRSIRDNIALCNPgAPFEHVIHAAKLAGAHDFISELpqGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFD 618
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 915259206 177 EPTSALDPELVGEVLAVMKDLAAsGMTMIVVTHEIGFAREvADEVVFMDQGVVVEQGPPSEVL 239
Cdd:TIGR01846 619 EATSALDYESEALIMRNMREICR-GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELL 679
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-233 |
3.28e-25 |
|
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: 103.75 E-value: 3.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyrvDAKGVVHrlhpkvvARQRRRIGMVFQ 99
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ------DIRDVTQ-------ASLRAAIGIVPQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLF----------PHLTAT-ANVMEApmrvrglskadARTQAL-DLLRRV-----------GLadradhypaQLSGGQ 156
Cdd:COG5265 440 DTVLFndtiayniayGRPDASeEEVEAA-----------ARAAQIhDFIESLpdgydtrvgerGL---------KLSGGE 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 157 QQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAsGMTMIVVTHEIGFAREvADEVVFMDQGVVVEQG 233
Cdd:COG5265 500 KQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
20-251 |
8.23e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 98.81 E-value: 8.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyrvdakgvVHRLHpkvvARQRRRIGMVFQ 99
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIS--------LLPLH----ARARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPHLTATANVMeAPMRVR-GLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEP 178
Cdd:PRK10895 86 EASIFRRLSVYDNLM-AVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 915259206 179 TSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDapREQRTRDFL 251
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ--DEHVKRVYL 235
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-239 |
1.65e-24 |
|
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: 101.66 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgYRVDAKGVvhrlhpkvvarqRRRIGMVFQ 99
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADL-KQWDRETF------------GKHIGYLPQ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPHlTATANV--MEAPMRVRGLSKADARTQALDLLRRvgLADRADHY----PAQLSGGQQQRVAIARALAMDPELM 173
Cdd:TIGR01842 400 DVELFPG-TVAENIarFGENADPEKIIEAAKLAGVHELILR--LPDGYDTVigpgGATLSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 915259206 174 LFDEPTSALDPElvGE--VLAVMKDLAASGMTMIVVTHEIGfAREVADEVVFMDQGVVVEQGPPSEVL 239
Cdd:TIGR01842 477 VLDEPNSNLDEE--GEqaLANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-229 |
1.84e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 4 LTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVdgermgyrvdAKGVvhrlh 83
Cdd:COG0488 1 LENLSKSFG----GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI----------PKGL----- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 84 pkvvarqrrRIGMVFQRFHLFPHLTATANVMEAPMRVRGLSKA-------------------------------DARTQA 132
Cdd:COG0488 62 ---------RIGYLPQEPPLDDDLTVLDTVLDGDAELRALEAEleeleaklaepdedlerlaelqeefealggwEAEARA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 133 LDLLRRVGLADRADHYP-AQLSGGQQQRVAIARALAMDPELMLFDEPTSALDPElvgevlAVM---KDLAASGMTMIVVT 208
Cdd:COG0488 133 EEILSGLGFPEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE------SIEwleEFLKNYPGTVLVVS 206
|
250 260
....*....|....*....|.
gi 915259206 209 HEIGFAREVADEVVFMDQGVV 229
Cdd:COG0488 207 HDRYFLDRVATRILELDRGKL 227
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-236 |
1.97e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 97.45 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCI--NELEDITAGSVVVDGERMgyrvdakgvvhrLHPKVVARQRRRIGMV 97
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDI------------LELSPDERARAGIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 98 FQ--------RFHLFPHlTATANVMEAPMRVRglskaDARTQALDLLRRVGL----ADRADHypAQLSGGQQQRVAIARA 165
Cdd:COG0396 83 FQypveipgvSVSNFLR-TALNARRGEELSAR-----EFLKLLKEKMKELGLdedfLDRYVN--EGFSGGEKKRNEILQM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 166 LAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTH------EIgfareVADEVVFMDQGVVVEQGPPS 236
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHyqrildYI-----KPDFVHVLVDGRIVKSGGKE 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-233 |
2.25e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 101.58 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrVDAKGVVhrlhpkvVARQRRRIGMVFQR 100
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDG------TDIRTVT-------RASLRRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 101 FHLFPHLTA------TANVMEAPMRvrglsKADARTQALDLLRR--VGLADRADHYPAQLSGGQQQRVAIARALAMDPEL 172
Cdd:PRK13657 418 AGLFNRSIEdnirvgRPDATDEEMR-----AAAERAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 915259206 173 MLFDEPTSALDPELVGEVLAVMkDLAASGMTMIVVTHEIGFAREvADEVVFMDQGVVVEQG 233
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAAL-DELMKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-231 |
3.52e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.52 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVdGE--RMGYrVDakgv 78
Cdd:COG0488 315 VLELEGLSKSYG----DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GEtvKIGY-FD---- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 79 vhrlhpkvvarQRRRigmvfqrfhlfpHLTATANVMEApmrVRGLSKADARTQALDLLRRVGLA-DRADHYPAQLSGGQQ 157
Cdd:COG0488 385 -----------QHQE------------ELDPDKTVLDE---LRDGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEK 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 915259206 158 QRVAIARALAMDPELMLFDEPTSALDPELVgEVLAVMkdLAA-SGmTMIVVTHEIGFAREVADEVVFMDQGVVVE 231
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEPTNHLDIETL-EALEEA--LDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-238 |
6.17e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 99.71 E-value: 6.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 16 SAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHRLHPkvvaRQRRRIG 95
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKP----------VRIRSP----RDAIRAG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 96 MVF-----QRFHLFPHLTATANVMEAPMRVRG----LSKADARTQALDLLRRVGL-ADRADHYPAQLSGGQQQRVAIARA 165
Cdd:COG1129 329 IAYvpedrKGEGLVLDLSIRENITLASLDRLSrgglLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 915259206 166 LAMDPELMLFDEPTSALDpelVG---EVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEV 238
Cdd:COG1129 409 LATDPKVLILDEPTRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-227 |
1.10e-23 |
|
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: 94.04 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 16 SAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHRLHPkvvaRQRRRIG 95
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKP----------VTRRSP----RDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 96 MVF-----QRFHLFPHLTATANVmeapmrvrglskadartqALdllrrvgladradhyPAQLSGGQQQRVAIARALAMDP 170
Cdd:cd03215 77 IAYvpedrKREGLVLDLSVAENI------------------AL---------------SSLLSGGNQQKVVLARWLARDP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 171 ELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQG 227
Cdd:cd03215 124 RVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-227 |
1.73e-23 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 94.07 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCI-NELEdITAGSVVVDGeRMGYrvdakgvvhrlhpkvVARQ-------- 90
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALlGELE-KLSGSVSVPG-SIAY---------------VSQEpwiqngti 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 91 RRRI--GMVF--QRFH-------------LFPHLTATaNVMEapmrvRGLSkadartqaldllrrvgladradhypaqLS 153
Cdd:cd03250 83 RENIlfGKPFdeERYEkvikacalepdleILPDGDLT-EIGE-----KGIN---------------------------LS 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 154 GGQQQRVAIARALAMDPELMLFDEPTSALDPElVGEVL---AVMKDLaASGMTMIVVTHEIGFAREvADEVVFMDQG 227
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDAH-VGRHIfenCILGLL-LNNKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-239 |
2.88e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 98.17 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrvdakgvvHRLHPKVVARQRRRIGMVFQR 100
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG-------------HDLRDYTLASLRNQVALVSQN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 101 FHLFpHLTATANVMEApmRVRGLSKAD----AR-TQALDLLRRV--GLADRADHYPAQLSGGQQQRVAIARALAMDPELM 173
Cdd:PRK11176 426 VHLF-NDTIANNIAYA--RTEQYSREQieeaARmAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPIL 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 915259206 174 LFDEPTSALDPELVGEVLAVMKDLAASgMTMIVVTHEIGfAREVADEVVFMDQGVVVEQGPPSEVL 239
Cdd:PRK11176 503 ILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELL 566
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-241 |
6.56e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.04 E-value: 6.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFghghSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVH 80
Cdd:PRK15439 11 LLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNP----------CA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPkvVARQRRRIGMVFQRFHLFPHLTATANVMeapmrvRGLSKADARTQAL-DLLRRVGLADRADHYPAQLSGGQQQR 159
Cdd:PRK15439 77 RLTP--AKAHQLGIYLVPQEPLLFPNLSVKENIL------FGLPKRQASMQKMkQLLAALGCQLDLDSSAGSLEVADRQI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 160 VAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVL 239
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLS 228
|
..
gi 915259206 240 DA 241
Cdd:PRK15439 229 TD 230
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-243 |
1.52e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 92.60 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDiTAGSVVVDGERMGyrvdakgvvhRLHPKVVARQR--------R 92
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLS----------DWSAAELARHRaylsqqqsP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 93 RIGM-VFQRFHLF-PHLTATANVMEAPMrvrglskadartqalDLLRRVGLADRADHYPAQLSGGQQQRVAIARAL---- 166
Cdd:COG4138 81 PFAMpVFQYLALHqPAGASSEAVEQLLA---------------QLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvw 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 167 -AMDPE--LMLFDEPTSALDpelVGEVLAV---MKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLD 240
Cdd:COG4138 146 pTINPEgqLLLLDEPMNSLD---VAQQAALdrlLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
...
gi 915259206 241 APR 243
Cdd:COG4138 223 PEN 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-209 |
2.42e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.64 E-value: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVV-DGERMgyrvdakgvvhrlhpkvvarqrrrigmVF 98
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV---------------------------LF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 99 --QRfhlfPHLtATANVMEA---PMRVRGLSKADARtqalDLLRRVGLA------DRADHYPAQLSGGQQQRVAIARALA 167
Cdd:COG4178 431 lpQR----PYL-PLGTLREAllyPATAEAFSDAELR----EALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLL 501
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 915259206 168 MDPELMLFDEPTSALDPELVGEVLAVMKDlAASGMTMIVVTH 209
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
13-234 |
1.32e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 90.71 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 13 HGHSAvhvLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyrvdakgvvhrlhPKVVARQRR 92
Cdd:PRK15056 18 NGHTA---LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ----------------PTRQALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 93 RIGMVFQRFHL---FPHLTATANVMEAPMRVRGLSKADARTQAL--DLLRRVGLADRADHYPAQLSGGQQQRVAIARALA 167
Cdd:PRK15056 79 LVAYVPQSEEVdwsFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIvtAALARVDMVEFRHRQIGELSGGQKKRVFLARAIA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 168 MDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVfMDQGVVVEQGP 234
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGP 224
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-231 |
1.55e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 92.93 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 3 ELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLrciNELEDIT-----AGSVVVDGERMGYRvdakg 77
Cdd:NF040905 3 EMRGITKTFP----GVKALDDVNLSVREGEIHALCGENGAGKSTLM---KVLSGVYphgsyEGEILFDGEVCRFK----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 78 vvhrlhpKVVARQRRRIGMVFQRFHLFPHLTATANVMEAPMRVRG--LSKADARTQALDLLRRVGLADRADHYPAQLSGG 155
Cdd:NF040905 71 -------DIRDSEALGIVIIHQELALIPYLSIAENIFLGNERAKRgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 915259206 156 QQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVE 231
Cdd:NF040905 144 KQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-233 |
2.83e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 92.60 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 24 VDLTVPRGSVTVILGPSGSGKSTLLrciNELEDITA--GSVVVDGermgyrvdakgvvHRLHPKVVARQRRRIGMVFQRF 101
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLL---NALLGFLPyqGSLKING-------------IELRELDPESWRKHLSWVGQNP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 102 HLFpHLTATANVMeapmrvrgLSKADARTQALD-LLRRVGLADRADHYP-----------AQLSGGQQQRVAIARALAMD 169
Cdd:PRK11174 433 QLP-HGTLRDNVL--------LGNPDASDEQLQqALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQP 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 915259206 170 PELMLFDEPTSALDpeLVGEVLaVMKDL--AASGMTMIVVTHEIGFAREVaDEVVFMDQGVVVEQG 233
Cdd:PRK11174 504 CQLLLLDEPTASLD--AHSEQL-VMQALnaASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQG 565
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-242 |
5.35e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 90.17 E-value: 5.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 18 VHVLRgVDLTVPRGSVTV---------------ILGPSGSGKSTLLRCINEL---EDITAGSVVVDGERmgyrvdakgvV 79
Cdd:PRK09473 15 VKDLR-VTFSTPDGDVTAvndlnfslragetlgIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGRE----------I 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 80 HRLHPKVVARQR-RRIGMVFQ--RFHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGLAD---RADHYPAQLS 153
Cdd:PRK09473 84 LNLPEKELNKLRaEQISMIFQdpMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 154 GGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQ 232
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 243
|
250
....*....|
gi 915259206 233 GPPSEVLDAP 242
Cdd:PRK09473 244 GNARDVFYQP 253
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-242 |
5.45e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.08 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyrvdakgvvhRLHPKVVARQRRrigmvfq 99
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE----------SWSSKAFARKVA------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 rfHLFPHLTATANvmeapMRVR--------------GLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARA 165
Cdd:PRK10575 89 --YLPQQLPAAEG-----MTVRelvaigrypwhgalGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAML 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 915259206 166 LAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAP 242
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-242 |
5.76e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 89.96 E-value: 5.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 15 HSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCI-NELED---ITAgsvvvdgERMGYR-VDakgvVHRLHPkvvaR 89
Cdd:COG4170 17 QGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcGITKDnwhVTA-------DRFRWNgID----LLKLSP----R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 90 QRRR-----IGMVFQ--RFHLFPHLTATANVMEA----PMRVRGLSKADAR-TQALDLLRRVGLADRAD---HYPAQLSG 154
Cdd:COG4170 82 ERRKiigreIAMIFQepSSCLDPSAKIGDQLIEAipswTFKGKWWQRFKWRkKRAIELLHRVGIKDHKDimnSYPHELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 155 GQQQRVAIARALAMDPELMLFDEPTSALDPELVGEV---LAVMKDLaaSGMTMIVVTHEIGFAREVADEVVFMDQGVVVE 231
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIfrlLARLNQL--QGTSILLISHDLESISQWADTITVLYCGQTVE 239
|
250
....*....|.
gi 915259206 232 QGPPSEVLDAP 242
Cdd:COG4170 240 SGPTEQILKSP 250
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
10-248 |
7.14e-21 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 89.86 E-value: 7.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 10 EFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINeleDITAGSVVVDGERMgyRVDAKGVVhRLHPkvvaR 89
Cdd:PRK15093 12 EFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIC---GVTKDNWRVTADRM--RFDDIDLL-RLSP----R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 90 QRRR-----IGMVFQRFH--LFPHLTATANVMEA----PMRVRGLSKADAR-TQALDLLRRVGLADRAD---HYPAQLSG 154
Cdd:PRK15093 82 ERRKlvghnVSMIFQEPQscLDPSERVGRQLMQNipgwTYKGRWWQRFGWRkRRAIELLHRVGIKDHKDamrSFPYELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 155 GQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQG 233
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
250
....*....|....*
gi 915259206 234 PPSEVLDAPREQRTR 248
Cdd:PRK15093 242 PSKELVTTPHHPYTQ 256
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-233 |
1.39e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 86.82 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 18 VHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrvdakgvvhRLHPKVvarqrrRIGMV 97
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--------------RVSSLL------GLGGG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 98 FQrfhlfPHLTATANVMeAPMRVRGLSKADARtqalDLLRRV----GLADRAD----HYpaqlSGGQQQRVAIARALAMD 169
Cdd:cd03220 95 FN-----PELTGRENIY-LNGRLLGLSRKEID----EKIDEIiefsELGDFIDlpvkTY----SSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 170 PELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQG 233
Cdd:cd03220 161 PDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-209 |
3.12e-20 |
|
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: 85.62 E-value: 3.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVvvdgermgyrvdakgvvhRLHPKVVARQRrriGMVFQ 99
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV------------------LLNGGPLDFQR---DSIAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPT 179
Cdd:cd03231 74 GLLYLGHAPGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|
gi 915259206 180 SALDPELVGEVLAVMKDLAASGMTMIVVTH 209
Cdd:cd03231 154 TALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
8-241 |
3.93e-20 |
|
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: 89.03 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 8 HKEFGHGHSAvHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyRVDakgvVHRLhpkvv 87
Cdd:TIGR01193 478 DVSYSYGYGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLK-DID----RHTL----- 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 88 arqRRRIGMVFQRFHLFPH-------LTATANVMEApMRVRGLSKADARTQALDLlrRVGLADRADHYPAQLSGGQQQRV 160
Cdd:TIGR01193 547 ---RQFINYLPQEPYIFSGsilenllLGAKENVSQD-EIWAACEIAEIKDDIENM--PLGYQTELSEEGSSISGGQKQRI 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 161 AIARALAMDPELMLFDEPTSALDpeLVGEVLAVMKDLAASGMTMIVVTHEIGFAREVaDEVVFMDQGVVVEQGPPSEVLD 240
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLD--TITEKKIVNNLLNLQDKTIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLD 697
|
.
gi 915259206 241 A 241
Cdd:TIGR01193 698 R 698
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-225 |
4.94e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.81 E-value: 4.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 3 ELTGIHKEFghghSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYR--VDAkgvvh 80
Cdd:PRK11288 6 SFDGIGKTF----PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAstTAA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 rLHPKVVarqrrrigMVFQRFHLFPHLTATANVM--EAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQ 158
Cdd:PRK11288 77 -LAAGVA--------IIYQELHLVPEMTVAENLYlgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 915259206 159 RVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEV-VFMD 225
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAItVFKD 215
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-229 |
4.99e-20 |
|
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: 85.60 E-value: 4.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 16 SAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMG-YRvdakgvvHR-LHPKVVarqrrr 93
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISqYE-------HKyLHSKVS------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 94 igMVFQRFHLFPHlTATANV--------MEAPMRVRGLSKADARTQALDLlrrvGLADRADHYPAQLSGGQQQRVAIARA 165
Cdd:cd03248 92 --LVGQEPVLFAR-SLQDNIayglqscsFECVKEAAQKAHAHSFISELAS----GYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 166 LAMDPELMLFDEPTSALDPELVGEVLAVMKDlAASGMTMIVVTHEIGFArEVADEVVFMDQGVV 229
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-209 |
5.22e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 84.86 E-value: 5.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 19 HVL-RGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvvhrlhpkvVARQRRRigmv 97
Cdd:PRK13538 14 RILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP------------------IRRQRDE---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 98 FQRFHLF--------PHLTATANVMEApMRVRGLSKADARTQALdllRRVGLADRADHYPAQLSGGQQQRVAIARALAMD 169
Cdd:PRK13538 72 YHQDLLYlghqpgikTELTALENLRFY-QRLHGPGDDEALWEAL---AQVGLAGFEDVPVRQLSAGQQRRVALARLWLTR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 915259206 170 PELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTH 209
Cdd:PRK13538 148 APLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-235 |
1.04e-19 |
|
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: 84.47 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrVDAKGV-VHRLhpkvvarqRRRIGMVF 98
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDG------VDISKIgLHDL--------RSRISIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 99 Q---------RFHLFPHLTAT-ANVMEAPMRVrglsKADARTQALDLlrrvGLADRADHYPAQLSGGQQQRVAIARALAM 168
Cdd:cd03244 85 QdpvlfsgtiRSNLDPFGEYSdEELWQALERV----GLKEFVESLPG----GLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 915259206 169 DPELMLFDEPTSALDPELVGEVLAVMKDlAASGMTMIVVTHEIgfaREVA--DEVVFMDQGVVVEQGPP 235
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRL---DTIIdsDRILVLDKGRVVEFDSP 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-209 |
1.52e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.77 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRvDAKGVVHRL-HpkvvarqrrRIGMVf 98
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDP-DVAEACHYLgH---------RNAMK- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 99 qrfhlfPHLTATANVmEAPMRVRGlskaDARTQALDLLRRVGLADRAdHYPAQ-LSGGQQQRVAIARALAMDPELMLFDE 177
Cdd:PRK13539 86 ------PALTVAENL-EFWAAFLG----GEELDIAAALEAVGLAPLA-HLPFGyLSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180 190
....*....|....*....|....*....|..
gi 915259206 178 PTSALDPELVGEVLAVMKDLAASGMTMIVVTH 209
Cdd:PRK13539 154 PTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-209 |
1.60e-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: 83.56 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvvhrlHPKVVARQRRRIGMVFQ 99
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP--------------LAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPHLTATANvmeapMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPT 179
Cdd:TIGR01189 81 LPGLKPELSALEN-----LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|
gi 915259206 180 SALDPELVGEVLAVMKDLAASGMTMIVVTH 209
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
11-231 |
2.10e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 83.85 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 11 FGHGHSAV--HVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAKGVVHrlhpkvva 88
Cdd:COG2401 34 FGVELRVVerYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDA-------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 89 rqrrrigmvfqrfhlfphltatanvmeapmrvrgLSKADARTQALDLLRRVGLAD----RADhyPAQLSGGQQQRVAIAR 164
Cdd:COG2401 106 ----------------------------------IGRKGDFKDAVELLNAVGLSDavlwLRR--FKELSTGQKFRFRLAL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 915259206 165 ALAMDPELMLFDEPTSALDPELVGEVLAVMKDLA-ASGMTMIVVTHEIGFAREVA-DEVVFMDQGVVVE 231
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLArRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-224 |
3.23e-19 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 86.38 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 26 LTVPR-GSVTVILGPSGSGKSTLLRcineledITAGSVV-----VDGErmgyrVDAKGVVHRlhpkvvarqrrrigmvFQ 99
Cdd:COG1245 93 LPVPKkGKVTGILGPNGIGKSTALK-------ILSGELKpnlgdYDEE-----PSWDEVLKR----------------FR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPHLTATAN-----------VMEAPMRVRG-----LSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIA 163
Cdd:COG1245 145 GTELQDYFKKLANgeikvahkpqyVDLIPKVFKGtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIA 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 164 RALAMDPELMLFDEPTSALDpelVGEVLAV---MKDLAASGMTMIVVTHEIGFAREVADEVVFM 224
Cdd:COG1245 225 AALLRDADFYFFDEPSSYLD---IYQRLNVarlIRELAEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-232 |
5.19e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.83 E-value: 5.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFghghSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrVDAKGvvh 80
Cdd:PRK10762 4 LLQLKGIDKAF----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKE----VTFNG--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 rlhPKvvARQRRRIGMVFQRFHLFPHLTATANVM---EAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQ 157
Cdd:PRK10762 73 ---PK--SSQEAGIGIIHQELNLIPQLTIAENIFlgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 915259206 158 QRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEV-VFMDQGVVVEQ 232
Cdd:PRK10762 148 QMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVtVFRDGQFIAER 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-235 |
5.55e-19 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 86.22 E-value: 5.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 24 VDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAKgvvhrlhpkvvarqRRRIGMVFQRFHL 103
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAV--------------RQSLGMCPQHNIL 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 104 FPHLTATANVMEAPmRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPTSALD 183
Cdd:TIGR01257 1015 FHHLTVAEHILFYA-QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 915259206 184 PELVGEVLAVMKDLaASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPP 235
Cdd:TIGR01257 1094 PYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-227 |
6.56e-19 |
|
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: 80.19 E-value: 6.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVvvdgermgyrvdakgvvhR 81
Cdd:cd03221 1 IELENLSKTYG----GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------------T 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPKVvarqrrRIGmvfqrfhlfphltatanvmeapmrvrglskadartqaldllrrvgladradhYPAQLSGGQQQRVA 161
Cdd:cd03221 59 WGSTV------KIG----------------------------------------------------YFEQLSGGEKMRLA 80
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVgEVLAVMkdLAASGMTMIVVTHEIGFAREVADEVVFMDQG 227
Cdd:cd03221 81 LAKLLLENPNLLLLDEPTNHLDLESI-EALEEA--LKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-221 |
1.85e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.21 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 3 ELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCineLEDIT-----AGSVVVDGErmgyrvdakg 77
Cdd:PRK13549 7 EMKNITKTFG----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKV---LSGVYphgtyEGEIIFEGE---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 78 vvhrlhpKVVAR-----QRRRIGMVFQRFHLFPHLTATANV-MEAPMRVRGLSKADARTQ-ALDLLRRVGLADRADHYPA 150
Cdd:PRK13549 70 -------ELQASnirdtERAGIAIIHQELALVKELSVLENIfLGNEITPGGIMDYDAMYLrAQKLLAQLKLDINPATPVG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 915259206 151 QLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEV 221
Cdd:PRK13549 143 NLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTI 213
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-238 |
2.01e-18 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 83.25 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHghsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTllrcinelEDITAGSVVVDGERMGYRVDAKGVVHR 81
Cdd:NF000106 14 VEVRGLVKHFGE----VKAVDGVDLDVREGTVLGVLGP*GAA**R--------GALPAHV*GPDAGRRPWRF*TWCANRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 LHPKVVARQRRRIGMVFQRFHLFPHLTATANVMEapmrvrgLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVA 161
Cdd:NF000106 82 ALRRTIG*HRPVR*GRRESFSGRENLYMIGR*LD-------LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEV 238
Cdd:NF000106 155 LAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-239 |
2.25e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 84.02 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIhkefGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyrvDAKgvvHR 81
Cdd:NF033858 2 ARLEGV----SHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA---DAR---HR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 82 lhpkvvARQRRRIGMVFQRF--HLFPHLTATANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHyPA-QLSGGQQQ 158
Cdd:NF033858 72 ------RAVCPRIAYMPQGLgkNLYPTLSVFENL-DFFGRLFGQDAAERRRRIDELLRATGLAPFADR-PAgKLSGGMKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 159 RVAIARALAMDPELMLFDEPTSALDP-------ELVGEVLAvmkdlAASGMTMIVVTHEIGFArEVADEVVFMDQGVVVE 231
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEPTTGVDPlsrrqfwELIDRIRA-----ERPGMSVLVATAYMEEA-ERFDWLVAMDAGRVLA 217
|
....*...
gi 915259206 232 QGPPSEVL 239
Cdd:NF033858 218 TGTPAELL 225
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-233 |
5.05e-18 |
|
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: 80.07 E-value: 5.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 4 LTGIHKEFGHG-HSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDakgvvhrl 82
Cdd:cd03267 19 LIGSLKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 83 hpkvvaRQRRRIGMVF-QRFHLFPHLTA--TANVMEapmRVRGLSKADARTqaldllRRVGLADRAD-----HYPA-QLS 153
Cdd:cd03267 91 ------KFLRRIGVVFgQKTQLWWDLPVidSFYLLA---AIYDLPPARFKK------RLDELSELLDleellDTPVrQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 154 GGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQ 232
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
.
gi 915259206 233 G 233
Cdd:cd03267 236 G 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-238 |
6.71e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.38 E-value: 6.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 14 GHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyrvdakgvvhRLHPkvvaRQRRR 93
Cdd:COG3845 267 DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDIT----------GLSP----RERRR 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 94 IGMVF-----QRFHLFPHLTATANVM-----EAPMRVRG-LSKADARTQALDLLRRVGLADRADHYPA-QLSGGQQQRVA 161
Cdd:COG3845 333 LGVAYipedrLGRGLVPDMSVAENLIlgryrRPPFSRGGfLDRKAIRAFAEELIEEFDVRTPGPDTPArSLSGGNQQKVI 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 162 IARALAMDPELMLFDEPTSALDpelVGEVLAV---MKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEV 238
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLD---VGAIEFIhqrLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-230 |
1.62e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 81.54 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 25 DLTVPRGSVTVILGPSGSGKSTLLRcineledITAGSVVVDGERMGYRVDAkgVVHRLH---PK--------VVARQRRR 93
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMK-------ILNGEVLLDDGRIIYEQDL--IVARLQqdpPRnvegtvydFVAEGIEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 94 IGMVFQRFHLFPHLTAT----------ANVMEApMRVRGLSKADARTQalDLLRRVGLAdrADHYPAQLSGGQQQRVAIA 163
Cdd:PRK11147 94 QAEYLKRYHDISHLVETdpseknlnelAKLQEQ-LDHHNLWQLENRIN--EVLAQLGLD--PDAALSSLSGGWLRKAALG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 164 RALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASgmtMIVVTHEIGFAREVADEVVFMDQGVVV 230
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGS---IIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-230 |
3.91e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 78.00 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGHghsaVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrvdaKGVVH 80
Cdd:PRK11614 5 MLSFDKVSAHYGK----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG---------KDITD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 RLHPKVVarqRRRIGMVFQRFHLFPHLTATANVmeapmrVRGLSKADaRTQALDLLRRV-----GLADRADHYPAQLSGG 155
Cdd:PRK11614 72 WQTAKIM---REAVAIVPEGRRVFSRMTVEENL------AMGGFFAE-RDQFQERIKWVyelfpRLHERRIQRAGTMSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 915259206 156 QQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVV 230
Cdd:PRK11614 142 EQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-210 |
4.13e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 80.31 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCIneleditAGSVVVDGermgyrvdAKGVVHRLHPKVVARQRRRIGMVFQ 99
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQGNN--------FTGTILANNRKPTKQILKRTGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPHLTATAN-VMEAPMRV-RGLSKADARTQALDLLRRVGLAD-----RADHYPAQLSGGQQQRVAIARALAMDPEL 172
Cdd:PLN03211 148 DDILYPHLTVRETlVFCSLLRLpKSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSL 227
|
170 180 190
....*....|....*....|....*....|....*...
gi 915259206 173 MLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHE 210
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-247 |
7.10e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 77.28 E-value: 7.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 27 TVPRGSVTVILGPSGSGKSTLLRCINELEDiTAGSVVVDGERMGYRVDAKGVVHRLHpkVVARQRRRIGM-VFQRFHLfp 105
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHRAY--LSQQQTPPFAMpVFQYLTL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 106 HLTATANVmeapmrvrglskADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARA-LAMDPE------LMLFDEP 178
Cdd:PRK03695 93 HQPDKTRT------------EAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDinpagqLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 915259206 179 TSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLDAPREQRT 247
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQV 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-227 |
8.73e-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: 79.10 E-value: 8.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINEL--EDITAGSVVVDGERMGYRvdakgv 78
Cdd:TIGR02633 1 LLEMKGIVKTFG----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKAS------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 79 vhrlhpKVVARQRRRIGMVFQRFHLFPHLTATANV-MEAPMRVRGLSKADART--QALDLLRRVGLADRADHYP-AQLSG 154
Cdd:TIGR02633 71 ------NIRDTERAGIVIIHQELTLVPELSVAENIfLGNEITLPGGRMAYNAMylRAKNLLRELQLDADNVTRPvGDYGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 915259206 155 GQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQG 227
Cdd:TIGR02633 145 GQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-183 |
2.06e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.52 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrvdakgvVHRLHPKvvaRQRRRIGMVFQ 99
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGED----------ISTLKPE---IYRQQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPHlTATANVMeAPMRVRGlsKADARTQALDLLRRVGLADRADHYP-AQLSGGQQQRVAIARALAMDPELMLFDEP 178
Cdd:PRK10247 89 TPTLFGD-TVYDNLI-FPWQIRN--QQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
....*
gi 915259206 179 TSALD 183
Cdd:PRK10247 165 TSALD 169
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-231 |
2.84e-16 |
|
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: 77.53 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 24 VDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyRVDAKGvvhrlhpkvVARQRRRIGMVFQRFHL 103
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ----PVTADN---------REAYRQLFSAVFSDFHL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 104 FPHLTatanvmeapmrvrGLSKADARTQALDLLRRVGLADRADHY-----PAQLSGGQQQRVAIARALAMDPELMLFDEP 178
Cdd:COG4615 418 FDRLL-------------GLDGEADPARARELLERLELDHKVSVEdgrfsTTDLSQGQRKRLALLVALLEDRPILVFDEW 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 915259206 179 TSALDP--------ELVGEvlavmkdLAASGMTMIVVTHEIGFArEVADEVVFMDQGVVVE 231
Cdd:COG4615 485 AADQDPefrrvfytELLPE-------LKARGKTVIAISHDDRYF-DLADRVLKMDYGKLVE 537
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-240 |
8.05e-16 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 76.91 E-value: 8.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLrcineleditaGSVVVDGERMGYRVDAKGVVhrlhpKVVARQRRRIGMVFQR 100
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLL-----------SALLAEMDKVEGHVHMKGSV-----AYVPQQAWIQNDSLRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 101 FHLFPHLTAtanvmeaPMRVRGLSKADARTQALDLLRRvglADRAD--HYPAQLSGGQQQRVAIARALAMDPELMLFDEP 178
Cdd:TIGR00957 718 NILFGKALN-------EKYYQQVLEACALLPDLEILPS---GDRTEigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 179 TSALDPElVGE-----VLAVMKDLAasGMTMIVVTHEIGFAREVaDEVVFMDQGVVVEQGPPSEVLD 240
Cdd:TIGR00957 788 LSAVDAH-VGKhifehVIGPEGVLK--NKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
9-242 |
9.22e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 76.29 E-value: 9.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 9 KEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrvdakgvvHRLHPKVVA 88
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD-------------IPLTKLQLD 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 89 RQRRRIGMVFQRFHLFPHlTATANVmeapmrvrGLSKADARTQAL-----------DLLR-------RVGlaDRAdhypA 150
Cdd:PRK10789 386 SWRSRLAVVSQTPFLFSD-TVANNI--------ALGRPDATQQEIehvarlasvhdDILRlpqgydtEVG--ERG----V 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 151 QLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAsGMTMIVVTHEIGFAREvADEVVFMDQGVVV 230
Cdd:PRK10789 451 MLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSALTE-ASEILVMQHGHIA 528
|
250
....*....|..
gi 915259206 231 EQGPPSEVLDAP 242
Cdd:PRK10789 529 QRGNHDQLAQQS 540
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-183 |
1.90e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 1 MVELTGIHKEFGhghsAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDgermgyrvdakgvvh 80
Cdd:PRK09544 4 LVSLENVSVSFG----QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 rlhpkvvarQRRRIGMVFQRFHLFPHLTATanvMEAPMRVR-GLSKADArtqaLDLLRRVGLADRADHYPAQLSGGQQQR 159
Cdd:PRK09544 65 ---------GKLRIGYVPQKLYLDTTLPLT---VNRFLRLRpGTKKEDI----LPALKRVQAGHLIDAPMQKLSGGETQR 128
|
170 180
....*....|....*....|....
gi 915259206 160 VAIARALAMDPELMLFDEPTSALD 183
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-224 |
1.90e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.23 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 26 LTVPR-GSVTVILGPSGSGKSTLLRcineledITAGSVV-----VDGErmgyrVDAKGVVHRlhpkvvarqrrrigmvFQ 99
Cdd:PRK13409 93 LPIPKeGKVTGILGPNGIGKTTAVK-------ILSGELIpnlgdYEEE-----PSWDEVLKR----------------FR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPHLTATAN-----------VMEAPMRVRG-----LSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIA 163
Cdd:PRK13409 145 GTELQNYFKKLYNgeikvvhkpqyVDLIPKVFKGkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIA 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 164 RALAMDPELMLFDEPTSALDpelVGEVLAV---MKDLaASGMTMIVVTHEIGFAREVADEVVFM 224
Cdd:PRK13409 225 AALLRDADFYFFDEPTSYLD---IRQRLNVarlIREL-AEGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-244 |
2.01e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.21 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 22 RGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYR--VDA--KGVVHrlhpkvVARQRRRIGmv 97
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRspLDAvkKGMAY------ITESRRDNG-- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 98 fqrfhLFPHLTATANVMEAP-MRVRGLSKA----DARTQaldllRRVGLADRA---------DHYPAQLSGGQQQRVAIA 163
Cdd:PRK09700 352 -----FFPNFSIAQNMAISRsLKDGGYKGAmglfHEVDE-----QRTAENQREllalkchsvNQNITELSGGNQQKVLIS 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 164 RALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVveqgppSEVLDAPR 243
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL------TQILTNRD 495
|
.
gi 915259206 244 E 244
Cdd:PRK09700 496 D 496
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
7-233 |
5.61e-15 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 71.14 E-value: 5.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 7 IHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINeleDITAGSVVVDGERMGYRVDAKGVVHRLHpkv 86
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA---NRTEGNVSVEGDIHYNGIPYKEFAEKYP--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 87 varqrRRIGMVFQRFHLFPHLTatanvmeapmrVRGLSKADARTQALDLLRRVgladradhypaqlSGGQQQRVAIARAL 166
Cdd:cd03233 83 -----GEIIYVSEEDVHFPTLT-----------VRETLDFALRCKGNEFVRGI-------------SGGERKRVSIAEAL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 915259206 167 AMDPELMLFDEPTSALDPELVGEVLAVMKDLA-ASGMTMIVVTHEIG-FAREVADEVVFMDQGVVVEQG 233
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSSTALEILKCIRTMAdVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-227 |
6.18e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.82 E-value: 6.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 19 HVLRGVDLTVPRGSVTVILGPSGSGKSTLLRcineledITAGsvvVDGERMGYRVDAKGVvhrlhpkvvarqrrRIGMVF 98
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------IMAG---VDKDFNGEARPQPGI--------------KVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 99 QRFHLFPHLTATANVMEAPMRVRGL-----------SKADARTQAL-----------------DLLRRVGLADRADHYP- 149
Cdd:TIGR03719 75 QEPQLDPTKTVRENVEEGVAEIKDAldrfneisakyAEPDADFDKLaaeqaelqeiidaadawDLDSQLEIAMDALRCPp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 150 -----AQLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAAsgmTMIVVTHEIGFAREVADEVVFM 224
Cdd:TIGR03719 155 wdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVTHDRYFLDNVAGWILEL 231
|
...
gi 915259206 225 DQG 227
Cdd:TIGR03719 232 DRG 234
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-209 |
6.74e-15 |
|
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: 70.26 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGsvvvdgermgyrvdakgvvhrlhpkvvarqrrRIGMVFQ 99
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG--------------------------------RIGMPEG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFphltatanVMEAPMRVRGLskadartqaldlLRRVgLAdradhYP--AQLSGGQQQRVAIARALAMDPELMLFDE 177
Cdd:cd03223 64 EDLLF--------LPQRPYLPLGT------------LREQ-LI-----YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|..
gi 915259206 178 PTSALDPELVGEVLAVMKDLaasGMTMIVVTH 209
Cdd:cd03223 118 ATSALDEESEDRLYQLLKEL---GITVISVGH 146
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-227 |
1.12e-14 |
|
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: 72.94 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 24 VDLTVPRGSVTVILGPSGSGKSTLLRCI-NELEDITAGSVVVDGERMGYRVDAKGVVHRLhpKVVARQRRRIGMVfqrfh 102
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNPAQAIRAGI--AMVPEDRKRHGIV----- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 103 lfPHLTATANVMEAPMR---VRGLSKADARTQALDL-LRRVGLADRADHYP-AQLSGGQQQRVAIARALAMDPELMLFDE 177
Cdd:TIGR02633 352 --PILGVGKNITLSVLKsfcFKMRIDAAAELQIIGSaIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 915259206 178 PTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQG 227
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-239 |
2.03e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.01 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCineLEDITAGSVVVDGERMGYRVDAKG-VVHRLHPKVVARQRRRIGMVF 98
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKA---LAGDLTGGGAPRGARVTGDVTLNGePLAAIDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 99 QRFHLF-----------PHLTATAnvmEAPMRVRGL-SKADARTQALDLLRRvgladradhYPAQLSGGQQQRVAIARAL 166
Cdd:PRK13547 93 QPAFAFsareivllgryPHARRAG---ALTHRDGEIaWQALALAGATALVGR---------DVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 167 AM---------DPELMLFDEPTSALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPS 236
Cdd:PRK13547 161 AQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
...
gi 915259206 237 EVL 239
Cdd:PRK13547 241 DVL 243
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-246 |
4.34e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 71.31 E-value: 4.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 24 VDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERmgyrVDAKGVvhrlhpkvvaRQRRRIGMVFQRFHL 103
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP----VDAGDI----------ATRRRVGYMSQAFSL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 104 FPHLTATAN-VMEApmRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPTSAL 182
Cdd:NF033858 351 YGELTVRQNlELHA--RLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGV 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 183 DP-------ELvgevlavMKDLA-ASGMTMIVVTHeigFAREVA--DEVVFMDQGVVVEQGPPSEVldapREQR 246
Cdd:NF033858 429 DPvardmfwRL-------LIELSrEDGVTIFISTH---FMNEAErcDRISLMHAGRVLASDTPAAL----VAAR 488
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-254 |
5.39e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.16 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 24 VDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyRVDAKGVVHrlhpkvvarQRRRIGMVFQRFHL 103
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK----PVTAEQPED---------YRKLFSAVFTDFHL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 104 FPHLtatanvmeapMRVRGLSKADARTQAldLLRRVGLADRADH-----YPAQLSGGQQQRVAIARALAMDPELMLFDEP 178
Cdd:PRK10522 409 FDQL----------LGPEGKPANPALVEK--WLERLKMAHKLELedgriSNLKLSKGQKKRLALLLALAEERDILLLDEW 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 179 TSALDP----ELVGEVLAVMKdlaASGMTMIVVTHEIGFArEVADEVVFMDQGVVveqgppSEVLDAPREQRTRDFLAHV 254
Cdd:PRK10522 477 AADQDPhfrrEFYQVLLPLLQ---EMGKTIFAISHDDHYF-IHADRLLEMRNGQL------SELTGEERDAASRDAVART 546
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-254 |
8.07e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 68.97 E-value: 8.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 27 TVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRvdakgvvhrlhP-KVVARQrrrigmvfqrfhlfp 105
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYK-----------PqYIKADY--------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 106 hltatanvmeaPMRVRGL--SK-ADARTQAL---DLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPT 179
Cdd:cd03237 75 -----------EGTVRDLlsSItKDFYTHPYfktEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 180 SALDPELVGEVLAVMKDLAASG-MTMIVVTHEIGFAREVADEVVFMDqgvvveqGPPSEVLDAPREQRTRD----FLAHV 254
Cdd:cd03237 144 AYLDVEQRLMASKVIRRFAENNeKTAFVVEHDIIMIDYLADRLIVFE-------GEPSVNGVANPPQSLRSgmnrFLKNL 216
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-233 |
9.72e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.58 E-value: 9.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDgermgyrvdakgvvhrlhpkvvarqrRRIGMVFQ 99
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE--------------------------RSIAYVPQ 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RfhlfphltatANVMEAPMRVRGLSKADARTQALDLLRRV------------GLADRADHYPAQLSGGQQQRVAIARALA 167
Cdd:PTZ00243 729 Q----------AWIMNATVRGNILFFDEEDAARLADAVRVsqleadlaqlggGLETEIGEKGVNLSGGQKARVSLARAVY 798
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 915259206 168 MDPELMLFDEPTSALDPElVGEvlAVMKDL---AASGMTMIVVTHEIGFArEVADEVVFMDQGVVVEQG 233
Cdd:PTZ00243 799 ANRDVYLLDDPLSALDAH-VGE--RVVEECflgALAGKTRVLATHQVHVV-PRADYVVALGDGRVEFSG 863
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-233 |
1.48e-13 |
|
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: 66.96 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 18 VHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINEleditagsvvvdgermgyrvdakgvvhrlhpkvvARQRRRIGMV 97
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY----------------------------------ASGKARLISF 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 98 FQRFhlFPHLTAtanvmeapmrvrglskadaRTQALDLLRRVGLADRADHYPAQ-LSGGQQQRVAIARALAMDPE--LML 174
Cdd:cd03238 54 LPKF--SRNKLI-------------------FIDQLQFLIDVGLGYLTLGQKLStLSGGELQRVKLASELFSEPPgtLFI 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 915259206 175 FDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREvADEVVFM------DQGVVVEQG 233
Cdd:cd03238 113 LDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-227 |
1.58e-13 |
|
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: 67.74 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 16 SAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCI-NELEDITaGSVvvdgermgyRVDAKGVVHRLHPKVVARQRRRI 94
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAIlGEMQTLE-GKV---------HWSNKNESEPSFEATRSRNRYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 95 GMVFQRFHLFpHLTATANV-MEAPM---RVRGLSKADARTQALDLL---RRVGLADRAdhypAQLSGGQQQRVAIARALA 167
Cdd:cd03290 82 AYAAQKPWLL-NATVEENItFGSPFnkqRYKAVTDACSLQPDIDLLpfgDQTEIGERG----INLSGGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 915259206 168 MDPELMLFDEPTSALDPELVGEVL--AVMKDLAASGMTMIVVTHEIGFAREvADEVVFMDQG 227
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-235 |
1.66e-13 |
|
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: 67.44 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrVDAKGV-VHRLhpkvvarqRRRIGMVF 98
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG------IDISTIpLEDL--------RSSLTIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 99 QRFHLFPHlTATANVmeapmrvrglskadartqaldllrrvglaDRADHYP--------------AQLSGGQQQRVAIAR 164
Cdd:cd03369 89 QDPTLFSG-TIRSNL-----------------------------DPFDEYSdeeiygalrvseggLNLSQGQRQLLCLAR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 915259206 165 ALAMDPELMLFDEPTSALDPELVGEVLAVMKDLaASGMTMIVVTHEIgfaREVA--DEVVFMDQGVVVEQGPP 235
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALIQKTIREE-FTNSTILTIAHRL---RTIIdyDKILVMDAGEVKEYDHP 207
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
31-227 |
2.40e-13 |
|
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: 66.50 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 31 GSVTVILGPSGSGKSTLLRCINELEdiTAGsvVVDGERM--GYRVDAKgvvhrlhpkvvarQRRRIGMVFQRFHLFPHLT 108
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAGRK--TAG--VITGEILinGRPLDKN-------------FQRSTGYVEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 109 atanVMEApMR----VRGLSKAdartqaldllrrvgladradhypaqlsggQQQRVAIARALAMDPELMLFDEPTSALDP 184
Cdd:cd03232 96 ----VREA-LRfsalLRGLSVE-----------------------------QRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 915259206 185 ELVGEVLAVMKDLAASGMTMIVVTHEIG---FarEVADEVVFMDQG 227
Cdd:cd03232 142 QAAYNIVRFLKKLADSGQAILCTIHQPSasiF--EKFDRLLLLKRG 185
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-210 |
2.70e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 69.37 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCineLEDITAGSVVVDGERMgyrVDAkgvvhrlhPKVVARQRRRIGMVFQ 99
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNV---LAERVTTGVITGGDRL---VNG--------RPLDSSFQRSIGYVQQ 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 R-FHLfphltATANVMEA---------PMRVRGLSKADARTQALDLLRRVGLADRADHYPAQ-LSGGQQQRVAIARALAM 168
Cdd:TIGR00956 844 QdLHL-----PTSTVRESlrfsaylrqPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVA 918
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 915259206 169 DPELMLF-DEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHE 210
Cdd:TIGR00956 919 KPKLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-234 |
4.11e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.80 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 18 VHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCineLEDI---TAGSVVVDG-----ERMGYrvdakgvvhrlhpkvvar 89
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKM---LTGIlvpTSGEVRVLGyvpfkRRKEF------------------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 90 qRRRIGMVF-QRFHLFPHLTA--TANVMEApmrVRGLSKADARtQALDLLRRV-GLAD------RadhypaQLSGGQQQR 159
Cdd:COG4586 94 -ARRIGVVFgQRSQLWWDLPAidSFRLLKA---IYRIPDAEYK-KRLDELVELlDLGElldtpvR------QLSLGQRMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 915259206 160 VAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDL-AASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGP 234
Cdd:COG4586 163 CELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-211 |
4.40e-13 |
|
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: 67.01 E-value: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 26 LTVPR-GSVTVILGPSGSGKSTLLRcineledITAGSVVVDGERMGYRVDAKGVV--------HRLHPKVVARQRRRIgM 96
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALK-------ILAGKLKPNLGKFDDPPDWDEILdefrgselQNYFTKLLEGDVKVI-V 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 97 VFQRFHLFPHlTATANVMEApmrvrgLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFD 176
Cdd:cd03236 92 KPQYVDLIPK-AVKGKVGEL------LKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190
....*....|....*....|....*....|....*
gi 915259206 177 EPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEI 211
Cdd:cd03236 165 EPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-227 |
5.57e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 4 LTGIHKEFghghSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAKGVVHRlh 83
Cdd:PRK10982 1 MSNISKSF----PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENG-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 84 pkvvarqrrrIGMVFQRFHLFPHLTATANVMEAPMRVRGL----SKADARTQAL--DLLRRVGLADRAdhypAQLSGGQQ 157
Cdd:PRK10982 75 ----------ISMVHQELNLVLQRSVMDNMWLGRYPTKGMfvdqDKMYRDTKAIfdELDIDIDPRAKV----ATLSVSQM 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 158 QRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQG 227
Cdd:PRK10982 141 QMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-233 |
5.81e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.23 E-value: 5.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 19 HVLRGVDLTVPRGSVTVILGPSGSGKSTLLRC-INELEDITAGSVVVDGeRMGYRvdakgvvhrlhPKVV----ARQRRR 93
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAmLGELPPRSDASVVIRG-TVAYV-----------PQVSwifnATVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 94 I--GMVFQrfhlfphltatANVMEAPMRVRGLSkadartQALDLLRRVGLADRADHyPAQLSGGQQQRVAIARALAMDPE 171
Cdd:PLN03130 699 IlfGSPFD-----------PERYERAIDVTALQ------HDLDLLPGGDLTEIGER-GVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 915259206 172 LMLFDEPTSALDPELVGEVL-AVMKDlAASGMTMIVVTHEIGFAREVaDEVVFMDQGVVVEQG 233
Cdd:PLN03130 761 VYIFDDPLSALDAHVGRQVFdKCIKD-ELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-238 |
1.28e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.31 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLLRC-INELEDITAGSVVVDGErMGYRVDAKGVVHrlhpkVVARQRRRIGMVFQ 99
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVIRGS-VAYVPQVSWIFN-----ATVRENILFGSDFE 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 rfhlfphltatanvmeaPMRVRGLSKADARTQALDLL---RRVGLADRAdhypAQLSGGQQQRVAIARALAMDPELMLFD 176
Cdd:PLN03232 707 -----------------SERYWRAIDVTALQHDLDLLpgrDLTEIGERG----VNISGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 915259206 177 EPTSALDPELVGEVL-AVMKDlAASGMTMIVVTHEIGFAREVaDEVVFMDQGVVVEQGPPSEV 238
Cdd:PLN03232 766 DPLSALDAHVAHQVFdSCMKD-ELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAEL 826
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
36-196 |
2.38e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.30 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 36 ILGPSGSGKSTLLRcineledITAGsvvVDGERMGYRVDAKGVvhrlhpkvvarqrrRIGMVFQRFHLFPHLTATANVME 115
Cdd:PRK11819 38 VLGLNGAGKSTLLR-------IMAG---VDKEFEGEARPAPGI--------------KVGYLPQEPQLDPEKTVRENVEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 116 APMRVRGL-----------SKADARTQAL-----------------DLLRRVGLADRADHYP------AQLSGGQQQRVA 161
Cdd:PRK11819 94 GVAEVKAAldrfneiyaayAEPDADFDALaaeqgelqeiidaadawDLDSQLEIAMDALRCPpwdakvTKLSGGERRRVA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELV-----------GEVLAVMKD 196
Cdd:PRK11819 174 LCRLLLEKPDMLLLDEPTNHLDAESVawleqflhdypGTVVAVTHD 219
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-254 |
3.44e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.90 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 18 VHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINeleditagsvvvdGERMGYRVDAKGVVH-RLHPKVVARQRRRIGM 96
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIA-------------SNTDGFHIGVEGVITyDGITPEEIKKHYRGDV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 97 VF---QRFHlFPHLTA-----TANVMEAP-MRVRGLSKADARTQALDL-LRRVGLADR-----ADHYPAQLSGGQQQRVA 161
Cdd:TIGR00956 141 VYnaeTDVH-FPHLTVgetldFAARCKTPqNRPDGVSREEYAKHIADVyMATYGLSHTrntkvGNDFVRGVSGGERKRVS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 162 IARALAMDPELMLFDEPTSALDPELVGEVLAVMKdlaasgmTMIVVTHEIGF---------AREVADEVVFMDQGVVVEQ 232
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDSATALEFIRALK-------TSANILDTTPLvaiyqcsqdAYELFDKVIVLYEGYQIYF 292
|
250 260 270
....*....|....*....|....*....|
gi 915259206 233 GPPSEVL--------DAPREQRTRDFLAHV 254
Cdd:TIGR00956 293 GPADKAKqyfekmgfKCPDRQTTADFLTSL 322
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
20-209 |
4.57e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.33 E-value: 4.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrvdakgvvhrlHPKVVARQRRRIGMVFq 99
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG----------------KTATRGDRSRFMAYLG- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 rfHLfPHLTATANVMEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPT 179
Cdd:PRK13543 89 --HL-PGLKADLSTLENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
170 180 190
....*....|....*....|....*....|
gi 915259206 180 SALDPELVGEVLAVMKDLAASGMTMIVVTH 209
Cdd:PRK13543 166 ANLDLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-230 |
5.65e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 5.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 24 VDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYR--VDA--KGVVhrLHPKvvarQRRRIGMVfq 99
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRspRDAirAGIM--LCPE----DRKAEGII-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 rfhlfphltATANVMEApmrvRGLSKADARTQALDLLRRVGLADRADHYPAQ--------------LSGGQQQRVAIARA 165
Cdd:PRK11288 344 ---------PVHSVADN----INISARRHHLRAGCLINNRWEAENADRFIRSlniktpsreqlimnLSGGNQQKAILGRW 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 915259206 166 LAMDPELMLFDEPTSALDpelVG---EVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVV 230
Cdd:PRK11288 411 LSEDMKVILLDEPTRGID---VGakhEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-238 |
7.26e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.19 E-value: 7.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTV-PRGSVTvILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGyrvdAKGVvhrlhpkvvaRQ-RRRIGMV 97
Cdd:PTZ00243 1325 VLRGVSFRIaPREKVG-IVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG----AYGL----------RElRRQFSMI 1389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 98 FQRFHLF---------PHLTATANVMEAPMRVRGLSKADARTQAldllrrvGLADRADHYPAQLSGGQQQRVAIARA-LA 167
Cdd:PTZ00243 1390 PQDPVLFdgtvrqnvdPFLEASSAEVWAALELVGLRERVASESE-------GIDSRVLEGGSNYSVGQRQLMCMARAlLK 1462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 168 MDPELMLFDEPTSALDPELVGEVLA-VMKdlAASGMTMIVVTHEIgfaREVA--DEVVFMDQGVVVEQGPPSEV 238
Cdd:PTZ00243 1463 KGSGFILMDEATANIDPALDRQIQAtVMS--AFSAYTVITIAHRL---HTVAqyDKIIVMDHGAVAEMGSPREL 1531
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
148-241 |
3.53e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.12 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 148 YPAQLSGGQQQRVAIARALAMDPELMLFDEPTSALDP---ELVGEVLAVMKDLAASgmTMIVVTHEIGFAREVADEVVFM 224
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKADK--TIITIAHRIASIKRSDKIVVFN 1432
|
90 100
....*....|....*....|.
gi 915259206 225 D---QGVVVE-QGPPSEVLDA 241
Cdd:PTZ00265 1433 NpdrTGSFVQaHGTHEELLSV 1453
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
20-209 |
4.52e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.96 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELED--ITAGSVVVDG---------ERMG--------YRVDAKGVVH 80
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGkdllelspeDRAGegifmafqYPVEIPGVSN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 81 R--LHPKVVARQRRRIGMVFQRFHLfphltatANVMEAPMRVRGLSKadartqalDLLRR---VGladradhypaqLSGG 155
Cdd:PRK09580 96 QffLQTALNAVRSYRGQEPLDRFDF-------QDLMEEKIALLKMPE--------DLLTRsvnVG-----------FSGG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 915259206 156 QQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTH 209
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
28-209 |
7.92e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 61.69 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 28 VPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDgermgyrvdakgvvhrlhpkvvarQRRRIGMVFQRfhlfPHL 107
Cdd:TIGR00954 475 VPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP------------------------AKGKLFYVPQR----PYM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 108 TATA--NVMEAPMRV-----RGLSKADARtQALDLL-------RRVGLADRADhYPAQLSGGQQQRVAIARALAMDPELM 173
Cdd:TIGR00954 527 TLGTlrDQIIYPDSSedmkrRGLSDKDLE-QILDNVqlthileREGGWSAVQD-WMDVLSGGEKQRIAMARLFYHKPQFA 604
|
170 180 190
....*....|....*....|....*....|....*.
gi 915259206 174 LFDEPTSALDPELVGEVLAVMKDLaasGMTMIVVTH 209
Cdd:TIGR00954 605 ILDECTSAVSVDVEGYMYRLCREF---GITLFSVSH 637
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
18-233 |
8.22e-11 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 59.96 E-value: 8.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 18 VHVLRGVDLTVPRGSVTVILGPSGSGKSTLlrcinELEDITAgsvvvDGERmgyrvdakgvvhRLHPKVVARQRRRIGMv 97
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSL-----AFDTIYA-----EGQR------------RYVESLSAYARQFLGQ- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 98 fqrfhlfphltatanvMEAPM--RVRGLSKADA----------------RTQALDLLR----RVGLADRAD-------HY 148
Cdd:cd03270 65 ----------------MDKPDvdSIEGLSPAIAidqkttsrnprstvgtVTEIYDYLRllfaRVGIRERLGflvdvglGY 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 149 ------PAQLSGGQQQRVAIARALAMDPE--LMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREvADE 220
Cdd:cd03270 129 ltlsrsAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADH 207
|
250
....*....|...
gi 915259206 221 VVFMDQGVVVEQG 233
Cdd:cd03270 208 VIDIGPGAGVHGG 220
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-241 |
9.75e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.50 E-value: 9.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgyrvdAKGVVHRLhpkvvarqRRRIGMVFQ 99
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI-----AKIGLHDL--------RFKITIIPQ 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFphlTATANVMEAPMRvrGLSKADARTqALDLLRRVG----LADRADHYPAQ----LSGGQQQRVAIARALAMDPE 171
Cdd:TIGR00957 1368 DPVLF---SGSLRMNLDPFS--QYSDEEVWW-ALELAHLKTfvsaLPDKLDHECAEggenLSVGQRQLVCLARALLRKTK 1441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 172 LMLFDEPTSALDPELVGEVLAVMKDlAASGMTMIVVTHEIGFAREVAdEVVFMDQGVVVEQGPPSEVLDA 241
Cdd:TIGR00957 1442 ILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
134-223 |
1.21e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 134 DLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAA-SGMTMIVVTHEIG 212
Cdd:PRK13409 436 EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEeREATALVVDHDIY 515
|
90
....*....|..
gi 915259206 213 FAREVADEV-VF 223
Cdd:PRK13409 516 MIDYISDRLmVF 527
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-241 |
1.41e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.89 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDG---ERMGYRVDAKGVVH-RLHPKVVARQrrrig 95
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplSSLSHSVLRQGVAMvQQDPVVLADT----- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 96 mvfqrfhLFPHLTATANVMEApmrvrGLSKADARTQALDLLRRV--GLADRADHYPAQLSGGQQQRVAIARALAMDPELM 173
Cdd:PRK10790 431 -------FLANVTLGRDISEE-----QVWQALETVQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 174 LFDEPTSALDPelvGEVLAVMKDLAA--SGMTMIVVTHEIGFAREvADEVVFMDQGVVVEQGPPSEVLDA 241
Cdd:PRK10790 499 ILDEATANIDS---GTEQAIQQALAAvrEHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
150-227 |
5.76e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.79 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 150 AQLSGGQQQRVAIARALAMDPELMLFDEPTSALDpelVG---EVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQ 226
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHE 480
|
.
gi 915259206 227 G 227
Cdd:PRK13549 481 G 481
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
20-233 |
5.85e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.11 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCI--NELEDITAGSVVVDGERMGYrvdakgvvhrLHPKvvARQRRRIGMV 97
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILD----------LEPE--ERAHLGIFLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 98 FQRfhlfphltatanvmeaPMRVRGLSKAD-------ARTQALDL---------------LRRVGLADRADHYPAQ--LS 153
Cdd:CHL00131 90 FQY----------------PIEIPGVSNADflrlaynSKRKFQGLpeldplefleiinekLKLVGMDPSFLSRNVNegFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 154 GGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHeigFARE----VADEVVFMDQGVV 229
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH---YQRLldyiKPDYVHVMQNGKI 230
|
....
gi 915259206 230 VEQG 233
Cdd:CHL00131 231 IKTG 234
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
19-233 |
6.21e-10 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 56.60 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 19 HVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCIneleditagSVVVdGERMgyrvdakgvvHRLHPKVVARQRRRIGMVF 98
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAI---------GLAL-GGAQ----------SATRRRSGVKAGCIVAAVS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 99 QRFHLFPHltatanvmeapmrvrglskadartqaldllrrvgladradhypaQLSGGQQQRVAIARALA---MDPE-LML 174
Cdd:cd03227 69 AELIFTRL--------------------------------------------QLSGGEKELSALALILAlasLKPRpLYI 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 915259206 175 FDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFArevADEVVFMDQGVVVEQG 233
Cdd:cd03227 105 LDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELA---ELADKLIHIKKVITGV 160
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-183 |
1.11e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.50 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 18 VHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGErmgyrvdakgvvHRLHPKVVARQRRRIGMV 97
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS------------HNLKDINLKWWRSKIGVV 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 98 FQRFHLFPH-------------------------------------------LTATANVMEAPMRVRGLSKADARTQAL- 133
Cdd:PTZ00265 466 SQDPLLFSNsiknnikyslyslkdlealsnyynedgndsqenknkrnscrakCAGDLNDMSNTTDSNELIEMRKNYQTIk 545
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 915259206 134 -----DLLRRVGLADRADHYP-----------AQLSGGQQQRVAIARALAMDPELMLFDEPTSALD 183
Cdd:PTZ00265 546 dsevvDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-223 |
1.42e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.87 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 27 TVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDgERMGYRvdakgvvhrlhPKVVARqrrrigmvfqrfhlfph 106
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISYK-----------PQYISP----------------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 107 ltatanvmEAPMRVRGLSKaDARTQALD-------LLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPT 179
Cdd:COG1245 413 --------DYDGTVEEFLR-SANTDDFGssyykteIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 915259206 180 SALDPELVGEVLAVMKDLAAS-GMTMIVVTHEIGFAREVADEV-VF 223
Cdd:COG1245 484 AHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLmVF 529
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-185 |
2.05e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 57.25 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHghsavHVL-RGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVdGE--RMGYrVDakgv 78
Cdd:TIGR03719 323 IEAENLTKAFGD-----KLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GEtvKLAY-VD---- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 79 vhrlhpkvvarQRRRigmvfqrfhlfpHLTATANVMEApmrVRG------LSKADARTQAL---------DLLRRVGlad 143
Cdd:TIGR03719 392 -----------QSRD------------ALDPNKTVWEE---ISGgldiikLGKREIPSRAYvgrfnfkgsDQQKKVG--- 442
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 915259206 144 radhypaQLSGGQQQRVAIARALAMDPELMLFDEPTSALDPE 185
Cdd:TIGR03719 443 -------QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
18-235 |
2.50e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 56.08 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 18 VHVLRGVDLTVPRGSVTVILGPSGSGKSTLlrcINElediTAGSVVvdgERMGYRVDAK-GVVHRLHP-----KVVARQR 91
Cdd:cd03271 8 ENNLKNIDVDIPLGVLTCVTGVSGSGKSSL---IND----TLYPAL---ARRLHLKKEQpGNHDRIEGlehidKVIVIDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 92 RRIGM-----------VF-------------QRFHlfphltatANVMEapMRVRGLSKAD-------------------A 128
Cdd:cd03271 78 SPIGRtprsnpatytgVFdeirelfcevckgKRYN--------RETLE--VRYKGKSIADvldmtveealeffenipkiA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 129 RTqaLDLLRRVGLAdradhY-----PA-QLSGGQQQRVAIARALAM---DPELMLFDEPTSALDPELVGEVLAVMKDLAA 199
Cdd:cd03271 148 RK--LQTLCDVGLG-----YiklgqPAtTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVD 220
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 915259206 200 SGMTMIVVTHEIGFAReVADEVVFMDQ------GVVVEQGPP 235
Cdd:cd03271 221 KGNTVVVIEHNLDVIK-CADWIIDLGPeggdggGQVVASGTP 261
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-184 |
3.30e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLrcineleditagSVVVDGERMGYRVDakgvvhrLHpkVVARQR-------- 91
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLL------------SLITGDHPQGYSND-------LT--LFGRRRgsgetiwd 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 92 --RRIGMVFQRFHLFPHLTATA-NVM------------EAPMRVRGLSKadartQALDLLrrvGLADR-ADHYPAQLSGG 155
Cdd:PRK10938 334 ikKHIGYVSSSLHLDYRVSTSVrNVIlsgffdsigiyqAVSDRQQKLAQ-----QWLDIL---GIDKRtADAPFHSLSWG 405
|
170 180
....*....|....*....|....*....
gi 915259206 156 QQQRVAIARALAMDPELMLFDEPTSALDP 184
Cdd:PRK10938 406 QQRLALIVRALVKHPTLLILDEPLQGLDP 434
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
152-227 |
5.54e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 5.54e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 915259206 152 LSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQG 227
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
16-238 |
1.61e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 55.02 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 16 SAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLlrcINE-LEDITAGSVVVDGERMGYRVDAKGVVHRlhPKVVARQRRRI 94
Cdd:TIGR00630 619 ARENNLKNITVSIPLGLFTCITGVSGSGKSTL---INDtLYPALANRLNGAKTVPGRYTSIEGLEHL--DKVIHIDQSPI 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 95 GM-----------VFQ--------------------RF----------------------HLFPHLTATANV-------- 113
Cdd:TIGR00630 694 GRtprsnpatytgVFDeirelfaetpeakvrgytpgRFsfnvkggrceacqgdgvikiemHFLPDVYVPCEVckgkrynr 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 114 --MEapMRVRGLSKAD--------AR---------TQALDLLRRVGLAdradhY-----PA-QLSGGQQQRVAIARAL-- 166
Cdd:TIGR00630 774 etLE--VKYKGKNIADvldmtveeAYeffeavpsiSRKLQTLCDVGLG-----YirlgqPAtTLSGGEAQRIKLAKELsk 846
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 915259206 167 -AMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAReVADEVVFMDQ------GVVVEQGPPSEV 238
Cdd:TIGR00630 847 rSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIK-TADYIIDLGPeggdggGTVVASGTPEEV 924
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
152-227 |
2.14e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 2.14e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 915259206 152 LSGGQQQRVAIARALAMDPELMLFDEPTSALDpelVG---EVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQG 227
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-227 |
2.61e-08 |
|
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: 51.61 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 30 RGSVTVILGPSGSGKSTLLRCI-NELEDITAGSVVVDGERMgyrvdakgvvhrlhpkvvarqrrrigmvfqrfhlfphlt 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDI--------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 109 atanvmeapmrvrglskadartqaLDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVG 188
Cdd:smart00382 42 ------------------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEA 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 915259206 189 EVLA------VMKDLAASGMTMIVVTHEIGF-----AREVADEVVFMDQG 227
Cdd:smart00382 98 LLLLleelrlLLLLKSEKNLTVILTTNDEKDlgpalLRRRFDRRIVLLLI 147
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
2-234 |
4.42e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.70 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLrcineleDITAGSVV---VDGE-RM-GY----- 71
Cdd:PLN03140 877 VDMPAEMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLM-------DVLAGRKTggyIEGDiRIsGFpkkqe 949
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 72 ---RVDAKGVVHRLH-PKVVARQrrriGMVFQRFhlfphltatanvMEAPMRVRGLSKADARTQALDLLRRVGLADRADH 147
Cdd:PLN03140 950 tfaRISGYCEQNDIHsPQVTVRE----SLIYSAF------------LRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVG 1013
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 148 YPA--QLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGF-AREVADEVVFM 224
Cdd:PLN03140 1014 LPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLM 1093
|
250
....*....|.
gi 915259206 225 DQ-GVVVEQGP 234
Cdd:PLN03140 1094 KRgGQVIYSGP 1104
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
152-229 |
4.48e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 4.48e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 915259206 152 LSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVV 229
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-239 |
5.83e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 5.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgYRVDAKGVVHrlhpkvvarQRRRIGMVFQ 99
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD----CDVAKFGLTD---------LRRVLSIIPQ 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFphlTATANVMEAPMRVR---GLSKADARTQALDLLRR--VGLADRADHYPAQLSGGQQQRVAIARALAMDPELML 174
Cdd:PLN03232 1318 SPVLF---SGTVRFNIDPFSEHndaDLWEALERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILV 1394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 915259206 175 FDEPTSALDPELVGEVLAVMKDLAASgMTMIVVTHEIGFAREvADEVVFMDQGVVVEQGPPSEVL 239
Cdd:PLN03232 1395 LDEATASVDVRTDSLIQRTIREEFKS-CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELL 1457
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
30-211 |
1.60e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 50.39 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 30 RGSVTVILGPSGSGKSTLLRCI------------NELEDI-----TAGSVVVDGERMG--YRVD-AKGVVHRLhpkVVAR 89
Cdd:COG0419 22 DDGLNLIVGPNGAGKSTILEAIryalygkarsrsKLRSDLinvgsEEASVELEFEHGGkrYRIErRQGEFAEF---LEAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 90 QRRRIGMVFQRFHL--FPHLTATANVMEAPMRVRGLSKADARTQALDLLRRV-GLADradhyPAQLSGGQQQRVAIARAL 166
Cdd:COG0419 99 PSERKEALKRLLGLeiYEELKERLKELEEALESALEELAELQKLKQEILAQLsGLDP-----IETLSGGERLRLALADLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 915259206 167 AmdpelMLFDepTSALDPELVGEVLAVMKDLAasgmtmiVVTHEI 211
Cdd:COG0419 174 S-----LILD--FGSLDEERLERLLDALEELA-------IITHVI 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
36-227 |
1.68e-07 |
|
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: 51.94 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 36 ILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAkgvVHR---LHPKVVARQRRRIGmvfqRFHLFPHltatan 112
Cdd:TIGR01257 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD---VHQnmgYCPQFDAIDDLLTG----REHLYLY------ 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 113 vmeapMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLA 192
Cdd:TIGR01257 2037 -----ARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWN 2111
|
170 180 190
....*....|....*....|....*....|....*
gi 915259206 193 VMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQG 227
Cdd:TIGR01257 2112 TIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
18-47 |
1.76e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 51.57 E-value: 1.76e-07
10 20 30
....*....|....*....|....*....|
gi 915259206 18 VHVLRGVDLTVPRGSVTVILGPSGSGKSTL 47
Cdd:COG0178 13 EHNLKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-210 |
1.87e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.33 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMgyrvdakgvvhrlhPKVVARQRRRIGMVFQ 99
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI--------------KKDLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPHLTATANVMeapmrvRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPELMLFDEPT 179
Cdd:PRK13540 82 RSGINPYLTLRENCL------YDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|.
gi 915259206 180 SALDPELVGEVLAVMKDLAASGMTMIVVTHE 210
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
152-249 |
2.04e-07 |
|
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: 49.49 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 152 LSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGM-TMIVVTHEIGFAREVADEvvfmdqgVVV 230
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDR-------IHV 144
|
90
....*....|....*....
gi 915259206 231 EQGPPSEVLDAPREQRTRD 249
Cdd:cd03222 145 FEGEPGVYGIASQPKGTRE 163
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-185 |
2.32e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.27 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 2 VELTGIHKEFGHghsavHVL-RGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVdGE--RMGYrVDakgv 78
Cdd:PRK11819 325 IEAENLSKSFGD-----RLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GEtvKLAY-VD---- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 79 vhrlhpkvvarQRRRigmvfqrfhlfpHLTATANVMEApmrVRGlskadartqALDLLrRVG---LADRAdhYPA----- 150
Cdd:PRK11819 394 -----------QSRD------------ALDPNKTVWEE---ISG---------GLDII-KVGnreIPSRA--YVGrfnfk 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 915259206 151 ---------QLSGGQQQRVAIARALAMDPELMLFDEPTSALDPE 185
Cdd:PRK11819 436 ggdqqkkvgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
151-222 |
2.46e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.40 E-value: 2.46e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 915259206 151 QLSGGQQQRVAIARALAMDPELMLFDEPTSALDpelVGEVLAVMKDLAASGMTMIVVTHeigfAREVADEVV 222
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSH----AREFLNTVV 408
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
152-210 |
2.69e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 2.69e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 915259206 152 LSGGQQQRVAIARALAMDPELMLFDEPTSALDpelVG---EVLAVMKDLAASGMTMIVVTHE 210
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSE 463
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-238 |
3.64e-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: 51.06 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCIneleditagsvvvdgerMGYRVDAKGVVhrlhpkvvaRQRRRIGMVFQ 99
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMI-----------------MGELEPSEGKI---------KHSGRISFSPQ 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPHlTATANVmeapmrVRGLSKADAR----TQALDLLRRVGLADRADHYP-----AQLSGGQQQRVAIARALAMDP 170
Cdd:TIGR01271 495 TSWIMPG-TIKDNI------IFGLSYDEYRytsvIKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDA 567
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 915259206 171 ELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREvADEVVFMDQGVVVEQGPPSEV 238
Cdd:TIGR01271 568 DLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSEL 634
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
151-239 |
8.81e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 8.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 151 QLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVV 230
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLA 214
|
....*....
gi 915259206 231 EQGPPSEVL 239
Cdd:PRK10938 215 ETGEREEIL 223
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
150-239 |
9.56e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.44 E-value: 9.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 150 AQLSGGQQQRVAIARALAmdPELM----LFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHE---IGFAREVAD--- 219
Cdd:PRK00635 475 ATLSGGEQERTALAKHLG--AELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLADRIIDigp 552
|
90 100
....*....|....*....|....*..
gi 915259206 220 -------EVVFmdqgvvveQGPPSEVL 239
Cdd:PRK00635 553 gagifggEVLF--------NGSPREFL 571
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-227 |
1.32e-06 |
|
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: 48.31 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCIneleditagsvvvdgerMGYRVDAKGVVhrlhpkvvaRQRRRIGMVFQ 99
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLI-----------------LGELEPSEGKI---------KHSGRISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 100 RFHLFPHlTATANVmeapmrVRGLSKADAR----TQALDLLRRVGLADRADHYP-----AQLSGGQQQRVAIARALAMDP 170
Cdd:cd03291 106 FSWIMPG-TIKENI------IFGVSYDEYRyksvVKACQLEEDITKFPEKDNTVlgeggITLSGGQRARISLARAVYKDA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 915259206 171 ELMLFDEPTSALDPELVGEVL--AVMKDLAASgmTMIVVTHEIGFAREvADEVVFMDQG 227
Cdd:cd03291 179 DLYLLDSPFGYLDVFTEKEIFesCVCKLMANK--TRILVTSKMEHLKK-ADKILILHEG 234
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
20-239 |
1.94e-06 |
|
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: 47.60 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGermgyrVD-AKGVVHRLhpkvvarqRRRIGMVF 98
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG------IDiSKLPLHTL--------RSRLSIIL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 99 Q---------RFHLFPHLTATANVMEAPMRVRGLSK-ADARTQALDLLRRVGladradhyPAQLSGGQQQRVAIARALAM 168
Cdd:cd03288 102 QdpilfsgsiRFNLDPECKCTDDRLWEALEIAQLKNmVKSLPGGLDAVVTEG--------GENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 915259206 169 DPELMLFDEPTSALDPElVGEVLAVMKDLAASGMTMIVVTHEIGFAREvADEVVFMDQGVVVEQGPPSEVL 239
Cdd:cd03288 174 KSSILIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
33-222 |
2.08e-06 |
|
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: 47.22 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 33 VTVILGPSGSGKSTLLRCIneleditagSVVVDGERmgyRVDAKGVVHRlhPKVVARQRRR--IGMVFQrfhlfphlTAT 110
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEAL---------KYALTGEL---PPNSKGGAHD--PKLIREGEVRaqVKLAFE--------NAN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 111 ANVMEApmrvrglskadarTQALDLLRRV------GLADRADHYPAQLSGGQQQ------RVAIARALAMDPELMLFDEP 178
Cdd:cd03240 82 GKKYTI-------------TRSLAILENVifchqgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEP 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 915259206 179 TSALDPELVGEVLA-VMKDLAA-SGMTMIVVTHEIGFaREVADEVV 222
Cdd:cd03240 149 TTNLDEENIEESLAeIIEERKSqKNFQLIVITHDEEL-VDAADHIY 193
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
18-47 |
2.82e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 48.15 E-value: 2.82e-06
10 20 30
....*....|....*....|....*....|
gi 915259206 18 VHVLRGVDLTVPRGSVTVILGPSGSGKSTL 47
Cdd:PRK00349 13 EHNLKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-239 |
3.18e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.81 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVpRGSVTV-ILGPSGSGKSTLLRCINELEDITAGSVVVDGermgYRVDAKGVvhrlhpkvvARQRRRIGMVF 98
Cdd:PLN03130 1254 VLHGLSFEI-SPSEKVgIVGRTGAGKSSMLNALFRIVELERGRILIDG----CDISKFGL---------MDLRKVLGIIP 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 99 Q---------RFHLFP---HltATANVMEApmrvrgLSKADARtqalDLLRR--VGLADRADHYPAQLSGGQQQRVAIAR 164
Cdd:PLN03130 1320 QapvlfsgtvRFNLDPfneH--NDADLWES------LERAHLK----DVIRRnsLGLDAEVSEAGENFSVGQRQLLSLAR 1387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915259206 165 ALAMDPELMLFDEPTSALDpelVGEVLAVMKDLAAS--GMTMIVVTHEIGFAREvADEVVFMDQGVVVEQGPPSEVL 239
Cdd:PLN03130 1388 ALLRRSKILVLDEATAAVD---VRTDALIQKTIREEfkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLL 1460
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
12-250 |
5.13e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.35 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 12 GHGHSAVHVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSVVVDGERMGYRVDAKgvvhrlhpkvvarqr 91
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAG--------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 92 rrigmvfqrfhLFPHLTATANVmEAPMRVRGLSKADARTQALDLLRRVGLADRADHYPAQLSGGQQQRVAIARALAMDPE 171
Cdd:PRK13546 96 -----------LSGQLTGIENI-EFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 172 LMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVVVEQGPPSEVLdaPR-EQRTRDF 250
Cdd:PRK13546 164 ILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL--PKyEAFLNDF 241
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
38-227 |
6.33e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 38 GPSGSGKSTLLRCI-NELEDiTAGSVVVD-GERMG-----------YRV-DakgVVHRLHPKV--VARQRRRIgmvfqrf 101
Cdd:PRK15064 34 GANGCGKSTFMKILgGDLEP-SAGNVSLDpNERLGklrqdqfafeeFTVlD---TVIMGHTELweVKQERDRI------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 102 HLFPHLTAtanvmEAPMRVRGLS---------KADARtqALDLLRRVGLADRaDHYP--AQLSGGQQQRVAIARALAMDP 170
Cdd:PRK15064 103 YALPEMSE-----EDGMKVADLEvkfaemdgyTAEAR--AGELLLGVGIPEE-QHYGlmSEVAPGWKLRVLLAQALFSNP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 915259206 171 ELMLFDEPTSALDPE----LVGEvlavmkdLAASGMTMIVVTHEIGFAREVADEVVFMDQG 227
Cdd:PRK15064 175 DILLLDEPTNNLDINtirwLEDV-------LNERNSTMIIISHDRHFLNSVCTHMADLDYG 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-211 |
2.45e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 44.46 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 3 ELTGIHKEFGHGhsavhVLRGVDLTVPRGSVTVILGPSGSGKSTLLRCINELEDiTAGSVVVDGermgyrVDAKGVVhrl 82
Cdd:cd03289 7 DLTAKYTEGGNA-----VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG------VSWNSVP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 83 hpkvVARQRRRIGMVFQRFHLFphltatanvmEAPMRvrglSKADARTQALD-----LLRRVGLADRADHYPAQL----- 152
Cdd:cd03289 72 ----LQKWRKAFGVIPQKVFIF----------SGTFR----KNLDPYGKWSDeeiwkVAEEVGLKSVIEQFPGQLdfvlv 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 915259206 153 ------SGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDlAASGMTMIVVTHEI 211
Cdd:cd03289 134 dggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRI 197
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
133-243 |
2.95e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.00 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 133 LDLLRRVGLA----DRAdhyPAQLSGGQQQRVAIARAL--AMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIV 206
Cdd:TIGR00630 469 LGFLIDVGLDylslSRA---AGTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIV 545
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 915259206 207 VTHEIGFAREvADEVVFMDQGV------VVEQGPPSEVLDAPR 243
Cdd:TIGR00630 546 VEHDEDTIRA-ADYVIDIGPGAgehggeVVASGTPEEILANPD 587
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
19-53 |
3.83e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.63 E-value: 3.83e-05
10 20 30
....*....|....*....|....*....|....*
gi 915259206 19 HVLRGVDLTVPRGSVTVILGPSGSGKSTLlrcINE 53
Cdd:COG0178 619 NNLKNVDVEIPLGVLTCVTGVSGSGKSTL---VND 650
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-231 |
4.01e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 16 SAVHVLRGVDLTVPRGSVTV-------ILGPSGSGKSTLLRCI-NELE------------------------DITAGSVV 63
Cdd:PRK10636 5 SSLQIRRGVRVLLDNATATInpgqkvgLVGKNGCGKSTLLALLkNEISadggsytfpgnwqlawvnqetpalPQPALEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 64 VDGERMgYRvdakgvvhRLHPKVVARQRRRIGmvfqrfhlfpHLTATANvmeapmrvrglSKADA------RTQALDLLR 137
Cdd:PRK10636 85 IDGDRE-YR--------QLEAQLHDANERNDG----------HAIATIH-----------GKLDAidawtiRSRAASLLH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 138 RVGLADRADHYPAQ-LSGGQQQRVAIARALAMDPELMLFDEPTSALDpelVGEVLAVMKDLAASGMTMIVVTHEIGFARE 216
Cdd:PRK10636 135 GLGFSNEQLERPVSdFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILISHDRDFLDP 211
|
250
....*....|....*
gi 915259206 217 VADEVVFMDQGVVVE 231
Cdd:PRK10636 212 IVDKIIHIEQQSLFE 226
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-229 |
4.55e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 20 VLRGVDLTVPRGSVTVILGPSGSGKSTLLRCI-NELEDITAGSVVVDGERMGY---------RVDAKGVVH--RLHPKVV 87
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLaGELAPVSGEIGLAKGIKLGYfaqhqleflRADESPLQHlaRLAPQEL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 88 ARQRRrigmvfqrfhlfphltatanvmeapmrvrglskadartqalDLLRRVGL-ADRADHYPAQLSGGQQQRVAIARAL 166
Cdd:PRK10636 407 EQKLR-----------------------------------------DYLGGFGFqGDKVTEETRRFSGGEKARLVLALIV 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 915259206 167 AMDPELMLFDEPTSALDPELVGEVLAVMKDLAASgmtMIVVTHEIGFAREVADEVVFMDQGVV 229
Cdd:PRK10636 446 WQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGA---LVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
133-243 |
5.64e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 133 LDLLRRVGLA----DRadhyPAQ-LSGGQQQRVAIARALAMdpELM--LF--DEPTSALDPELVGEVLAVMKDLAASGMT 203
Cdd:COG0178 466 LGFLVDVGLDyltlDR----SAGtLSGGEAQRIRLATQIGS--GLVgvLYvlDEPSIGLHQRDNDRLIETLKRLRDLGNT 539
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 915259206 204 MIVVTHEigfaREV---ADEVVFM------DQGVVVEQGPPSEVLDAPR 243
Cdd:COG0178 540 VIVVEHD----EDTiraADYIIDIgpgageHGGEVVAQGTPEEILKNPD 584
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
133-238 |
6.34e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 133 LDLLRRVGLAdradhY-----PA-QLSGGQQQRVAIARALAM---DPELMLFDEPTSALDPELVGEVLAVMKDLAASGMT 203
Cdd:COG0178 807 LQTLQDVGLG-----YiklgqPAtTLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNT 881
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 915259206 204 MIVVTHEIgfarEV---ADEVVFM-----DQ-GVVVEQGPPSEV 238
Cdd:COG0178 882 VVVIEHNL----DViktADWIIDLgpeggDGgGEIVAEGTPEEV 921
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
19-48 |
6.89e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.89 E-value: 6.89e-05
10 20 30
....*....|....*....|....*....|
gi 915259206 19 HVLRGVDLTVPRGSVTVILGPSGSGKSTLL 48
Cdd:pfam13555 10 GTFDGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
21-54 |
1.05e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.14 E-value: 1.05e-04
10 20 30
....*....|....*....|....*....|....
gi 915259206 21 LRGVDLTVPRGSVTVILGPSGSGKSTLlrcINEL 54
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTL---INET 655
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
24-224 |
1.79e-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: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 24 VDLTVPRGsVTVILGPSGSGKSTLLRCI--------NELEDITAGSVVVDGERMGYRVDAKGV--VHRLHPKVVARQRRR 93
Cdd:COG3950 19 IDFDNPPR-LTVLVGENGSGKTTLLEAIalalsgllSRLDDVKFRKLLIRNGEFGDSAKLILYygTSRLLLDGPLKKLER 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 94 IgmvfqRFHLFPHLTATANVMEAPMRVRGLSK-------------ADARTQALDLLR-------------RVGLADRAD- 146
Cdd:COG3950 98 L-----KEEYFSRLDGYDSLLDEDSNLREFLEwlreyledlenklSDELDEKLEAVRealnkllpdfkdiRIDRDPGRLv 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 147 --------HYPAQLSGGQQQRVA----IARALAM------DPELM----LFDEPTSALDPELVGEVLAVMKDLAASgMTM 204
Cdd:COG3950 173 ildkngeeLPLNQLSDGERSLLAlvgdLARRLAElnpaleNPLEGegivLIDEIDLHLHPKWQRRILPDLRKIFPN-IQF 251
|
250 260
....*....|....*....|
gi 915259206 205 IVVTHEIGFAREVADEVVFM 224
Cdd:COG3950 252 IVTTHSPLILSSLEDEEVIV 271
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
149-209 |
2.40e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.61 E-value: 2.40e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915259206 149 PAQLSGGQQQ---RVAIARALAMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTH 209
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
18-47 |
3.11e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 3.11e-04
10 20 30
....*....|....*....|....*....|
gi 915259206 18 VHVLRGVDLTVPRGSVTVILGPSGSGKSTL 47
Cdd:TIGR00630 9 EHNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
144-222 |
3.19e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 144 RADHYP-----AQLSGGQQQRVAIARAL---AMDPELMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAR 215
Cdd:PRK00635 797 GLDYLPlgrplSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK 876
|
....*..
gi 915259206 216 eVADEVV 222
Cdd:PRK00635 877 -VADYVL 882
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
133-255 |
3.67e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 133 LDLLRRVGLAdradhY-----PA-QLSGGQQQRVAIARALAMDPE---LMLFDEPTSALDPELVGEVLAVMKDLAASGMT 203
Cdd:PRK00349 811 LQTLVDVGLG-----YiklgqPAtTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNT 885
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 915259206 204 MIVVTHEIgfarEV---ADEVVFM-----DQ-GVVVEQGPPSEVLDAPrEQRTRDFLAHVL 255
Cdd:PRK00349 886 VVVIEHNL----DViktADWIIDLgpeggDGgGEIVATGTPEEVAKVE-ASYTGRYLKPVL 941
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-62 |
4.38e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 4.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 915259206 2 VELTGIHKEFGHGHsavhVLRGVDLTVPRGSVTVILGPSGSGKSTLLRC-INELEdITAGSV 62
Cdd:PRK15064 320 LEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTlVGELE-PDSGTV 376
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
23-229 |
4.68e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 23 GVDLTvprgSVTVILGPSGSGKSTLLRCIN-ELEDITagsvvvdgermgyrvdakGVVHRlHPKVvarqrrRIGmVFQRF 101
Cdd:PLN03073 531 GIDLD----SRIAMVGPNGIGKSTILKLISgELQPSS------------------GTVFR-SAKV------RMA-VFSQH 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 102 HLfPHLTATANVMEAPMRV-RGLSKADARTQaldlLRRVGLADRADHYPA-QLSGGQQQRVAIARALAMDPELMLFDEPT 179
Cdd:PLN03073 581 HV-DGLDLSSNPLLYMMRCfPGVPEQKLRAH----LGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPS 655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 915259206 180 SALDpelVGEVLAVMKDLAASGMTMIVVTHEIGFAREVADEVVFMDQGVV 229
Cdd:PLN03073 656 NHLD---LDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
25-62 |
5.07e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.68 E-value: 5.07e-04
10 20 30
....*....|....*....|....*....|....*...
gi 915259206 25 DLTVPRGSVTVILGPSGSGKSTLLRCINELEDITAGSV 62
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDALRFLSDAARGGL 52
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-248 |
5.59e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 131 QALDLLRRVGLA-----DRADhypaQLSGGQQQRVAIARALAMDPE--LMLFDEPTSALDPELVGEVLAVMKDLAASGMT 203
Cdd:PRK00635 1366 NRLTFIDKVGLSyitlgQEQD----TLSDGEHYRLHLAKKISSNLTdiIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNT 1441
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 915259206 204 MIVVTHEiGFAREVADEVVFMDQGVVVEQG----PPSEVLDAPREQRTR 248
Cdd:PRK00635 1442 VIATDRS-GSLAEHADHLIHLGPGSGPQGGyllsTSALKQSQPDLHNTR 1489
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
19-48 |
6.80e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 6.80e-04
10 20 30
....*....|....*....|....*....|
gi 915259206 19 HVLRGVDLTVPRGSVTVILGPSGSGKSTLL 48
Cdd:PRK00635 949 HNLKHIDLSLPRNALTAVTGPSASGKHSLV 978
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
33-51 |
1.11e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.02 E-value: 1.11e-03
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
28-47 |
1.37e-03 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 38.74 E-value: 1.37e-03
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
30-62 |
1.59e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.53 E-value: 1.59e-03
10 20 30
....*....|....*....|....*....|...
gi 915259206 30 RGSVTVILGPSGSGKSTLLRCINELEDITAGSV 62
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
151-198 |
1.92e-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: 1.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 915259206 151 QLSGGQQQRVAIARALAM---DPELM-LFDEPTSALDPELVGEVLAVMKDLA 198
Cdd:cd03272 158 QLSGGQKSLVALALIFAIqkcDPAPFyLFDEIDAALDAQYRTAVANMIKELS 209
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
150-227 |
3.47e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.66 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 150 AQLSGGQQQRVAIARALAMDPE---LMLFDEPTSALDPELVGEVLAVMKDLAASGMTMIVVTHEIGFAREvADEVVFMDQ 226
Cdd:PRK00635 1698 SSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQ-ADYLIEMGP 1776
|
.
gi 915259206 227 G 227
Cdd:PRK00635 1777 G 1777
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
35-53 |
4.23e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 36.36 E-value: 4.23e-03
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
33-51 |
4.49e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.75 E-value: 4.49e-03
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
6-84 |
7.09e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 37.23 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 6 GIHKEFGHGHSAVHVLRGVDLTVPrgsVTVILGPSGSGKSTLL-RCINELEDITAGSVVVDGERmGYR--VDA-KGVVHR 81
Cdd:COG3451 182 GIYLLNTRSGTPVFFDFHDGLDNG---NTLILGPSGSGKSFLLkLLLLQLLRYGARIVIFDPGG-SYEilVRAlGGTYID 257
|
...
gi 915259206 82 LHP 84
Cdd:COG3451 258 LSP 260
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
34-133 |
8.48e-03 |
|
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442728 [Multi-domain] Cd Length: 402 Bit Score: 36.89 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 34 TVILGPSGSGKSTLLrCINELEDITAG-SVVVdgermgyrVDAKGVVHRLhpkvVARQRRRIGMVFQRFHLF-PHLTATA 111
Cdd:COG3505 2 VLVIGPTGSGKTVGL-VIPNLTQLARGeSVVV--------TDPKGDLAEL----TAGFRRRAGYDVYVFDPFdPERSHRW 68
|
90 100
....*....|....*....|..
gi 915259206 112 NVMEapmRVRGLSKADARTQAL 133
Cdd:COG3505 69 NPLD---EIRDPADAQELAEAL 87
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
150-196 |
9.63e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 34.52 E-value: 9.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 915259206 150 AQLSGGQQQR---VAIARALAM----------DPELMLFDEPTSALDPELVGEVLAVMKD 196
Cdd:pfam13558 31 GGLSGGEKQLlayLPLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| |
