|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-250 |
0e+00 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 513.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISQQKGLI 80
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQPRT 240
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRT 240
|
250
....*....|
gi 489956327 241 RQFLEKFLMQ 250
Cdd:PRK11264 241 RQFLEKFLLQ 250
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-247 |
3.19e-165 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 455.99 E-value: 3.19e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKGLIRRL 83
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVD------GEDLTDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQPRTRQF 243
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAF 235
|
....
gi 489956327 244 LEKF 247
Cdd:COG1126 236 LSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-222 |
2.41e-134 |
|
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: 376.87 E-value: 2.41e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKGLIRRL 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIID------GLKLTDDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03262 75 RQKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-244 |
8.03e-132 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 372.60 E-value: 8.03e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDT-----GKPISQQK 77
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLkpdrdGELVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 78 GLIRRLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:COG4598 88 RQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQ 237
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKS 247
|
....*..
gi 489956327 238 PRTRQFL 244
Cdd:COG4598 248 ERLRQFL 254
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-245 |
1.71e-112 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 322.81 E-value: 1.71e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPIsqqkglIRRL 83
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVD------ERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQPRTRQF 243
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEF 235
|
..
gi 489956327 244 LE 245
Cdd:PRK09493 236 LQ 237
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-244 |
1.12e-99 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 293.91 E-value: 1.12e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQ--QK 77
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVD------GVDLTAlsER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 78 GLiRRLRQHVGFVFQSFNLFPHRTVLENIiEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:COG1135 76 EL-RAARRKIGMIFQHFNLLSSRTVAENV-ALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQ 236
Cdd:COG1135 154 ALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQ 233
|
....*...
gi 489956327 237 QPRTRQFL 244
Cdd:COG1135 234 SELTRRFL 241
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-244 |
5.66e-97 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 283.44 E-value: 5.66e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSaIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISQQKglI 80
Cdd:COG4161 1 MS-IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKA--I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAkALFANPQQPRT 240
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQTEAF 236
|
....
gi 489956327 241 RQFL 244
Cdd:COG4161 237 AHYL 240
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-248 |
1.78e-96 |
|
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: 282.87 E-value: 1.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRV-GDITID----TGKPISQQKG 78
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVeGEQLYHmpgrNGPLVPADEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 79 LIRRLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQ 237
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|.
gi 489956327 238 PRTRQFLEKFL 248
Cdd:TIGR03005 241 ERTREFLSKVI 251
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-244 |
7.98e-95 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 278.05 E-value: 7.98e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNlVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISQQKglIR 81
Cdd:PRK11124 2 SIQLNG-INCFYGAHqALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKA--IR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 RLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAlFANPQQPRTR 241
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAFK 237
|
...
gi 489956327 242 QFL 244
Cdd:PRK11124 238 NYL 240
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-225 |
5.49e-90 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 265.37 E-value: 5.49e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSA-IDVKNLVKKFH----GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPisQ 75
Cdd:COG1136 1 MSPlLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSE--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 76 QKGLIRRlrQHVGFVFQSFNLFPHRTVLENIiEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
Cdd:COG1136 79 ELARLRR--RHIGFVFQFFNLLPELTALENV-ALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956327 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARdVADRAIFMDQGRIVEQ 225
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgTTIVMVTHDPELAA-RADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-222 |
2.03e-88 |
|
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: 260.89 E-value: 2.03e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPisqqKGL 79
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSE----KEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 80 IRRLRQHVGFVFQSFNLFPHRTVLENIiEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:cd03255 77 AAFRRRHIGFVFQSFNLLPDLTALENV-ELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDvADRAIFMDQGRI 222
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-244 |
3.64e-88 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 261.83 E-value: 3.64e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISQQ-----KG 78
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvadKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 79 LIRRLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGLAGK-ETSYPRRLSGGQQQRVAIAR 157
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQ 237
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
....*..
gi 489956327 238 PRTRQFL 244
Cdd:PRK10619 246 PRLQQFL 252
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-236 |
1.81e-87 |
|
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: 259.05 E-value: 1.81e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKGL 79
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVD------GTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 80 -IRRLRQHVGFVFQSFNLFPHRTVLENIiEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
Cdd:cd03258 76 eLRKARRRIGMIFQHFNLLSSRTVFENV-ALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956327 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQ 236
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELGlTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-241 |
6.05e-86 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 259.26 E-value: 6.05e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTGKPISqqkgli 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGLPPE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRlrqHVGFVFQSFNLFPHRTVLENIIEGPViVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:COG3842 76 KR---NVGMVFQDYALFPHLTVAENVAFGLR-MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFanpQQPR 239
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIY---ERPA 228
|
..
gi 489956327 240 TR 241
Cdd:COG3842 229 TR 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-245 |
6.56e-86 |
|
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: 264.46 E-value: 6.56e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKF-----HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKG 78
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD------GKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 79 L-IRRLRQHVGFVFQ----SFNlfPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGL-AGKETSYPRRLSGGQQQR 152
Cdd:COG1123 335 RsLRELRRRVQMVFQdpysSLN--PRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
250
....*....|....
gi 489956327 232 FANPQQPRTRQFLE 245
Cdd:COG1123 493 FANPQHPYTRALLA 506
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-236 |
3.06e-82 |
|
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: 245.70 E-value: 3.06e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKglIRR 82
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD------GKDITKKN--LRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 LRQHVGFVFQsfN----LFpHRTVLENIIEGPVIvKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
Cdd:COG1122 73 LRRKVGLVFQ--NpddqLF-APTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956327 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQ 236
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-244 |
3.48e-82 |
|
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: 246.04 E-value: 3.48e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQ--QKGLi 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD------GQDITGlsEKEL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRLRQHVGFVFQSFNLFPHRTVLENI----IEGPVIvkgePKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
Cdd:COG1127 78 YELRRRIGMLFQGGALFDSLTVFENVafplREHTDL----SEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANP 235
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
....*....
gi 489956327 236 qQPRTRQFL 244
Cdd:COG1127 234 -DPWVRQFL 241
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-231 |
1.44e-81 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 244.58 E-value: 1.44e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 2 SAIDVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPisqqKGLi 80
Cdd:COG3638 1 PMLELRNLSKRYPGGTpALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRG----RAL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRLRQHVGFVFQSFNLFPHRTVLENIIEG--------PVIVKGEPKEDaTVRARELLAKVGLAGKETSYPRRLSGGQQQR 152
Cdd:COG3638 76 RRLRRRIGMIFQQFNLVPRLSVLTNVLAGrlgrtstwRSLLGLFPPED-RERALEALERVGLADKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNlHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
3-244 |
5.20e-81 |
|
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: 243.36 E-value: 5.20e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDtGKPISQQKGLIRR 82
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFD-GQDIYDKKIDVVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 LRQHVGFVFQSFNLFPhRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGL----AGKETSYPRRLSGGQQQRVAIARA 158
Cdd:TIGR00972 80 LRRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQP 238
Cdd:TIGR00972 159 LAVEPEVLLLDEPTSALDPIATGKIEELIQELK-KKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEK 237
|
....*.
gi 489956327 239 RTRQFL 244
Cdd:TIGR00972 238 RTEDYI 243
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-243 |
5.88e-79 |
|
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: 237.40 E-value: 5.88e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISQQkglirRL 83
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELY-----RL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENIiEGPVIVKGE-PKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENV-AFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANpQQPRTR 241
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKELGlTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS-DDPLVR 233
|
..
gi 489956327 242 QF 243
Cdd:cd03261 234 QF 235
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-224 |
2.50e-78 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 236.91 E-value: 2.50e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFH----GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPIsqq 76
Cdd:COG1116 5 APALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD------GKPV--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 77 kgliRRLRQHVGFVFQSFNLFPHRTVLENIIEGPVIvKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
Cdd:COG1116 76 ----TGPGPDRGVVFQEPALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 157 RALAMRPDVILFDEPTSALDP----ELVGEVLntiRQLAQEKRTMVIVTHemsfarDV------ADRAIFMDQ--GRIVE 224
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDAltreRLQDELL---RLWQETGKTVLFVTH------DVdeavflADRVVVLSArpGRIVE 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-244 |
4.80e-78 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 238.89 E-value: 4.80e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSaIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPIsqqkgli 80
Cdd:COG1118 1 MS-IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPP------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 rRLRqHVGFVFQSFNLFPHRTVLENIIEGPViVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:COG1118 73 -RER-RVGFVFQHYALFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 161 MRPDVILFDEPTSALD----PELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQ 236
Cdd:COG1118 150 VEPEVLLLDEPFGALDakvrKELRRWLRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPA 226
|
....*...
gi 489956327 237 QPRTRQFL 244
Cdd:COG1118 227 TPFVARFL 234
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-245 |
2.74e-77 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 233.42 E-value: 2.74e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKgliRRL 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVL------GEDVARDP---AEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENIIegpVI--VKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:COG1131 72 RRRIGYVPQEPALYPDLTVRENLR---FFarLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALfanpqqprTR 241
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL--------KA 220
|
....
gi 489956327 242 QFLE 245
Cdd:COG1131 221 RLLE 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-245 |
8.66e-77 |
|
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: 232.39 E-value: 8.66e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKF----HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKG 78
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFD------GRPVTRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 79 liRRLRQHVGFVFQ----SFNlfPHRTVLENIIEgPVIVKGEPKEDAtvRARELLAKVGLAGKE-TSYPRRLSGGQQQRV 153
Cdd:COG1124 75 --KAFRRRVQMVFQdpyaSLH--PRHTVDRILAE-PLRIHGLPDREE--RIAELLEQVGLPPSFlDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|...
gi 489956327 233 ANPQQPRTRQFLE 245
Cdd:COG1124 228 AGPKHPYTRELLA 240
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-228 |
4.87e-76 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 229.55 E-value: 4.87e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKGL-IR 81
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN------GQDLSRLKRReIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 RLRQHVGFVFQSFNLFPHRTVLENIiEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:COG2884 76 YLRRRIGVVFQDFRLLPDRTVYENV-ALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-244 |
4.30e-75 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 231.23 E-value: 4.30e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPisqqKGL 79
Cdd:PRK11153 2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSE----KEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 80 iRRLRQHVGFVFQSFNLFPHRTVLENIIEgPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:PRK11153 78 -RKARRQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQP 238
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHP 235
|
....*.
gi 489956327 239 RTRQFL 244
Cdd:PRK11153 236 LTREFI 241
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-221 |
1.24e-74 |
|
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: 224.37 E-value: 1.24e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKGLIRRL 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID------GEDLTDLEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENIIEGpvivkgepkedatvrarellakvglagketsyprrLSGGQQQRVAIARALAMRP 163
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-231 |
1.28e-74 |
|
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: 226.68 E-value: 1.28e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISqqkglIRR 82
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKA-----LRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 LRQHVGFVFQSFNLFPHRTVLENIIEG--------PVIVKGEPKEDaTVRARELLAKVGLAGKETSYPRRLSGGQQQRVA 154
Cdd:cd03256 76 LRRQIGMIFQQFNLIERLSVLENVLSGrlgrrstwRSLFGLFPKEE-KQRALAALERVGLLDKAYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956327 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-226 |
1.16e-73 |
|
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: 223.17 E-value: 1.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTGKPISqqkglirrl 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPE--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENIIEGPViVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGLK-LRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-244 |
4.60e-73 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 224.97 E-value: 4.60e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKglIRR 82
Cdd:COG1125 2 IEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILID------GEDIRDLD--PVE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 LRQHVGFVFQSFNLFPHRTVLENIiegpVIV---KGEPKEDATVRARELLAKVGLAGKETS--YPRRLSGGQQQRVAIAR 157
Cdd:COG1125 74 LRRRIGYVIQQIGLFPHMTVAENI----ATVprlLGWDKERIRARVDELLELVGLDPEEYRdrYPHELSGGQQQRVGVAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 158 ALAMRPDVILFDEPTSALDP----ELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
Cdd:COG1125 150 ALAADPPILLMDEPFGALDPitreQLQDELLRLQREL---GKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILA 226
|
250
....*....|.
gi 489956327 234 NPQQPRTRQFL 244
Cdd:COG1125 227 NPANDFVADFV 237
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-244 |
1.38e-72 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 222.22 E-value: 1.38e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 2 SAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTiRV-GDITIDtGKPISQQKGLI 80
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGA-RVeGEILLD-GEDIYDPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRLRQHVGFVFQSFNLFPHrTVLENIIEGPVIVKGEPKEDATVRARELLAKVGL----AGKETSYPRRLSGGQQQRVAIA 156
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQ 236
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDPISTAKIEELILELK-KDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPK 245
|
....*...
gi 489956327 237 QPRTRQFL 244
Cdd:COG1117 246 DKRTEDYI 253
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-225 |
2.20e-72 |
|
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: 220.42 E-value: 2.20e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHG----QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPIsqqkgl 79
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVD------GEPV------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 80 iRRLRQHVGFVFQSFNLFPHRTVLENIIEGPVIvKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:cd03293 69 -TGPGPDRGYVFQQDALLPWLTVLDNVALGLEL-QGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956327 160 AMRPDVILFDEPTSALDP---ELVGEVLntIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQ--GRIVEQ 225
Cdd:cd03293 147 AVDPDVLLLDEPFSALDAltrEQLQEEL--LDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-235 |
3.00e-72 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 224.18 E-value: 3.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTGKPISQqkgli 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRlrqhVGFVFQSFNLFPHRTVLENiIEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:COG3839 75 RN----IAMVFQSYALYPHMTVYEN-IAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHE----MSFardvADRAIFMDQGRIVEQGPAKALFANP 235
Cdd:COG3839 150 REPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-231 |
2.80e-71 |
|
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: 217.82 E-value: 2.80e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDtGKPISQQKGLIRRL 83
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLD-GKDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPhRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGLAG--KETSYPRRLSGGQQQRVAIARALAM 161
Cdd:cd03260 80 RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-226 |
1.11e-70 |
|
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: 216.22 E-value: 1.11e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKGL 79
Cdd:cd03257 2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFD------GKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 80 IRRLR-QHVGFVFQ----SFNlfPHRTVLENIIEGPVIVKGEPKEDATVRAR-ELLAKVGLAGK-ETSYPRRLSGGQQQR 152
Cdd:cd03257 76 LRKIRrKEIQMVFQdpmsSLN--PRMTIGEQIAEPLRIHGKLSKKEARKEAVlLLLVGVGLPEEvLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956327 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELgLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-221 |
1.53e-70 |
|
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: 215.41 E-value: 1.53e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 6 VKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKglIRRL 83
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD------GKDLTKLS--LKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNL-FPHRTVLENIIEGPVIvKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:cd03225 74 RRKVGLVFQNPDDqFFGPTVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489956327 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-241 |
7.02e-70 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 217.23 E-value: 7.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI-NLLEQP--EGGTIRVGditidtGKPISQQ 76
Cdd:COG0444 2 LEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlGLLPPPgiTSGEILFD------GEDLLKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 77 KG-LIRRLR-QHVGFVFQ----SFNlfPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGLAGKET---SYPRRLSG 147
Cdd:COG0444 76 SEkELRKIRgREIQMIFQdpmtSLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERrldRYPHELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGlAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250
....*....|....*
gi 489956327 227 PAKALFANPQQPRTR 241
Cdd:COG0444 234 PVEELFENPRHPYTR 248
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-230 |
1.74e-68 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 210.75 E-value: 1.74e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 2 SAIDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQ-- 75
Cdd:COG4181 7 PIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLA------GQDLFAld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 76 QKGLIRRLRQHVGFVFQSFNLFPHRTVLENIIEgPVIVKGEPkeDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
Cdd:COG4181 81 EDARARLRARHVGFVFQSFQLLPTLTALENVML-PLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956327 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKA 230
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGtTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-246 |
2.19e-68 |
|
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: 211.01 E-value: 2.19e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKGLirR 82
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFID------GEDIREQDPV--E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 LRQHVGFVFQSFNLFPHRTVLENIIEGPVIvKGEPKEDATVRARELLAKVGLAGKE--TSYPRRLSGGQQQRVAIARALA 160
Cdd:cd03295 73 LRRKIGYVIQQIGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQPR 239
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDF 231
|
....*..
gi 489956327 240 TRQFLEK 246
Cdd:cd03295 232 VAEFVGA 238
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-247 |
6.05e-68 |
|
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: 210.77 E-value: 6.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 16 QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISqqkglIRRLRQHVGFVFQsfn 95
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKK-----LKDLRKKVGLVFQ--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 96 lFPH-----RTVLENIIEGPVIVkGEPKEDATVRARELLAKVGL--AGKETSyPRRLSGGQQQRVAIARALAMRPDVILF 168
Cdd:TIGR04521 90 -FPEhqlfeETVYKDIAFGPKNL-GLSEEEAEERVKEALELVGLdeEYLERS-PFELSGGQMRRVAIAGVLAMEPEVLIL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 169 DEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPqqprtrQFLEKF 247
Cdd:TIGR04521 167 DEPTAGLDPKGRKEILDLFKRLHKEKgLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV------DELEKI 240
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-237 |
2.90e-67 |
|
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: 216.31 E-value: 2.90e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLeQPEGGTIRvGDITIDtGKPISQQKGLI 80
Cdd:COG1123 4 LLEVRDLSVRYPGGDvpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL-LPHGGRIS-GEVLLD-GRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRlrQHVGFVFQSF--NLFPHrTVLENIIEGPVIvKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
Cdd:COG1123 81 RG--RRIGMVFQDPmtQLNPV-TVGDQIAEALEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQ 237
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-231 |
2.41e-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: 205.61 E-value: 2.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgDITIDtGKPISQQKGL-IR 81
Cdd:TIGR02315 2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSG-----SILLE-GTDITKLRGKkLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 RLRQHVGFVFQSFNLFPHRTVLENIIEG--------PVIVKGEPKEDaTVRARELLAKVGLAGKETSYPRRLSGGQQQRV 153
Cdd:TIGR02315 76 KLRRRIGMIFQHYNLIERLTVLENVLHGrlgykptwRSLLGRFSEED-KERALSALERVGLADKAYQRADQLSGGQQQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956327 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
Cdd:TIGR02315 155 AIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINlHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-245 |
1.54e-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: 204.41 E-value: 1.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 7 KNLVKKFHGQTV-LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQ-QKGLIRRLR 84
Cdd:cd03294 27 KEEILKKTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLID------GQDIAAmSRKELRELR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 85 QH-VGFVFQSFNLFPHRTVLENIIEGpVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03294 101 RKkISMVFQSFALLPHRTVLENVAFG-LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQPRTRQ 242
Cdd:cd03294 180 DILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVRE 259
|
...
gi 489956327 243 FLE 245
Cdd:cd03294 260 FFR 262
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-244 |
4.05e-64 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 199.60 E-value: 4.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTvLHgIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTGKPISQQKglirrl 83
Cdd:COG3840 2 LRLDDLTYRYGDFP-LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-TALPPAERP------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 rqhVGFVFQSFNLFPHRTVLENIIEG--PvivKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:COG3840 73 ---VSMLFQENNLFPHLTVAQNIGLGlrP---GLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQPRT 240
Cdd:COG3840 147 KRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
....
gi 489956327 241 RQFL 244
Cdd:COG3840 227 AAYL 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-244 |
1.46e-63 |
|
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: 198.33 E-value: 1.46e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTGKPISQqkglirr 82
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQE------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 lRQhVGFVFQSFNLFPHRTVLENIIEGPVIVKGE---PKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:cd03296 74 -RN-VGFVFQHYALFRHMTVFDNVAFGLRVKPRSerpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQP 238
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASP 231
|
....*.
gi 489956327 239 RTRQFL 244
Cdd:cd03296 232 FVYSFL 237
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-235 |
1.82e-63 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 203.03 E-value: 1.82e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKF-----------------------HGQTV-LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPE 56
Cdd:COG4175 1 MPKIEVRNLYKIFgkrperalklldqgkskdeilekTGQTVgVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 57 GGTIRVGDITIDTgkpISQQKglIRRLRQH-VGFVFQSFNLFPHRTVLENIiEGPVIVKGEPKEDATVRARELLAKVGLA 135
Cdd:COG4175 81 AGEVLIDGEDITK---LSKKE--LRELRRKkMSMVFQHFALLPHRTVLENV-AFGLEIQGVPKAERRERAREALELVGLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 136 GKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP----ELVGEVLntirQL-AQEKRTMVIVTHEMSFARDV 210
Cdd:COG4175 155 GWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrEMQDELL----ELqAKLKKTIVFITHDLDEALRL 230
|
250 260
....*....|....*....|....*
gi 489956327 211 ADRAIFMDQGRIVEQGPAKALFANP 235
Cdd:COG4175 231 GDRIAIMKDGRIVQIGTPEEILTNP 255
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-222 |
2.14e-62 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 194.26 E-value: 2.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPIsqqkglirRL 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPP--------EW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHrTVLENIIEGPVIVKGEPKEDatvRARELLAKVGLA----GKETSyprRLSGGQQQRVAIARAL 159
Cdd:COG4619 73 RRQVAYVPQEPALWGG-TVRDNLPFPFQLRERKFDRE---RALELLERLGLPpdilDKPVE---RLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEgRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-234 |
5.79e-62 |
|
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: 195.34 E-value: 5.79e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISQqkglir 81
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWE------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 rLRQHVGFVFQS-FNLFPHRTV-------LENIiegpvivkGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRV 153
Cdd:TIGR04520 75 -IRKKVGMVFQNpDNQFVGATVeddvafgLENL--------GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIF 224
|
..
gi 489956327 233 AN 234
Cdd:TIGR04520 225 SQ 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-236 |
3.26e-61 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 192.27 E-value: 3.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTGKPISQ--QKGLIR 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI-TGLPPHEiaRLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 rlrqhvgfVFQSFNLFPHRTVLENIIEGPVIVKGEP---------KEDATVRARELLAKVGLAGKETSYPRRLSGGQQQR 152
Cdd:cd03219 80 --------TFQIPRLFPELTVLENVMVAAQARTGSGlllararreEREARERAEELLERVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
....
gi 489956327 233 ANPQ 236
Cdd:cd03219 232 NNPR 235
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-236 |
6.82e-61 |
|
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: 191.30 E-value: 6.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTGKPISqqkglirrl 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPH--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENIIEGpVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03300 71 KRPVNTVFQNYALFPHLTVFENIAFG-LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQ 236
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-232 |
9.14e-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: 191.80 E-value: 9.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKGliRR 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLD------GRDLASLSR--RE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 LRQHVGFVFQS----FNL----------FPHRTVLEniiegpvivkGEPKEDATVrARELLAKVGLAGKETSYPRRLSGG 148
Cdd:COG1120 73 LARRIAYVPQEppapFGLtvrelvalgrYPHLGLFG----------RPSAEDREA-VEEALERTGLEHLADRPVDELSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
Cdd:COG1120 142 ERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
....*
gi 489956327 228 AKALF 232
Cdd:COG1120 222 PEEVL 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-241 |
1.89e-60 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 193.41 E-value: 1.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKF---------HGQTV--LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKP 72
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFD------GQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 73 ISQQKGL-IRRLRQHVGFVFQ----SFNlfPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGL----AGKetsYPR 143
Cdd:COG4608 82 ITGLSGReLRPLRRRMQMVFQdpyaSLN--PRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrpehADR---YPH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 144 RLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:COG4608 157 EFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDL-QDELglTYLFISHDLSVVRHISDRVAVMYLGK 235
|
250 260
....*....|....*....|
gi 489956327 222 IVEQGPAKALFANPQQPRTR 241
Cdd:COG4608 236 IVEIAPRDELYARPLHPYTQ 255
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-222 |
2.74e-60 |
|
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: 187.60 E-value: 2.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKGLIRRl 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL------GKDIKKEPEEVKR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 rqHVGFVFQSFNLFPHRTVLENIiegpvivkgepkedatvrarellakvglagketsyprRLSGGQQQRVAIARALAMRP 163
Cdd:cd03230 74 --RIGYLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-247 |
3.62e-60 |
|
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: 193.33 E-value: 3.62e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISqqkgli 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQG------GRDIT------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 rRL---RQHVGFVFQSFNLFPHRTVLENIIEGpVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:TIGR03265 70 -RLppqKRDYGIVFQSYALFPNLTVADNIAYG-LKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFanpQ 236
Cdd:TIGR03265 148 ALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIY---R 224
|
250
....*....|.
gi 489956327 237 QPRTRqFLEKF 247
Cdd:TIGR03265 225 HPATP-FVADF 234
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-236 |
7.87e-60 |
|
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: 189.48 E-value: 7.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTGKPISQ--QKG 78
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-TGLPPHRiaRLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 79 LIRrlrqhvgfVFQSFNLFPHRTVLENIIEGPVIVKGEP--------------KEDATVRARELLAKVGLAGKETSYPRR 144
Cdd:COG0411 81 IAR--------TFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreEREARERAEELLERVGLADRADEPAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 145 LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
250
....*....|...
gi 489956327 224 EQGPAKALFANPQ 236
Cdd:COG0411 233 AEGTPAEVRADPR 245
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-250 |
4.47e-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: 4.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKpisqqkgliRRL 83
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP---------REA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENI-IEGPVivKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIrYFAEL--YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQPRtrq 242
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEEN--- 227
|
....*...
gi 489956327 243 fLEKFLMQ 250
Cdd:COG4555 228 -LEDAFVA 234
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-217 |
3.73e-58 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 183.59 E-value: 3.73e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDItiDTGKPISQQKGLIRRlrQ 85
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQ--ETPPLNSKKASKFRR--E 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 86 HVGFVFQSFNLFPHRTVLENIIEGPVIVKGePKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKL-SKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489956327 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFM 217
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-248 |
7.43e-58 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 187.62 E-value: 7.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgDITID----TGKPISQQKGL 79
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEG-----QIFIDgedvTHRSIQQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 80 IrrlrqhvgfVFQSFNLFPHRTVLENIIEGpVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:PRK11432 82 M---------VFQSYALFPHMSLGENVGYG-LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFanpQQP 238
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY---RQP 228
|
250
....*....|
gi 489956327 239 RTRqFLEKFL 248
Cdd:PRK11432 229 ASR-FMASFM 237
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-231 |
1.59e-57 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 183.37 E-value: 1.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPIsqqkgli 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLF------GKPP------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRLRQHVGFVFQSFNL---FPhRTVLEniiegpvIV-----------KGEPKEDATvRARELLAKVGLAGKETSYPRRLS 146
Cdd:COG1121 71 RRARRRIGYVPQRAEVdwdFP-ITVRD-------VVlmgrygrrglfRRPSRADRE-AVDEALERVGLEDLADRPIGELS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 147 GGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGP 221
|
....*
gi 489956327 227 PAKAL 231
Cdd:COG1121 222 PEEVL 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-234 |
3.85e-57 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 181.48 E-value: 3.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKkFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKgLIRR 82
Cdd:cd03224 1 LEVENLNA-GYGKSqILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFD------GRDITGLP-PHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 LRQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKvgLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:cd03224 73 ARAGIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956327 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAN 234
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-245 |
8.83e-57 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 189.13 E-value: 8.83e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHG----QTVLHGIDLEVEQGEVVAIIGPSGSGKT-TLLRSINLLeqPEGGTIRVGDITID----TGK 71
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLL--PDPAAHPSGSILFDgqdlLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 72 PISQqkglIRRLR-QHVGFVFQ----SFNlfPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGLAGKET---SYPR 143
Cdd:COG4172 82 SERE----LRRIRgNRIAMIFQepmtSLN--PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERrldAYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 144 RLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMaLLLITHDLGVVRRFADRVAVMRQGEI 235
|
250 260
....*....|....*....|...
gi 489956327 223 VEQGPAKALFANPQQPRTRQFLE 245
Cdd:COG4172 236 VEQGPTAELFAAPQHPYTRKLLA 258
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-236 |
1.17e-56 |
|
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: 180.56 E-value: 1.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTGKPISqqkgli 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI-TGLPPH------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKEDATV--------RARELLAKvgLAGketsyprRLSGGQQQR 152
Cdd:COG0410 74 RIARLGIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLervyelfpRLKERRRQ--RAG-------TLSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
....
gi 489956327 233 ANPQ 236
Cdd:COG0410 225 ADPE 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-248 |
3.17e-56 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 183.36 E-value: 3.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSaIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQqkgLI 80
Cdd:PRK10851 1 MS-IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH------GTDVSR---LH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRLRQhVGFVFQSFNLFPHRTVLENIIEG-PVIVKGEPKEDATVRAR--ELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:PRK10851 71 ARDRK-VGFVFQHYALFRHMTVFDNIAFGlTVLPRRERPNAAAIKAKvtQLLEMVQLAHLADRYPAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGpakalfaNPQ 236
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG-------TPD 222
|
250
....*....|....*.
gi 489956327 237 Q----PRTRQFLEkFL 248
Cdd:PRK10851 223 QvwrePATRFVLE-FM 237
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-233 |
4.57e-56 |
|
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: 190.43 E-value: 4.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTgkpISqqkglI 80
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQ---ID-----P 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRLRQHVGFVFQSFNLFpHRTVLENIIEGpvivkgepKEDATV-RARELLAKVGLAGKETSYP-----------RRLSGG 148
Cdd:COG2274 545 ASLRRQIGVVLQDVFLF-SGTIRENITLG--------DPDATDeEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPA 228
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTH 693
|
....*
gi 489956327 229 KALFA 233
Cdd:COG2274 694 EELLA 698
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-226 |
6.93e-55 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 178.36 E-value: 6.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQT-----VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTI----------------RV 62
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 63 GDITIDTGKPISQQKGLIRRLRQHVGFVFQ--SFNLFpHRTVLENIIEGPVIVkGEPKEDATVRARELLAKVGLagkETS 140
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGL---DES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 141 Y----PRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIF 216
Cdd:PRK13651 158 YlqrsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIF 237
|
250
....*....|
gi 489956327 217 MDQGRIVEQG 226
Cdd:PRK13651 238 FKDGKIIKDG 247
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
11-246 |
9.99e-55 |
|
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: 179.66 E-value: 9.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 11 KKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISqqkgLIRRLRQHVGFV 90
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVE----LREVRRKKIGMV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 91 FQSFNLFPHRTVLENIIEGPVIVkGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDE 170
Cdd:TIGR01186 77 FQQFALFPHMTILQNTSLGPELL-GWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 171 PTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQPRTRQFLEK 246
Cdd:TIGR01186 156 AFSALDPLIRDSMQDELKKLqATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-245 |
1.58e-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: 183.35 E-value: 1.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQ-----------TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI-NLLEQpeGGTIRVGditidtGK 71
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALlRLIPS--EGEIRFD------GQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 72 PISQQKG-LIRRLRQHVGFVFQ----SFNlfPHRTVLENIIEGPVIVK-GEPKEDATVRARELLAKVGL-AGKETSYPRR 144
Cdd:COG4172 348 DLDGLSRrALRPLRRRMQVVFQdpfgSLS--PRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLdPAARHRYPHE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 145 LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDL-QREHglAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
250 260
....*....|....*....|...
gi 489956327 223 VEQGPAKALFANPQQPRTRQFLE 245
Cdd:COG4172 505 VEQGPTEQVFDAPQHPYTRALLA 527
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-222 |
1.70e-54 |
|
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: 174.52 E-value: 1.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidTGKPISQQKG-LIR 81
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRV------NGQDVSDLRGrAIP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 RLRQHVGFVFQSFNLFPHRTVLENIIEgPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:cd03292 75 YLRRKIGVVFQDFRLLPDRNVYENVAF-ALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956327 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-236 |
3.31e-54 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 176.36 E-value: 3.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKpisQQKGLiRRLRQHVGFVFQsfnlFP 98
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGK---KNKKL-KPLRKKVGIVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 99 H-----RTVLENIIEGPvIVKGEPKEDATVRARELLAKVGLAGK-ETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:PRK13634 95 EhqlfeETVEKDICFGP-MNFGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956327 173 SALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQ 236
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKEKGlTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-221 |
3.57e-54 |
|
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: 171.66 E-value: 3.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPisqqkgliRRLRQ 85
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL--------EELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 86 HVGFVFQsfnlfphrtvleniiegpvivkgepkedatvrarellakvglagketsyprrLSGGQQQRVAIARALAMRPDV 165
Cdd:cd00267 74 RIGYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489956327 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-221 |
6.10e-54 |
|
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: 171.41 E-value: 6.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHG--QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPisqqkgliR 81
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDL--------E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 RLRQHVGFVFQSFNLFpHRTVLENIiegpvivkgepkedatvrarellakvglagketsyprrLSGGQQQRVAIARALAM 161
Cdd:cd03228 73 SLRKNIAYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGR 221
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAKG-KTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-245 |
7.37e-54 |
|
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: 182.27 E-value: 7.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKGli 80
Cdd:COG4987 333 SLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG------GVDLRDLDE-- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRLRQHVGFVFQSFNLFpHRTVLENIIegpvIVKGEPKEDAtvrARELLAKVGLAGKETSYP-----------RRLSGGQ 149
Cdd:COG4987 405 DDLRRRIAVVPQRPHLF-DTTLRENLR----LARPDATDEE---LWAALERVGLGDWLAALPdgldtwlgeggRRLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAK 229
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG-RTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHE 554
|
250
....*....|....*.
gi 489956327 230 ALFAnpQQPRTRQFLE 245
Cdd:COG4987 555 ELLA--QNGRYRQLYQ 568
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-226 |
7.39e-54 |
|
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: 171.46 E-value: 7.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 5 DVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKglIRRLR 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD------GKDLASLS--PKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 85 QHVGFVFQSfnlfphrtvleniiegpvivkgepkedatvrarelLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPD 164
Cdd:cd03214 73 RKIAYVPQA-----------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956327 165 VILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERgKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-226 |
1.03e-53 |
|
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: 172.44 E-value: 1.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPisqqkglirrL 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP----------K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENiIEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03301 71 DRDIAMVFQNYALYPHMTVYDN-IAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-221 |
6.23e-53 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 170.51 E-value: 6.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKG-LIR 81
Cdd:TIGR02673 2 IEFHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIA------GEDVNRLRGrQLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 RLRQHVGFVFQSFNLFPHRTVLENIIEgPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:TIGR02673 76 LLRRRIGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:TIGR02673 155 SPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-235 |
1.35e-52 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 174.37 E-value: 1.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTGKPISQQkglirrl 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPAENR------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 rqHVGFVFQSFNLFPHRTVLENIIEGpVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:PRK09452 87 --HVNTVFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANP 235
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKAL-QRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-227 |
1.65e-52 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 178.82 E-value: 1.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLE---QPEGGTIRVGDITIDTgkpISQQkglirRLRQHVGFVF 91
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTL---VNLLLrfyDPTSGRILIDGVDIRD---LTLE-----SLRRQIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 92 QSFNLFpHRTVLENIIEGpvivkgepKEDAT----------VRARELLAK--------VGLAGketsypRRLSGGQQQRV 153
Cdd:COG1132 421 QDTFLF-SGTIRENIRYG--------RPDATdeeveeaakaAQAHEFIEAlpdgydtvVGERG------VNLSGGQRQRI 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGP 227
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMKG-RTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-235 |
1.97e-52 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 173.75 E-value: 1.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 22 IDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITI-DTGKPISqqkglIRRLRQHVGFVFQSFNLFPHR 100
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqDSARGIF-----LPPHRRRIGYVFQEARLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 101 TVLENIIEGpviVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELV 180
Cdd:COG4148 93 SVRGNLLYG---RKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489956327 181 GEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANP 235
Cdd:COG4148 170 AEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-244 |
3.38e-51 |
|
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: 166.74 E-value: 3.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFhGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPIsqqkglirrl 83
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENIIEGpVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQPRTRQ 242
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAE 228
|
..
gi 489956327 243 FL 244
Cdd:cd03299 229 FL 230
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-234 |
3.77e-51 |
|
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: 174.95 E-value: 3.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 2 SAIDVKNLVKKFH-GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISqqkgli 80
Cdd:COG4988 335 PSIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS------ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 rrLRQHVGFVFQSFNLFpHRTVLENIIEGpvivkgepKEDATVRA-RELLAKVGLAGKETSYP-----------RRLSGG 148
Cdd:COG4988 409 --WRRQIAWVPQNPYLF-AGTIRENLRLG--------RPDASDEElEAALEAAGLDEFVAALPdgldtplgeggRGLSGG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPA 228
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG-RTVILITHRLALLAQ-ADRILVLDDGRIVEQGTH 555
|
....*.
gi 489956327 229 KALFAN 234
Cdd:COG4988 556 EELLAK 561
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-226 |
6.08e-51 |
|
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: 165.55 E-value: 6.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 22 IDLEVEqGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTgkpiSQQKGLIRRLRQHVGFVFQSFNLFPHRT 101
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD----SRKKINLPPQQRKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 102 VLENIIEGpvIVKGEPKEDaTVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVG 181
Cdd:cd03297 92 VRENLAFG--LKRKRNRED-RISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489956327 182 EVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03297 169 QLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-233 |
1.80e-50 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 166.34 E-value: 1.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKglIR 81
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG------GMVLSEET--VW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 RLRQHVGFVFQS-FNLFPHRTV-------LENIiegpvivkGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRV 153
Cdd:PRK13635 78 DVRRQVGMVFQNpDNQFVGATVqddvafgLENI--------GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLsITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
.
gi 489956327 233 A 233
Cdd:PRK13635 229 K 229
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-173 |
2.03e-50 |
|
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: 162.05 E-value: 2.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKglIRRLRQHVGFVFQSFNLFP 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLD------GQDLTDDE--RKSLRKEIGYVFQDPQLFP 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956327 99 HRTVLENIIEGpVIVKGEPKEDATVRARELLAKVGLAGKE----TSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:pfam00005 73 RLTVRENLRLG-LLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-239 |
1.42e-49 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 163.71 E-value: 1.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidTGKPISQQKGLIRR 82
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI------KGEPIKYDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 LRQHVGFVFQSFN--LFPhRTVLENIIEGPVIVkGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK13639 76 VRKTVGIVFQNPDdqLFA-PTVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956327 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQPR 239
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-244 |
6.06e-49 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 163.60 E-value: 6.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNL--VKK--FHGQ-TV--LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDItiDTGKPi 73
Cdd:PRK11308 6 LQAIDLKKHypVKRglFKPErLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQ--DLLKA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 74 sqQKGLIRRLRQHVGFVFQ----SFNlfPHRTVlENIIEGPVIVKGE-PKEDATVRARELLAKVGLAGKETS-YPRRLSG 147
Cdd:PRK11308 83 --DPEAQKLLRQKIQIVFQnpygSLN--PRKKV-GQILEEPLLINTSlSAAERREKALAMMAKVGLRPEHYDrYPHMFSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsYVFISHDLSVVEHIADEVMVMYLGRCVEKG 237
|
250
....*....|....*...
gi 489956327 227 PAKALFANPQQPRTRQFL 244
Cdd:PRK11308 238 TKEQIFNNPRHPYTQALL 255
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-247 |
6.45e-49 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 170.29 E-value: 6.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKG--LIRRLRQHVGFVFQSFN 95
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVA------GQDVATLDAdaLAQLRREHFGFIFQRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 96 LFPHRTVLENIiEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSAL 175
Cdd:PRK10535 97 LLSHLTAAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 176 DPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAK--------ALFANPQQPRTRQFLEKF 247
Cdd:PRK10535 176 DSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQekvnvaggTEPVVNTASGWRQFVSGF 254
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-226 |
7.09e-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: 160.01 E-value: 7.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQkglirrlRQ 85
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF------GKPLEKE-------RK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 86 HVGFVFQSFNL---FPhRTVLENIIEGPVIVKG---EPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:cd03235 69 RIGYVPQRRSIdrdFP-ISVRDVVLMGLYGHKGlfrRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDqGRIVEQG 226
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
18-222 |
1.24e-48 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 159.50 E-value: 1.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTGKPISQQKGLIRRLrqhVGFVFQSFNLF 97
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEV-TNLSYSQKIILRREL---IGYIFQSFNLI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 98 PHRTVLENIiEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:NF038007 96 PHLSIFDNV-ALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489956327 178 ELVGEVLNTIRQLAQEKRTMVIVTHEMSfARDVADRAIFMDQGRI 222
Cdd:NF038007 175 KNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-235 |
1.48e-48 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 162.71 E-value: 1.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQT-----VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITI--------DTG 70
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkknnheLIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 71 KPISQQKGLIRRLRQHVGFVFQ--SFNLFpHRTVLENIIEGPVIVkGEPKEDATVRARELLAKVGLagkETSY----PRR 144
Cdd:PRK13631 102 NPYSKKIKNFKELRRRVSMVFQfpEYQLF-KDTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGL---DDSYlersPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 145 LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
250
....*....|.
gi 489956327 225 QGPAKALFANP 235
Cdd:PRK13631 257 TGTPYEIFTDQ 267
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-223 |
4.87e-48 |
|
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: 157.80 E-value: 4.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 5 DVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQqkgliRRL 83
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLN------GKPIKA-----KER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQS--FNLFpHRTVLENIIEGpvivkGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:cd03226 70 RKSIGYVMQDvdYQLF-TDSVREELLLG-----LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956327 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-244 |
2.42e-47 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 157.24 E-value: 2.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINlleqpeggtiRVGDI--------TID-TGKPIS 74
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSIN----------RMNDLnpevtitgSIVyNGHNIY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 75 QQKGLIRRLRQHVGFVFQSFNLFPHrTVLENIIEGPVI--VKGEPKEDATVRARELLAKVGLAGKETSYPRR--LSGGQQ 150
Cdd:PRK14239 76 SPRTDTVDLRKEIGMVFQQPNPFPM-SIYENVVYGLRLkgIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSAlgLSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQ 233
|
250
....*....|....
gi 489956327 231 LFANPQQPRTRQFL 244
Cdd:PRK14239 234 MFMNPKHKETEDYI 247
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-244 |
3.09e-47 |
|
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: 156.53 E-value: 3.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKGLiRRLRQ 85
Cdd:TIGR03410 3 VSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLD------GEDITKLPPH-ERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 86 HVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKE-DATVRA-----RELLAkvglagketsypRR---LSGGQQQRVAIA 156
Cdd:TIGR03410 76 GIAYVPQGREIFPRLTVEENLLTGLAALPRRSRKiPDEIYElfpvlKEMLG------------RRggdLSGGQQQQLAIA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALfanp 235
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL---- 219
|
....*....
gi 489956327 236 QQPRTRQFL 244
Cdd:TIGR03410 220 DEDKVRRYL 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-203 |
5.62e-47 |
|
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: 154.94 E-value: 5.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKgliRRL 83
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWN------GEPIRDAR---EDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENIIegpVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:COG4133 74 RRRLAYLGHADGLKPELTVRENLR---FWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE 203
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-231 |
6.43e-47 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 162.50 E-value: 6.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPI-------SQ 75
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD------GEPVrfrsprdAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 76 QKGlirrlrqhVGFVFQSFNLFPHRTVLENIIEGpvivkGEPKEDATV-------RARELLAKVGLAGKETSYPRRLSGG 148
Cdd:COG1129 78 AAG--------IAIIHQELNLVPNLSVAENIFLG-----REPRRGGLIdwramrrRARELLARLGLDIDPDTPVGDLSVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
Cdd:COG1129 145 QQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPV 224
|
...
gi 489956327 229 KAL 231
Cdd:COG1129 225 AEL 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-244 |
8.74e-47 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 156.16 E-value: 8.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSIN-LLEQPEGGTIRvGDITIdTGKPISQQKGL 79
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrLLELNEEARVE-GEVRL-FGRNIYSPDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 80 IRRLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVK-GEPKEDATVRARELLAKVGL----AGKETSYPRRLSGGQQQRVA 154
Cdd:PRK14267 80 PIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGlVKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAN 234
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
250
....*....|
gi 489956327 235 PQQPRTRQFL 244
Cdd:PRK14267 239 PEHELTEKYV 248
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-244 |
1.59e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 156.02 E-value: 1.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDtGKPISQQKGLIRr 82
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLG-GRSIFNYRDVLE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 LRQHVGFVFQSFNLFPhRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGL----AGKETSYPRRLSGGQQQRVAIARA 158
Cdd:PRK14271 99 FRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQP 238
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
....*.
gi 489956327 239 RTRQFL 244
Cdd:PRK14271 257 ETARYV 262
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-231 |
2.49e-46 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 154.93 E-value: 2.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKG--LI 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLN------GRPLADWSPaeLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RR---LRQH--VGFVFqsfnlfphrTVLENIIEGPVIVKGEPKEDATVrARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
Cdd:PRK13548 76 RRravLPQHssLSFPF---------TVEEVVAMGRAPHGLSRAEDDAL-VAAALAQVDLAHLAGRDYPQLSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 156 ARALA------MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQG-P 227
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIvVLHDLNLAARYADRIVLLHQGRLVADGtP 225
|
....
gi 489956327 228 AKAL 231
Cdd:PRK13548 226 AEVL 229
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-207 |
6.98e-46 |
|
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: 151.81 E-value: 6.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKGLIRRLRQHVGFVFQSF 94
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLID------GEPLDYSRKGLLERRQRVGLVFQDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 95 N--LFpHRTVLENIIEGPVIVKGEPKEdATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:TIGR01166 78 DdqLF-AADVDQDVAFGPLNLGLSEAE-VERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|....*
gi 489956327 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFA 207
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-244 |
7.42e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 154.04 E-value: 7.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGgTIRVGDITIDTGKPISQQKGLI 80
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELES-EVRVEGRVEFFNQNIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRLRQHVGFVFQSFNLFPhRTVLENIIEGPVIVKGEPK------EDATVRARELLAKVglAGKETSYPRRLSGGQQQRVA 154
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKleiddiVESALKDADLWDEI--KHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLA-QEKRTMVIVTHEMSFARDVADRAIFMDQ-----GRIVEQGPA 228
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLT 240
|
250
....*....|....*.
gi 489956327 229 KALFANPQQPRTRQFL 244
Cdd:PRK14258 241 KKIFNSPHDSRTREYV 256
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-235 |
1.99e-45 |
|
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: 154.57 E-value: 1.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 34 IIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPisqqkglirrLRQHVGFVFQSFNLFPHRTVLENIIEgPVIV 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP----------HLRHINMVFQSYALFPHMTVEENVAF-GLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 114 KGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQE 193
Cdd:TIGR01187 70 RKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI-QE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489956327 194 KR--TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANP 235
Cdd:TIGR01187 149 QLgiTFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-226 |
2.02e-45 |
|
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: 151.50 E-value: 2.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHG--QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGkpisqqkglIR 81
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTD---------RK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 RLRQHVGFVFQSFNLFPHRTVLENI-IEGpvIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:cd03263 72 AARQSLGYCPQFDALFDELTVREHLrFYA--RLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956327 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
8-226 |
3.67e-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: 150.34 E-value: 3.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 8 NLVKKFHGQTVLHgIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPIsqqkglirrlRQHV 87
Cdd:cd03298 4 DKIRFSYGEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA----------DRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 88 GFVFQSFNLFPHRTVLENIIEGPVI-VKGEPKEDATVRAreLLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVI 166
Cdd:cd03298 73 SMLFQENNLFAHLTVEQNVGLGLSPgLKLTAEDRQAIEV--ALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956327 167 LFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-222 |
7.03e-45 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 151.37 E-value: 7.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDitidtgKPISQQKGLIRrlrq 85
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT------APLAEAREDTR---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 86 hvgFVFQSFNLFPHRTVLENIIEGpviVKGEPKEdatvRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:PRK11247 85 ---LMFQDARLLPWKKVIDNVGLG---LKGQWRD----AALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489956327 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHGfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-234 |
7.22e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 152.12 E-value: 7.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSaIDVKNLVKKFHGQT-----VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTGKPISq 75
Cdd:PRK13637 1 MS-IKIENLTHIYMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 76 qkglIRRLRQHVGFVFQ--SFNLFpHRTVLENIIEGPVIVkGEPKEDATVRARELLAKVGLAG---KETSyPRRLSGGQQ 150
Cdd:PRK13637 78 ----LSDIRKKVGLVFQypEYQLF-EETIEKDIAFGPINL-GLSEEEIENRVKRAMNIVGLDYedyKDKS-PFELSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
Cdd:PRK13637 151 RRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPR 230
|
....*
gi 489956327 230 ALFAN 234
Cdd:PRK13637 231 EVFKE 235
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-227 |
7.25e-45 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 151.04 E-value: 7.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKG--LIR 81
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLN------GRPLAAWSPweLAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 R---LRQH--VGFVFqsfnlfphrTVLENIIEGpVIVKGEPKEDATVRARELLAKVGLAG-KETSYPRrLSGGQQQRVAI 155
Cdd:COG4559 76 RravLPQHssLAFPF---------TVEEVVALG-RAPHGSSAAQDRQIVREALALVGLAHlAGRSYQT-LSGGEQQRVQL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956327 156 ARALA-------MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
Cdd:COG4559 145 ARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGT 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-244 |
1.09e-44 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 150.78 E-value: 1.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHG----QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPIsQQ 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLD------GVPV-TG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 77 KGLIRrlrqhvGFVFQSFNLFPHRTVLENIIEGPVIvKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
Cdd:COG4525 74 PGADR------GVVFQKDALLPWLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 157 RALAMRPDVILFDEPTSALDP---ELVGEVLNTIRQLAQekRTMVIVTHEMSFARDVADRAIFMD--QGRIVEQ------ 225
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDAltrEQMQELLLDVWQRTG--KGVFLITHSVEEALFLATRLVVMSpgPGRIVERleldfs 224
|
250 260
....*....|....*....|....*
gi 489956327 226 ------GPAKALFANPQQPRTRQFL 244
Cdd:COG4525 225 rrflagEDARAIKSDPAFIALREEL 249
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-234 |
1.40e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 151.01 E-value: 1.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHG------QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDItiDTGKpisqqK 77
Cdd:PRK13633 5 IKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGL--DTSD-----E 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 78 GLIRRLRQHVGFVFQSfnlfPHRTVLENIIE-----GPVIVKGEPKEdatVRAR--ELLAKVGLAGKETSYPRRLSGGQQ 150
Cdd:PRK13633 78 ENLWDIRNKAGMVFQN----PDNQIVATIVEedvafGPENLGIPPEE---IRERvdESLKKVGMYEYRRHAPHLLSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAK 229
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGiTIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPK 229
|
....*
gi 489956327 230 ALFAN 234
Cdd:PRK13633 230 EIFKE 234
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-231 |
1.65e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 151.41 E-value: 1.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISqqkgliRR 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD------GEPLD------PE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 LRQHVGFVFQSFNLFPHRTVLEniiegpVIV-----KGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:COG4152 69 DRRRIGYLPEERGLYPKMKVGE------QLVylarlKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-221 |
2.48e-44 |
|
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: 148.74 E-value: 2.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSA-IDVKNLVKKF--HGQ-----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRV--GDITIDTG 70
Cdd:COG4778 1 MTTlLEVENLSKTFtlHLQggkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 71 KPISQQkglIRRLRQH-VGFVFQSFNLFPHRTVLENIIEgPVIVKGEPKEDATVRARELLAKVGLagketsyPRRL---- 145
Cdd:COG4778 81 QASPRE---ILALRRRtIGYVSQFLRVIPRVSALDVVAE-PLLERGVDREEARARARELLARLNL-------PERLwdlp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 146 ----SGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:COG4778 150 patfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-232 |
6.63e-44 |
|
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: 148.31 E-value: 6.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQP-EGGTIRVGDitidtgkpisQQKGL 79
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFG----------ERRGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 80 --IRRLRQHVGFVFQSFNLFPHR--TVLEniiegpVIVKG---------EPKEDATVRARELLAKVGLAGKETSYPRRLS 146
Cdd:COG1119 71 edVWELRKRIGLVSPALQLRFPRdeTVLD------VVLSGffdsiglyrEPTDEQRERARELLELLGLAHLADRPFGTLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 147 GGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQ 225
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAA 224
|
....*..
gi 489956327 226 GPAKALF 232
Cdd:COG1119 225 GPKEEVL 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-237 |
8.31e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 149.16 E-value: 8.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTGKpisQQKGLIRRLRQHVGFVFQsfnlFP 98
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITI-THK---TKDKYIRPVRKRIGMVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 99 HRTVLENIIEGPVIVK----GEPKEDATVRARELLAKVGLAGKETSY-PRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:PRK13646 95 ESQLFEDTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956327 174 ALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQ 237
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDEnKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKK 239
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-226 |
1.52e-43 |
|
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: 146.18 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGeVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtgkPISQQKglirrL 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQK-----L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLEnIIEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03264 71 RRRIGYLPQEFGVYPNFTVRE-FLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-226 |
1.60e-43 |
|
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: 146.21 E-value: 1.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRV-GDITIDTGKPisqqkglirr 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdGKSYQKNIEA---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 lRQHVGFVFQSFNLFPHRTVLENIIEGPVIvKGEPKEdatvRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:cd03268 71 -LRRIGALIEAPGFYPNLTARENLRLLARL-LGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-244 |
1.71e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 147.37 E-value: 1.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQ--PEGgtiRV-GDITIDtGKPISQQK 77
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEA---RVsGEVYLD-GQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 78 glIRRLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVK-GEPKEDATVRARELLAKVGL----AGKETSYPRRLSGGQQQR 152
Cdd:PRK14247 77 --VIELRRRVQMVFQIPNPIPNLSIFENVALGLKLNRlVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM-TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
250
....*....|..
gi 489956327 233 ANPQQPRTRQFL 244
Cdd:PRK14247 234 TNPRHELTEKYV 245
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-236 |
2.36e-43 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 146.71 E-value: 2.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTGKPISqqkgli 80
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLPMH------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRLRQHVGFVFQSFNLFPHRTVLENI---IEgpviVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:COG1137 74 KRARLGIGYLPQEASIFRKLTVEDNIlavLE----LRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQekRTM-VIVT-HEMSFARDVADRAIFMDQGRIVEQGPAKALFANP 235
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKE--RGIgVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
|
.
gi 489956327 236 Q 236
Cdd:COG1137 228 L 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-233 |
2.41e-43 |
|
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: 153.42 E-value: 2.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 21 GIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGT--IRVGDITIDTGKPISQQKGlirRLRQHVGFVFQSFNLFP 98
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPDGRG---RAKRYIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 99 HRTVLENIIEGpvIVKGEPKEDATVRARELLAKVGLAGKET-----SYPRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:TIGR03269 379 HRTVLDNLTEA--IGLELPDELARMKAVITLKMVGFDEEKAeeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956327 174 ALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-231 |
2.56e-43 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 147.47 E-value: 2.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 2 SAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLL----EQPEGGTIRVGDITIDTGKpisqQK 77
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRTVQREGR----LA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 78 GLIRRLRQHVGFVFQSFNLFPHRTVLENIIEGPVivKGEP---------KEDATVRARELLAKVGLAGKETSYPRRLSGG 148
Cdd:PRK09984 79 RDIRKSRANTGYIFQQFNLVNRLSVLENVLIGAL--GSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQGP 227
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYALRYCERIVALRQGHVFYDGS 236
|
....
gi 489956327 228 AKAL 231
Cdd:PRK09984 237 SQQF 240
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-232 |
4.05e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 147.20 E-value: 4.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGkpiSQQKGlIRRLRQHVGFVFQsfnlFP 98
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITST---SKNKD-IKQIRKKVGLVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 99 H-----RTVLENIIEGPVIVkGEPKEDATVRARELLAKVGLAGK--ETSyPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK13649 95 EsqlfeETVLKDVAFGPQNF-GVSQEEAEALAREKLALVGISESlfEKN-PFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956327 172 TSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-223 |
1.75e-42 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 141.80 E-value: 1.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQqKGLIRRL 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD------GKEVSF-ASPRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQsfnlfphrtvleniiegpvivkgepkedatvrarellakvglagketsyprrLSGGQQQRVAIARALAMRP 163
Cdd:cd03216 74 RAGIAMVYQ----------------------------------------------------LSVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-238 |
2.23e-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: 147.57 E-value: 2.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 22 IDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTgkpiSQQKGLIRRLRQHVGFVFQSFNLFPHRT 101
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFD----SRKGIFLPPEKRRIGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 102 VLENIIEGPVIVKGEPKEDATVRARELLAKVGLAGKetsYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVG 181
Cdd:TIGR02142 92 VRGNLRYGMKRARPSERRISFERVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489956327 182 EVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQP 238
Cdd:TIGR02142 169 EILPYLERLHAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLP 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-226 |
3.56e-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: 142.80 E-value: 3.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidTGKPISQQKglirrl 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF------DGKPLDIAA------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENIIEGPVIvKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-226 |
1.40e-41 |
|
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: 141.54 E-value: 1.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 23 DLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPisqqkglirrLRQHVGFVFQSFNLFPHRTV 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP----------YQRPVSMLFQENNLFAHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 103 LENI---IEGPVIVKGEPKEDATVRAREllakVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPEL 179
Cdd:TIGR01277 88 RQNIglgLHPGLKLNAEQQEKVVDAAQQ----VGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489956327 180 VGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:TIGR01277 164 REEMLALVKQLCSERqRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-225 |
1.58e-41 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 144.99 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPisqqkgl 79
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 80 irRLRQhVGFVFQSFNLFPHRTVLENIIEGPVIvKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:PRK11650 74 --ADRD-IAMVFQNYALYPHMSVRENMAYGLKI-RGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIvEQ 225
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGGVA-EQ 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-231 |
1.78e-41 |
|
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: 141.35 E-value: 1.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVG--DITIDTGKpisqqkglir 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAghDVVREPRE---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 rLRQHVGFVFQSFNLFPHRTVLENI-IEGPVivKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:cd03265 71 -VRRRIGIVFQDLSVDDELTGWENLyIHARL--YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956327 161 MRPDVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-246 |
2.26e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 142.44 E-value: 2.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 2 SAIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDtgkpisqqKGL 79
Cdd:PRK13632 6 VMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS--------KEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 80 IRRLRQHVGFVFQS-FNLFPHRTV-------LENiiegpvivKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQ 151
Cdd:PRK13632 78 LKEIRKKIGIIFQNpDNQFIGATVeddiafgLEN--------KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 152 RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKA 230
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTrKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKE 228
|
250
....*....|....*.
gi 489956327 231 LFANpqqprtRQFLEK 246
Cdd:PRK13632 229 ILNN------KEILEK 238
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-233 |
3.45e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 142.18 E-value: 3.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQT---VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRV-GD-ITIDTgkpisq 75
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDlLTEEN------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 76 qkglIRRLRQHVGFVFQS-FNLFPHRTV-------LENiiegpvivKGEPKEDATVRARELLAKVGLAGKETSYPRRLSG 147
Cdd:PRK13650 76 ----VWDIRHKIGMVFQNpDNQFVGATVeddvafgLEN--------KGIPHEEMKERVNEALELVGMQDFKEREPARLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSfarDVA--DRAIFMDQGRIVE 224
Cdd:PRK13650 144 GQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVIsITHDLD---EVAlsDRVLVMKNGQVES 220
|
....*....
gi 489956327 225 QGPAKALFA 233
Cdd:PRK13650 221 TSTPRELFS 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-232 |
3.87e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 142.57 E-value: 3.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTgkpISQQKGlIRRLRQHVGFVFQsfnlFP 98
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSS---TSKQKE-IKPVRKKVGVVFQ----FP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 99 H-----RTVLENIIEGPVIVkGEPKEDATVRARELLAKVGLAGK--ETSyPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK13643 94 EsqlfeETVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLADEfwEKS-PFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956327 172 TSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-233 |
4.04e-41 |
|
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: 140.44 E-value: 4.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 14 HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGgtirvGDITIDtGKPISQQKglIRRLRQHVGFVFQS 93
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQK-----GQILID-GIDIRDIS--RKSLRSMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 94 FNLFPhRTVLENIIEGPVIVKGEPKEDA--TVRARELLAK--------VGLAGKetsyprRLSGGQQQRVAIARALAMRP 163
Cdd:cd03254 86 TFLFS-GTIMENIRLGRPNATDEEVIEAakEAGAHDFIMKlpngydtvLGENGG------NLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-229 |
6.02e-41 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 146.71 E-value: 6.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISqqkglIRR 82
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILID------GKPVR-----IRS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 ----LRQHVGFVFQSFNLFPHRTVLENIIEG--PVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
Cdd:COG3845 74 prdaIALGIGMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956327 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-235 |
6.08e-41 |
|
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: 140.37 E-value: 6.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTGKPISqqkgliRRL 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLPMH------KRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENII---EgpviVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:cd03218 74 RLGIGYLPQEASIFRKLTVEENILavlE----IRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956327 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANP 235
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-231 |
6.38e-41 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 140.10 E-value: 6.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 23 DLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITiDTGKPISQQKglirrlrqhVGFVFQSFNLFPHRTV 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRP---------VSMLFQENNLFSHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 103 LENIIEG--PVIvkgepKEDATVRA--RELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPE 178
Cdd:PRK10771 89 AQNIGLGlnPGL-----KLNAAQREklHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489956327 179 LVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
Cdd:PRK10771 164 LRQEMLTLVSQVCQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
3-239 |
9.35e-41 |
|
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: 148.09 E-value: 9.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISqqkgli 80
Cdd:TIGR03375 463 EIEFRNVSFAYPGQEtpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAD------ 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 rrLRQHVGFVFQSFNLFpHRTVLENIIEGpvivkgepkeDATVRARELLAKVGLAGKET---SYP-----------RRLS 146
Cdd:TIGR03375 537 --LRRNIGYVPQDPRLF-YGTLRDNIALG----------APYADDEEILRAAELAGVTEfvrRHPdgldmqigergRSLS 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 147 GGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFArDVADRAIFMDQGRIVEQG 226
Cdd:TIGR03375 604 GGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK-TLVLVTHRTSLL-DLVDRIIVMDNGRIVADG 681
|
250
....*....|...
gi 489956327 227 PAKALFANPQQPR 239
Cdd:TIGR03375 682 PKDQVLEALRKGR 694
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-245 |
1.56e-40 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 139.97 E-value: 1.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSA-IDVKNLVKKFHGQT---------VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTG 70
Cdd:COG4167 1 MSAlLEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 71 KpisqqkglIRRLRQHVGFVFQ----SFNlfPHRTVLEnIIEGPVIVKgepkEDATVRAREL-----LAKVGLAGKETS- 140
Cdd:COG4167 81 D--------YKYRCKHIRMIFQdpntSLN--PRLNIGQ-ILEEPLRLN----TDLTAEEREErifatLRLVGLLPEHANf 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 141 YPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMD 218
Cdd:COG4167 146 YPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLEL-QEKLgiSYIYVSQHLGIVKHISDKVLVMH 224
|
250 260
....*....|....*....|....*..
gi 489956327 219 QGRIVEQGPAKALFANPQQPRTRQFLE 245
Cdd:COG4167 225 QGEVVEYGKTAEVFANPQHEVTKRLIE 251
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-244 |
1.67e-40 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 143.05 E-value: 1.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPisqqkglirrL 83
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP----------Y 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENIIEGpviVKGE--PKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:PRK11607 90 QRPINMMFQSYALFPHMTVEQNIAFG---LKQDklPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 162 RPDVILFDEPTSALDPELVGEV-LNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQPRT 240
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
....
gi 489956327 241 RQFL 244
Cdd:PRK11607 247 AEFI 250
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-226 |
2.31e-40 |
|
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: 138.49 E-value: 2.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISqqkgli 80
Cdd:cd03245 2 RIEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 rrLRQHVGFVFQSFNLFpHRTVLENIIEGPVIVKGEpkedatvrarELLAKVGLAGKeTSYPRR---------------L 145
Cdd:cd03245 76 --LRRNIGYVPQDVTLF-YGTLRDNITLGAPLADDE----------RILRAAELAGV-TDFVNKhpngldlqigergrgL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 146 SGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFArDVADRAIFMDQGRIVEQ 225
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK-TLIIITHRPSLL-DLVDRIIVMDSGRIVAD 219
|
.
gi 489956327 226 G 226
Cdd:cd03245 220 G 220
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-227 |
4.49e-40 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 139.05 E-value: 4.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHG---------QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidTGK 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW------RGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 72 PISQQKGLIRR-LRQHVGFVFQ----SFNlfPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGLAGKETS-YPRRL 145
Cdd:PRK10419 75 PLAKLNRAQRKaFRRDIQMVFQdsisAVN--PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDkRPPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 146 SGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
...
gi 489956327 225 QGP 227
Cdd:PRK10419 233 TQP 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-247 |
4.78e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 139.58 E-value: 4.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGD--ITIDTGkpisqQKGLiRRLRQHVGFVFQsfnl 96
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhITPETG-----NKNL-KKLRKKVSLVFQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 97 FPH-----RTVLENIIEGPVIVkGEPKEDATVRARELLAKVGLAGKETSY-PRRLSGGQQQRVAIARALAMRPDVILFDE 170
Cdd:PRK13641 93 FPEaqlfeNTVLKDVEFGPKNF-GFSEDEAKEKALKWLKKVGLSEDLISKsPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 171 PTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQ--------QPRTRQ 242
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwlkkhyldEPATSR 251
|
....*
gi 489956327 243 FLEKF 247
Cdd:PRK13641 252 FASKL 256
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-226 |
5.64e-40 |
|
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: 144.17 E-value: 5.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTL---LRSINLLEQPEGGTI----------------RVGD 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLmhvLRGMDQYEPTSGRIIyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 65 ITIDTGKPISQQ--------KGLIRRLRQHVGFVFQ-SFNLFPHRTVLENIIEG-PVIvkGEPKEDATVRARELLAKVGL 134
Cdd:TIGR03269 81 PCPVCGGTLEPEevdfwnlsDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEAlEEI--GYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 135 AGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADR 213
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGiSMVLTSHWPEVIEDLSDK 238
|
250
....*....|...
gi 489956327 214 AIFMDQGRIVEQG 226
Cdd:TIGR03269 239 AIWLENGEIKEEG 251
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-233 |
1.75e-39 |
|
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: 136.59 E-value: 1.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtgKPISQQKglirrLRQHVGFVFQSF 94
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI---REVTLDS-----LRRAIGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 95 NLFpHRTVLENIIEGPVIVKGEPKEDATVRAR---ELLA-------KVGLAGketsypRRLSGGQQQRVAIARALAMRPD 164
Cdd:cd03253 85 VLF-NDTIGYNIRYGRPDATDEEVIEAAKAAQihdKIMRfpdgydtIVGERG------LKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956327 165 VILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-236 |
3.68e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 136.79 E-value: 3.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFH-GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidTGKPISQQKglIR 81
Cdd:PRK13647 4 IIEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKV------MGREVNAEN--EK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 RLRQHVGFVFQSFN--LFPhRTVLENIIEGPVIVKGEPKEdATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:PRK13647 76 WVRSKVGLVFQDPDdqVFS-STVWDDVAFGPVNMGLDKDE-VERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGpAKALFANPQ 236
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDED 229
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-236 |
5.03e-39 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 139.01 E-value: 5.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPisQQKGli 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP--AERG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 rrlrqhVGFVFQSFNLFPHRTVLENIIEGpVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK11000 77 ------VGMVFQSYALYPHLSVAENMSFG-LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQ 236
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-241 |
6.76e-39 |
|
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: 141.81 E-value: 6.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPisqqkgliRRLRQHVGFVFQSF 94
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR--------EELGRHIGYLPQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 95 NLFPHrTVLENIiegpvivkGEPKEDATVRAREL---------LAK-----VGLAGketsypRRLSGGQQQRVAIARALA 160
Cdd:COG4618 416 ELFDG-TIAENIar-----fGDADPEKVVAAAKLagvhemilrLPDgydtrIGEGG------ARLSGGQRQRIGLARALY 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 161 MRPDVILFDEPTSALDPElvGE--VLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALFANPQQP 238
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDE--GEaaLAAAIRALKARGATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVLARLARP 560
|
...
gi 489956327 239 RTR 241
Cdd:COG4618 561 AAA 563
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-227 |
7.12e-39 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 134.15 E-value: 7.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPE---GGTIRVGDITIDTGKPisqqkglirr 82
Cdd:COG4136 4 LENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 LRQHVGFVFQSFNLFPHRTVLENIIEGpvIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:COG4136 74 EQRRIGILFQDDLLFPHLSVGENLAFA--LPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956327 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHemsfarDVADRAifmDQGRIVEQGP 227
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIpALLVTH------DEEDAP---AAGRVLDLGN 208
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
8-225 |
9.19e-39 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 134.56 E-value: 9.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 8 NLVKKFH-GQT---VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgditIDTGKPISQQKGLIR-R 82
Cdd:PRK11629 10 NLCKRYQeGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV------IFNGQPMSKLSSAAKaE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 LRQH-VGFVFQSFNLFPHRTVLENIIEgPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:PRK11629 84 LRNQkLGFIYQFHHLLPDFTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956327 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVaDRAIFMDQGRIVEQ 225
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTaFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
14-207 |
9.59e-39 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 134.52 E-value: 9.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 14 HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidTGKPISQQKGLIR-RLR-QHVGFVF 91
Cdd:PRK10584 21 HELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSL------VGQPLHQMDEEARaKLRaKHVGFVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 92 QSFNLFPHRTVLENIiEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK10584 95 QSFMLIPTLNALENV-ELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 489956327 172 TSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFA 207
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLA 210
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
15-235 |
9.67e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 135.89 E-value: 9.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDItiDTGKPISQQKglIRRLrqhVGFVFQSF 94
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGI--DTGDFSKLQG--IRKL---VGIVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 95 NL-FPHRTVLENIIEGPVIVKGEPKEdatVRAR--ELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK13644 87 ETqFVGRTVEEDLAFGPENLCLPPIE---IRKRvdRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 172 TSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFANP 235
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-227 |
9.79e-39 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 135.21 E-value: 9.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKG--LIR 81
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVD------GLDVATTPSreLAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 R---LRQHVGFVFQ-------SFNLFPHRtvleniiegpvivKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQ 151
Cdd:COG4604 76 RlaiLRQENHINSRltvrelvAFGRFPYS-------------KGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 152 RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELgKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-234 |
9.93e-39 |
|
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: 134.59 E-value: 9.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLvkKFH-----GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLEQ---PEGGTIrvgdiTIDtGKPISQ 75
Cdd:cd03249 1 IEFKNV--SFRypsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTV---VSLLERfydPTSGEI-----LLD-GVDIRD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 76 QKglIRRLRQHVGFVFQSFNLFPhRTVLENIIEGpvivkgepKEDATVRARELLAKVGLA---------GKET---SYPR 143
Cdd:cd03249 70 LN--LRWLRSQIGLVSQEPVLFD-GTIAENIRYG--------KPDATDEEVEEAAKKANIhdfimslpdGYDTlvgERGS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 144 RLSGGQQQRVAIARALAMRPDVILFDEPTSALDPE---LVGEVLNTIRqlaqEKRTMVIVTHEMSFARDvADRAIFMDQG 220
Cdd:cd03249 139 QLSGGQKQRIAIARALLRNPKILLLDEATSALDAEsekLVQEALDRAM----KGRTTIVIAHRLSTIRN-ADLIAVLQNG 213
|
250
....*....|....
gi 489956327 221 RIVEQGPAKALFAN 234
Cdd:cd03249 214 QVVEQGTHDELMAQ 227
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-231 |
1.28e-38 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 136.37 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 11 KKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVG--DITIDTgkpisqqkgliRRLRQHVG 88
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAgyDVVREP-----------RKVRRSIG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 89 FVFQSFNLFPHRTVLENIiEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILF 168
Cdd:TIGR01188 70 IVPQYASVDEDLTGRENL-EMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956327 169 DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
Cdd:TIGR01188 149 DEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-233 |
1.39e-38 |
|
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: 134.28 E-value: 1.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKF--HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKpisqqkglIR 81
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT--------LA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 RLRQHVGFVFQSFNLFpHRTVLENIIEGpvivkgepKEDATVRARELLAKVGLA---------GKETSYPRR---LSGGQ 149
Cdd:cd03251 73 SLRRQIGLVSQDVFLF-NDTVAENIAYG--------RPGATREEVEEAARAANAhefimelpeGYDTVIGERgvkLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAK 229
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHE 221
|
....
gi 489956327 230 ALFA 233
Cdd:cd03251 222 ELLA 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
19-245 |
1.65e-38 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 134.91 E-value: 1.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDtGKPISQQKGLIRRLRQHVGFVFQSFNLFP 98
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFH-GKNLYAPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 99 hRTVLENIIEGPVI--VKGEPKE--DATVRARELLAKVGLAGKETSYPrrLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:PRK14243 105 -KSIYDNIAYGARIngYKGDMDElvERSLRQAALWDEVKDKLKQSGLS--LSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 175 LDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMD---------QGRIVEQGPAKALFANPQQPRTRQFLE 245
Cdd:PRK14243 182 LDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSPQQQATRDYVS 260
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-222 |
9.25e-38 |
|
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: 130.03 E-value: 9.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHG--QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKglIR 81
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD------GADISQWD--PN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 RLRQHVGFVFQSFNLFPHrTVLENIiegpvivkgepkedatvrarellakvglagketsyprrLSGGQQQRVAIARALAM 161
Cdd:cd03246 73 ELGDHVGYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956327 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQGRI 222
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
15-243 |
1.02e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 133.43 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKGLIRRLRQHVGFVFQS- 93
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFD------GKPIDYSRKGLMKLRESVGMVFQDp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 94 -FNLFPhRTVLENIIEGPVIVkGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:PRK13636 92 dNQLFS-ASVYQDVSFGAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956327 173 SALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQPRTRQF 243
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKVNL 241
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-244 |
1.06e-37 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 136.32 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 24 LEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDItiDTGKPISQQKGLIRRlrQHVGFVFQSFNLFPHRTVL 103
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGV--DIAKISDAELREVRR--KKIAMVFQSFALMPHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 104 ENIIEGpVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEV 183
Cdd:PRK10070 125 DNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956327 184 LNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQPRTRQFL 244
Cdd:PRK10070 204 QDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-220 |
1.51e-37 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 131.43 E-value: 1.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidTGKPIsQQKGLIRRLrqhvgfVFQSFNLFP 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL------EGKQI-TEPGPDRMV------VFQNYSLLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 99 HRTVLENI-IEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:TIGR01184 68 WLTVRENIaLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489956327 178 ELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQG 220
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-226 |
2.80e-37 |
|
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: 130.47 E-value: 2.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLeQPEGGTIRvGDITIDtGKPISQQKglirrLRQHVGFVFQSFNLF 97
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-VEGGGTTS-GQILFN-GQPRKPDQ-----FQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 98 PHRTVLENIIEGPVIVKGEPKEDATVRAR---ELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:cd03234 94 PGLTVRETLTYTAILRLPRKSSDAIRKKRvedVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489956327 175 LDPELVGEVLNTIRQLAQEKRTMVIVTHE-MSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-217 |
2.89e-37 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 137.03 E-value: 2.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 2 SAIDVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISqqkgli 80
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS------ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 rrLRQHVGFVFQSFNLFPhRTVLENIIEGpvivKGEPKEDATVRArelLAKVGLAGKETSYP-----------RRLSGGQ 149
Cdd:TIGR02857 394 --WRDQIAWVPQHPFLFA-GTIAENIRLA----RPDASDAEIREA---LERAGLDEFVAALPqgldtpigeggAGLSGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956327 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFM 217
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-244 |
4.43e-37 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 130.98 E-value: 4.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQqKGLIRr 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLD------GKPVEG-PGAER- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 lrqhvGFVFQSFNLFPHRTVLENIIEGpVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:PRK11248 73 -----GVVFQNEGLLPWRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAAN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMV-IVTHEMSFARDVADRAIFM--DQGRIVEQ------------GP 227
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVlLITHDIEEAVFMATELVLLspGPGRVVERlplnfarrfvagES 226
|
250
....*....|....*..
gi 489956327 228 AKALFANPQQPRTRQFL 244
Cdd:PRK11248 227 SRSIKSDPQFIAMREYV 243
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
3-233 |
4.54e-37 |
|
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: 137.78 E-value: 4.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFH--GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgdiTIDtGKPISqqkGL- 79
Cdd:TIGR03797 451 AIEVDRVTFRYRpdGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSV-----FYD-GQDLA---GLd 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 80 IRRLRQHVGFVFQSFNLFPHrTVLENIIEGPVIvkgePKEDATVRAREllakVGLAGKETSYP-----------RRLSGG 148
Cdd:TIGR03797 522 VQAVRRQLGVVLQNGRLMSG-SIFENIAGGAPL----TLDEAWEAARM----AGLAEDIRAMPmgmhtviseggGTLSGG 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPA 228
Cdd:TIGR03797 593 QRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL---KVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTY 668
|
....*
gi 489956327 229 KALFA 233
Cdd:TIGR03797 669 DELMA 673
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-241 |
6.14e-37 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 132.52 E-value: 6.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 21 GIDLEVEQGEVVAIIGPSGSGKTTLLRS-INLLEQPEGGTIRVG-DITidtgkpiSQQKGLIRRLRQHVGFVFQ----SF 94
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAiIGLVKATDGEVAWLGkDLL-------GMKDDEWRAVRSDIQMIFQdplaSL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 95 NlfPHRTVLENIIEG-----PVIVKGEPKEdatvRARELLAKVGLAGKETS-YPRRLSGGQQQRVAIARALAMRPDVILF 168
Cdd:PRK15079 112 N--PRMTIGEIIAEPlrtyhPKLSRQEVKD----RVKAMMLKVGLLPNLINrYPHEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 169 DEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQPRTR 241
Cdd:PRK15079 186 DEPVSALDVSIQAQVVNLLQQLQREMGlSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTK 259
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-226 |
8.91e-37 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 128.44 E-value: 8.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 14 HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINllEQPEGGTIRvGDITIDtGKPISQqkgliRRLRQHVGFVFQS 93
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALA--GRRTGLGVS-GEVLIN-GRPLDK-----RSFRKIIGYVPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 94 FNLFPHRTVLENIiegpvivkgepkedatvrarELLAKVglagketsypRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:cd03213 91 DILHPTLTVRETL--------------------MFAAKL----------RGLSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489956327 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS---FArdVADRAIFMDQGRIVEQG 226
Cdd:cd03213 141 GLDSSSALQVMSLLRRLADTGRTIICSIHQPSseiFE--LFDKLLLLSQGRVIYFG 194
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-233 |
1.74e-36 |
|
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: 128.76 E-value: 1.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISqqkglirrLRQHVGFVFQSF 94
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW--------LRRQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 95 NLFpHRTVLENIIEGPvivKGEPKEDATVRAR-----ELLAKVGLaGKETSYPRR---LSGGQQQRVAIARALAMRPDVI 166
Cdd:cd03252 86 VLF-NRSIRDNIALAD---PGMSMERVIEAAKlagahDFISELPE-GYDTIVGEQgagLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 167 LFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-244 |
2.52e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 129.01 E-value: 2.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 2 SAIDVKNLVKKF---HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISQQKG 78
Cdd:PRK14246 6 SAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 79 LirRLRQHVGFVFQSFNLFPHRTVLENIIEgPVIVKG-EPKEDATVRARELLAKVGL----AGKETSYPRRLSGGQQQRV 153
Cdd:PRK14246 86 I--KLRKEVGMVFQQPNPFPHLSIYDNIAY-PLKSHGiKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
Cdd:PRK14246 163 TIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI-AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
250
....*....|.
gi 489956327 234 NPQQPRTRQFL 244
Cdd:PRK14246 242 SPKNELTEKYV 252
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
15-223 |
2.71e-36 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 128.07 E-value: 2.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKGL-IRRLRQHVGFVFQS 93
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFS------GHDITRLKNReVPFLRRQIGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 94 FNLFPHRTVLENIiEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:PRK10908 88 HHLLMDRTVYDNV-AIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489956327 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-244 |
1.38e-35 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 127.12 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 2 SAIDVKNLVKKFHGQTVlHGIDLEVEQGEVVAIIGPSGSGKT-TLLRSINLLeqPEGGTIRVGDITIDtGKPISQQKgli 80
Cdd:PRK10418 3 QQIELRNIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGIL--PAGVRQTAGRVLLD-GKPVAPCA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 rrLR-QHVGFVFQ----SFNlfPHRTVLENIIEgPVIVKGEPKEDATVRAreLLAKVGLAGKET---SYPRRLSGGQQQR 152
Cdd:PRK10418 76 --LRgRKIATIMQnprsAFN--PLHTMHTHARE-TCLALGKPADDATLTA--ALEAVGLENAARvlkLYPFEMSGGMLQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
250
....*....|...
gi 489956327 232 FANPQQPRTRQFL 244
Cdd:PRK10418 229 FNAPKHAVTRSLV 241
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-213 |
5.02e-35 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 123.88 E-value: 5.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 13 FHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidTGKPIS---QQKGLIRRL----RQ 85
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA-----GGARVAyvpQRSEVPDSLpltvRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 86 HVgfvfqSFNLFPHRTVLeniiegpvivkGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:NF040873 77 LV-----AMGRWARRGLW-----------RRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489956327 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADR 213
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADP 187
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-233 |
7.06e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 126.46 E-value: 7.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 2 SAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidTGKPISQQKgliR 81
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISL------CGEPVPSRA---R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 RLRQHVGFVFQSFNLFPHRTVLENIIegpVIVKGEPKEDATVRAR--ELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:PRK13537 77 HARQRVGVVPQFDNLDPDFTVRENLL---VFGRYFGLSAAAARALvpPLLEFAKLENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-235 |
7.33e-35 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 128.42 E-value: 7.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITID--TGKPISQQkg 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEalSARAASRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 79 lirrlrqhVGFVFQ----SFNlFPHRTVLEnIIEGPVIVKGEPKEDATVRA-RELLAKVGLAGKETSYPRRLSGGQQQRV 153
Cdd:PRK09536 79 --------VASVPQdtslSFE-FDVRQVVE-MGRTPHRSRFDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLT 228
|
..
gi 489956327 234 NP 235
Cdd:PRK09536 229 AD 230
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-234 |
7.41e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 126.28 E-value: 7.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTG-KPISQqkglIRRLRQHVGFVFQ--SFN 95
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlKKIKE----VKRLRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 96 LFpHRTVLENIIEGPVIVkGEPKEDATVRARELLAKVGLAGKETS-YPRRLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:PRK13645 103 LF-QETIEKDIAFGPVNL-GENKQEAYKKVPELLKLVQLPEDYVKrSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956327 175 LDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAN 234
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
1.32e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 125.30 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidTGKPISQQKgl 79
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLI------RGEPITKEN-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 80 IRRLRQHVGFVFQSFN--LFPhRTVLENIIEGPVIVkGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:PRK13652 73 IREVRKFVGLVFQNPDdqIFS-PTVEQDIAFGPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956327 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANP 235
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-235 |
1.74e-34 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 130.61 E-value: 1.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 16 QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgdiTIDtGKPISQQKGliRRLRQHVGFVFQSFN 95
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV-----LLD-GVPLVQYDH--HYLHRQVALVGQEPV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 96 LFpHRTVLENIIEGpviVKGEPKEDATVRARELLAKVGLAGKETSYPR-------RLSGGQQQRVAIARALAMRPDVILF 168
Cdd:TIGR00958 566 LF-SGSVRENIAYG---LTDTPDEEIMAAAKAANAHDFIMEFPNGYDTevgekgsQLSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956327 169 DEPTSALDPElvgevlntIRQLAQE-----KRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFANP 235
Cdd:TIGR00958 642 DEATSALDAE--------CEQLLQEsrsraSRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-233 |
1.96e-34 |
|
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: 129.84 E-value: 1.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgDITIDtGKPIsqQKGLIRRLRQHVGFVFQSF 94
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSG-----QILLD-GHDL--ADYTLASLRRQVALVSQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 95 NLFpHRTVLENIIEGPVIVKGEPKEDATVRARELLAKV-----GLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFD 169
Cdd:TIGR02203 416 VLF-NDTIANNIAYGRTEQADRAEIERALAAAYAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILD 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 170 EPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
Cdd:TIGR02203 495 EATSALDNESERLVQAALERLMQG-RTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLA 556
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-244 |
2.30e-34 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 129.98 E-value: 2.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 29 GEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISQQKglirrLRQHVGFVFQS--FNLFPHRTVLENI 106
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQA-----LRRDIQFIFQDpyASLDPRQTVGDSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 107 IEgPVIVKG-EPKEDATVRARELLAKVGLAGKET-SYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVL 184
Cdd:PRK10261 425 ME-PLRVHGlLPGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQII 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956327 185 NTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQPRTRQFL 244
Cdd:PRK10261 504 NLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-226 |
2.56e-34 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 129.31 E-value: 2.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLEQ---PEGGTIRVGDITIdtgkpisqqKGLIRR-LRQHVGFVFQSF 94
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRvfdPQSGRILIDGTDI---------RTVTRAsLRRNIAVVFQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 95 NLFpHRTVLENIIEGpvivkgepKEDAT----VRARELLAKVG-LAGKETSYP-------RRLSGGQQQRVAIARALAMR 162
Cdd:PRK13657 419 GLF-NRSIEDNIRVG--------RPDATdeemRAAAERAQAHDfIERKPDGYDtvvgergRQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 163 PDVILFDEPTSALDPEL---VGEVLNTIRQlaqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQG 226
Cdd:PRK13657 490 PPILILDEATSALDVETeakVKAALDELMK----GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-232 |
3.23e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 124.09 E-value: 3.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDitidtgKPISQQKglIR 81
Cdd:PRK13648 8 IVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN------QAITDDN--FE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 RLRQHVGFVFQS-FNLFPHRTV-------LENiiegpvivKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRV 153
Cdd:PRK13648 80 KLRKHIGIVFQNpDNQFVGSIVkydvafgLEN--------HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIIsITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-247 |
4.58e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 128.79 E-value: 4.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKGli 80
Cdd:PRK11160 338 SLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLN------GQPIADYSE-- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRLRQHVGFVFQSFNLFPHrTVLENIIegpvIVKGEPKEDATVrarELLAKVGLAGKETSYP----------RRLSGGQQ 150
Cdd:PRK11160 410 AALRQAISVVSQRVHLFSA-TLRDNLL----LAAPNASDEALI---EVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAKA 230
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK-TVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQE 559
|
250
....*....|....*..
gi 489956327 231 LFAnpQQPRTRQFLEKF 247
Cdd:PRK11160 560 LLA--QQGRYYQLKQRL 574
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-226 |
4.79e-34 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 120.88 E-value: 4.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQ--TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPeggtiRVGDITIDtGKPISQQKGLir 81
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKP-----QQGEITLD-GVPVSDLEKA-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 rLRQHVGFVFQSFNLFpHRTVLENIiegpvivkgepkedatvrarellakvglagketsyPRRLSGGQQQRVAIARALAM 161
Cdd:cd03247 73 -LSSLISVLNQRPYLF-DTTLRNNL-----------------------------------GRRFSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956327 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSfARDVADRAIFMDQGRIVEQG 226
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK-TLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-222 |
6.25e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 127.87 E-value: 6.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidtgkpisqQKGLirrlrq 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-------------PKGL------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 86 HVGFVFQSFNLFPHRTVLENIIEGPVIVK-------------GEPKED------------------ATVRARELLAKVGL 134
Cdd:COG0488 62 RIGYLPQEPPLDDDLTVLDTVLDGDAELRaleaeleeleaklAEPDEDlerlaelqeefealggweAEARAEEILSGLGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 135 AGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDpelvgevLNTIR----QLAQEKRTMVIVTHEMSFARD 209
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIEwleeFLKNYPGTVLVVSHDRYFLDR 214
|
250
....*....|...
gi 489956327 210 VADRAIFMDQGRI 222
Cdd:COG0488 215 VATRILELDRGKL 227
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-245 |
1.13e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 122.57 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTgkpISQQKglIRRL 83
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPA---MSRSR--LYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENI-------IEGPvivkgEPKEDATVRARelLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
Cdd:PRK11831 83 RKRMSMLFQSGALFTDMNVFDNVayplrehTQLP-----APLLHSTVMMK--LEAVGLRGAAKLMPSELSGGMARRAALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANP 235
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
250
....*....|
gi 489956327 236 qQPRTRQFLE 245
Cdd:PRK11831 236 -DPRVRQFLD 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-244 |
1.35e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 127.13 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKT-TLLRSINLLEQPEGGTIRvGDITIDTGKPISQQKG 78
Cdd:PRK15134 6 LAIENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVVYPS-GDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 79 LIRRLR-QHVGFVFQS--FNLFPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGL---AGKETSYPRRLSGGQQQR 152
Cdd:PRK15134 85 TLRGVRgNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
250
....*....|...
gi 489956327 232 FANPQQPRTRQFL 244
Cdd:PRK15134 245 FSAPTHPYTQKLL 257
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-245 |
1.62e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 126.74 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 7 KNLVKKFHGQ-TVLHGIDLEVEQGEVVAIIGPSGSGKTT----LLRSINlleqpeggtiRVGDITIDtGKPISQqkgLIR 81
Cdd:PRK15134 289 KGILKRTVDHnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN----------SQGEIWFD-GQPLHN---LNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 R----LRQHVGFVFQSFN--LFPHRTVLENIIEG-----PVIVKGEPKEdatvRARELLAKVGL-AGKETSYPRRLSGGQ 149
Cdd:PRK15134 355 RqllpVRHRIQVVFQDPNssLNPRLNVLQIIEEGlrvhqPTLSAAQREQ----QVIAVMEEVGLdPETRHRYPAEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPA 228
Cdd:PRK15134 431 RQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLfISHDLHVVRALCHQVIVLRQGEVVEQGDC 510
|
250
....*....|....*..
gi 489956327 229 KALFANPQQPRTRQFLE 245
Cdd:PRK15134 511 ERVFAAPQQEYTRQLLA 527
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-226 |
1.78e-33 |
|
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: 127.24 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 17 TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRsinLLEQ---PEGGTIRVGDITIDTgkpISQQKglirrLRQHVGFVFQS 93
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLAR---LLFRfydVTSGRILIDGQDIRD---VTQAS-----LRAAIGIVPQD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 94 FNLFpHRTVLENIIEGpvivkgepKEDATvrARELLAKVGLA-----------GKETSYPRR---LSGGQQQRVAIARAL 159
Cdd:COG5265 441 TVLF-NDTIAYNIAYG--------RPDAS--EEEVEAAARAAqihdfieslpdGYDTRVGERglkLSGGEKQRVAIARTL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQG 226
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQAALREVARG-RTTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-223 |
2.19e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 121.35 E-value: 2.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTV-----LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINlleqpegGTIRV--GDITIDtGKPISQQ 76
Cdd:COG1101 2 LELKNLSKTFNPGTVnekraLDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIA-------GSLPPdsGSILID-GKDVTKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 77 KgLIRRLRqHVGFVFQ--SFNLFPHRTVLENII------EGPVIVKGEPKEDatvRA--RELLAKVGLaGKEtsypRR-- 144
Cdd:COG1101 74 P-EYKRAK-YIGRVFQdpMMGTAPSMTIEENLAlayrrgKRRGLRRGLTKKR---RElfRELLATLGL-GLE----NRld 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 145 -----LSGGQQQrvaiARALAM----RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRA 214
Cdd:COG1101 144 tkvglLSGGQRQ----ALSLLMatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNRL 219
|
....*....
gi 489956327 215 IFMDQGRIV 223
Cdd:COG1101 220 IMMHEGRII 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-244 |
2.72e-33 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 126.89 E-value: 2.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 6 VKNLVKKFH--GQTV--LHGIDLEVEQGEVVAIIGPSGSGKT-TLLRSINLLEQpEGGTIRVGDI--------TIDTGKp 72
Cdd:PRK10261 15 VENLNIAFMqeQQKIaaVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMllrrrsrqVIELSE- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 73 isQQKGLIRRLR-QHVGFVFQS--FNLFPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGLAGKET---SYPRRLS 146
Cdd:PRK10261 93 --QSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTilsRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 147 GGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQ 225
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIfITHDMGVVAEIADRVLVMYQGEAVET 250
|
250
....*....|....*....
gi 489956327 226 GPAKALFANPQQPRTRQFL 244
Cdd:PRK10261 251 GSVEQIFHAPQHPYTRALL 269
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-226 |
5.76e-33 |
|
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: 119.39 E-value: 5.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQT----VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgdiTIDtGKPISQQKgl 79
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA-----TVD-GFDVVKEP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 80 iRRLRQHVGFVFQSFNLFPHRTVLENIiEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:cd03266 74 -AEARRRLGFVSDSTGLYDRLTARENL-EYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-229 |
9.46e-33 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 119.42 E-value: 9.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MS-AIDVKNLVKKFHGQ----------------------TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEG 57
Cdd:COG1134 1 MSsMIEVENVSKSYRLYhepsrslkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 58 GTIRV-GDIT--IDTGkpisqqkglirrlrqhVGFVfqsfnlfPHRTVLENIIEGPVIVkGEPKEDATVRARELLAKVGL 134
Cdd:COG1134 81 GRVEVnGRVSalLELG----------------AGFH-------PELTGRENIYLNGRLL-GLSRKEIDEKFDEIVEFAEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 135 aGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADR 213
Cdd:COG1134 137 -GDFIDQPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDR 215
|
250
....*....|....*.
gi 489956327 214 AIFMDQGRIVEQGPAK 229
Cdd:COG1134 216 AIWLEKGRLVMDGDPE 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-235 |
9.48e-33 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 119.71 E-value: 9.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTGKPiSQQ---KGLIRr 82
Cdd:PRK11300 8 VSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI-EGLP-GHQiarMGVVR- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 lrqhvgfVFQSFNLFPHRTVLEN------------IIEG----PVIVKGEpkEDATVRARELLAKVGLagkeTSYPRR-- 144
Cdd:PRK11300 85 -------TFQHVRLFREMTVIENllvaqhqqlktgLFSGllktPAFRRAE--SEALDRAATWLERVGL----LEHANRqa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 145 --LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:PRK11300 152 gnLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
250
....*....|....
gi 489956327 222 IVEQGPAKALFANP 235
Cdd:PRK11300 232 PLANGTPEEIRNNP 245
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
10-242 |
1.14e-32 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 121.91 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 10 VKKFHGQTVLHgIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDIT-IDTGKPISqqkgLIRRLRqHVG 88
Cdd:PRK11144 6 FKQQLGDLCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFDAEKGIC----LPPEKR-RIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 89 FVFQSFNLFPHRTVLENIIEGpviVKGEPKEdatvrarELLAKVGLAGKE---TSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:PRK11144 80 YVFQDARLFPHYKVRGNLRYG---MAKSMVA-------QFDKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQ----QPRT 240
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmrpwLPKE 229
|
..
gi 489956327 241 RQ 242
Cdd:PRK11144 230 EQ 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-221 |
1.85e-32 |
|
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: 117.57 E-value: 1.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInLLE-QPEGGTIRVGDitidtgkpisqqkglirrlrqHVGFVFQS--- 93
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-LGElEKLSGSVSVPG---------------------SIAYVSQEpwi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 94 FNlfphRTVLENIIEGPVIvkGEPKEDATVRARELLAKVGL--AGKETSYPRR---LSGGQQQRVAIARALAMRPDVILF 168
Cdd:cd03250 78 QN----GTIRENILFGKPF--DEERYEKVIKACALEPDLEIlpDGDLTEIGEKginLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489956327 169 DEPTSALDPElVGEVL--NTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGR 221
Cdd:cd03250 152 DDPLSAVDAH-VGRHIfeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-239 |
3.72e-32 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 117.69 E-value: 3.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTgKPISQqkgli 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISL-LPLHA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 rRLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK10895 75 -RARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956327 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQPR 239
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-241 |
5.56e-32 |
|
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: 117.62 E-value: 5.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISQQKGLIRRL 83
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 -RQHVGFVFQSFNLFPHRTVLE--NIIEGPVIVKGEPKEDATVRARELLAKVGL-AGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:TIGR02323 84 mRTEWGFVHQNPRDGLRMRVSAgaNIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQP 238
Cdd:TIGR02323 164 VTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGlAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHP 243
|
...
gi 489956327 239 RTR 241
Cdd:TIGR02323 244 YTQ 246
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-236 |
1.07e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 117.59 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgdITIDtGKPISQQKglIRRLRQHVGFVFQS-FNL 96
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSK--ITVD-GITLTAKT--VWDIREKVGIVFQNpDNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 97 FPHRTV-------LENiiegpvivKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFD 169
Cdd:PRK13640 97 FVGATVgddvafgLEN--------RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956327 170 EPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFANPQ 236
Cdd:PRK13640 169 ESTSMLDPAGKEQILKLIRKLKKKNNlTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-222 |
1.95e-31 |
|
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: 114.07 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 10 VKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPIsqqkgliRRLRQHVGF 89
Cdd:cd03215 7 VRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPR-------DAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 90 V---FQSFNLFPHRTVLENIIegpvivkgepkedatvrarellakvglagketsYPRRLSGGQQQRVAIARALAMRPDVI 166
Cdd:cd03215 80 VpedRKREGLVLDLSVAENIA---------------------------------LSSLLSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489956327 167 LFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-224 |
1.99e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 120.94 E-value: 1.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDiTIdtgkpisqqkglirrl 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE-TV---------------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 rqHVGFVFQSF-NLFPHRTVLENIIEGpvivkGEPKEDATVRAreLLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAM 161
Cdd:COG0488 379 --KIGYFDQHQeELDPDKTVLDELRDG-----APGGTEQEVRG--YLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956327 162 RPDVILFDEPTSALDPELVgEVLNTIrqLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETL-EALEEA--LDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-236 |
4.25e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 115.96 E-value: 4.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQT---VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSIN-LLEQPEGgtirvgDITIDTGKPISQQkgl 79
Cdd:PRK13642 5 LEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDgLFEEFEG------KVKIDGELLTAEN--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 80 IRRLRQHVGFVFQS-FNLFPHRTVLENIIEGpVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
Cdd:PRK13642 76 VWNLRRKIGMVFQNpDNQFVGATVEDDVAFG-MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956327 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFANPQ 236
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-236 |
4.39e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 115.21 E-value: 4.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTGKPISQqkglIRRLRq 85
Cdd:COG4674 13 VEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDL-TGLDEHE----IARLG- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 86 hVGFVFQSFNLFPHRTVLENIIegpVIVKGEP--------KEDATVRAR--ELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
Cdd:COG4674 87 -IGRKFQKPTVFEELTVFENLE---LALKGDRgvfaslfaRLTAEERDRieEVLETIGLTDKADRLAGLLSHGQKQWLEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 156 ARALAMRPDVILFDEPTSALDP---ELVGEVLNTIRQlaqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
Cdd:COG4674 163 GMLLAQDPKLLLLDEPVAGMTDaetERTAELLKSLAG----KHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQ 238
|
....
gi 489956327 233 ANPQ 236
Cdd:COG4674 239 ADPR 242
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-244 |
4.60e-31 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 115.41 E-value: 4.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTI--RVGDITIDTGKPISQQKgliRR- 82
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyRMRDGQLRDLYALSEAE---RRr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 -LRQHVGFVFQSF--NLFPHRTVLENIIEgPVIVKGEpKEDATVRAREL--LAKVGLAGKETS-YPRRLSGGQQQRVAIA 156
Cdd:PRK11701 86 lLRTEWGFVHQHPrdGLRMQVSAGGNIGE-RLMAVGA-RHYGDIRATAGdwLERVEIDAARIDdLPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANP 235
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGlAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDP 243
|
....*....
gi 489956327 236 QQPRTrQFL 244
Cdd:PRK11701 244 QHPYT-QLL 251
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
3-233 |
8.09e-31 |
|
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: 120.23 E-value: 8.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISqqkgli 80
Cdd:TIGR01846 455 AITFENIRFRYAPDSpeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAW------ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 rrLRQHVGFVFQSFNLFpHRTVLENI-IEGPVIvkgepkEDATVRARELLAK-----VGLA-GKETSYPRR---LSGGQQ 150
Cdd:TIGR01846 529 --LRRQMGVVLQENVLF-SRSIRDNIaLCNPGA------PFEHVIHAAKLAGahdfiSELPqGYNTEVGEKganLSGGQR 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKA 230
Cdd:TIGR01846 600 QRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR-GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEE 677
|
...
gi 489956327 231 LFA 233
Cdd:TIGR01846 678 LLA 680
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-244 |
2.94e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 114.84 E-value: 2.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 22 IDLEVEQGEVVAIIGPSGSGKT-TLLRSINLLEQPegGTIRVGDITIDtGKPISQQKGLIRR--LRQHVGFVFQS--FNL 96
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKLEFN-GQDLQRISEKERRnlVGAEVAMIFQDpmTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 97 FPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGL---AGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:PRK11022 103 NPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956327 174 ALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANPQQPRTRQFL 244
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALL 254
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-202 |
3.00e-30 |
|
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: 117.85 E-value: 3.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgdiTIDTGKPISQQKGLIRRLrqhVGFVFQSF 94
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV-----TLDGVPVSSLDQDEVRRR---VSVCAQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 95 NLFpHRTVLENIIEGpvivkgepKEDAT-VRARELLAKVGLA--------GKET---SYPRRLSGGQQQRVAIARALAMR 162
Cdd:TIGR02868 419 HLF-DTTVRENLRLA--------RPDATdEELWAALERVGLAdwlralpdGLDTvlgEGGARLSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489956327 163 PDVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTH 202
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
19-226 |
3.10e-30 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 118.07 E-value: 3.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLEQ---PEGGTIRVGDITIDTgkpISQQKglirrLRQHVGFVFQSFN 95
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKTTL---INLLQRvydPTVGQILIDGIDINT---VTRES-----LRKSIATVFQDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 96 LFpHRTVLENIIEGpvivkgepKEDATV------------------RARELLAKVGLAGKetsyprRLSGGQQQRVAIAR 157
Cdd:TIGR01192 420 LF-NRSIRENIRLG--------REGATDeevyeaakaaaahdfilkRSNGYDTLVGERGN------RLSGGERQRLAIAR 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956327 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQG 226
Cdd:TIGR01192 485 AILKNAPILVLDEATSALDVETEARVKNAIDALRKN-RTTFIIAHRLSTVRN-ADLVLFLDQGRLIEKG 551
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-234 |
2.05e-29 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 110.35 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSinLLEQPEGGTirvGDITIDtGKPISQQKgLIRRLRQHVGFVFQSFNLF 97
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGT--LCGDPRATS---GRIVFD-GKDITDWQ-TAKIMREAVAIVPEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 98 PHRTVLENIIEGPVIVKGEPKEDATVRARELLAKvgLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:PRK11614 93 SRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 178 ELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAN 234
Cdd:PRK11614 171 IIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-223 |
5.10e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.96 E-value: 5.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 10 VKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPIsqqkgliRRLRQHVGF 89
Cdd:COG1129 259 VEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPR-------DAIRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 90 V---FQSFNLFPHRTVLENII--------EGPVIVKGepKEDAtvRARELLAKVGLAGKETSYP-RRLSGGQQQRVAIAR 157
Cdd:COG1129 332 VpedRKGEGLVLDLSIRENITlasldrlsRGGLLDRR--RERA--LAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAK 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956327 158 ALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:COG1129 408 WLATDPKVLILDEPTRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-226 |
1.18e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 108.95 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDitidtgKPISQQKGliRRL 83
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD------KPISMLSS--RQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQsfnlfpHRTVLENIIEGPVIVKGE-----------PKEDATV-RARELLAKVGLAGKETSyprRLSGGQQQ 151
Cdd:PRK11231 75 ARRLALLPQ------HHLTPEGITVRELVAYGRspwlslwgrlsAEDNARVnQAMEQTRINHLADRRLT---DLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956327 152 RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
15-233 |
2.52e-28 |
|
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: 112.91 E-value: 2.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKglIRRLRQHVGFVFQSF 94
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN------GFSLKDID--RHTLRQFINYLPQEP 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 95 NLFPHrTVLENIIEGPVIVKGEPKEDATVRARELLAKV-----GLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFD 169
Cdd:TIGR01193 558 YIFSG-SILENLLLGAKENVSQDEIWAACEIAEIKDDIenmplGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILD 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 170 EPTSALDPELVGEVLNTIRQLaQEKrTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKALFA 233
Cdd:TIGR01193 637 ESTSNLDTITEKKIVNNLLNL-QDK-TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLD 697
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-227 |
3.01e-28 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 112.45 E-value: 3.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 17 TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLrsiNLLEQ-PEGGTIRVGDITIDtGKPISQQKglirrLRQHVGFVFQSFN 95
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFrSPKGVKGSGSVLLN-GMPIDAKE-----MRAISAYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 96 LFPHRTVLENIIEGPVIVKGE--PKEDATVRARELLAKVGL---AGKETSYPRR---LSGGQQQRVAIARALAMRPDVIL 167
Cdd:TIGR00955 110 FIPTLTVREHLMFQAHLRMPRrvTKKEKRERVDEVLQALGLrkcANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956327 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS---FarDVADRAIFMDQGRIVEQGP 227
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSselF--ELFDKIILMAEGRVAYLGS 250
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-229 |
4.03e-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: 106.07 E-value: 4.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPE--GGTIRVGDITIdTGKPISQqkglirRL 83
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDI-TDLPPEE------RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSfnlfphrtvleniiegPVIVKGepkedatVRARELLAKVGLAgketsyprrLSGGQQQRVAIARALAMRP 163
Cdd:cd03217 76 RLGIFLAFQY----------------PPEIPG-------VKNADFLRYVNEG---------FSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH-EMSFARDVADRAIFMDQGRIVEQGPAK 229
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-228 |
5.91e-28 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 106.69 E-value: 5.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI--NLLEQPEGGTIRVGDITIdTGKPISQqkglirRL 83
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDI-LELSPDE------RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQS---------FNLFphRTVLENIIEGPVIVKGEPKEdatvrARELLAKVGLAgkeTSYPRR-----LSGGQ 149
Cdd:COG0396 76 RAGIFLAFQYpveipgvsvSNFL--RTALNARRGEELSAREFLKL-----LKEKMKELGLD---EDFLDRyvnegFSGGE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHemsFAR----DVADRAIFMDQGRIVEQ 225
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH---YQRildyIKPDFVHVLVDGRIVKS 222
|
...
gi 489956327 226 GPA 228
Cdd:COG0396 223 GGK 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-221 |
1.16e-27 |
|
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: 103.30 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInlleqpeggtirVGDITIDTGKPISQQKGLIRRL 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI------------AGELEPDEGIVTWGSTVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQhvgfvfqsfnlfphrtvleniiegpvivkgepkedatvrarellakvglagketsyprrLSGGQQQRVAIARALAMRP 163
Cdd:cd03221 69 EQ-----------------------------------------------------------LSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489956327 164 DVILFDEPTSALDPELVgEVLntIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:cd03221 90 NLLLLDEPTNHLDLESI-EAL--EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-222 |
1.54e-27 |
|
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: 105.25 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLE---QPEGGTIRVgditidTGKPISQQKGliRRLRQHVGFVFQSF 94
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTV---VALLEnfyQPQGGQVLL------DGKPISQYEH--KYLHSKVSLVGQEP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 95 NLFPhRTVLENIIEGPVIVKGEPKEDATVRAR-----ELLAK-----VGLAGKEtsyprrLSGGQQQRVAIARALAMRPD 164
Cdd:cd03248 98 VLFA-RSLQDNIAYGLQSCSFECVKEAAQKAHahsfiSELASgydteVGEKGSQ------LSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489956327 165 VILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRI 222
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-233 |
3.72e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 105.47 E-value: 3.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 12 KFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgditIDTGKPISQQKGLIRRLRQHVGFVF 91
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV------LWQGKPLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 92 QSfnlfPHRTVLENIIEGPVIVK----GEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVIL 167
Cdd:PRK13638 84 QD----PEQQIFYTDIDSDIAFSlrnlGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956327 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-226 |
3.87e-27 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 108.72 E-value: 3.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKP-ISQQKGlirr 82
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHkLAAQLG---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 lrqhVGFVFQSFNLFPHRTVLENIIEGPVIVK---GEPKED---ATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
Cdd:PRK09700 82 ----IGIIYQELSVIDELTVLENLYIGRHLTKkvcGVNIIDwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-202 |
5.25e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 108.74 E-value: 5.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 2 SAIDVKNL-VKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLeQPEGGtirvGDITIDTGKPI---SQQK 77
Cdd:COG4178 361 GALALEDLtLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL-WPYGS----GRIARPAGARVlflPQRP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 78 GLIR-RLRQHVgfvfqsfnLFPHRTvleniiegpvivkgEPKEDATVRarELLAKVGLA------GKETSYPRRLSGGQQ 150
Cdd:COG4178 436 YLPLgTLREAL--------LYPATA--------------EAFSDAELR--EALEAVGLGhlaerlDEEADWDQVLSLGEQ 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489956327 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTH 202
Cdd:COG4178 492 QRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-226 |
5.33e-27 |
|
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: 103.77 E-value: 5.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 17 TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidTGKPISQqkglirrLRQHVGFVfqsfnl 96
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV------RGRVSSL-------LGLGGGFN------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 97 fPHRTVLENI-IEGpvIVKGEPKEDATVRARELLAKVGLaGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:cd03220 97 -PELTGRENIyLNG--RLLGLSRKEIDEKIDEIIEFSEL-GDFIDLPvKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489956327 175 LDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03220 173 GDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-228 |
9.17e-27 |
|
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: 107.82 E-value: 9.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 16 QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPisqqkgliRRLRQHVGFVFQSFN 95
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDR--------ETFGKHIGYLPQDVE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 96 LFPHrTVLENIIEgpvivKGEPKEDATVRARELLAKV-----GLA-GKETSYPRR---LSGGQQQRVAIARALAMRPDVI 166
Cdd:TIGR01842 403 LFPG-TVAENIAR-----FGENADPEKIIEAAKLAGVhelilRLPdGYDTVIGPGgatLSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 167 LFDEPTSALDPElvGE--VLNTIRQLAQEKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPA 228
Cdd:TIGR01842 477 VLDEPNSNLDEE--GEqaLANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGER 537
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-224 |
1.17e-26 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 102.73 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 16 QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI--NLLEQPEGGTIRVGDITIDTGKPIsqqkglirrlrqhvgfvfqs 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFGREASL-------------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 94 fnlfphrtvLENIiegpvivkgePKEDATVRARELLAKVGLAgkeTSY-----PRRLSGGQQQRVAIARALAMRPDVILF 168
Cdd:COG2401 103 ---------IDAI----------GRKGDFKDAVELLNAVGLS---DAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489956327 169 DEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVA-DRAIFMDQGRIVE 224
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLARRAGiTLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-226 |
2.26e-26 |
|
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: 102.41 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 6 VKNLVK-KFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITidtgkPISQQKGLIRRLr 84
Cdd:cd03267 23 LKSLFKrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV-----PWKRRKKFLRRI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 85 qhvGFVF-------------QSFNLFPHrtvleniiegpviVKGEPKEDATVRARELLAKVGLaGKETSYP-RRLSGGQQ 150
Cdd:cd03267 97 ---GVVFgqktqlwwdlpviDSFYLLAA-------------IYDLPPARFKKRLDELSELLDL-EELLDTPvRQLSLGQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03267 160 MRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTsHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
11-205 |
4.25e-26 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 106.50 E-value: 4.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 11 KKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTirvGDITIDTGKPISQqkgLIRRlrqhVGFV 90
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFT---GTILANNRKPTKQ---ILKR----TGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 91 FQSFNLFPHRTVLENIIEGPVI--VKGEPKEDATVRARELLAKVGLAGKET-----SYPRRLSGGQQQRVAIARALAMRP 163
Cdd:PLN03211 146 TQDDILYPHLTVRETLVFCSLLrlPKSLTKQEKILVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINP 225
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPS 267
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-210 |
8.50e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 100.56 E-value: 8.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPisqqkgliRRLRQHVGFVFQSF 94
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP--------EIYRQQVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 95 NLFPHrTVLENIIEGPVIVKGEPKEDATVRArelLAKVGLAgkETSYPRR---LSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK10247 91 TLFGD-TVYDNLIFPWQIRNQQPDPAIFLDD---LERFALP--DTILTKNiaeLSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489956327 172 TSALDPELVGEVLNTIRQLAQEKRTMVI-VTH---EMSFARDV 210
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLwVTHdkdEINHADKV 207
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-227 |
8.51e-26 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 100.65 E-value: 8.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKF--HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTirvgdITIDtGKPISQQkGLiR 81
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGS-----ILID-GVDISKI-GL-H 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 RLRQHVGFVFQSFNLFPHrTVLENIieGPvivKGEPKEDATVRArelLAKVGLAGKETSYPRRL-----------SGGQQ 150
Cdd:cd03244 75 DLRSRISIIPQDPVLFSG-TIRSNL--DP---FGEYSDEELWQA---LERVGLKEFVESLPGGLdtvveeggenlSVGQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGP 227
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-231 |
8.92e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 102.99 E-value: 8.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidTGKPISQQkglI 80
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV------LGVPVPAR---A 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRLRQHVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKEDATVrARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK13536 110 RLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAV-IPSLLEFARLESKADARVSDLSGGMKRRLTLARALI 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956327 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-231 |
1.04e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 104.63 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 7 KNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLeQPEGGTirVGDITIDtGKPI-------SQQKGL 79
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGTY--EGEIIFE-GEELqasnirdTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 80 IrrlrqhvgFVFQSFNLFPHRTVLENIIEGPVIVKGEPKEDATV--RARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:PRK13549 85 A--------IIHQELALVKELSVLENIFLGNEITPGGIMDYDAMylRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-226 |
1.14e-25 |
|
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: 100.17 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgDITIDtGKPISqqkgliRRL 83
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSG-----EIIFD-GHPWT------RKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENIiEGPVIVKGEPKEdatvRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:TIGR03740 69 LHKIGSLIESPPLYENLTARENL-KVHTTLLGLPDS----RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHP 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:TIGR03740 144 KLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQG 206
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-238 |
1.82e-25 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 102.11 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGgtiRVGDITIDTGKPIS-- 74
Cdd:PRK09473 10 DALLDVKDLRVTFSTPdgdvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANG---RIGGSATFNGREILnl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 75 QQKGLiRRLR-QHVGFVFQ----SFNlfPHRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGL--AGKE-TSYPRRLS 146
Cdd:PRK09473 87 PEKEL-NKLRaEQISMIFQdpmtSLN--PYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMpeARKRmKMYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 147 GGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQ 225
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEY 243
|
250
....*....|...
gi 489956327 226 GPAKALFANPQQP 238
Cdd:PRK09473 244 GNARDVFYQPSHP 256
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-226 |
2.46e-25 |
|
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: 104.71 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 6 VKNLVKKFH--GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGkpisqqkglIRRL 83
Cdd:TIGR01257 931 VKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN---------LDAV 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENIIEGPVIvKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:TIGR01257 1002 RQSLGMCPQHNILFHHLTVAEHILFYAQL-KGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDA 1080
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:TIGR01257 1081 KVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-231 |
3.00e-25 |
|
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: 103.37 E-value: 3.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLeQPEGGTirVGDITIDtGKPIsQQKGLIRRL 83
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGTW--DGEIYWS-GSPL-KASNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENIIEGPVIV-KGEPKEDA--TVRARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARAL 159
Cdd:TIGR02633 77 RAGIVIIHQELTLVPELSVAENIFLGNEITlPGGRMAYNamYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956327 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-202 |
3.56e-25 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 98.20 E-value: 3.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKGLirrLRQ 85
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWN------GTPLAEQRDE---PHE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 86 HVGFVFQSFNLFPHRTVLENI-----IEGPvivkgepkEDATVRarELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:TIGR01189 74 NILYLGHLPGLKPELSALENLhfwaaIHGG--------AQRTIE--DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489956327 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH 202
Cdd:TIGR01189 144 SRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-226 |
4.99e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 103.00 E-value: 4.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHG-IDLEVEQGEVVAIIGPSGSGKTTLLrsiNLLEQ--PEGGTIRVGDITIdtgkpisqqkgli 80
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLL---NALLGflPYQGSLKINGIEL------------- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRL-----RQHVGFVFQSFNLFpHRTVLENIIEGPVIVKGEPKEDATVRAR--ELLAKV--GLAG--KETSypRRLSGGQ 149
Cdd:PRK11174 414 RELdpeswRKHLSWVGQNPQLP-HGTLRDNVLLGNPDASDEQLQQALENAWvsEFLPLLpqGLDTpiGDQA--AGLSVGQ 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVaDRAIFMDQGRIVEQG 226
Cdd:PRK11174 491 AQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ-TTLMVTHQLEDLAQW-DQIWVMQDGQIVQQG 565
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-244 |
7.20e-25 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 99.09 E-value: 7.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKK-------FHGQTV--LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgDITIDtGKPIS 74
Cdd:PRK15112 5 LEVRNLSKTfryrtgwFRRQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSG-----ELLID-DHPLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 75 QqkGLIRRLRQHVGFVFQ--SFNLFPhRTVLENIIEGPVIVKGE-PKEDATVRARELLAKVGLAGKETSY-PRRLSGGQQ 150
Cdd:PRK15112 79 F--GDYSYRSQRIRMIFQdpSTSLNP-RQRISQILDFPLRLNTDlEPEQREKQIIETLRQVGLLPDHASYyPHMLAPGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLEL-QEKQgiSYIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
250
....*....|....*.
gi 489956327 229 KALFANPQQPRTRQFL 244
Cdd:PRK15112 235 ADVLASPLHELTKRLI 250
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-224 |
3.25e-24 |
|
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: 100.64 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 22 IDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKglIRRLRQHVGFVFQSFNLFPHrt 101
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLD------GQPVTADN--REAYRQLFSAVFSDFHLFDR-- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 102 vleniiegpviVKGEPKEDATVRARELLAKVGLAGKeTSY------PRRLSGGQQQRVAIARALAMRPDVILFDEPTSAL 175
Cdd:COG4615 421 -----------LLGLDGEADPARARELLERLELDHK-VSVedgrfsTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQ 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 176 DP--------ELVGEvlntirqLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVE 224
Cdd:COG4615 489 DPefrrvfytELLPE-------LKARGKTVIAISHDDRYF-DLADRVLKMDYGKLVE 537
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-227 |
6.00e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 99.74 E-value: 6.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPI-SQQKGLIrr 82
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAkAHQLGIY-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 lrqhvgFVFQSFNLFPHRTVLENIIegpvivKGEPK-EDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALaM 161
Cdd:PRK15439 90 ------LVPQEPLLFPNLSVKENIL------FGLPKrQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGL-M 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 162 RPDVIL-FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
Cdd:PRK15439 157 RDSRILiLDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-207 |
1.11e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 94.49 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 20 HGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQQKGLIRRlrqhvgfvfqsfNLF-- 97
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ------GEPIRRQRDEYHQ------------DLLyl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 98 -------PHRTVLENI-----IEGPVivkgepKEDATVRArelLAKVGLAGKETSYPRRLSGGQQQRVAIAR-ALAMRPD 164
Cdd:PRK13538 80 ghqpgikTELTALENLrfyqrLHGPG------DDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARlWLTRAPL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489956327 165 VILfDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVT--HEMSFA 207
Cdd:PRK13538 151 WIL-DEPFTAIDKQGVARLEALLAQHA-EQGGMVILTthQDLPVA 193
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-234 |
1.58e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 96.69 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFH--------GQTV-------------LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIR 61
Cdd:COG4586 1 IIEVENLSKTYRvyekepglKGALkglfrreyreveaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 62 VGDITidtgkPISQQKglirRLRQHVGFVF-------------QSFNLFPHrtvleniiegpviVKGEPKEDATVRAREL 128
Cdd:COG4586 81 VLGYV-----PFKRRK----EFARRIGVVFgqrsqlwwdlpaiDSFRLLKA-------------IYRIPDAEYKKRLDEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 129 LAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFA 207
Cdd:COG4586 139 VELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTsHDMDDI 218
|
250 260
....*....|....*....|....*..
gi 489956327 208 RDVADRAIFMDQGRIVEQGPAKALFAN 234
Cdd:COG4586 219 EALCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-202 |
5.38e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.63 E-value: 5.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISQQkglirrlrQHVGfvfqsf 94
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAC--------HYLG------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 95 nlfpHR-------TVLENI-----IEGpvivkgepkeDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:PRK13539 80 ----HRnamkpalTVAENLefwaaFLG----------GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSN 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489956327 163 PDVILFDEPTSALDPELVGEVLNTIR-QLAQEkrTMVIV-TH 202
Cdd:PRK13539 146 RPIWILDEPTAALDAAAVALFAELIRaHLAQG--GIVIAaTH 185
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-224 |
7.45e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.52 E-value: 7.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 8 NLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPisQQKGLIRR-LRQH 86
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID------GQE--MRFASTTAaLAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 87 VGFVFQSFNLFPHRTVLENIIEGPVIVKGE--PKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPD 164
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGQLPHKGGivNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956327 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADR-AIFMDqGRIVE 224
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAiTVFKD-GRYVA 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3-235 |
5.78e-22 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 94.39 E-value: 5.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDItidtgkPISQQKglIRR 82
Cdd:PRK10789 315 DVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI------PLTKLQ--LDS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 LRQHVGFVFQSFNLFPHrTVLENIIEGpvivkgepKEDATVRARELLAKvgLA-----------GKETSYPRR---LSGG 148
Cdd:PRK10789 387 WRSRLAVVSQTPFLFSD-TVANNIALG--------RPDATQQEIEHVAR--LAsvhddilrlpqGYDTEVGERgvmLSGG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPA 228
Cdd:PRK10789 456 QKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNH 533
|
....*..
gi 489956327 229 KALFANP 235
Cdd:PRK10789 534 DQLAQQS 540
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-202 |
6.19e-22 |
|
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: 89.86 E-value: 6.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidTGKPISQQKGLIRRL 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLL------NGGPLDFQRDSIARG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGfvfQSFNLFPHRTVLENIIEGPVIVKGEPKEDAtvrarelLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03231 75 LLYLG---HAPGIKTTLSVLENLRFWHADHSDEQVEEA-------LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGR 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH 202
Cdd:cd03231 145 PLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-231 |
8.82e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.55 E-value: 8.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 6 VKNL-VKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTGKPISQqkglIRRL- 83
Cdd:COG3845 260 VENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI-TGLSPRE----RRRLg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 -------RQHVGfvfqsfnLFPHRTVLENII----------EGPVIVKGEPKEDAT-------VRARELLAKVglagket 139
Cdd:COG3845 335 vayipedRLGRG-------LVPDMSVAENLIlgryrrppfsRGGFLDRKAIRAFAEelieefdVRTPGPDTPA------- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 140 sypRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIF 216
Cdd:COG3845 401 ---RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLD---VGaieFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAV 474
|
250
....*....|....*
gi 489956327 217 MDQGRIVEQGPAKAL 231
Cdd:COG3845 475 MYEGRIVGEVPAAEA 489
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-226 |
1.83e-21 |
|
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: 88.62 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKF--HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKpisqqkglIR 81
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP--------LE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 RLRQHVGFVFQSfnlfphrtvleniiegPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:cd03369 79 DLRSSLTIIPQD----------------PTLFSGTIRSNLDPFDEYSDEEIYGALRVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956327 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQG 226
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-234 |
2.62e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 92.88 E-value: 2.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 16 QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLrSINLLEQPeggtirvgditidtgkPISQQKGLIRRLRQHVGFVFQSFN 95
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLI-SAMLGELP----------------PRSDASVVIRGTVAYVPQVSWIFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 96 lfphRTVLENIIEGPVI--VKGEPKEDATVRARELLAKVGlaGKETSYPRR---LSGGQQQRVAIARALAMRPDVILFDE 170
Cdd:PLN03130 693 ----ATVRDNILFGSPFdpERYERAIDVTALQHDLDLLPG--GDLTEIGERgvnISGGQKQRVSMARAVYSNSDVYIFDD 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 171 PTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKALFAN 234
Cdd:PLN03130 767 PLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-233 |
2.65e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 92.39 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLeqpeggT----IRVGDITIDtGKPISQQKglIRRLRQHVGFVFQSF 94
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTI---ANLL------TrfydIDEGEILLD-GHDLRDYT--LASLRNQVALVSQNV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 95 NLFpHRTVLENIiegpvivkGEPKEDATVRAR-ELLAKVGLA---------GKETSYPRR---LSGGQQQRVAIARALAM 161
Cdd:PRK11176 427 HLF-NDTIANNI--------AYARTEQYSREQiEEAARMAYAmdfinkmdnGLDTVIGENgvlLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956327 162 RPDVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLA 567
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-226 |
2.71e-21 |
|
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: 88.09 E-value: 2.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 11 KKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEqpeGGTIRV-GDITIDtGKPIsqqKGLIRRLRQHVGF 89
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT---EGNVSVeGDIHYN-GIPY---KEFAEKYPGEIIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 90 VFQSFNLFPHRTVLENIiegpvivkgepkeDATVRARellakvglaGKEtsYPRRLSGGQQQRVAIARALAMRPDVILFD 169
Cdd:cd03233 88 VSEEDVHFPTLTVRETL-------------DFALRCK---------GNE--FVRGISGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956327 170 EPTSALDPELVGEVLNTIRQLAQEKRTMVIVTheMSFARDVA----DRAIFMDQGRIVEQG 226
Cdd:cd03233 144 NSTRGLDSSTALEILKCIRTMADVLKTTTFVS--LYQASDEIydlfDKVLVLYEGRQIYYG 202
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-202 |
5.83e-21 |
|
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: 86.44 E-value: 5.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgditidtGKPisqqkglirrLRQHVGFVfqsf 94
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------GMP----------EGEDLLFL---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 95 nlfPHRTVLeniiegpvivkgepkedATVRARELLAkvglagketsYP--RRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:cd03223 70 ---PQRPYL-----------------PLGTLREQLI----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEAT 119
|
170 180 190
....*....|....*....|....*....|.
gi 489956327 173 SALDPelvgEVLNTIRQLAQEKRTMVI-VTH 202
Cdd:cd03223 120 SALDE----ESEDRLYQLLKELGITVIsVGH 146
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-231 |
8.82e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.12 E-value: 8.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 7 KNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidTGKPISQ--QKGLIRRlr 84
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL------DGEHIQHyaSKEVARR-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 85 qhVGFVFQSFNLFPHRTVLENIIEG-----PVIVKGEPK-EDATVRARELLAKVGLAGKETSyprRLSGGQQQRVAIARA 158
Cdd:PRK10253 83 --IGLLAQNATTPGDITVQELVARGryphqPLFTRWRKEdEEAVTKAMQATGITHLADQSVD---TLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-190 |
1.73e-20 |
|
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: 89.99 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDiTIdtgkpisqqkglirrl 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE-TV---------------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 rqHVGFVFQSF-NLFPHRTVLENIIEG-PVIVKGepkeDATVRARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALA 160
Cdd:TIGR03719 386 --KLAYVDQSRdALDPNKTVWEEISGGlDIIKLG----KREIPSRAYVGRFNFKGSDQQKKvGQLSGGERNRVHLAKTLK 459
|
170 180 190
....*....|....*....|....*....|
gi 489956327 161 MRPDVILFDEPTSALDpelvgevLNTIRQL 190
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLD-------VETLRAL 482
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-233 |
4.34e-20 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 89.23 E-value: 4.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI-NLLEQPEGGTirvgditidtgkpisqqkglirRLRQHVGFVFQSfNLF 97
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALlAEMDKVEGHV----------------------HMKGSVAYVPQQ-AWI 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 98 PHRTVLENIIEGPVIvkGEPKEDATVRARELLAKVGL--AGKETSYPRR---LSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:TIGR00957 711 QNDSLRENILFGKAL--NEKYYQQVLEACALLPDLEIlpSGDRTEIGEKgvnLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956327 173 SALDPELVGEVL-NTIRQLAQEK-RTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKALFA 233
Cdd:TIGR00957 789 SAVDAHVGKHIFeHVIGPEGVLKnKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
14-232 |
8.02e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 85.70 E-value: 8.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 14 HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINlleqpegGTIRV--GDITIdTGKPISQQkglirrLRQH-VGFV 90
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALM-------GFVRLasGKISI-LGQPTRQA------LQKNlVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 91 FQSFNL---FPhrTVLENIIE----GPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:PRK15056 84 PQSEEVdwsFP--VLVEDVVMmgryGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIfMDQGRIVEQGPAKALF 232
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTF 229
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-245 |
1.27e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 86.11 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKF---HGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInLLEQPEGGTI-----RVGDITIdTGK 71
Cdd:COG4170 1 MPLLDIRNLTIEIdtpQGRVkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAI-CGITKDNWHVtadrfRWNGIDL-LKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 72 PISQQKGLIRRlrqHVGFVFQ--SFNLFPHRTVLENIIEgpVI----VKG---EPKEDATVRARELLAKVGLAGKE---T 139
Cdd:COG4170 79 SPRERRKIIGR---EIAMIFQepSSCLDPSAKIGDQLIE--AIpswtFKGkwwQRFKWRKKRAIELLHRVGIKDHKdimN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 140 SYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMD 218
Cdd:COG4170 154 SYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLY 233
|
250 260
....*....|....*....|....*..
gi 489956327 219 QGRIVEQGPAKALFANPQQPRTRQFLE 245
Cdd:COG4170 234 CGQTVESGPTEQILKSPHHPYTKALLR 260
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-227 |
1.45e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 84.88 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI--NLLE--QPEGGTIRvGDITIDtGKPISQQKGL-IRRLR----- 84
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGggAPRGARVT-GDVTLN-GEPLAAIDAPrLARLRavlpq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 85 -QHVGFVFQ-----SFNLFPH--RTVLENIIEGPVIvkgepkedatVRARELLAKVGLAGKETSyprRLSGGQQQRVAIA 156
Cdd:PRK13547 91 aAQPAFAFSareivLLGRYPHarRAGALTHRDGEIA----------WQALALAGATALVGRDVT---TLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 157 RALAM---------RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:PRK13547 158 RVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLaIVHDPNLAARHADRIAMLADGAIVAHG 237
|
.
gi 489956327 227 P 227
Cdd:PRK13547 238 A 238
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-231 |
1.95e-19 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 85.94 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 2 SAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTllrsinlleqpegGTIRVGDITIDTGKP-------IS 74
Cdd:NF000106 12 NAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-------------GALPAHV*GPDAGRRpwrf*twCA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 75 QQKGLIRRLRQHVGFVFQSFNLFPHRTVLENIIEGPVIvkgePKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVA 154
Cdd:NF000106 79 NRRALRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDL----SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
Cdd:NF000106 155 LAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-225 |
1.97e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.60 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAI-DVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIR-VGDITIDTGKPISQQKG 78
Cdd:PRK10762 1 MQALlQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 79 lirrlrqhVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKED---ATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
Cdd:PRK10762 81 --------IGIIHQELNLIPQLTIAENIFLGREFVNRFGRIDwkkMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956327 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADR-AIFMDQGRIVEQ 225
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDvTVFRDGQFIAER 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-234 |
2.90e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 86.57 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQT---VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInLLEQPEGGTIRVgditidtgkpisqqkgl 79
Cdd:PLN03232 614 AISIKNGYFSWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM-LGELSHAETSSV----------------- 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 80 irRLRQHVGFVFQSFNLFpHRTVLENIIEGPvivKGEPKE-----DATVRAREL-------LAKVGLAGKEtsyprrLSG 147
Cdd:PLN03232 676 --VIRGSVAYVPQVSWIF-NATVRENILFGS---DFESERywraiDVTALQHDLdllpgrdLTEIGERGVN------ISG 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGP 227
Cdd:PLN03232 744 GQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGT 822
|
....*..
gi 489956327 228 AKALFAN 234
Cdd:PLN03232 823 FAELSKS 829
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-220 |
2.95e-19 |
|
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: 82.29 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSinLLEQPEGGTIRvGDITIDtGKPISQQkglirrLRQHVGFVFQSFNLFP 98
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDV--LAGRKTAGVIT-GEILIN-GRPLDKN------FQRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 99 HRTVLENIiegpvivkgepkedatvrarELLAKVglagketsypRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPE 178
Cdd:cd03232 93 NLTVREAL--------------------RFSALL----------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489956327 179 LVGEVLNTIRQLAQEKRTMVIVTHEMS---FARdvADRAIFMDQG 220
Cdd:cd03232 143 AAYNIVRFLKKLADSGQAILCTIHQPSasiFEK--FDRLLLLKRG 185
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-229 |
3.60e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 83.35 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI-NLLEQPeggtirvGDITIDtGKPISQQKG--LIRR---LRQHV--GF- 89
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMaGLLPGQ-------GEILLN-GRPLSDWSAaeLARHrayLSQQQspPFa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 90 --VFQSFNLFPHRTVLENIIEGPVivkgepkedatvraRELLAKVGLAGKetsYPR---RLSGGQQQRVAIARAL----- 159
Cdd:COG4138 84 mpVFQYLALHQPAGASSEAVEQLL--------------AQLAEALGLEDK---LSRpltQLSGGEWQRVRLAAVLlqvwp 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956327 160 AMRPD--VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
Cdd:COG4138 147 TINPEgqLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-224 |
4.23e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 85.79 E-value: 4.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 22 IDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPisqqkgliRRLRQHVGFVFQSFNLFPHrt 101
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP--------EDYRKLFSAVFTDFHLFDQ-- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 102 vleniIEGPvivKGEPKEDATVRA----RELLAKVGLAGKETSYPrRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:PRK10522 412 -----LLGP---EGKPANPALVEKwlerLKMAHKLELEDGRISNL-KLSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489956327 178 ----ELVGEVLNTIRQLAQekrTMVIVTHEMSFArDVADRAIFMDQGRIVE 224
Cdd:PRK10522 483 hfrrEFYQVLLPLLQEMGK---TIFAISHDDHYF-IHADRLLEMRNGQLSE 529
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-231 |
5.22e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.30 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISQ--QKGLIRRlrqhVGFVFQ 92
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLD------AQPLESwsSKAFARK----VAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 93 SFNLFPHRTVLENIIEGPVIVKGE----PKEDATvRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILF 168
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGRYPWHGAlgrfGAADRE-KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 169 DEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQERGLTVIaVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-224 |
1.30e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 5 DVKNLVKKFHGQtvLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISQQK---GLIR 81
Cdd:PRK09700 267 EVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKkgmAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 RLRQHVGFvfqsfnlFPHRTVLENIIEGPVIVKG----------EPKEDATVRARELLAKVGLAGKETSYpRRLSGGQQQ 151
Cdd:PRK09700 345 ESRRDNGF-------FPNFSIAQNMAISRSLKDGgykgamglfhEVDEQRTAENQRELLALKCHSVNQNI-TELSGGNQQ 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956327 152 RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-178 |
1.53e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 84.40 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDiTIdtgkpisqqkglirrl 83
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE-TV---------------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 rqHVGFVFQSF-NLFPHRTVLENIIEGPVIVK-GepkeDATVRARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALA 160
Cdd:PRK11819 388 --KLAYVDQSRdALDPNKTVWEEISGGLDIIKvG----NREIPSRAYVGRFNFKGGDQQKKvGVLSGGERNRLHLAKTLK 461
|
170
....*....|....*...
gi 489956327 161 MRPDVILFDEPTSALDPE 178
Cdd:PRK11819 462 QGGNVLLLDEPTNDLDVE 479
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
7-224 |
2.03e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 83.69 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 7 KNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLrsiNLLeqpEG----GTIRvGDITIDtgkpisqqkGLIRR 82
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLM---KVL---SGvyphGSYE-GEILFD---------GEVCR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 LR-----QHVGFVF--QSFNLFPHRTVLENIIEGpvivkGEPK-------EDATVRARELLAKVGLAGKETSYPRRLSGG 148
Cdd:NF040905 69 FKdirdsEALGIVIihQELALIPYLSIAENIFLG-----NERAkrgvidwNETNRRARELLAKVGLDESPDTLVTDIGVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956327 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:NF040905 144 KQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-223 |
3.44e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 5 DVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGditidtGKPISqqkglIRRLR 84
Cdd:PRK11288 255 EVRLRLDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLD------GKPID-----IRSPR 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 85 QHV--GFVF-----QSFNLFPHRTVLENI-IE--------GPVIVKGEPKEDATVRARELlaKVGLAGKETSYpRRLSGG 148
Cdd:PRK11288 324 DAIraGIMLcpedrKAEGIIPVHSVADNInISarrhhlraGCLINNRWEAENADRFIRSL--NIKTPSREQLI-MNLSGG 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956327 149 QQQRVAIARALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGID---VGakhEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-220 |
2.80e-17 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 77.76 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISQQKglirRLRQHVGFVFQSF 94
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRS----RNRYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 95 NLFpHRTVLENIIEGPVIVKGEPKedATVRARELLAKVGLA--GKETSYPRR---LSGGQQQRVAIARALAMRPDVILFD 169
Cdd:cd03290 89 WLL-NATVEENITFGSPFNKQRYK--AVTDACSLQPDIDLLpfGDQTEIGERginLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489956327 170 EPTSALDPELVGEVLNT--IRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQG 220
Cdd:cd03290 166 DPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-223 |
3.01e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 80.32 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInlleqpeggtirVGDITIDTGKPISQQKGLIRR 82
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL------------VGELEPDSGTVKWSENANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 LRQHVGFVFQSfnlfpHRTVLENIIEgpviVKGEPKEDATVRAreLLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAM 161
Cdd:PRK15064 387 YAQDHAYDFEN-----DLTLFDWMSQ----WRQEGDDEQAVRG--TLGRLLFSQDDIKKSvKVLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956327 162 RPDVILFDEPTSALDPELVgEVLNTirQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESI-ESLNM--ALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-233 |
6.03e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 79.76 E-value: 6.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLEqpegG--TIRVGDITIDtGKPISQQKGl 79
Cdd:PRK10790 340 RIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTL---ASLLM----GyyPLTEGEIRLD-GRPLSSLSH- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 80 iRRLRQHVGFVFQSFNLFPHrTVLENIIEGPVIvkgepKEDATVRArelLAKVGLAGKETSYP-----------RRLSGG 148
Cdd:PRK10790 411 -SVLRQGVAMVQQDPVVLAD-TFLANVTLGRDI-----SEEQVWQA---LETVQLAELARSLPdglytplgeqgNNLSVG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 149 QQQRVAIARALAMRPDVILFDEPTSALDP---ELVGEVLNTIRqlaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQ 225
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSgteQAIQQALAAVR----EHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQ 555
|
....*...
gi 489956327 226 GPAKALFA 233
Cdd:PRK10790 556 GTHQQLLA 563
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-248 |
1.58e-16 |
|
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: 76.29 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 24 LEVEQG-----EVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdTGKP---ISQQKGLIRRLRQHVGFVFQSFN 95
Cdd:cd03237 15 LEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPqyiKADYEGTVRDLLSSITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 96 LFPHRTV----LENIIEgpvivkgepkedatvraRELlakvglagketsypRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:cd03237 94 YFKTEIAkplqIEQILD-----------------REV--------------PELSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956327 172 TSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIfmdqgrIVEQGPAKALFANPQQPRtRQFLEKFL 248
Cdd:cd03237 143 SAYLDVEQRLMASKVIRRFAENnEKTAFVVEHDIIMIDYLADRLI------VFEGEPSVNGVANPPQSL-RSGMNRFL 213
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-223 |
3.23e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 77.68 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINlleqpeggtirvGDITIDTGKPISQQKGLI 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN------------GEVLLDDGRIIYEQDLIV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRLRQHvgfvfqsfnlfPHR----TVLENIIEG--------------PVIVKGEPKED-----ATV-------------- 123
Cdd:PRK11147 69 ARLQQD-----------PPRnvegTVYDFVAEGieeqaeylkryhdiSHLVETDPSEKnlnelAKLqeqldhhnlwqlen 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 124 RARELLAKVGL-AGKETSyprRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPElvgevlnTIRQLAQ----EKRTMV 198
Cdd:PRK11147 138 RINEVLAQLGLdPDAALS---SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE-------TIEWLEGflktFQGSII 207
|
250 260
....*....|....*....|....*
gi 489956327 199 IVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:PRK11147 208 FISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-204 |
6.16e-16 |
|
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: 76.75 E-value: 6.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 27 EQGEVVAIIGPSGSGKTTllrSINLLeqpeGGTIR--VGDItidtGKPISQQKgLIRRlrqhvgfvFQSFNLFPHrtvLE 104
Cdd:COG1245 97 KKGKVTGILGPNGIGKST---ALKIL----SGELKpnLGDY----DEEPSWDE-VLKR--------FRGTELQDY---FK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 105 NIIEG--------------PVIVKGEPKE-----DATVRARELLAKVGLagkETSYPRR---LSGGQQQRVAIARALAMR 162
Cdd:COG1245 154 KLANGeikvahkpqyvdliPKVFKGTVREllekvDERGKLDELAEKLGL---ENILDRDiseLSGGELQRVAIAAALLRD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489956327 163 PDVILFDEPTSALDpelVGEVLN---TIRQLAQEKRTMVIVTHEM 204
Cdd:COG1245 231 ADFYFFDEPSSYLD---IYQRLNvarLIRELAEEGKYVLVVEHDL 272
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-221 |
6.81e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 76.51 E-value: 6.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidtgkpisqQKGLirrlrqHVGFVFQSF 94
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-------------QPGI------KVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 95 NLFPHRTVLENIIEGPVIVK-------------GEPKED---------------ATVRARELLAKVGLAGKETSYP---- 142
Cdd:TIGR03719 78 QLDPTKTVRENVEEGVAEIKdaldrfneisakyAEPDADfdklaaeqaelqeiiDAADAWDLDSQLEIAMDALRCPpwda 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 143 --RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVG--EvlntiRQLAQEKRTMVIVTHEMSFARDVADRAIFMD 218
Cdd:TIGR03719 158 dvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAwlE-----RHLQEYPGTVVAVTHDRYFLDNVAGWILELD 232
|
...
gi 489956327 219 QGR 221
Cdd:TIGR03719 233 RGR 235
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-231 |
9.97e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 76.32 E-value: 9.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRV-------GDITIdtgkpisq 75
Cdd:NF033858 266 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvdaGDIAT-------- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 76 qkglirrlRQHVGFVFQSFNLFPHRTVLENIiegpvivkgE--------PKEDATVRARELLAKVGLAGKETSYPRRLSG 147
Cdd:NF033858 338 --------RRRVGYMSQAFSLYGELTVRQNL---------ElharlfhlPAAEIAARVAEMLERFDLADVADALPDSLPL 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 148 GQQQRVAIARALAMRPDVILFDEPTSALDP-------ELVGEvlntirqLAQEKR-TMVIVTHEMSFA-RdvADRAIFMD 218
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVDPvardmfwRLLIE-------LSREDGvTIFISTHFMNEAeR--CDRISLMH 471
|
250
....*....|...
gi 489956327 219 QGRIVEQGPAKAL 231
Cdd:NF033858 472 AGRVLASDTPAAL 484
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-234 |
1.15e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 76.32 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQ--TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtgkpisQQKGLi 80
Cdd:PLN03130 1237 SIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI-------SKFGL- 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRLRQHVGFVFQS---------FNLFP---HRTV-LENIIEgpvivKGEPKEDATVRARELLAKVGLAGKEtsyprrLSG 147
Cdd:PLN03130 1309 MDLRKVLGIIPQApvlfsgtvrFNLDPfneHNDAdLWESLE-----RAHLKDVIRRNSLGLDAEVSEAGEN------FSV 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRqlaQEKR--TMVIVTHEMSFARDvADRAIFMDQGRIVEQ 225
Cdd:PLN03130 1378 GQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIR---EEFKscTMLIIAHRLNTIID-CDRILVLDAGRVVEF 1453
|
....*....
gi 489956327 226 GPAKALFAN 234
Cdd:PLN03130 1454 DTPENLLSN 1462
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-236 |
1.38e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.97 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidTGKPISQQkGLiRRLRQHvgfvfqsFNLF 97
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRV------NGREIGAY-GL-RELRRQ-------FSMI 1389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 98 PHRTVLeniIEGPVIVKGEPKEDATV----RARELlakVGLAGKETSY-----PRRLSG------GQQQRVAIARALAMR 162
Cdd:PTZ00243 1390 PQDPVL---FDGTVRQNVDPFLEASSaevwAALEL---VGLRERVASEsegidSRVLEGgsnysvGQRQLMCMARALLKK 1463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 163 -PDVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMsfaRDVA--DRAIFMDQGRIVEQGPAKALFANPQ 236
Cdd:PTZ00243 1464 gSGFILMDEATANIDPALDRQIQATVMS-AFSAYTVITIAHRL---HTVAqyDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-190 |
1.56e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 75.44 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLrSINLLEQPEGGTirvGDITIdtgkpISQQKG---LI 80
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL-SLITGDHPQGYS---NDLTL-----FGRRRGsgeTI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRLRQHVGFVFQSFNLfPHR---TVLENIIEG---PVIVKGEPKEDATVRARELLAKVGLAGKETSYP-RRLSGGQQQRV 153
Cdd:PRK10938 332 WDIKKHIGYVSSSLHL-DYRvstSVRNVILSGffdSIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLA 410
|
170 180 190
....*....|....*....|....*....|....*..
gi 489956327 154 AIARALAMRPDVILFDEPTSALDPelvgevLNtiRQL 190
Cdd:PRK10938 411 LIVRALVKHPTLLILDEPLQGLDP------LN--RQL 439
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-224 |
4.43e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.22 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 3 AIDVKNLVKKFHGQtvlhgidleVEQGEVVAIIGPSGSGKTTLLRSinLLEQ--PEGGTIRVGditidtgkpisqQKGLI 80
Cdd:PRK11147 328 QIDGKQLVKDFSAQ---------VQRGDKIALIGPNGCGKTTLLKL--MLGQlqADSGRIHCG------------TKLEV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 RRLRQHVGfvfqsfNLFPHRTVLENIIEGpvivkgepKEDATV--RARELLakvglagketSY-------PRR------- 144
Cdd:PRK11147 385 AYFDQHRA------ELDPEKTVMDNLAEG--------KQEVMVngRPRHVL----------GYlqdflfhPKRamtpvka 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 145 LSGGQQQRVAIARaLAMRP-DVILFDEPTSALDPELVgEVLNTIrqLAQEKRTMVIVTHEMSFARD-VADRAIFMDQGRI 222
Cdd:PRK11147 441 LSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDVETL-ELLEEL--LDSYQGTVLLVSHDRQFVDNtVTECWIFEGNGKI 516
|
..
gi 489956327 223 VE 224
Cdd:PRK11147 517 GR 518
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-241 |
5.16e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 73.30 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPE----GGTIRVGDItiDTGKP 72
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSdgwvKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDI--DLLRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 73 ISQQKgliRRLRQH-VGFVFQSFN--LFPHRTVLENIIEG--PVIVKGEPKEDATVRAR---ELLAKVGLAGKE---TSY 141
Cdd:PRK15093 79 SPRER---RKLVGHnVSMIFQEPQscLDPSERVGRQLMQNipGWTYKGRWWQRFGWRKRraiELLHRVGIKDHKdamRSF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 142 PRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQG 220
Cdd:PRK15093 156 PYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNtTILLISHDLQMLSQWADKINVLYCG 235
|
250 260
....*....|....*....|.
gi 489956327 221 RIVEQGPAKALFANPQQPRTR 241
Cdd:PRK15093 236 QTVETAPSKELVTTPHHPYTQ 256
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-215 |
8.59e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.30 E-value: 8.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 24 LEVE-----QGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrVGDITIdTGKPisqqkglirrlrQHVgfvfqsfnlfp 98
Cdd:PRK13409 355 LEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-DPELKI-SYKP------------QYI----------- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 99 hrtvleniiegpvivkgEPKEDATVRA---------------RELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:PRK13409 410 -----------------KPDYDGTVEDllrsitddlgssyykSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489956327 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAI 215
Cdd:PRK13409 473 DLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREaTALVVDHDIYMIDYISDRLM 525
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-205 |
1.60e-14 |
|
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: 70.86 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 18 VLHGIDLeVEQGEVVAIIGPSGSGKTTLLRsinlleqpeggtIRVGDITIDTGKPISQQ--KGLIRRLRqhvGFVFQSFn 95
Cdd:cd03236 16 KLHRLPV-PREGQVLGLVGPNGIGKSTALK------------ILAGKLKPNLGKFDDPPdwDEILDEFR---GSELQNY- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 96 lfphrtvLENIIEGPV--IVKGE-----PKEdATVRARELLAKVGLAGKETSYPRR-------------LSGGQQQRVAI 155
Cdd:cd03236 79 -------FTKLLEGDVkvIVKPQyvdliPKA-VKGKVGELLKKKDERGKLDELVDQlelrhvldrnidqLSGGELQRVAI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489956327 156 ARALAMRPDVILFDEPTSALDpelVGEVLN---TIRQLAQEKRTMVIVTHEMS 205
Cdd:cd03236 151 AAALARDADFYFFDEPSSYLD---IKQRLNaarLIRELAEDDNYVLVVEHDLA 200
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-204 |
2.10e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.15 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 26 VEQGEVVAIIGPSGSGKTTLLRsinlleqpeggtIRVGDITIDTGKPISQ--QKGLIRRLRqhvGFVFQSFnlfphrtvL 103
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVK------------ILSGELIPNLGDYEEEpsWDEVLKRFR---GTELQNY--------F 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 104 ENIIEG--------------PVIVKGepkedatvRARELLAKVGLAGKETSYPRR-------------LSGGQQQRVAIA 156
Cdd:PRK13409 153 KKLYNGeikvvhkpqyvdliPKVFKG--------KVRELLKKVDERGKLDEVVERlglenildrdiseLSGGELQRVAIA 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489956327 157 RALAMRPDVILFDEPTSALDpelVGEVLN---TIRQLAqEKRTMVIVTHEM 204
Cdd:PRK13409 225 AALLRDADFYFFDEPTSYLD---IRQRLNvarLIRELA-EGKYVLVVEHDL 271
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-220 |
3.31e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.68 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSinLLEQPEGGTIRVGDITIDtGKPIsqQKGLIRRlrqhVGFVFQSFNLF 97
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNV--LAERVTTGVITGGDRLVN-GRPL--DSSFQRS----IGYVQQQDLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 98 PHRTVLENII-----EGPVIVKGEPKEDATVRARELL-------AKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPDV 165
Cdd:TIGR00956 849 PTSTVRESLRfsaylRQPKSVSKSEKMEYVEEVIKLLemesyadAVVGVPGEG------LNVEQRKRLTIGVELVAKPKL 922
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489956327 166 ILF-DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS---FARdvADRAIFMDQG 220
Cdd:TIGR00956 923 LLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSailFEE--FDRLLLLQKG 979
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-244 |
3.40e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.68 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 8 NLVKKFHGQT---VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINllEQPEGGTIRV-GDITIDTgkpISQQKgLIRRL 83
Cdd:TIGR00956 63 RKLKKFRDTKtfdILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIA--SNTDGFHIGVeGVITYDG---ITPEE-IKKHY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRTVLENI-----IEGPVI-VKGEPKEDATVRAREL-LAKVGLA-GKET----SYPRRLSGGQQQ 151
Cdd:TIGR00956 137 RGDVVYNAETDVHFPHLTVGETLdfaarCKTPQNrPDGVSREEYAKHIADVyMATYGLShTRNTkvgnDFVRGVSGGERK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 152 RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMS-FARDVADRAIFMDQGRIVEQGP-- 227
Cdd:TIGR00956 217 RVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiYQCSqDAYELFDKVIVLYEGYQIYFGPad 296
|
250 260
....*....|....*....|...
gi 489956327 228 -AKALFAN-----PQQPRTRQFL 244
Cdd:TIGR00956 297 kAKQYFEKmgfkcPDRQTTADFL 319
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-215 |
4.40e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 71.35 E-value: 4.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 25 EVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRvGDITIdTGKPisqqkglirrlrQHVgfvfqsfnlfphrtvle 104
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKI-SYKP------------QYI----------------- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 105 niiegpvivkgEPKEDATVRarELLAKVGLAGKETSY-------P-----------RRLSGGQQQRVAIARALAMRPDVI 166
Cdd:COG1245 411 -----------SPDYDGTVE--EFLRSANTDDFGSSYykteiikPlgleklldknvKDLSGGELQRVAIAACLSRDADLY 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489956327 167 LFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAI 215
Cdd:COG1245 478 LLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLM 527
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-229 |
4.50e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.58 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 25 EVEQGEVVAIIGPSGSGKTTLLRSI-NLLEQPeggtirvGDITIDtGKPISQ--QKGLIRR---LRQHVG--F---VFQS 93
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMaGLLPGS-------GSIQFA-GQPLEAwsAAELARHrayLSQQQTppFampVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 94 FNLFPHrtvleniiegpvivKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA-LAMRPDV------I 166
Cdd:PRK03695 90 LTLHQP--------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956327 167 LFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRD 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
145-222 |
9.74e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.03 E-value: 9.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 145 LSGGQQQRVAIARALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
.
gi 489956327 222 I 222
Cdd:PRK10762 473 I 473
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
18-178 |
1.26e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.57 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidTGKPISQQKglirRLRqHVGFVFQSFNLF 97
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI------DGKTATRGD----RSR-FMAYLGHLPGLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 98 PHRTVLENIiegpVIVKGEPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:PRK13543 95 ADLSTLENL----HFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
.
gi 489956327 178 E 178
Cdd:PRK13543 171 E 171
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-233 |
1.69e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.77 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTV-LHGIDLEVEQGEVVAIIGPSGSGKTTLL------RSInlleqpEGGTIRV--GDITIdtgkpisqqkgliRRLRQ 85
Cdd:NF033858 12 GKTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKI------QQGRVEVlgGDMAD-------------ARHRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 86 HVG----FVFQSF--NLFPHRTVLENI-----IEGpvivkgepkEDATVRAR---ELLAKVGL-------AGKetsyprr 144
Cdd:NF033858 73 AVCpriaYMPQGLgkNLYPTLSVFENLdffgrLFG---------QDAAERRRridELLRATGLapfadrpAGK------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 145 LSGGQQQRVAIARALAMRPDVILFDEPTSALDP-------ELVgevlNTIRqlaQEKRTM-VIV-THEMSFARDVaDRAI 215
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPlsrrqfwELI----DRIR---AERPGMsVLVaTAYMEEAERF-DWLV 208
|
250
....*....|....*...
gi 489956327 216 FMDQGRIVEQGPAKALFA 233
Cdd:NF033858 209 AMDAGRVLATGTPAELLA 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-220 |
2.11e-13 |
|
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: 69.66 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 26 VEQGEVVAIIGPSGSGKTTLLRSINlleqpeggtirvGDITIDTGKPISQQKGLIRRLRQhvgfVFQSFNLFPHRTVLEN 105
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLT------------GDTTVTSGDATVAGKSILTNISD----VHQNMGYCPQFDAIDD 2025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 106 IIEGP------VIVKGEPKEDATVRARELLAKVGLagkeTSYPRRL----SGGQQQRVAIARALAMRPDVILFDEPTSAL 175
Cdd:TIGR01257 2026 LLTGRehlylyARLRGVPAEEIEKVANWSIQSLGL----SLYADRLagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489956327 176 DPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQG 220
Cdd:TIGR01257 2102 DPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-204 |
2.90e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.45 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRvgditidtgkpisqqkgliRRL 83
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-------------------RNG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGFVFQSFNLFPHRtvleniiegPVIVKGEPKEDATVRARELLA--KVGLAGKETSYP-RRLSGGQQQRVAIARALA 160
Cdd:PRK09544 66 KLRIGYVPQKLYLDTTL---------PLTVNRFLRLRPGTKKEDILPalKRVQAGHLIDAPmQKLSGGETQRVLLARALL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489956327 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEM 204
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLmVSHDL 181
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-231 |
3.68e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.22 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 7 KNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgditIDTGKPIsQQKGLIRRLRQH 86
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI------LFQGKEI-DFKSSKEALENG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 87 VGFVFQSFNLFPHRTVLENI------IEGPVIVKGEPKEDATVRARELLAKVGLAGKETSyprrLSGGQQQRVAIARALA 160
Cdd:PRK10982 75 ISMVHQELNLVLQRSVMDNMwlgrypTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVAT----LSVSQMQMIEIAKAFS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956327 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
Cdd:PRK10982 151 YNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-226 |
5.04e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.74 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEqpeggtirvgDITIDTGKPISQQKGLIR-- 81
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRE----------DYEVTGGTVEFKGKDLLEls 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 ---RLRQHVGFVFQSFNLFP---HRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYPRR-----LSGGQQ 150
Cdd:PRK09580 72 pedRAGEGIFMAFQYPVEIPgvsNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRsvnvgFSGGEK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVA-DRAIFMDQGRIVEQG 226
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-228 |
8.52e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.82 E-value: 8.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInlLEQPeGGTIRVGDITIDtGKPISQqkgLIRRL 83
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--AGHP-AYKILEGDILFK-GESILD---LEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 RQHVGfVFQSFnlfphrtvleniiEGPVIVKGEPKED---ATVRAR---------------ELLA-KVGLAGKETSYPRR 144
Cdd:CHL00131 81 RAHLG-IFLAF-------------QYPIEIPGVSNADflrLAYNSKrkfqglpeldpleflEIINeKLKLVGMDPSFLSR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 145 -----LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHemsFAR--D--VADRAI 215
Cdd:CHL00131 147 nvnegFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH---YQRllDyiKPDYVH 223
|
250
....*....|...
gi 489956327 216 FMDQGRIVEQGPA 228
Cdd:CHL00131 224 VMQNGKIIKTGDA 236
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-226 |
1.84e-12 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 63.88 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInlleqpeggtirvgditIDTGKPISQQKGLIRRLRQHVGFVFQsfnlfp 98
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG-----------------LYASGKARLISFLPKFSRNKLIFIDQ------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 99 hrtvLENIIegpvivkgepkedatvrarellaKVGLA----GKETSyprRLSGGQQQRVAIARALAMRPD--VILFDEPT 172
Cdd:cd03238 68 ----LQFLI-----------------------DVGLGyltlGQKLS---TLSGGELQRVKLASELFSEPPgtLFILDEPS 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFM------DQGRIVEQG 226
Cdd:cd03238 118 TGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVL-SSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-220 |
2.30e-12 |
|
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: 65.26 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 14 HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRvgditiDTGKpisqqkglirrlrqhVGFVFQS 93
Cdd:cd03291 48 VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK------HSGR---------------ISFSSQF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 94 FNLFPHrTVLENIIEG---------PVIVKGEPKEDATVRARE---LLAKVGLAgketsyprrLSGGQQQRVAIARALAM 161
Cdd:cd03291 107 SWIMPG-TIKENIIFGvsydeyrykSVVKACQLEEDITKFPEKdntVLGEGGIT---------LSGGQRARISLARAVYK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489956327 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQG 220
Cdd:cd03291 177 DADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLK-KADKILILHEG 234
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-234 |
5.34e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.38 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIdtgkpisqqkglirrlrqhvgfvfQSFNLF 97
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV------------------------AKFGLT 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 98 PHRTVLENIIEGPVIVKG------------------EPKEDATVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:PLN03232 1307 DLRRVLSIIPQSPVLFSGtvrfnidpfsehndadlwEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARAL 1386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 160 AMRPDVILFDEPTSALDPELVGEVLNTIRqlaQEKR--TMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAN 234
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIR---EEFKscTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-227 |
8.70e-12 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 64.87 E-value: 8.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 29 GEVVAIIGPSGSGKTTLLRSinLLEQPEGGTIRvGDITIdTGKPISQQKglIRRLRqhvGFVFQSFNLFPHRTVLENIIE 108
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDV--LAGRKTGGYIE-GDIRI-SGFPKKQET--FARIS---GYCEQNDIHSPQVTVRESLIY 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 109 G-----PVIVKGEPKEDATVRARELL-------AKVGLAGKETsyprrLSGGQQQRVAIARALAMRPDVILFDEPTSALD 176
Cdd:PLN03140 977 SaflrlPKEVSKEEKMMFVDEVMELVeldnlkdAIVGLPGVTG-----LSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489956327 177 PELVGEVLNTIRQLAQEKRTMVIVTHEMSF-ARDVADRAIFMDQ-GRIVEQGP 227
Cdd:PLN03140 1052 ARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLMKRgGQVIYSGP 1104
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-222 |
8.88e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.30 E-value: 8.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 22 IDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPisqqkglirRLRQHVGFVF-----QSFNL 96
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST---------AQRLARGLVYlpedrQSSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 97 FPHRTVLENIIEGPVIVKG---EPKEDATV--RARELLAkVGLAGKETSYpRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK15439 353 YLDAPLAWNVCALTHNRRGfwiKPARENAVleRYRRALN-IKFNHAEQAA-RTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489956327 172 TSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-235 |
9.62e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.41 E-value: 9.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSinLLEQPEggtirvgditidtgkpISQQKGLIRRlrqhvgfvfqSFNLF 97
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQS--LLSQFE----------------ISEGRVWAER----------SIAYV 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 98 PHRTVLEN-IIEGPVIVKGEpkEDA-----TVRARELLAKVGL--AGKETSYPRR---LSGGQQQRVAIARALAMRPDVI 166
Cdd:PTZ00243 727 PQQAWIMNaTVRGNILFFDE--EDAarladAVRVSQLEADLAQlgGGLETEIGEKgvnLSGGQKARVSLARAVYANRDVY 804
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 167 LFDEPTSALDPElVGE-VLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFANP 235
Cdd:PTZ00243 805 LLDDPLSALDAH-VGErVVEECFLGALAGKTRVLATHQVHVV-PRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-212 |
1.47e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISQQKglirrl 83
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQ------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 84 rqhVGFVFQSFNLFPHRTVLENIIEGPVIVKGEPKEDATVRARELlakvglaGKETSYP-RRLSGGQQQRVAIARALAMR 162
Cdd:PRK13540 76 ---LCFVGHRSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSL-------EHLIDYPcGLLSSGQKRQVALLRLWMSK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489956327 163 PDVILFDEPTSALDpELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVAD 212
Cdd:PRK13540 146 AKLWLLDEPLVALD-ELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-223 |
1.56e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.66 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInlLEQPEGGTIRvGDITIDtGKPIS-------------------QQKG 78
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSV--FGRSYGRNIS-GTVFKD-GKEVDvstvsdaidaglayvtedrKGYG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 79 LIrrLRQHVGFVFQSFNL--FPHRTVLENIIEgpVIVKGEPKEDATVRARELLAKVGlagketsyprRLSGGQQQRVAIA 156
Cdd:NF040905 351 LN--LIDDIKRNITLANLgkVSRRGVIDENEE--IKVAEEYRKKMNIKTPSVFQKVG----------NLSGGNQQKVVLS 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 157 RALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:NF040905 417 KWLFTDPDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-221 |
1.76e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 10 VKKFHGQ--TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgditidtgkpisqQKGLirrlrqHV 87
Cdd:PRK11819 12 VSKVVPPkkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP-------------APGI------KV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 88 GFVFQSFNLFPHRTVLENIIEGPVIVK-------------GEPKED---------------ATVRARELLAKVGLAGKET 139
Cdd:PRK11819 73 GYLPQEPQLDPEKTVRENVEEGVAEVKaaldrfneiyaayAEPDADfdalaaeqgelqeiiDAADAWDLDSQLEIAMDAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 140 SYP------RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVG--EvlntiRQLAQEKRTMVIVTHEMSFARDVA 211
Cdd:PRK11819 153 RCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAwlE-----QFLHDYPGTVVAVTHDRYFLDNVA 227
|
250
....*....|
gi 489956327 212 DRAIFMDQGR 221
Cdd:PRK11819 228 GWILELDRGR 237
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-247 |
2.25e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.99 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRV-GDITIdtgkpISQQKGLIRRLrqhvgfvfqsfnlf 97
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkGSAAL-----IAISSGLNGQL-------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 98 phrTVLENiIEGPVIVKGEPKEdatvRARELLAKV---GLAGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:PRK13545 101 ---TGIEN-IELKGLMMGLTKE----KIKEIIPEIiefADIGKFIYQPvKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFANpqqprTRQFLEKF 247
Cdd:PRK13545 173 VGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH-----YDEFLKKY 241
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-222 |
2.39e-11 |
|
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: 62.92 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 22 IDLEVEQGEVVAIIGPSGSGKTTLLRSI-NLLEQPEGGTIRVGDITIDTGKP---ISQQKGLIRRLRQHVGFVFQ----- 92
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNPaqaIRAGIAMVPEDRKRHGIVPIlgvgk 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 93 -----SFNLFPHRTVLENIIEGPVIvkGEPKEDATVRARELLAKVGlagketsyprRLSGGQQQRVAIARALAMRPDVIL 167
Cdd:TIGR02633 359 nitlsVLKSFCFKMRIDAAAELQII--GSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489956327 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-216 |
2.89e-11 |
|
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: 59.69 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 28 QGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISQQKGLIRRLRQHVGfvfqsfnlfphrtvlenii 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASG------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 108 egpvivkgepkedatvrarellakvglagketsyprrlSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVL--- 184
Cdd:smart00382 62 --------------------------------------SGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlle 103
|
170 180 190
....*....|....*....|....*....|....*
gi 489956327 185 ---NTIRQLAQEKRTMVIVTHEMSFARDVADRAIF 216
Cdd:smart00382 104 elrLLLLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-248 |
3.50e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 60.28 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 25 EVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTgKPisqqkglirrlrQHVgfvfqsfnlfphrtvle 104
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVY-KP------------QYI----------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 105 niiegpvivkgepkedatvrarellakvglagketsyprRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVL 184
Cdd:cd03222 71 ---------------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAA 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956327 185 NTIRQLAQE-KRTMVIVTHEMSFARDVADRAIfmdqgrIVEQGPAKALFANPQQPrTRQFLEKFL 248
Cdd:cd03222 112 RAIRRLSEEgKKTALVVEHDLAVLDYLSDRIH------VFEGEPGVYGIASQPKG-TREGINRFL 169
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-220 |
3.55e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.01 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 14 HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRvgditiDTGKpisqqkglirrlrqhVGFVFQS 93
Cdd:TIGR01271 437 YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK------HSGR---------------ISFSPQT 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 94 FNLFPHrTVLENIIEG---------PVIVKGEPKEDATVRARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPD 164
Cdd:TIGR01271 496 SWIMPG-TIKDNIIFGlsydeyrytSVIKACQLEEDIALFPEKDKTVLGEGGIT------LSGGQRARISLARAVYKDAD 568
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489956327 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQG 220
Cdd:TIGR01271 569 LYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-222 |
4.52e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 2 SAIDVKNLVKKfhgqtVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINlleqpegGTIR---VGDITIDtGKPISqqkg 78
Cdd:PRK13549 266 TAWDPVNPHIK-----RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLF-------GAYPgrwEGEIFID-GKPVK---- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 79 lIRR----LRQHVGFVFQS---FNLFPHRTVLENII--------EGPVIvkGEPKEDATVRARELLAKVglagkETSYPR 143
Cdd:PRK13549 329 -IRNpqqaIAQGIAMVPEDrkrDGIVPVMGVGKNITlaaldrftGGSRI--DDAAELKTILESIQRLKV-----KTASPE 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 144 ----RLSGGQQQRVAIARALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIF 216
Cdd:PRK13549 401 laiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLV 477
|
....*.
gi 489956327 217 MDQGRI 222
Cdd:PRK13549 478 MHEGKL 483
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
145-224 |
2.17e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 145 LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR--- 221
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLvag 471
|
...
gi 489956327 222 IVE 224
Cdd:PRK10982 472 IVD 474
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
134-208 |
4.58e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 4.58e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956327 134 LAGKETSyprRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPE---LVGEVLNTIRqlAQEKRTMVIVTHEMSFAR 208
Cdd:PTZ00265 572 LVGSNAS---KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseyLVQKTINNLK--GNENRITIIIAHRLSTIR 644
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
80-205 |
1.02e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.50 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 80 IRRLRQHVGFVFQSFNLFpHRTVLENIIEGpvivkgepKEDATVRARELLAKVG--------LAGKETS----YPRRLSG 147
Cdd:PTZ00265 1291 LKDLRNLFSIVSQEPMLF-NMSIYENIKFG--------KEDATREDVKRACKFAaidefiesLPNKYDTnvgpYGKSLSG 1361
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956327 148 GQQQRVAIARALAMRPDVILFDEPTSALDP---ELVGEVLNTIRQLAQekRTMVIVTHEMS 205
Cdd:PTZ00265 1362 GQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKAD--KTIITIAHRIA 1420
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-189 |
1.97e-09 |
|
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: 57.61 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKF--HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEggtirvGDITIDTgkpISQQKGLIR 81
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE------GEIQIDG---VSWNSVTLQ 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 RLRQHVGFVFQSFNLFPHrTVLENIiegpvivkgEPKEDATVRARELLA-KVGLAGKETSYPRR-----------LSGGQ 149
Cdd:TIGR01271 1289 TWRKAFGVIPQKVFIFSG-TFRKNL---------DPYEQWSDEEIWKVAeEVGLKSVIEQFPDKldfvlvdggyvLSNGH 1358
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489956327 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQ 189
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-233 |
2.42e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINlleqpeggtirvGDITIDTGKPISQQKGLI 80
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALA------------GELPLLSGERQSQFSHIT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 81 R----RLRQHVGFVFQSFN---LFPH-----RTVLENIIEGpvivkgepkEDATVRARELLAKVGLagkETSYPRR---L 145
Cdd:PRK10938 69 RlsfeQLQKLVSDEWQRNNtdmLSPGeddtgRTTAEIIQDE---------VKDPARCEQLAQQFGI---TALLDRRfkyL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 146 SGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQ 225
Cdd:PRK10938 137 STGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAET 216
|
250
....*....|...
gi 489956327 226 GP-----AKALFA 233
Cdd:PRK10938 217 GEreeilQQALVA 229
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-233 |
3.32e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.88 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITI-DTGkpisqqkglIRRLRQHVGFVFQSFNL 96
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIaKIG---------LHDLRFKITIIPQDPVL 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 97 FPHrTVLENIieGPVivkGEPKEDATVRARELlakVGLAGKETSYPRRL-----------SGGQQQRVAIARALAMRPDV 165
Cdd:TIGR00957 1372 FSG-SLRMNL--DPF---SQYSDEEVWWALEL---AHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956327 166 ILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDVAdRAIFMDQGRIVEQGPAKALFA 233
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-189 |
3.96e-09 |
|
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: 55.63 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKF--HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEggtirvGDITIDTgkpISQQKGLIR 81
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE------GDIQIDG---VSWNSVPLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 82 RLRQHVGFVFQSFNLF--PHRTVLENiiegpvivKGEPKEDATVRAREllaKVGLAGKETSYPRR-----------LSGG 148
Cdd:cd03289 74 KWRKAFGVIPQKVFIFsgTFRKNLDP--------YGKWSDEEIWKVAE---EVGLKSVIEQFPGQldfvlvdggcvLSHG 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489956327 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQ 189
Cdd:cd03289 143 HKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ 183
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
121-222 |
5.49e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.05 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 121 ATVRARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDpelvgevLNTIRQLAQE----KR 195
Cdd:PRK15064 131 AEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------INTIRWLEDVlnerNS 203
|
90 100 110
....*....|....*....|....*....|.
gi 489956327 196 TMVIVTHEMSFARDV----ADraifMDQGRI 222
Cdd:PRK15064 204 TMIIISHDRHFLNSVcthmAD----LDYGEL 230
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-212 |
3.97e-08 |
|
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: 51.84 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 31 VVAIIGPSGSGKTTLLRSINLL---EQPEGGTIRVGDITIDTGKPISQQKGLIRRLRQHVGF-VFQSFNlfphrtVLENI 106
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKYAltgELPPNSKGGAHDPKLIREGEVRAQVKLAFENANGKKYtITRSLA------ILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 107 IegpvIVKGEPKEDATVRAREllakvglagketsyprRLSGGQQQ------RVAIARALAMRPDVILFDEPTSALDPELV 180
Cdd:cd03240 98 I----FCHQGESNWPLLDMRG----------------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENI 157
|
170 180 190
....*....|....*....|....*....|....
gi 489956327 181 GEVLNTI--RQLAQEKRTMVIVTHEMSFaRDVAD 212
Cdd:cd03240 158 EESLAEIieERKSQKNFQLIVITHDEEL-VDAAD 190
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-233 |
9.65e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 51.45 E-value: 9.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLVKKFHG--QTVLHGIDLEVEQGEVVAIIGPSGSGKTTL----LRSINLLEqpeggtirvGDITIDtGKPISqqK 77
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD---------GKIVID-GIDIS--K 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 78 GLIRRLRQHVGFVFQS---------FNLFPHRTVLENIIegpvivkGEPKEDATVRARELLAKVGLAGKETSYPRRLSGG 148
Cdd:cd03288 88 LPLHTLRSRLSIILQDpilfsgsirFNLDPECKCTDDRL-------WEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 149 QQQRVAIARALAMRPDVILFDEPTSALDPElVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPA 228
Cdd:cd03288 161 QRQLFCLARAFVRKSSILIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTP 238
|
....*
gi 489956327 229 KALFA 233
Cdd:cd03288 239 ENLLA 243
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
29-202 |
1.09e-07 |
|
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: 50.05 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 29 GEVVAIIGPSGSGKTTLLRSINLLeqpeggtirvgditidtgkpisqqkglirrlrqhvgFVFQSFNLFPHRTVLENIIE 108
Cdd:cd03227 21 GSLTIITGPNGSGKSTILDAIGLA------------------------------------LGGAQSATRRRSGVKAGCIV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 109 gpvivkgepkedATVRARELLAKVGLagketsyprrlSGGQQQRVAIARALA----MRPDVILFDEPTSALDPELVGEVL 184
Cdd:cd03227 65 ------------AAVSAELIFTRLQL-----------SGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALA 121
|
170
....*....|....*...
gi 489956327 185 NTIRQLAQEKRTMVIVTH 202
Cdd:cd03227 122 EAILEHLVKGAQVIVITH 139
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
121-210 |
2.42e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 121 ATVRARELLAKVGLAGK-ETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDpelVGEVLNTIRQLAQEKRTMVI 199
Cdd:PLN03073 320 AEARAASILAGLSFTPEmQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIV 396
|
90
....*....|.
gi 489956327 200 VTHEMSFARDV 210
Cdd:PLN03073 397 VSHAREFLNTV 407
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-222 |
2.62e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 21 GIDLEVEqgevVAIIGPSGSGKTTLLRSINLLEQPEGGTI-RVGDITIDTgkpISQQkglirrlrqHVGFVFQSFN--LF 97
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVfRSAKVRMAV---FSQH---------HVDGLDLSSNplLY 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 98 PHRTVleniiegpvivKGEPKEdatvRARELLAKVGLAGKETSYPR-RLSGGQQQRVAIARALAMRPDVILFDEPTSALD 176
Cdd:PLN03073 595 MMRCF-----------PGVPEQ----KLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489956327 177 PELVgEVLntIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PLN03073 660 LDAV-EAL--IQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
15-205 |
3.06e-07 |
|
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: 50.90 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgdiTIDT-GKP--ISQQKGLIRR-LRQHVGFV 90
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL-----TKPAkGKLfyVPQRPYMTLGtLRDQIIYP 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 91 FQSFNLFPH---RTVLENIIEgpvivkgepkedaTVRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVIL 167
Cdd:TIGR00954 539 DSSEDMKRRglsDKDLEQILD-------------NVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190
....*....|....*....|....*....|....*....
gi 489956327 168 FDEPTSALDPELVGEvlntIRQLAQEKR-TMVIVTHEMS 205
Cdd:TIGR00954 606 LDECTSAVSVDVEGY----MYRLCREFGiTLFSVSHRKS 640
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
23-216 |
3.88e-07 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 50.00 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 23 DLEVE-QGEVVAIIGPSGSGKTTLLRSINL-LEQPEGGTIRVGD-------------ITIDTGKPISQ--QKGLIRRLRQ 85
Cdd:COG3593 16 DLSIElSDDLTVLVGENNSGKSSILEALRLlLGPSSSRKFDEEDfylgddpdlpeieIELTFGSLLSRllRLLLKEEDKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 86 HVGFVFQSFN--LFPHRTVLENIIEGPVIVKGEPKE---DATVRARELLAK---VGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:COG3593 96 ELEEALEELNeeLKEALKALNELLSEYLKELLDGLDlelELSLDELEDLLKslsLRIEDGKELPLDRLGSGFQRLILLAL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956327 158 ALAM-------RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIF 216
Cdd:COG3593 176 LSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVPLENIR 241
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
124-224 |
5.41e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 124 RARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDpelVGEVLNTIRQLAQEKRTMVIVTH 202
Cdd:PRK10636 128 RAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILISH 204
|
90 100
....*....|....*....|..
gi 489956327 203 EMSFARDVADRAIFMDQGRIVE 224
Cdd:PRK10636 205 DRDFLDPIVDKIIHIEQQSLFE 226
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-202 |
7.69e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.47 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 4 IDVKNLvKKFHGQTVlhgIDLEveqGEVVAIIGPSGSGKTTLLRSINLL---EQPEGGTIRVGDITIDTGKP-------I 73
Cdd:COG0419 5 LRLENF-RSYRDTET---IDFD---DGLNLIVGPNGAGKSTILEAIRYAlygKARSRSKLRSDLINVGSEEAsvelefeH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 74 SQQKGLIRRlRQHVGFVFQSFNLFPHRTVLENIIEGPVIVK-----GEPKEDATVRARELLAKVGLAGK------ETSYP 142
Cdd:COG0419 78 GGKRYRIER-RQGEFAEFLEAKPSERKEALKRLLGLEIYEElkerlKELEEALESALEELAELQKLKQEilaqlsGLDPI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 143 RRLSGGQQQRVAIARALAMrpdviLFDepTSALDPELVGEVLNTIRQLAqekrtmvIVTH 202
Cdd:COG0419 157 ETLSGGERLRLALADLLSL-----ILD--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-226 |
9.07e-07 |
|
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: 48.41 E-value: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTL-------------LRSINLLEQPEGGTIRVGDITIDTGKP--IS-QQKGLIRR 82
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLSAYARQFLGQMDKPDVDSIEGLSpaIAiDQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 83 LRQHVGFVFQSFNLFphRTVLENIiegpvivkgepkedaTVRAR-ELLAKVGLA----GKETSyprRLSGGQQQRVAIAR 157
Cdd:cd03270 91 PRSTVGTVTEIYDYL--RLLFARV---------------GIRERlGFLVDVGLGyltlSRSAP---TLSGGEAQRIRLAT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 158 ALAMRPDVIL--FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFM------DQGRIVEQG 226
Cdd:cd03270 151 QIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIR-AADHVIDIgpgagvHGGEIVAQG 226
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-222 |
2.82e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 16 QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLeqpeGGTIrvgditidtgKPISQQKGLIRRLRqhVGFVFQsfn 95
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTL---IKLL----AGEL----------APVSGEIGLAKGIK--LGYFAQ--- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 96 lfpHRTVLENIIEGPV--IVKGEPKEdATVRARELLAKVGLAG-KETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:PRK10636 383 ---HQLEFLRADESPLqhLARLAPQE-LEQKLRDYLGGFGFQGdKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489956327 173 SALDPELvgevlntiRQLAQE-----KRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PRK10636 459 NHLDLDM--------RQALTEalidfEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
16-178 |
3.11e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.40 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 16 QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDT-GKPisqqkglirrlrqHVGFVFQSF 94
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiAKP-------------YCTYIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 95 NLFPHRTVLENIIEGPVIVKGEPKEDATV---RARELLakvglagKETSYprRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK13541 80 GLKLEMTVFENLKFWSEIYNSAETLYAAIhyfKLHDLL-------DEKCY--SLSSGMQKIVAIARLIACQSDLWLLDEV 150
|
....*..
gi 489956327 172 TSALDPE 178
Cdd:PRK13541 151 ETNLSKE 157
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-247 |
6.00e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.35 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTI-RVGDITIdtgkpISQQKGLIRRLrqhvgfvfqsfnlf 97
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdRNGEVSV-----IAISAGLSGQL-------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 98 phrTVLENIIEGPVIVKGEPKEdatvrARELLAKV---GLAGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:PRK13546 101 ---TGIENIEFKMLCMGFKRKE-----IKAMTPKIiefSELGEFIYQPvKKYSSGMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956327 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFanpqqPRTRQFLEKF 247
Cdd:PRK13546 173 VGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL-----PKYEAFLNDF 241
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
145-232 |
1.15e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 145 LSGGQQQRVAIARALAMRPDVILF--DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE---MSFArdvadraifmdq 219
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGITYilDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLA------------ 544
|
90
....*....|...
gi 489956327 220 GRIVEQGPAKALF 232
Cdd:PRK00635 545 DRIIDIGPGAGIF 557
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
19-227 |
1.80e-05 |
|
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: 44.91 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI------NLL----EQPEGGTIRVGDITIDTGKPISQQkgLI-RRLRQ-- 85
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTlypalaRRLhlkkEQPGNHDRIEGLEHIDKVIVIDQS--PIgRTPRSnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 86 --HVGfVFQSF-NLFP--------HRTVLENIIEGPVI--VKGEPKEDA--------TVRAR-ELLAKVGLA----GKET 139
Cdd:cd03271 89 atYTG-VFDEIrELFCevckgkryNRETLEVRYKGKSIadVLDMTVEEAleffenipKIARKlQTLCDVGLGyiklGQPA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 140 SYprrLSGGQQQRVAIARALAMR---PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIF 216
Cdd:cd03271 168 TT---LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK-CADWIID 243
|
250
....*....|....*..
gi 489956327 217 MDQ------GRIVEQGP 227
Cdd:cd03271 244 LGPeggdggGQVVASGT 260
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-204 |
2.39e-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: 2.39e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956327 145 LSGGQQQRVAIARALAMR---PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEM 204
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| ABC_ATPase |
pfam09818 |
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. ... |
146-241 |
1.46e-04 |
|
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. This entry also includes MRB1590 from Trypanosoma brucei brucei has a central ATPase domain homologous to this domain.
Pssm-ID: 462914 Cd Length: 282 Bit Score: 42.20 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 146 SGGQQQRVAIARALAMRPDVILFDEPTSA--------LDPELVG---EVLNTIRQLAQEKR-----TMVIVTHEMSFARD 209
Cdd:pfam09818 159 SGSTSQAANIMEALEAGASLLLIDEDTSAtnfmirdeRMQALVSkdkEPITPFVDRVRSLYddlgvSTILVVGGSGDYLD 238
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489956327 210 VADRAIFMDQGR----------IVEQGPAKALFANPQQPRTR 241
Cdd:pfam09818 239 VADTVILMDEYRpsdvteeakeIAEELPTGRYEEASKFGPPR 280
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
99-202 |
1.61e-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: 41.99 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 99 HRTVLENIIEGPVIVKGEPKEDATVRARELLAKVGLAGKETSYprRLSGGQQQ---RVAIARALAMRPDVILFDEPTSAL 175
Cdd:pfam13304 193 KLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAF--ELSDGTKRllaLLAALLSALPKGGLLLIDEPESGL 270
|
90 100
....*....|....*....|....*..
gi 489956327 176 DPELVGEVLNTIRQLAQEKRTMVIVTH 202
Cdd:pfam13304 271 HPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
13-52 |
2.93e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.96 E-value: 2.93e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 489956327 13 FHGQTVlhgidlEVEQGEVVAIIGPSGSGKTTLLRSINLL 52
Cdd:pfam13555 12 FDGHTI------PIDPRGNTLLTGPSGSGKSTLLDAIQTL 45
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
145-227 |
6.78e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 145 LSGGQQQRVAIARAL---AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADraifmdqgR 221
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VAD--------Y 880
|
....*.
gi 489956327 222 IVEQGP 227
Cdd:PRK00635 881 VLELGP 886
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-236 |
1.08e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 145 LSGGQQQRVAIARALAMRPDVILF--DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQ--- 219
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIR-AADYVIDIGPgag 567
|
90 100
....*....|....*....|
gi 489956327 220 ---GRIVEQGPAKALFANPQ 236
Cdd:TIGR00630 568 ehgGEVVASGTPEEILANPD 587
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
10-202 |
1.28e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.79 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 10 VKKFHGQTVLHGIDLE-VEQGEVVAIIGPSGSGKTTLLRSINLleQPEGGTIRVGDiTIDTGKPISQQKGLIRrlrqhVG 88
Cdd:cd03279 8 LKNFGPFREEQVIDFTgLDNNGLFLICGPTGAGKSTILDAITY--ALYGKTPRYGR-QENLRSVFAPGEDTAE-----VS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 89 FVFQSFNLFpHRtvleniiegpviVKGEPKEDATVRARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAM------ 161
Cdd:cd03279 80 FTFQLGGKK-YR------------VERSRGLDYDQFTRIVLLPQGEFDRFLARPvSTLSGGETFLASLSLALALsevlqn 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489956327 162 ----RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH 202
Cdd:cd03279 147 rggaRLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISH 191
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
31-75 |
1.72e-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: 38.91 E-value: 1.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 489956327 31 VVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGDITIDTGKPISQ 75
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGI 45
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
31-145 |
1.84e-03 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 37.67 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 31 VVAIIGPSGSGKTTLLRsiNLLEQPegGTIRVGD------ITIDTGKPISQQKGLIRRLRQHVgfvfqsfnlfpHRTVLE 104
Cdd:pfam13671 1 LILLVGLPGSGKSTLAR--RLLEEL--GAVRLSSdderkrLFGEGRPSISYYTDATDRTYERL-----------HELARI 65
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 489956327 105 NIIEG-PVIVkgepkeDAT-VRARELLAKVGLAgKETSYPRRL 145
Cdd:pfam13671 66 ALRAGrPVIL------DATnLRRDERARLLALA-REYGVPVRI 101
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
143-246 |
2.10e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.06 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 143 RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIvtheMSFAR------DVADRAIF 216
Cdd:PLN03140 335 RGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVL----MSLLQpapetfDLFDDIIL 410
|
90 100 110
....*....|....*....|....*....|....*...
gi 489956327 217 MDQGRIVEQGPAKAL--------FANPQQPRTRQFLEK 246
Cdd:PLN03140 411 LSEGQIVYQGPRDHIleffescgFKCPERKGTADFLQE 448
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
8-62 |
2.19e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 39.02 E-value: 2.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489956327 8 NLVKKFHGQTVLHGIDLeveQGEVVAIIGPSGSGKTTLLRSI--NLLEQPEGGTIRV 62
Cdd:COG5635 162 NLLERIESLKRLELLEA---KKKRLLILGEPGSGKTTLLRYLalELAERYLDAEDPI 215
|
|
| MobB |
COG1763 |
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ... |
31-46 |
2.19e-03 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 441369 [Multi-domain] Cd Length: 162 Bit Score: 37.85 E-value: 2.19e-03
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
145-248 |
2.34e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 145 LSGGQQQRVAIARALAMRPD---VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMsfarDV---ADRAIFM- 217
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNL----DViktADWIIDLg 902
|
90 100 110
....*....|....*....|....*....|....*.
gi 489956327 218 ----DQ-GRIVEQGPAKALFANPQQPrTRQFLEKFL 248
Cdd:COG0178 903 peggDGgGEIVAEGTPEEVAKVKASY-TGRYLKEYL 937
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
31-49 |
2.88e-03 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 37.90 E-value: 2.88e-03
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
136-201 |
4.46e-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: 37.62 E-value: 4.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956327 136 GKETSYPRRLSGGQQQRVAIARALAM-RPD---VILFDEPTSALDPELVGEVLNTIRQLAqeKRTMVIVT 201
Cdd:cd03272 150 QDEQQEMQQLSGGQKSLVALALIFAIqKCDpapFYLFDEIDAALDAQYRTAVANMIKELS--DGAQFITT 217
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
145-189 |
5.54e-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: 35.29 E-value: 5.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489956327 145 LSGGQQQR---VAIARALAM----------RPDVILFDEPTSALDPELVGEVLNTIRQ 189
Cdd:pfam13558 33 LSGGEKQLlayLPLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
23-52 |
5.66e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.60 E-value: 5.66e-03
10 20 30
....*....|....*....|....*....|
gi 489956327 23 DLEVEQGEVVAIIGPSGSGKTTLLRSINLL 52
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDALRFL 44
|
|
| BMS1 |
cd01882 |
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ... |
31-71 |
6.03e-03 |
|
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is an essential, evolutionarily conserved, nucleolar protein. Its depletion interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Bms1, the putative endonuclease Rc11, and the essential U3 small nucleolar RNA form a stable subcomplex that is believed to control an early step in the formation of the 40S subumit. The C-terminal domain of Bms1 contains a GTPase-activating protein (GAP) that functions intramolecularly. It is believed that Rc11 activates Bms1 by acting as a guanine-nucleotide exchange factor (GEF) to promote GDP/GTP exchange, and that activated (GTP-bound) Bms1 delivers Rc11 to the preribosomes.
Pssm-ID: 206669 [Multi-domain] Cd Length: 231 Bit Score: 36.93 E-value: 6.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 489956327 31 VVAIIGPSGSGKTTLLRSinLLEQPEGGTIRV--GDITIDTGK 71
Cdd:cd01882 41 VVVVVGPPGVGKSTLIRS--LIKRYTKQNLSDikGPITIVTGK 81
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
32-69 |
6.31e-03 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 36.04 E-value: 6.31e-03
10 20 30
....*....|....*....|....*....|....*...
gi 489956327 32 VAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgdITIDT 69
Cdd:cd01127 2 TLVLGTTGSGKTTSIVIPLLDQAARGGSV----IITDP 35
|
|
| PEPCK_HprK |
cd00820 |
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the ... |
15-64 |
6.77e-03 |
|
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the first committed step in the diversion of tricarboxylic acid cycle intermediates toward gluconeogenesis. It catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate to yield phosphoenolpyruvate and carbon dioxide, using a nucleotide molecule (ATP or GTP) for the phosphoryl transfer, and has a strict requirement for divalent metal ions for activity. PEPCK's separate into two phylogenetic groups based on their nucleotide substrate specificity (the ATP-, and GTP-dependent groups).HprK/P, the bifunctional histidine-containing protein kinase/phosphatase, controls the phosphorylation state of the phosphocarrier protein HPr and regulates the utilization of carbon sources by gram-positive bacteria. It catalyzes both the ATP-dependent phosphorylation of HPr and its dephosphorylation by phosphorolysis. PEPCK and the C-terminal catalytic domain of HprK/P are structurally similar with conserved active site residues suggesting that these two phosphotransferases have related functions.
Pssm-ID: 238418 [Multi-domain] Cd Length: 107 Bit Score: 35.35 E-value: 6.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 489956327 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLlrsinLLEQPEGGTIRVGD 64
Cdd:cd00820 1 GTTSLHGVLVDVYGKVGVLITGDSGIGKTEL-----ALELIKRKHRLVGD 45
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
26-54 |
6.92e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.07 E-value: 6.92e-03
10 20 30
....*....|....*....|....*....|
gi 489956327 26 VEQGE-VVAIIGPSGSGKTTLLRSinLLEQ 54
Cdd:COG3267 39 LAQGGgFVVLTGEVGTGKTTLLRR--LLER 66
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
28-71 |
7.60e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 36.37 E-value: 7.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 489956327 28 QGEVVAIIGPSGSGKTTLlrsINLLeQPEgGTIRVGDITIDTGK 71
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTL---LNAL-LPE-LDLRTGEISEKLGR 143
|
|
| YejR |
COG0523 |
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ... |
39-68 |
7.73e-03 |
|
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];
Pssm-ID: 440289 [Multi-domain] Cd Length: 318 Bit Score: 37.07 E-value: 7.73e-03
10 20 30
....*....|....*....|....*....|....*
gi 489956327 39 GSGKTTLLRsiNLLEQPEGGTIRV-----GDITID 68
Cdd:COG0523 14 GAGKTTLLN--HLLANPEGRRIAVivnefGEVGID 46
|
|
| |
